|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-288 |
2.14e-132 |
|
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: 375.53 E-value: 2.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqkl 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD-ITGL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 hpddflhpaqlgrriyykmfgGTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRHLLAGILNTRGYRQAESQAL 161
Cdd:COG0411 72 ---------------------PPHRIARLGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:COG0411 131 ERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLGAEEEE 288
Cdd:COG0411 211 HDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEAYLGEEAAA 257
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-283 |
3.84e-130 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 369.70 E-value: 3.84e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdvIQVLgqk 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH-----IEGL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhPDdflhpaqlgrriyykmfggtHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRHLLAGILNTRGYRQAESQA 160
Cdd:PRK11300 73 --PG--------------------HQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:PRK11300 131 LDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLG 283
Cdd:PRK11300 211 EHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYLG 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-277 |
1.58e-106 |
|
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: 308.98 E-value: 1.58e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDviqvlgqklhpdd 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-ITG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flHPAqlgrriyykmfggtHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRHLLAGilntrGYRQAESQALDRAF 165
Cdd:cd03219 67 --LPP--------------HEIARLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLA-----RARREEREARERAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRqQHGITVLLIEHDMG 245
Cdd:cd03219 126 ELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMD 204
|
250 260 270
....*....|....*....|....*....|..
gi 490250751 246 MVMEISDHIIVLDHGDVIARGAPQAIQANASV 277
Cdd:cd03219 205 VVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-283 |
8.96e-60 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 190.71 E-value: 8.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviqvlgqk 80
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhpaqlgrriyykMFGGTHLVN-------RAGLARTFQNIRLFREMSVIENLLVAQHTqvNRHLLAGILNTRGy 153
Cdd:COG4674 68 -------------------LFGGTDLTGldeheiaRLGIGRKFQKPTVFEELTVFENLELALKG--DRGVFASLFARLT- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 rQAESQALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQH 233
Cdd:COG4674 126 -AEERDRIEEV---LETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490250751 234 giTVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLG 283
Cdd:COG4674 202 --SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPRVIEVYLG 249
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-283 |
2.60e-58 |
|
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: 186.34 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqVLGQKlh 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-------ITGLP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 pddflhpaqlgrriyykmfggTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTqvnrhllagilntRGYRQAESQALD 162
Cdd:COG0410 72 ---------------------PHRIARLGIGYVPEGRRIFPSLTVEENLLLGAYA-------------RRDRAEVRADLE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVV-EMvdcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIE 241
Cdd:COG0410 118 RVYELFPRLkER---RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVE 193
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLG 283
Cdd:COG0410 194 QNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-287 |
2.96e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSivlrarekvtdvIQVLGQKLHPDd 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE------------VRVLGEDVARD- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhPAQLGRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENLlvaqhtqvnrHLLAGIlntrgYRQAESQALDRAF 165
Cdd:COG1131 68 ---PAEVRRRIGY----------------VPQEPALYPDLTVRENL----------RFFARL-----YGLPRKEARERID 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMG 245
Cdd:COG1131 114 ELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLE 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490250751 246 MVMEISDHIIVLDHGDVIARGAPQAIQANA--SVIAAYLGAEEE 287
Cdd:COG1131 193 EAERLCDRVAIIDKGRIVADGTPDELKARLleDVFLELTGEEAR 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-274 |
8.99e-55 |
|
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: 176.86 E-value: 8.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqVLGQKlhpdd 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD-------ITGLP----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmfggTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHtqvnrhllagilntRGYRQAESQALDRAF 165
Cdd:cd03224 69 ------------------PHERARAGIGYVPEGRRIFPELTVEENLLLGAY--------------ARRRAKRKARLERVY 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlevvEM----VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIE 241
Cdd:cd03224 117 ------ELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVE 189
|
250 260 270
....*....|....*....|....*....|...
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:cd03224 190 QNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-273 |
3.56e-51 |
|
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: 168.23 E-value: 3.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL------------VDGQD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHpddflhpaQLGRRIYYKMfggthlvnRAGLARTFQNIRLFREMSVIENllVA----QHTQVNrhllagilntrgyrqa 156
Cdd:COG1127 69 IT--------GLSEKELYEL--------RRRIGMLFQGGALFDSLTVFEN--VAfplrEHTDLS---------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 157 ESQALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGIT 236
Cdd:COG1127 115 EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLT 194
|
250 260 270
....*....|....*....|....*....|....*..
gi 490250751 237 VLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:COG1127 195 SVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-281 |
2.99e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 163.34 E-value: 2.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQK 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV------------RLFGKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhPAQLGRRIYYkmfggthLVNRAGLARTFQnirlfreMSVIEnlLVAQHTQVNRHLLagilntRGYRQAESQA 160
Cdd:COG1121 70 --------PRRARRRIGY-------VPQRAEVDWDFP-------ITVRD--VVLMGRYGRRGLF------RRPSRADREA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:COG1121 120 VDEA---LERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVV 195
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGdVIARGAPQAIQANASVIAAY 281
Cdd:COG1121 196 THDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-274 |
1.65e-47 |
|
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: 158.87 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVLgqklhpdd 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgRRIYYkMFGGTHLVNRaglartfqnirlfreMSVIENLlvaqhtqvnrHLLAgilntRGYRQAESQALDRAF 165
Cdd:COG4555 74 --------RQIGV-LPDERGLYDR---------------LTVRENI----------RYFA-----ELYGLFDEELKKRIE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMG 245
Cdd:COG4555 115 ELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQ 193
|
250 260
....*....|....*....|....*....
gi 490250751 246 MVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG4555 194 EVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-273 |
1.30e-46 |
|
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: 156.57 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFG-GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrareKVTDVIQVLGQKLHpd 84
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI----DGTDINKLKGKALR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dflhpaQLGRRIyykmfggthlvnraglARTFQNIRLFREMSVIENLLVAQHTQvnRHLLAGILNtrGYRQAESQaldRA 164
Cdd:cd03256 75 ------QLRRQI----------------GMIFQQFNLIERLSVLENVLSGRLGR--RSTWRSLFG--LFPKEEKQ---RA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 FYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDM 244
Cdd:cd03256 126 LAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV 205
|
250 260
....*....|....*....|....*....
gi 490250751 245 GMVMEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:cd03256 206 DLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-271 |
3.58e-46 |
|
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: 155.18 E-value: 3.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLmmHF---GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSivlrarekvtdvIQVLGQKLH 82
Cdd:COG1122 1 IELENL--SFsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGE------------VLVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 PDDFlhpAQLGRRIyykmfggthlvnraGLarTFQNIR--LFrEMSVIENllVAQhtqvnrhllaGILNtRGYRQAEsqA 160
Cdd:COG1122 67 KKNL---RELRRKV--------------GL--VFQNPDdqLF-APTVEED--VAF----------GPEN-LGLPREE--I 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:COG1122 112 RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIV 190
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG1122 191 THDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-273 |
5.95e-46 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 154.58 E-value: 5.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLHPdd 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV------------LIDGEDISG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 fLHPAQLgrriyykmfggTHLVNRAGLArtFQNIRLFREMSVIENllVA----QHTQVNRHLLAgilntrgyrqaesqal 161
Cdd:cd03261 67 -LSEAEL-----------YRLRRRMGML--FQSGALFDSLTVFEN--VAfplrEHTRLSEEEIR---------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:cd03261 115 EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVT 194
|
250 260 270
....*....|....*....|....*....|..
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:cd03261 195 HDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-283 |
1.59e-45 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 153.65 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklhp 83
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED-ITHL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflhP----AQLGrrIYYkmfggthlvnragLArtfQNIRLFREMSVIENLL-VAQHTQVNRHllagilntrgYRQAES 158
Cdd:COG1137 71 -----PmhkrARLG--IGY-------------LP---QEASIFRKLTVEDNILaVLELRKLSKK----------EREERL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALdrafywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVL 238
Cdd:COG1137 118 EEL------LEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVL 190
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490250751 239 LIEHDmgmVME---ISDHIIVLDHGDVIARGAPQAIQANASVIAAYLG 283
Cdd:COG1137 191 ITDHN---VREtlgICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-285 |
3.02e-45 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 152.81 E-value: 3.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklhPd 84
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQD-ITHL---------P- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dflhpaqlgrriyykmfggTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRhllagilnTRGYRQAESQALdra 164
Cdd:TIGR04406 70 -------------------MHERARLGIGYLPQEASIFRKLTVEENIMAVLEIRKDL--------DRAEREERLEAL--- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 fywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDM 244
Cdd:TIGR04406 120 ---LEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNV 195
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490250751 245 GMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLGAE 285
Cdd:TIGR04406 196 RETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQ 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-257 |
5.72e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 158.64 E-value: 5.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKL 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD------------GEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HPDDFLHpAQlgrriyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAQhtQVNRhllAGILNTRG-YRQAEsQA 160
Cdd:COG1129 69 RFRSPRD-AQ-----------------AAGIAIIHQELNLVPNLSVAENIFLGR--EPRR---GGLIDWRAmRRRAR-EL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRafywLEVveMVDcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:COG1129 125 LAR----LGL--DID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYI 196
|
250
....*....|....*..
gi 490250751 241 EHDMGMVMEISDHIIVL 257
Cdd:COG1129 197 SHRLDEVFEIADRVTVL 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-283 |
9.33e-45 |
|
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: 151.54 E-value: 9.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTdviqvlgqKLHPDd 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD-IT--------KLPMH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flHPAQLGrrIYYkmfggthlvnragLArtfQNIRLFREMSVIENLLVaqhtqvnrhllagILNTRGYRQAEsqALDRAF 165
Cdd:cd03218 71 --KRARLG--IGY-------------LP---QEASIFRKLTVEENILA-------------VLEIRGLSKKE--REEKLE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMG 245
Cdd:cd03218 116 ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVR 194
|
250 260 270
....*....|....*....|....*....|....*...
gi 490250751 246 MVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLG 283
Cdd:cd03218 195 ETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-271 |
8.75e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.17 E-value: 8.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqk 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-VTGL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhPAQlgRRiyykmfgGTHLVnraglartFQNIRLFREMSVIENllVAQHtqvnrhllagiLNTRGYRQAESQA 160
Cdd:COG3842 73 --------PPE--KR-------NVGMV--------FQDYALFPHLTVAEN--VAFG-----------LRMRGVPKAEIRA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 ldRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:COG3842 115 --RVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYV 192
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG3842 193 THDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-268 |
8.94e-44 |
|
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: 148.67 E-value: 8.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 8 VEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDviqvlgqklhpddfl 87
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 88 hPAQLGRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENLLVaqhtqvnrhlLAGILNTRGYRQAEsqaldRAFYW 167
Cdd:cd03265 68 -PREVRRRIGI----------------VFQDLSVDDELTGWENLYI----------HARLYGVPGAERRE-----RIDEL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 168 LEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMV 247
Cdd:cd03265 116 LDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEA 195
|
250 260
....*....|....*....|.
gi 490250751 248 MEISDHIIVLDHGDVIARGAP 268
Cdd:cd03265 196 EQLCDRVAIIDHGRIIAEGTP 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-268 |
1.69e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.80 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQK 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID------------GKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDflhPAQlgrriyykmfggthlVNRAGLARTFQNIRLFREMSVIENLLVAqhtqvNRHLLAGILNTRGYRQAESQA 160
Cdd:COG3845 69 VRIRS---PRD---------------AIALGIGMVHQHFMLVPNLTVAENIVLG-----LEPTKGGRLDRKAARARIREL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRafYWLEvvemVDcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:COG3845 126 SER--YGLD----VD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFI 197
|
250 260
....*....|....*....|....*...
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAP 268
Cdd:COG3845 198 THKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-266 |
2.08e-43 |
|
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: 147.29 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 7 RVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQklhpddf 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI------------RVFGK------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 87 lHPAQLGRRIYYkmfggthLVNRAGLARTFqnirlfrEMSVIENLLVAqhtqvnrhLLAGILNTRGYRQAESQALDRAfy 166
Cdd:cd03235 62 -PLEKERKRIGY-------VPQRRSIDRDF-------PISVRDVVLMG--------LYGHKGLFRRLSKADKAKVDEA-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 167 wLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRqQHGITVLLIEHDMGM 246
Cdd:cd03235 117 -LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGL 194
|
250 260
....*....|....*....|
gi 490250751 247 VMEISDHIIVLDHGdVIARG 266
Cdd:cd03235 195 VLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-271 |
5.21e-43 |
|
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: 147.44 E-value: 5.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFG-GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvTDVIQVLGQKLHp 83
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEG----TDITKLRGKKLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflhpaQLGRRIyykmfggthlvnraglARTFQNIRLFREMSVIENLLvaqHTQVNRH-LLAGILNTrgYRQAESQald 162
Cdd:TIGR02315 76 -------KLRRRI----------------GMIFQHYNLIERLTVLENVL---HGRLGYKpTWRSLLGR--FSEEDKE--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEH 242
Cdd:TIGR02315 125 RALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLH 204
|
250 260
....*....|....*....|....*....
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:TIGR02315 205 QVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-288 |
6.24e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.13 E-value: 6.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHF-GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLh 82
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEI------------LVDGQDV- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 pdDFLHPAQLgRRIyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAQhtqVNRH-LLAGILntRGYRQAEsqaL 161
Cdd:COG3638 68 --TALRGRAL-RRL------------RRRIGMIFQQFNLVPRLSVLTNVLAGR---LGRTsTWRSLL--GLFPPED---R 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:COG3638 125 ERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNL 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIqaNASVIAAYLGAEEEE 288
Cdd:COG3638 205 HQVDLARRYADRIIGLRDGRVVFDGPPAEL--TDAVLREIYGGEAEE 249
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-260 |
1.45e-42 |
|
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: 143.69 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSivlrarekvtdvIQVLGQKLHPDd 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE------------IKVLGKDIKKE- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhPAQLGRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENLlvaqhtqvnrhllagilntrgyrqaesqaldraf 165
Cdd:cd03230 68 ---PEEVKRRIGY----------------LPEEPSLYENLTVRENL---------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlevvemvdcanrlagTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMG 245
Cdd:cd03230 95 -----------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILE 156
|
250
....*....|....*
gi 490250751 246 MVMEISDHIIVLDHG 260
Cdd:cd03230 157 EAERLCDRVAILNNG 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-273 |
2.07e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLHPD 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV------------LWDGEPLDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dflHPAQLG-----RRIYYKMfggthlvnraglartfqnirlfremSVIENLLvaqhtqvnrhLLAGIlntRGYRQAEsq 159
Cdd:COG4152 69 ---DRRRIGylpeeRGLYPKM-------------------------KVGEQLV----------YLARL---KGLSKAE-- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLL 239
Cdd:COG4152 106 AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIF 184
|
250 260 270
....*....|....*....|....*....|....
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:COG4152 185 SSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-271 |
6.27e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 144.37 E-value: 6.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQKLHPD 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT------------VDGEDLTDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DfLHPAQLGRRIyykmfgGthLVnraglartFQNIRLFREMSVIENLLVAQhtqvnRHLLagilntrgyRQAESQALDRA 164
Cdd:COG1126 69 K-KDINKLRRKV------G--MV--------FQQFNLFPHLTVLENVTLAP-----IKVK---------KMSKAEAEERA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 FYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDM 244
Cdd:COG1126 118 MELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEM 196
|
250 260
....*....|....*....|....*..
gi 490250751 245 GMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG1126 197 GFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-269 |
1.08e-40 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 140.72 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGI--KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqvlgqklhp 83
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflHPAQLGRRIYYKMfggthlvnraglartfQNIRLFREMSVIENLlvaqhtqvnrHLLAGIlntRGYRQAESQALDR 163
Cdd:cd03263 69 ----DRKAARQSLGYCP----------------QFDALFDELTVREHL----------RFYARL---KGLPKSEIKEEVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHD 243
Cdd:cd03263 116 LL--LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHS 191
|
250 260
....*....|....*....|....*.
gi 490250751 244 MGMVMEISDHIIVLDHGDVIARGAPQ 269
Cdd:cd03263 192 MDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-260 |
1.50e-40 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 138.86 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKLHPDD 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI------------DGEDLTDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQlgrriyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAqhtqvnrhllagilntrgyrqaesqaldraf 165
Cdd:cd03229 69 DELPPL-----------------RRRIGMVFQDFALFPHLTVLENIALG------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:cd03229 101 ------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLD 162
|
250
....*....|....*
gi 490250751 246 MVMEISDHIIVLDHG 260
Cdd:cd03229 163 EAARLADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-274 |
1.51e-40 |
|
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: 146.97 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHF-----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviq 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD---------- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 76 vlGQKLHPDDFLHPAQLGRRIYYkmfggthlVnraglartFQNIR--LFREMSVIEnllvaqhtqvnrHLLAGILNTRGY 153
Cdd:COG1123 326 --GKDLTKLSRRSLRELRRRVQM--------V--------FQDPYssLNPRMTVGD------------IIAEPLRLHGLL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 RQAEsqALDRAFYWLEVVEMV-DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQAlsRIIRF---L 229
Cdd:COG1123 376 SRAE--RRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQA--QILNLlrdL 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490250751 230 RQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG1123 451 QRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-271 |
3.11e-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: 139.62 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFyratggsIVLRAREKVTDVIQVLGQKLhPDD 85
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRL-------NDLIPGAPDEGEVLLDGKDI-YDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIyykmfggthlvnraGLArtFQNIRLFReMSVIENLLVAQHtqvnrhlLAGILNTRGYRQAESQALDRAF 165
Cdd:cd03260 73 DVDVLELRRRV--------------GMV--FQKPNPFP-GSIYDNVAYGLR-------LHGIKLKEELDERVEEALRKAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVvemvdcANRL-AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhgITVLLIEHDM 244
Cdd:cd03260 129 LWDEV------KDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNM 200
|
250 260
....*....|....*....|....*..
gi 490250751 245 GMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:cd03260 201 QQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-266 |
1.20e-39 |
|
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: 137.35 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtdVIQVLGQklhpdD 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG------------EITFDGK-----S 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIyykmfgGThLVNRAGlartfqnirLFREMSVIENLLVAQhtqvnrhLLAGILNtrgyrqaesQALDRAf 165
Cdd:cd03268 64 YQKNIEALRRI------GA-LIEAPG---------FYPNLTARENLRLLA-------RLLGIRK---------KRIDEV- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMG 245
Cdd:cd03268 111 --LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLS 187
|
250 260
....*....|....*....|.
gi 490250751 246 MVMEISDHIIVLDHGDVIARG 266
Cdd:cd03268 188 EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-266 |
1.61e-39 |
|
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: 137.27 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklhpdd 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD-VTGV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhPAQLgRRIyykmfggthlvnraglARTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQAESQAldRAF 165
Cdd:cd03259 68 ---PPER-RNI----------------GMVFQDYALFPHLTVAENIAFG-------------LKLRGVPKAEIRA--RVR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:cd03259 113 ELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQE 192
|
250 260
....*....|....*....|.
gi 490250751 246 MVMEISDHIIVLDHGDVIARG 266
Cdd:cd03259 193 EALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-260 |
1.46e-38 |
|
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: 134.90 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLHPDDflhPAQLGRR 95
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV------------LVDGKDLTKLS---LKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 IYYkmfggthlvnraglarTFQNIR--LFREmSVIENLLVAqhtqvnrhllagiLNTRGYRQAESQAldRAFYWLEVVEM 173
Cdd:cd03225 77 VGL----------------VFQNPDdqFFGP-TVEEEVAFG-------------LENLGLPEEEIEE--RVEEALELVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDH 253
Cdd:cd03225 125 EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADR 203
|
....*..
gi 490250751 254 IIVLDHG 260
Cdd:cd03225 204 VIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-271 |
3.11e-38 |
|
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: 135.17 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKLHPd 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL------------DGRDLAS- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dfLHPAQLGRRIYYkmfggthlvnraglartfqnirlfremsvienllVAQHTQVNRHL------LAGILNTRGYRQAES 158
Cdd:COG1120 68 --LSRRELARRIAY----------------------------------VPQEPPAPFGLtvrelvALGRYPHLGLFGRPS 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAFYW-LEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITV 237
Cdd:COG1120 112 AEDREAVEEaLERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTV 191
|
250 260 270
....*....|....*....|....*....|....
gi 490250751 238 LLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG1120 192 VMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-260 |
5.15e-38 |
|
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: 133.42 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGQKlhpdd 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-------DGLKLTDDK----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmfggTHLVN-RAGLARTFQNIRLFREMSVIENLLVAQhTQVnrhllagilntRGYRQAEsqALDRA 164
Cdd:cd03262 69 ------------------KNINElRQKVGMVFQQFNLFPHLTVLENITLAP-IKV-----------KGMSKAE--AEERA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 FYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDM 244
Cdd:cd03262 117 LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEM 195
|
250
....*....|....*.
gi 490250751 245 GMVMEISDHIIVLDHG 260
Cdd:cd03262 196 GFAREVADRVIFMDDG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-271 |
1.41e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.04 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdviqVLGQKLHPDD 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR--------DLFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgRRIyykmfgGthLVnraglartFQNIRLFREMSVIENllVAqhtqvnrhllAGiLNTRGYRQAESQAldRAF 165
Cdd:COG1118 75 --------RRV------G--FV--------FQHYALFPHMTVAEN--IA----------FG-LRVRPPSKAEIRA--RVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRQQH---GITVLLIEH 242
Cdd:COG1118 116 ELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGAL---DAKVRKELRRWLRRLHdelGGTTVFVTH 192
|
250 260
....*....|....*....|....*....
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG1118 193 DQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-266 |
1.49e-37 |
|
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: 132.63 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviqvlgqK 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-----------------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDFLHPAQLGRRIYYKMFGgthLVnraglartFQNIR--LFREMSVienllvaqhtqvnRHLLAGILNTRGYRQAES 158
Cdd:cd03257 64 FDGKDLLKLSRRLRKIRRKEIQ---MV--------FQDPMssLNPRMTI-------------GEQIAEPLRIHGKLSKKE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAFYWLEVVEMV-DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQA-LSRIIRFLRQQHGIT 236
Cdd:cd03257 120 ARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD-VSVQAqILDLLKKLQEELGLT 198
|
250 260 270
....*....|....*....|....*....|
gi 490250751 237 VLLIEHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:cd03257 199 LLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-282 |
6.81e-37 |
|
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: 131.11 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqVLGQKLHpdd 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGED-------ITKLPPH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgRRIyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRqaESQALDRAF 165
Cdd:TIGR03410 71 --------ERA------------RAGIAYVPQGREIFPRLTVEENLLTG-------------LAALPRR--SRKIPDEIY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEmvDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:TIGR03410 116 ELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLD 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 490250751 246 MVMEISDHIIVLDHGDVIARGapQAIQANASVIAAYL 282
Cdd:TIGR03410 194 FARELADRYYVMERGRVVASG--AGDELDEDKVRRYL 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-284 |
3.85e-36 |
|
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: 129.38 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklHPDD 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED-ATDV--------PVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENllVAQHTQVNRhllagilntRGYRQAESQALDRAF 165
Cdd:cd03296 74 --------RNVGF----------------VFQHYALFRHMTVFDN--VAFGLRVKP---------RSERPPEAEIRAKVH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRQQH---GITVLLIEH 242
Cdd:cd03296 119 ELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL---DAKVRKELRRWLRRLHdelHVTTVFVTH 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAI--QANASVIAAYLGA 284
Cdd:cd03296 196 DQEEALEVADRVVVMNKGRIEQVGTPDEVydHPASPFVYSFLGE 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-264 |
6.42e-36 |
|
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: 126.39 E-value: 6.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHpdd 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------GKEVS--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmFGGTHLVNRAGLARTFQnirlfremsvienllvaqhtqvnrhllagilntrgyrqaesqaldraf 165
Cdd:cd03216 66 ---------------FASPRDARRAGIAMVYQ------------------------------------------------ 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMG 245
Cdd:cd03216 83 ------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLD 143
|
250
....*....|....*....
gi 490250751 246 MVMEISDHIIVLDHGDVIA 264
Cdd:cd03216 144 EVFEIADRVTVLRDGRVVG 162
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-260 |
7.52e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.05 E-value: 7.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqv 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 77 lgqklhpddflhPAQLGRRIyykmfggthlvnraGLArtFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQA 156
Cdd:COG1116 75 ------------VTGPGPDR--------------GVV--FQEPALLPWLTVLDNVALG-------------LELRGVPKA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 157 EsqALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGIT 236
Cdd:COG1116 114 E--RRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKT 191
|
250 260
....*....|....*....|....*..
gi 490250751 237 VLLIEHDmgmVME---ISDHIIVLDHG 260
Cdd:COG1116 192 VLFVTHD---VDEavfLADRVVVLSAR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-266 |
9.62e-36 |
|
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: 127.40 E-value: 9.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtdVIQVLGQKLHPDD 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG------------EVLFDGKPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlGRRIYYkmfggthLVNRAGlartfqnirLFREMSVIENLL-VAQHTQVNRHllagilntrgyrqaesQALDRA 164
Cdd:cd03269 69 -------RNRIGY-------LPEERG---------LYPKMKVIDQLVyLAQLKGLKKE----------------EARRRI 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 FYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDM 244
Cdd:cd03269 110 DEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQM 188
|
250 260
....*....|....*....|..
gi 490250751 245 GMVMEISDHIIVLDHGDVIARG 266
Cdd:cd03269 189 ELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-260 |
1.40e-35 |
|
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: 127.22 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGG----IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQKL 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR------------VDGTDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HPddfLHPAQLgrriyykmfggTHLVNRAgLARTFQNIRLFREMSVIENLLVAQHtqvnrhlLAGILNTrgyrqaesQAL 161
Cdd:cd03255 69 SK---LSEKEL-----------AAFRRRH-IGFVFQSFNLLPDLTALENVELPLL-------LAGVPKK--------ERR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:cd03255 119 ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVT 198
|
250
....*....|....*....
gi 490250751 242 HDMGMVmEISDHIIVLDHG 260
Cdd:cd03255 199 HDPELA-EYADRIIELRDG 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-271 |
2.36e-35 |
|
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: 127.51 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtDVIQVLGQKLH 82
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG-----------NDVRLFGERRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 PDDflhPAQLGRRIyykmfgGthLVNrAGLARTFQnirlfREMSVIEnllvaqhtqVnrhLLAGILNTRG-YRQAESQAL 161
Cdd:COG1119 70 GED---VWELRKRI------G--LVS-PALQLRFP-----RDETVLD---------V---VLSGFFDSIGlYREPTDEQR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:COG1119 121 ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVT 200
|
250 260 270
....*....|....*....|....*....|
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG1119 201 HHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-271 |
8.80e-35 |
|
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: 126.80 E-value: 8.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLHPDDFLHPAQLGRRIyy 98
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTV------------TIDGRDITAKKKKKLKDLRKKV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 kmfggthlvnraGLArtFQN--IRLFrEMSVIE-------NLlvaqhtqvnrhllagilntrGYRQAEsqALDRAFYWLE 169
Cdd:TIGR04521 85 ------------GLV--FQFpeHQLF-EETVYKdiafgpkNL--------------------GLSEEE--AEERVKEALE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 170 VVEM-VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVM 248
Cdd:TIGR04521 128 LVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVA 207
|
250 260
....*....|....*....|...
gi 490250751 249 EISDHIIVLDHGDVIARGAPQAI 271
Cdd:TIGR04521 208 EYADRVIVMHKGKIVLDGTPREV 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-264 |
1.14e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.16 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFG----GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLG 78
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL------------IDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKLH--PDDFLhpAQLgRRiyyKMFGgthLVnraglartFQNIRLFREMSVIENLLVAQhtqvnrhLLAGIlntrgyrqA 156
Cdd:COG1136 70 QDISslSEREL--ARL-RR---RHIG---FV--------FQFFNLLPELTALENVALPL-------LLAGV--------S 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 157 ESQALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGIT 236
Cdd:COG1136 118 RKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTT 197
|
250 260
....*....|....*....|....*...
gi 490250751 237 VLLIEHDMGmVMEISDHIIVLDHGDVIA 264
Cdd:COG1136 198 IVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-212 |
2.27e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.99 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPDDFLHPaqlgrriyykm 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD------------GQDLTDDERKSL----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnRAGLARTFQNIRLFREMSVIENLLvaqhtqvnrhlLAGILNTRGYRQAESQALDrafyWLEVVEMVDCANRL 180
Cdd:pfam00005 58 --------RKEIGYVFQDPQLFPRLTVRENLR-----------LGLLLKGLSKREKDARAEE----ALEKLGLGDLADRP 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 490250751 181 AG----TLSYGQQRRLEIARAMCTRPEMICLDEPAA 212
Cdd:pfam00005 115 VGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-266 |
5.49e-34 |
|
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: 121.77 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 7 RVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKLHPddf 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------DGKDLAS--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 87 LHPAQLGRRIYYkmfggthlvnraglartfqnirlfremsvienllVAQhtqvnrhllagilntrgyrqaesqaldrafy 166
Cdd:cd03214 66 LSPKELARKIAY----------------------------------VPQ------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 167 WLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGM 246
Cdd:cd03214 81 ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNL 160
|
250 260
....*....|....*....|
gi 490250751 247 VMEISDHIIVLDHGDVIARG 266
Cdd:cd03214 161 AARYADRVILLKDGRIVAQG 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-285 |
5.71e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 123.85 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvTDVIQVLGqklhp 83
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-----DEDISLLP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflhpaqlgrriyykmfggTHLVNRAGLARTFQNIRLFREMSVIENLLvaqhtqvnrhllaGILNTRGYRQAESQAlDR 163
Cdd:PRK10895 72 --------------------LHARARRGIGYLPQEASIFRRLSVYDNLM-------------AVLQIRDDLSAEQRE-DR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRqQHGITVLLIEHD 243
Cdd:PRK10895 118 ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHN 196
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490250751 244 MGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLGAE 285
Cdd:PRK10895 197 VRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGED 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-280 |
1.60e-33 |
|
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: 128.10 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF--GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGgsivlrareKVTDVIQVLGQK 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG---------RISGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LhpdDFLHPAQLGRRIYYkmfggthlvnraglarTFQNIrlfreMSVIENLLVAQHtqvnrhlLAGILNTRGYRQAEsqA 160
Cdd:COG1123 73 L---LELSEALRGRRIGM----------------VFQDP-----MTQLNPVTVGDQ-------IAEALENLGLSRAE--A 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:COG1123 120 RARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLI 199
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAA 280
Cdd:COG1123 200 THDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-257 |
4.03e-33 |
|
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: 120.65 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGG----IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqvlgqkl 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 hpddflhpaqlgrriyykmfggthlVNRAGLART--FQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGyrQAESQ 159
Cdd:cd03293 68 -------------------------VTGPGPDRGyvFQQDALLPWLTVLDNVALG-------------LELQG--VPKAE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLL 239
Cdd:cd03293 108 ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLL 187
|
250
....*....|....*...
gi 490250751 240 IEHDMGMVMEISDHIIVL 257
Cdd:cd03293 188 VTHDIDEAVFLADRVVVL 205
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-271 |
5.89e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 123.99 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTdviqvlgqklhpdd 85
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRD-IT-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIyykmfggthlvnraglarTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQAEsqALDRAF 165
Cdd:TIGR03265 70 RLPPQKRDYGI------------------VFQSYALFPNLTVADNIAYG-------------LKNRGMGRAE--VAERVA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:TIGR03265 117 ELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQE 196
|
250 260
....*....|....*....|....*.
gi 490250751 246 MVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:TIGR03265 197 EALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-276 |
7.32e-33 |
|
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: 121.06 E-value: 7.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFG----GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDV-------- 73
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP-VTRRrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 74 IQVLGQklHPDDFLHPAQLGRRIyykmfggthlvnragLARTFQNIRLFREMSVIENLLvaqhTQVNrhllagilntrgy 153
Cdd:COG1124 81 VQMVFQ--DPYASLHPRHTVDRI---------------LAEPLRIHGLPDREERIAELL----EQVG------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 rqaesqaLDRAFywlevvemvdcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVeTQAlsRIIRFL---R 230
Cdd:COG1124 127 -------LPPSF-----------LDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVS-VQA--EILNLLkdlR 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490250751 231 QQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANAS 276
Cdd:COG1124 186 EERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-263 |
2.81e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.62 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF-GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSivlrarekvtdvIQVLGQ---K 80
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQ------------VLVNGQdlsR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDFlhpAQLGRRIyykmfggthlvnraGLarTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQAESQA 160
Cdd:COG2884 69 LKRREI---PYLRRRI--------------GV--VFQDFRLLPDRTVYENVALP-------------LRVTGKSRKEIRR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 ldRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvetqALS-RIIRFLRQ--QHGITV 237
Cdd:COG2884 117 --RVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP----ETSwEIMELLEEinRRGTTV 190
|
250 260
....*....|....*....|....*.
gi 490250751 238 LLIEHDMGMVMEISDHIIVLDHGDVI 263
Cdd:COG2884 191 LIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-283 |
4.63e-32 |
|
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: 118.49 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklhpdd 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-ITNL------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhPAqlgrriyykmfggthlvNRAGLARTFQNIRLFREMSVIENLlvaqhtqvnrhllAGILNTRGYRQAESQAldRAF 165
Cdd:cd03300 68 ---PP-----------------HKRPVNTVFQNYALFPHLTVFENI-------------AFGLRLKKLPKAEIKE--RVA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:cd03300 113 EALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQE 192
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490250751 246 MVMEISDHIIVLDHGDVIARGAPQAI--QANASVIAAYLG 283
Cdd:cd03300 193 EALTMSDRIAVMNKGKIQQIGTPEEIyeEPANRFVADFIG 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-260 |
1.33e-31 |
|
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: 115.03 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 7 RVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlgqkLHPDDF 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID---------------GKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 87 LHPAQLGRRIYYkmfggthlvnraglarTFQnirlfremsvienllvaqhtqvnrhllagilntrgyrqaesqaldrafy 166
Cdd:cd00267 66 LPLEELRRRIGY----------------VPQ------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 167 wlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGM 246
Cdd:cd00267 81 -----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPEL 142
|
250
....*....|....
gi 490250751 247 VMEISDHIIVLDHG 260
Cdd:cd00267 143 AELAADRVIVLKDG 156
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-266 |
1.70e-31 |
|
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: 116.91 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 14 HFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvTDVIQVLGQKLHpddflhpaQLG 93
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG----TDLTLLSGKELR--------KAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 RRIyykmfggthlvnraGLarTFQNIRLFREMSVIENLlvaqhtqvnrhllAGILNTRGYRQAESQAldRAFYWLEVVEM 173
Cdd:cd03258 82 RRI--------------GM--IFQHFNLLSSRTVFENV-------------ALPLEIAGVPKAEIEE--RVLELLELVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDH 253
Cdd:cd03258 131 EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDR 210
|
250
....*....|...
gi 490250751 254 IIVLDHGDVIARG 266
Cdd:cd03258 211 VAVMEKGEVVEEG 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-284 |
3.31e-31 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 116.52 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDviqvlgqk 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD-ITD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhpaqlgrriyykmfGGTHLVNRAGLARTFQNIRLFREMSVIENLLvaqhtqvnrhlLAGILNTRGYRQaesQA 160
Cdd:PRK11614 72 ---------------------WQTAKIMREAVAIVPEGRRVFSRMTVEENLA-----------MGGFFAERDQFQ---ER 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEvvEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:PRK11614 117 IKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLV 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLGA 284
Cdd:PRK11614 194 EQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-263 |
8.91e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.52 E-value: 8.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNC------LTGFYRATGgSIVLRARekvtDViq 75
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGARVEG-EILLDGE----DI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 76 vlgqkLHPDdfLHPAQLGRRIyykmfgGthLVnraglartFQNIRLFReMSVIENllVA----QHTQVNRHLLAGIlntr 151
Cdd:COG1117 81 -----YDPD--VDVVELRRRV------G--MV--------FQKPNPFP-KSIYDN--VAyglrLHGIKSKSELDEI---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 152 gyrqAEsQALDRAFYWLEVvemvdcANRL---AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRF 228
Cdd:COG1117 131 ----VE-ESLRKAALWDEV------KDRLkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE 199
|
250 260 270
....*....|....*....|....*....|....*
gi 490250751 229 LRQQHgiTVLLIEHDMGMVMEISDHIIVLDHGDVI 263
Cdd:COG1117 200 LKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-285 |
1.70e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.83 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqvLGQklhpdd 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP--------LAA------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 fLHPAQLGRRiyykmfggthlvnRAGLartfqnirlfremsvienllvAQHTQVNRHLLA------GILNTRGYRQAESQ 159
Cdd:COG4559 68 -WSPWELARR-------------RAVL---------------------PQHSSLAFPFTVeevvalGRAPHGSSAAQDRQ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMC-------TRPEMICLDEPAAGLNPVETQALSRIIRFLRQQ 232
Cdd:COG4559 113 IVREA---LALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490250751 233 hGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIqANASVIAAYLGAE 285
Cdd:COG4559 190 -GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV-LTDELLERVYGAD 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-286 |
2.24e-30 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.74 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdviqVLgQKLHPDDFLHPAQlgRRIYYkmfg 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--------VL-QDSARGIFLPPHR--RRIGY---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 103 gthlVnraglartFQNIRLFREMSVIENLLVAQHtqvnrhllagilntRGYRQAESQALDrafywlEVVEMVDCA---NR 179
Cdd:COG4148 82 ----V--------FQEARLFPHLSVRGNLLYGRK--------------RAPRAERRISFD------EVVELLGIGhllDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDH 259
Cdd:COG4148 130 RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ 209
|
250 260
....*....|....*....|....*..
gi 490250751 260 GDVIARGAPQAIQANASViAAYLGAEE 286
Cdd:COG4148 210 GRVVASGPLAEVLSRPDL-LPLAGGEE 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-238 |
2.47e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.96 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPDd 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN------------GEPIRDA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhPAQLGRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENLlvaqhtqvnrHLLAGILNTRGYRQAESQALDRaf 165
Cdd:COG4133 70 ---REDYRRRLAY----------------LGHADGLKPELTVRENL----------RFWAALYGLRADREAIDEALEA-- 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250751 166 ywlevVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVL 238
Cdd:COG4133 119 -----VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-287 |
2.63e-30 |
|
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: 113.93 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGI-KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtDVIQvlgqklhpd 84
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIRE--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dfLHPAQLGRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENL-LVAQhtqvnrhLLagilntrGYRQAESQAldR 163
Cdd:cd03295 68 --QDPVELRRKIGY----------------VIQQIGLFPHMTVEENIaLVPK-------LL-------KWPKEKIRE--R 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFYWLEVVEMVDC--ANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:cd03295 114 ADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVT 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAI---QANASViAAYLGAEEE 287
Cdd:cd03295 194 HDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPANDFV-AEFVGADRL 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-274 |
3.63e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 14 HFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGqklhpddflhPAQLG 93
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-------DGLKVND----------PKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 RRIYYKmfggthlvnrAGLarTFQNIRLFREMSVIENLLVaqhtqvnrhllaGILNTRGYRQAESQALDRAFywLEVVEM 173
Cdd:PRK09493 73 RLIRQE----------AGM--VFQQFYLFPHLTALENVMF------------GPLRVRGASKEEAEKQAREL--LAKVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDH 253
Cdd:PRK09493 127 AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASR 205
|
250 260
....*....|....*....|.
gi 490250751 254 IIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK09493 206 LIFIDKGRIAEDGDPQVLIKN 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-271 |
6.88e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.86 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDviqvlgqklhpdd 85
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-VTD------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 fLHPAQlgRRIyykmfggthlvnraglARTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQAE-SQALDRA 164
Cdd:COG3839 70 -LPPKD--RNI----------------AMVFQSYALYPHMTVYENIAFP-------------LKLRKVPKAEiDRRVREA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 fywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNP---VETQALsriIRFLRQQHGITVLLIE 241
Cdd:COG3839 118 ---AELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrVEMRAE---IKRLHRRLGTTTIYVT 191
|
250 260 270
....*....|....*....|....*....|
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG3839 192 HDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-285 |
1.91e-28 |
|
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: 108.96 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKaLNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArEKVTDviqvlgqkLHPDD 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG-KDITN--------LPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgRRIYYkmfggthlvnraglarTFQNIRLFREMSVIENLlvaqhtqvnrhllAGILNTRGYRQAEsqaLDRAF 165
Cdd:cd03299 71 --------RDISY----------------VPQNYALFPHMTVYKNI-------------AYGLKKRKVDKKE---IERKV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywLEVVEMVDCA---NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEH 242
Cdd:cd03299 111 --LEIAEMLGIDhllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTH 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAIQANAS--VIAAYLGAE 285
Cdd:cd03299 189 DFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKneFVAEFLGFN 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-282 |
3.59e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF-GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKL 81
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV------------KVMGREV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HPddflhpaqlgRRIYYkmfggthLVNRAGLarTFQNI--RLFrEMSVIENllVAqhtqvnrhllAGILNTrGYRQAEsq 159
Cdd:PRK13647 70 NA----------ENEKW-------VRSKVGL--VFQDPddQVF-SSTVWDD--VA----------FGPVNM-GLDKDE-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLL 239
Cdd:PRK13647 115 VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIV 193
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYL 282
Cdd:PRK13647 194 ATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-266 |
5.53e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.17 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQK 80
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL------------VDGVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPddfLHPAQLgRRIyykmfggthlvnRAGLARTFQNIRLFREMSVIEN----LLVAqhtqvnrhllagilntrGYRQA 156
Cdd:COG1135 69 LTA---LSEREL-RAA------------RRKIGMIFQHFNLLSSRTVAENvalpLEIA-----------------GVPKA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 157 ESQAldRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGIT 236
Cdd:COG1135 116 EIRK--RVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLT 193
|
250 260 270
....*....|....*....|....*....|
gi 490250751 237 VLLIEHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:COG1135 194 IVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-274 |
7.16e-28 |
|
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: 112.54 E-value: 7.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPddfLHPAQLGRR 95
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN------------GVDLSD---LDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 IYYkmfggthlVNraglartfQNIRLFrEMSVIENLLVAQhtqvnrhllagilntrgyRQAESQALDRAfywLEVVEMVD 175
Cdd:COG4988 413 IAW--------VP--------QNPYLF-AGTIRENLRLGR------------------PDASDEELEAA---LEAAGLDE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 CANRL-----------AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHDM 244
Cdd:COG4988 455 FVAALpdgldtplgegGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRL 532
|
250 260 270
....*....|....*....|....*....|
gi 490250751 245 GmVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG4988 533 A-LLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-274 |
7.41e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 7.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrAREKVTdviqvlgqklhpddflhpAQLGRRIYY 98
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI-AGYHIT------------------PETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 KmfggthLVNRAGLARTFQNIRLFrEMSVIENLLVaqhtqvnrhllaGILNtrgYRQAESQALDRAFYWLEVVEM-VDCA 177
Cdd:PRK13641 82 K------LRKKVSLVFQFPEAQLF-ENTVLKDVEF------------GPKN---FGFSEDEAKEKALKWLKKVGLsEDLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIirFLR-QQHGITVLLIEHDMGMVMEISDHIIV 256
Cdd:PRK13641 140 SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQL--FKDyQKAGHTVILVTHNMDDVAEYADDVLV 217
|
250
....*....|....*...
gi 490250751 257 LDHGDVIARGAPQAIQAN 274
Cdd:PRK13641 218 LEHGKLIKHASPKEIFSD 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-271 |
9.43e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.79 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 15 FGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlraREKVTDViqvlgQKLHPDDflhpaqlgR 94
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI----RFHGTDV-----SRLHARD--------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 95 RIYYkmfggthlvnraglarTFQNIRLFREMSVIENL-----LVAQHTQVNRHLLagilntrgyRQAESQAldrafywLE 169
Cdd:PRK10851 75 KVGF----------------VFQHYALFRHMTVFDNIafgltVLPRRERPNAAAI---------KAKVTQL-------LE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 170 VVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRQQH---GITVLLIEHDMGM 246
Cdd:PRK10851 123 MVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL---DAQVRKELRRWLRQLHeelKFTSVFVTHDQEE 199
|
250 260
....*....|....*....|....*
gi 490250751 247 VMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK10851 200 AMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-266 |
2.00e-27 |
|
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: 106.26 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGqklhpddflhpaqlgrRIY 97
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV------------RVAG----------------LVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 YKmfggthlvnraglartfQNIRLFREMSVIenllVAQHTQVNRHLLAgilntrgyrqAESQALDRAFYWL--------- 168
Cdd:cd03267 86 WK-----------------RRKKFLRRIGVV----FGQKTQLWWDLPV----------IDSFYLLAAIYDLpparfkkrl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 169 -EVVEMVDCANRL---AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDM 244
Cdd:cd03267 135 dELSELLDLEELLdtpVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
250 260
....*....|....*....|..
gi 490250751 245 GMVMEISDHIIVLDHGDVIARG 266
Cdd:cd03267 215 KDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-266 |
2.08e-27 |
|
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: 105.91 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDviqvlgqk 80
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhPAQLGRRIyykmfgGTHlvnraglartFQNIRLFREMSVIENLLvaqhtqvnrhLLAGILNTRGyrQAESQA 160
Cdd:cd03266 73 --------PAEARRRL------GFV----------SDSTGLYDRLTARENLE----------YFAGLYGLKG--DELTAR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFywlEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:cd03266 117 LEELA---DRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFS 192
|
250 260
....*....|....*....|....*.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:cd03266 193 THIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-273 |
2.36e-27 |
|
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: 111.46 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGG--IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDviqvlGQKLhp 83
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-------D-----GIDL-- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflhpAQLGRRIYYKMFGgthLVnraglartFQNIRLFrEMSVIENLLVAQHT----QVNRHL-LAGILntrgyrqAES 158
Cdd:COG2274 540 ------RQIDPASLRRQIG---VV--------LQDVFLF-SGTIRENITLGDPDatdeEIIEAArLAGLH-------DFI 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAfYWLEVVEMvdcanrlAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvETQAlsRIIRFLRQ-QHGITV 237
Cdd:COG2274 595 EALPMG-YDTVVGEG-------GSNLSGGQRQRLAIARALLRNPRILILDEATSALDA-ETEA--IILENLRRlLKGRTV 663
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250751 238 LLIEHDMGMVmEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:COG2274 664 IIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-274 |
2.45e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTT---VFNCLTGFYratggsivlrAREKVTDVIQVLGQK 80
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTllrVFNRLIELY----------PEARVSGEVYLDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDFLhpaQLGRRIyyKMfggthlvnraglarTFQNIRLFREMSVIENllVAQHTQVNRhllagILNTRGYRQAE-SQ 159
Cdd:PRK14247 72 IFKMDVI---ELRRRV--QM--------------VFQIPNPIPNLSIFEN--VALGLKLNR-----LVKSKKELQERvRW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVVEMVDCAnrlAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIirFLRQQHGITVLL 239
Cdd:PRK14247 126 ALEKAQLWDEVKDRLDAP---AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESL--FLELKKDMTIVL 200
|
250 260 270
....*....|....*....|....*....|....*
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK14247 201 VTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-270 |
3.82e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.25 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFyrATGGSIVLRAREKVTDVIQVLGQklhp 83
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQREGR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflhpaqLGRRIYYkmfggthlvNRAGLARTFQNIRLFREMSVIENLLVAQ--HTQVNRHLLAGIlnTRGYRQAESQAL 161
Cdd:PRK09984 77 --------LARDIRK---------SRANTGYIFQQFNLVNRLSVLENVLIGAlgSTPFWRTCFSWF--TREQKQRALQAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRafywlevVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIE 241
Cdd:PRK09984 138 TR-------VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTL 210
|
250 260
....*....|....*....|....*....
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQA 270
Cdd:PRK09984 211 HQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-264 |
6.15e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 109.63 E-value: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYR--ATGGSIVLRarekvtdviqvlG 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFE------------G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKLHpddflhpaqlgrriyykmFGGTHLVNRAGLARTFQNIRLFREMSVIENLLVAqhtqvNRHLLAGILN-TRGYRQAE 157
Cdd:PRK13549 69 EELQ------------------ASNIRDTERAGIAIIHQELALVKELSVLENIFLG-----NEITPGGIMDyDAMYLRAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 158 SqaldrafyWLEVVEM-VDCANRLaGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRqQHGIT 236
Cdd:PRK13549 126 K--------LLAQLKLdINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIA 195
|
250 260
....*....|....*....|....*...
gi 490250751 237 VLLIEHDMGMVMEISDHIIVLDHGDVIA 264
Cdd:PRK13549 196 CIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-266 |
7.19e-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: 104.20 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGsITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQklhpDD 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIR------------IDGQ----DV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIYYkmfggthlvnragLArtfQNIRLFREMSVIENLlvaqhtqvnRHL--LAGILNTRgyrqaESQALDR 163
Cdd:cd03264 64 LKQPQKLRRRIGY-------------LP---QEFGVYPNFTVREFL---------DYIawLKGIPSKE-----VKARVDE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHD 243
Cdd:cd03264 114 V---LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHI 188
|
250 260
....*....|....*....|...
gi 490250751 244 MGMVMEISDHIIVLDHGDVIARG 266
Cdd:cd03264 189 VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-284 |
1.03e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.45 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 9 EHLMMHFggikalndvNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPddfLH 88
Cdd:COG3840 12 GDFPLRF---------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN------------GQDLTA---LP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 89 PAQlgRRIyykmfggTHLvnraglartFQNIRLFREMSVIENLLVAQHTqvNRHLlagilnTRGYRQAESQALDRafywl 168
Cdd:COG3840 68 PAE--RPV-------SML---------FQENNLFPHLTVAQNIGLGLRP--GLKL------TAEQRAQVEQALER----- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 169 evVEMVDCANRLAGTLSYGQQRRLEIARAMCT-RPEMIcLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMV 247
Cdd:COG3840 117 --VGLAGLLDRLPGQLSGGQRQRVALARCLVRkRPILL-LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDA 193
|
250 260 270
....*....|....*....|....*....|....*....
gi 490250751 248 MEISDHIIVLDHGDVIARGAPQAIQA--NASVIAAYLGA 284
Cdd:COG3840 194 ARIADRVLLVADGRIAADGPTAALLDgePPPALAAYLGI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-274 |
1.98e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.06 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlRAREKVTDVIQVLGQKlhp 83
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITIDTARSLSQQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddflhpAQLGRRIyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLvaqhtqvnrhllAGILNTRGYRQAESQALDR 163
Cdd:PRK11264 77 ------KGLIRQL------------RQHVGFVFQNFNLFPHRTVLENII------------EGPVIVKGEPKEEATARAR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGiTVLLIEHD 243
Cdd:PRK11264 127 EL--LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHE 203
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 244 MGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK11264 204 MSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-278 |
2.03e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFG-GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlgq 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 80 klhpddflhpaqlGRRIYYKMFGGTHLVNRAGLARTFQNIRLFrEMSVIENLLVaqhtqvnrhllaGILNTRGYRQAESQ 159
Cdd:PRK13636 67 -------------GKPIDYSRKGLMKLRESVGMVFQDPDNQLF-SASVYQDVSF------------GAVNLKLPEDEVRK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLL 239
Cdd:PRK13636 121 RVDNA---LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIII 197
|
250 260 270
....*....|....*....|....*....|....*....
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVI 278
Cdd:PRK13636 198 ATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-264 |
2.29e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.69 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVtdviqvlgqklhpdd 85
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmFGGTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTQ----VNRHLLagilNTRGYRQAESQAL 161
Cdd:PRK11288 70 ---------------FASTTAALAAGVAIIYQELHLVPEMTVAENLYLGQLPHkggiVNRRLL----NYEAREQLEHLGV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DrafywlevvemVDCANRLaGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIE 241
Cdd:PRK11288 131 D-----------IDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVS 197
|
250 260
....*....|....*....|...
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIA 264
Cdd:PRK11288 198 HRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-266 |
2.40e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.95 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKvtdviqvlgQK 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY---------NK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDflhPAQLGRRIYYkmfggthlvnraglartfQNIRLFREMSVIENLLVAQHTqVNRHLLAGILNTRGYRQAESQA 160
Cdd:PRK09700 72 LDHKL---AAQLGIGIIY------------------QELSVIDELTVLENLYIGRHL-TKKVCGVNIIDWREMRVRAAMM 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVdcanrlaGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:PRK09700 130 LLRVGLKVDLDEKV-------ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYI 201
|
250 260
....*....|....*....|....*.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:PRK09700 202 SHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-260 |
2.95e-26 |
|
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: 101.31 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKLhpddflhpAQLGRRIYY 98
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------DGVDL--------RDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 KMFGgthLVnraglartFQNIRLFrEMSVIENLLvaqhtqvnrhllagilntrgyrqaesqaldrafywlevvemvdcan 178
Cdd:cd03228 76 KNIA---YV--------PQDPFLF-SGTIRENIL---------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 179 rlagtlSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQqhGITVLLIEHDMGMVmEISDHIIVLD 258
Cdd:cd03228 98 ------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLD 168
|
..
gi 490250751 259 HG 260
Cdd:cd03228 169 DG 170
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-283 |
5.46e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.80 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArEKVTD-VIQvlgq 79
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG-EDVTHrSIQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 80 klhpddflhpaqlgrriyykmfggthlvNRaGLARTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQAE-S 158
Cdd:PRK11432 77 ----------------------------QR-DICMVFQSYALFPHMSLGENVGYG-------------LKMLGVPKEErK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVL 238
Cdd:PRK11432 115 QRVKEA---LELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490250751 239 LIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI--QANASVIAAYLG 283
Cdd:PRK11432 192 YVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELyrQPASRFMASFMG 238
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-274 |
6.36e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.31 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLhpddflhPAQLGRRIYYKmfg 102
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD------------GENI-------PAMSRSRLYTV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 103 gthlvnRAGLARTFQNIRLFREMSVIENLL--VAQHTQVNRHLLAGILNTRgyrqaesqaldrafywLEVVEMVDCANRL 180
Cdd:PRK11831 83 ------RKRMSMLFQSGALFTDMNVFDNVAypLREHTQLPAPLLHSTVMMK----------------LEAVGLRGAAKLM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHG 260
Cdd:PRK11831 141 PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK 220
|
250
....*....|....
gi 490250751 261 DVIARGAPQAIQAN 274
Cdd:PRK11831 221 KIVAHGSAQALQAN 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-263 |
6.52e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.01 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI-VL------RAREKVTDVIQVLGQK--LHPDdflH 88
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrVLgyvpfkRRKEFARRIGVVFGQRsqLWWD---L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 89 PAQ----LGRRIY------YKmfggthlvnraglartfQNIRLFREMSVIENLLvaqHTQVnrhllagilntrgyRQaes 158
Cdd:COG4586 112 PAIdsfrLLKAIYripdaeYK-----------------KRLDELVELLDLGELL---DTPV--------------RQ--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 qaldrafywlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQAlsRIIRFLR---QQHGI 235
Cdd:COG4586 155 -------------------------LSLGQRMRCELAAALLHRPKILFLDEPTIGLD-VVSKE--AIREFLKeynRERGT 206
|
250 260
....*....|....*....|....*...
gi 490250751 236 TVLLIEHDMGMVMEISDHIIVLDHGDVI 263
Cdd:COG4586 207 TILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-271 |
1.13e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.64 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtDVIQVLGQK 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ----DITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHpddflhpaqlgrriyykmfggthlVNRaglarTFQNIRLFREMSVIENllVAqhtqvnrhllagiLNTRGYRQAESQA 160
Cdd:PRK09452 86 RH------------------------VNT-----VFQSYALFPHMTVFEN--VA-------------FGLRMQKTPAAEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:PRK09452 122 TPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFV 201
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK09452 202 THDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-263 |
1.42e-25 |
|
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: 100.41 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 7 RVEHLMMHFG-GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlgqklhpDD 85
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN------------------GK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIYYKMfggthlvnraglartfQNIR--LFREmSVIENLLVaqhtqvnrhllaGILNTRGYRQAESQALDR 163
Cdd:cd03226 63 PIKAKERRKSIGYVM----------------QDVDyqLFTD-SVREELLL------------GLKELDAGNEQAETVLKD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 afywLEVVEMVDcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHD 243
Cdd:cd03226 114 ----LDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHD 185
|
250 260
....*....|....*....|
gi 490250751 244 MGMVMEISDHIIVLDHGDVI 263
Cdd:cd03226 186 YEFLAKVCDRVLLLANGAIV 205
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-274 |
2.07e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 101.42 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdvIQVLGQK---LH 82
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEE-----IRLKPDRdgeLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 PDDflhPAQLgRRIyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAQhtqvnRHLLagilntrgyRQAESQALD 162
Cdd:COG4598 84 PAD---RRQL-QRI------------RTRLGMVFQSFNLWSHMTVLENVIEAP-----VHVL---------GRPKAEAIE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEH 242
Cdd:COG4598 134 RAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH 212
|
250 260 270
....*....|....*....|....*....|..
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG4598 213 EMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-274 |
3.07e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDVIQVLGQk 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT-INLVRDKDGQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhpaqlgrriyYKMFGGTHL-VNRAGLARTFQNIRLFREMSVIENLLVAQhtqvnrhllagiLNTRGYRQAEsq 159
Cdd:PRK10619 79 -----------------LKVADKNQLrLLRTRLTMVFQHFNLWSHMTVLENVMEAP------------IQVLGLSKQE-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVVEMVDCAN-RLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVL 238
Cdd:PRK10619 128 ARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMV 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250751 239 LIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK10619 207 VVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-262 |
5.08e-25 |
|
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: 99.25 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklHPDD 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDL--------PPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmfggthlvnrAGLARTFQNIRLFREMSVIENLlvaqhtqvnrhllAGILNTRGYRQAESQALDRaf 165
Cdd:cd03301 72 ------------------------RDIAMVFQNYALYPHMTVYDNI-------------AFGLKLRKVPKDEIDERVR-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlEVVEMVDCA---NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNP-VETQALSRIIRfLRQQHGITVLLIE 241
Cdd:cd03301 113 ---EVAELLQIEhllDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAkLRVQMRAELKR-LQQRLGTTTIYVT 188
|
250 260
....*....|....*....|.
gi 490250751 242 HDMGMVMEISDHIIVLDHGDV 262
Cdd:cd03301 189 HDQVEAMTMADRIAVMNDGQI 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-269 |
6.66e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 6.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdviqvLGQklhpdd 85
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP--------LAD------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 fLHPAQLGRRiyykmfggthlvnRAGLartfqnirlfremsvienllvAQHTQVNRHLLA------GILNTRGYRQAESQ 159
Cdd:PRK13548 69 -WSPAELARR-------------RAVL---------------------PQHSSLSFPFTVeevvamGRAPHGLSRAEDDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMC------TRPEMICLDEPAAGLNPVETQALSRIIRFLRQQH 233
Cdd:PRK13548 114 LVAAA---LAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHER 190
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250751 234 GITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQ 269
Cdd:PRK13548 191 GLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-272 |
1.41e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.77 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKL 81
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY------------LGKEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HpddflhpaqlgrriyykmFGGTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTqVNRhlLAGILNTRGYRQAesqal 161
Cdd:PRK10762 69 T------------------FNGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREF-VNR--FGRIDWKKMYAEA----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEmvdCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIE 241
Cdd:PRK10762 123 DKLLARLNLRF---SSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYIS 198
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIQ 272
Cdd:PRK10762 199 HRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-278 |
1.79e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI-------------VLRAREKVTDVIQvlgqklHP 83
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydkksLLEVRKTVGIVFQ------NP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 DDflhpaqlgrriyyKMFGGThlvnraglartfqnirlfremsvienllvaqhtqVNRHLLAGILNTrGYRQAESQalDR 163
Cdd:PRK13639 88 DD-------------QLFAPT----------------------------------VEEDVAFGPLNL-GLSKEEVE--KR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHD 243
Cdd:PRK13639 118 VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHD 196
|
250 260 270
....*....|....*....|....*....|....*
gi 490250751 244 MGMVMEISDHIIVLDHGDVIARGAPQAIQANASVI 278
Cdd:PRK13639 197 VDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-279 |
2.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFGG-----IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrareKVTDViqVL 77
Cdd:PRK13631 19 DIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI------QVGDI--YI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 78 GQKLHPDDFLHpAQLGRRIyyKMFggTHLVNRAGLARTFQNIRLFRemsvienllvaqhTQVNRHLLAGILNtrgYRQAE 157
Cdd:PRK13631 91 GDKKNNHELIT-NPYSKKI--KNF--KELRRRVSMVFQFPEYQLFK-------------DTIEKDIMFGPVA---LGVKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 158 SQALDRAFYWLEVVEM-VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGIT 236
Cdd:PRK13631 150 SEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490250751 237 VLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIA 279
Cdd:PRK13631 229 VFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-274 |
2.45e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVfncltgfyratggsivLRAREKVTDviqvlgqk 80
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTL----------------LRSINRMND-------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDFLHPAQL--GRRIYYKMFGGTHLVNRAGLarTFQNIRLFrEMSVIENLLVAQHtqvnrhlLAGILNTRGYRQAES 158
Cdd:PRK14239 57 LNPEVTITGSIVynGHNIYSPRTDTVDLRKEIGM--VFQQPNPF-PMSIYENVVYGLR-------LKGIKDKQVLDEAVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAFYWLEVvemvdcANRL---AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgi 235
Cdd:PRK14239 127 KSLKGASIWDEV------KDRLhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY-- 198
|
250 260 270
....*....|....*....|....*....|....*....
gi 490250751 236 TVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK14239 199 TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-280 |
2.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQvlgQKLHPddflhpaqlgrriyy 98
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN---KKLKP--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 kmfggthLVNRAGLARTFQNIRLFREMsvienllvaqhtqVNRHLLAGILNtrgYRQAESQALDRAFYWLEVVEMV-DCA 177
Cdd:PRK13634 83 -------LRKKVGIVFQFPEHQLFEET-------------VEKDICFGPMN---FGVSEEDAKQKAREMIELVGLPeELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVL 257
Cdd:PRK13634 140 ARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
250 260
....*....|....*....|...
gi 490250751 258 DHGDVIARGAPQAIQANASVIAA 280
Cdd:PRK13634 220 HKGTVFLQGTPREIFADPDELEA 242
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-274 |
3.35e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 101.77 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHF--GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKLHP 83
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL------------GGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddfLHPAQLGRRIyykmfggthlvnrAGLArtfQNIRLFReMSVIENLLVAQHTQVNRHLLagilntrgyrqaesQALDR 163
Cdd:COG4987 402 ---LDEDDLRRRI-------------AVVP---QRPHLFD-TTLRENLRLARPDATDEELW--------------AALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 A--FYWLE---------VVEmvdcanrLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALsrIIRFLRQQ 232
Cdd:COG4987 448 VglGDWLAalpdgldtwLGE-------GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL--LADLLEAL 518
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490250751 233 HGITVLLIEHDMgMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG4987 519 AGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-252 |
3.42e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCltgFYRATGGSIVLRAREKVTdviqVLGQKL 81
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRC---FNRLNDLIPGFRVEGKVT----FHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HPDDfLHPAQLGRRIyykmfggthlvnraGLarTFQNIRLFREmSVIENllVAQHTQVNrhllagilntrGYR----QAE 157
Cdd:PRK14243 80 YAPD-VDPVEVRRRI--------------GM--VFQKPNPFPK-SIYDN--IAYGARIN-----------GYKgdmdELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 158 SQALDRAFYWLEVVemvDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTV 237
Cdd:PRK14243 129 ERSLRQAALWDEVK---DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TI 203
|
250
....*....|....*
gi 490250751 238 LLIEHDMGMVMEISD 252
Cdd:PRK14243 204 IIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-271 |
3.44e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIK--ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI-----------VLRAR 67
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 68 EKVTDVIQvlgqklHPDDflhpaqlgrriyykMFGGThlvnraglarTFQNIRLFRemsvIENLLVAQHTQVNRhllagi 147
Cdd:PRK13635 81 RQVGMVFQ------NPDN--------------QFVGA----------TVQDDVAFG----LENIGVPREEMVER------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 148 lntrgyrqaESQALDRafywlevVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIR 227
Cdd:PRK13635 121 ---------VDQALRQ-------VGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490250751 228 FLRQQHGITVLLIEHDMGMVMEiSDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK13635 185 QLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-273 |
5.04e-24 |
|
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: 101.42 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGF--YRATGGSIVLRA-----------REKVTD 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHValcekcgyverPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 73 VIQVLGQKLHPD--DFLHPAQLGRRIYYKMfggthlvNRAGLARTFQnirLFREMSVIENLLVAqhtqvnrhllagiLNT 150
Cdd:TIGR03269 81 PCPVCGGTLEPEevDFWNLSDKLRRRIRKR-------IAIMLQRTFA---LYGDDTVLDNVLEA-------------LEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 151 RGYRQAEsqALDRAfywLEVVEMVDCANR---LAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIR 227
Cdd:TIGR03269 138 IGYEGKE--AVGRA---VDLIEMVQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490250751 228 FLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:TIGR03269 213 EAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-282 |
7.20e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.01 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLhpdD 85
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL------------NIAGHQF---D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FlhPAQLGRRIYYKMfggthlvnRAGLARTFQNIRLFREMSVIENLLVAQhtqvnrhllagilnTRGYRQAESQALDRAF 165
Cdd:COG4161 68 F--SQKPSEKAIRLL--------RQKVGMVFQQYNLWPHLTVMENLIEAP--------------CKVLGLSKEQAREKAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLrQQHGITVLLIEHDMG 245
Cdd:COG4161 124 KLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVE 202
|
250 260 270
....*....|....*....|....*....|....*...
gi 490250751 246 MVMEISDHIIVLDHGDVIARG-APQAIQANASVIAAYL 282
Cdd:COG4161 203 FARKVASQVVYMEKGRIIEQGdASHFTQPQTEAFAHYL 240
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-269 |
1.07e-23 |
|
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: 96.14 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL-----------RAREKVTDVIQvlgqklhpD 84
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidirdisrkSLRSMIGVVLQ--------D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DFLhpaqlgrriyykmFGGThlvnraglarTFQNIRLFREMS----VIENLLVAQHTQVNRHLlagilnTRGYrqaESQA 160
Cdd:cd03254 86 TFL-------------FSGT----------IMENIRLGRPNAtdeeVIEAAKEAGAHDFIMKL------PNGY---DTVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRafywlevvemvdcanrlAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRqqHGITVLLI 240
Cdd:cd03254 134 GEN-----------------GGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIII 194
|
250 260
....*....|....*....|....*....
gi 490250751 241 EHDMGMVMEiSDHIIVLDHGDVIARGAPQ 269
Cdd:cd03254 195 AHRLSTIKN-ADKILVLDDGKIIEEGTHD 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-266 |
2.24e-23 |
|
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: 95.05 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVE---RGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdVIQVLGQKLHpddfLHPAQlgRR 95
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-----VLFDSRKKIN----LPPQQ--RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 IYYkmfggthlvnraglarTFQNIRLFREMSVIENLLVAqhtqvnrhllagilnTRGYRQAESQalDRAFYWLEVVEMVD 175
Cdd:cd03297 77 IGL----------------VFQQYALFPHLNVRENLAFG---------------LKRKRNREDR--ISVDELLDLLGLDH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 CANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHII 255
Cdd:cd03297 124 LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
250
....*....|.
gi 490250751 256 VLDHGDVIARG 266
Cdd:cd03297 204 VMEDGRLQYIG 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-266 |
2.82e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.76 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVLGQk 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhpAQLgRRIYYKMFGGTHLVNRAGLARTfqnirlfremsvienllVAQHTQVNRHLLAgiLNTRGYRQAESQA 160
Cdd:PRK11701 81 ---------AER-RRLLRTEWGFVHQHPRDGLRMQ-----------------VSAGGNIGERLMA--VGARHYGDIRATA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDrafyWLEVVEMVdcANR---LAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQA-LSRIIRFLRQQHGIT 236
Cdd:PRK11701 132 GD----WLERVEID--AARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGLVRELGLA 204
|
250 260 270
....*....|....*....|....*....|
gi 490250751 237 VLLIEHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:PRK11701 205 VVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-268 |
3.25e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGQKLhpddflhpaqlgrriyy 98
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-------DGVDITDKKV----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 KMfggTHLVNRAGLARTFQNIRLFREmsVIENLLVaqHTQVNRHLLAGILNTRGYRQAESQALDRAFYwlevvemvdcAN 178
Cdd:PRK13637 77 KL---SDIRKKVGLVFQYPEYQLFEE--TIEKDIA--FGPINLGLSEEEIENRVKRAMNIVGLDYEDY----------KD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 179 RLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLD 258
Cdd:PRK13637 140 KSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMN 219
|
250
....*....|
gi 490250751 259 HGDVIARGAP 268
Cdd:PRK13637 220 KGKCELQGTP 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-285 |
3.81e-23 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 98.74 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYR--ATGGSIVLRAREKVTDVIQVlgqklh 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 pddflhpaqlgrriyykmfggthlVNRAGLARTFQNIRLFREMSVIENLLVAQHtqvnrhllagiLNTRGYRQAESQALD 162
Cdd:TIGR02633 75 ------------------------TERAGIVIIHQELTLVPELSVAENIFLGNE-----------ITLPGGRMAYNAMYL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVEMVDCAN-RLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLrQQHGITVLLIE 241
Cdd:TIGR02633 120 RAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYIS 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVIARGAPQAIQANaSVIAAYLGAE 285
Cdd:TIGR02633 199 HKLNEVKAVCDTICVIRDGQHVATKDMSTMSED-DIITMMVGRE 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-278 |
7.44e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIK--ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyratggsiVLRAREKVTDVIQVLG 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLING---------LLLPDDNPNSKITVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKLHPDDFLHpaqlgrriyykmfggthLVNRAGLarTFQNIrlfremsviENLLVAqhTQVNRHLLAGILNtRGYRQAES 158
Cdd:PRK13640 72 ITLTAKTVWD-----------------IREKVGI--VFQNP---------DNQFVG--ATVGDDVAFGLEN-RAVPRPEM 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAFywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVL 238
Cdd:PRK13640 121 IKIVRDV--LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVI 198
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490250751 239 LIEHDMGMVmEISDHIIVLDHGDVIARGAPQAIQANASVI 278
Cdd:PRK13640 199 SITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-266 |
9.66e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLhpdD 85
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL------------NIAGNHF---D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHP--AQLGRRIyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAQhTQVnrhllAGIlntrgyrqAESQALDR 163
Cdd:PRK11124 68 FSKTpsDKAIREL------------RRNVGMVFQQYNLWPHLTVQQNLIEAP-CRV-----LGL--------SKDQALAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLrQQHGITVLLIEHD 243
Cdd:PRK11124 122 AEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHE 200
|
250 260
....*....|....*....|...
gi 490250751 244 MGMVMEISDHIIVLDHGDVIARG 266
Cdd:PRK11124 201 VEVARKTASRVVYMENGHIVEQG 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-263 |
1.05e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 97.17 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYrATG---GSIVLRarekvtdviqvlGQKL 81
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFD------------GEVC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HpddflhpaqlgrriyykmFGGTHLVNRAGLARTFQNIRLFREMSVIENLLVAqhtqvNRHLLAGILNTRgyrqaesQAL 161
Cdd:NF040905 68 R------------------FKDIRDSEALGIVIIHQELALIPYLSIAENIFLG-----NERAKRGVIDWN-------ETN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIE 241
Cdd:NF040905 118 RRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIIS 196
|
250 260
....*....|....*....|..
gi 490250751 242 HDMGMVMEISDHIIVLDHGDVI 263
Cdd:NF040905 197 HKLNEIRRVADSITVLRDGRTI 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-256 |
1.13e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.57 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHF---GGI--------KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARek 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 70 vtDVIQVLGQKLHPddflhpaqLGRRIyykmfggtHLVnraglartFQ------NIRlfreMSVIEnlLVAQHTQVNRhl 143
Cdd:COG4608 81 --DITGLSGRELRP--------LRRRM--------QMV--------FQdpyaslNPR----MTVGD--IIAEPLRIHG-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 144 lagiLNTRGYRQAESQALdrafywLEVVEM-VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQAl 222
Cdd:COG4608 127 ----LASKAERRERVAEL------LELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIQA- 194
|
250 260 270
....*....|....*....|....*....|....*..
gi 490250751 223 sRII---RFLRQQHGITVLLIEHDMGMVMEISDHIIV 256
Cdd:COG4608 195 -QVLnllEDLQDELGLTYLFISHDLSVVRHISDRVAV 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-260 |
4.46e-22 |
|
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: 91.76 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdvIQVLGqklhPDDFLhpaqlgrriyykm 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPG----PDRMV------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnraglarTFQNIRLFREMSVIENLLVAQHtQVNRHLlagilntrgyRQAESQALDRAFywLEVVEMVDCANRL 180
Cdd:TIGR01184 59 --------------VFQNYSLLPWLTVRENIALAVD-RVLPDL----------SKSERRAIVEEH--IALVGLTEAADKR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHG 260
Cdd:TIGR01184 112 PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
4.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRatggsivLRAREKVTDVIQVLGQKLHPdd 85
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-------LESEVRVEGRVEFFNQNIYE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgRRIYYKMFggthlvnRAGLARTFQNIRLFrEMSVIENL-----LVAQHTQVNrhlLAGILNTrgyrqaesqA 160
Cdd:PRK14258 79 --------RRVNLNRL-------RRQVSMVHPKPNLF-PMSVYDNVaygvkIVGWRPKLE---IDDIVES---------A 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVdcaNRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:PRK14258 131 LKDADLWDEIKHKI---HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIV 207
|
250
....*....|..
gi 490250751 241 EHDMGMVMEISD 252
Cdd:PRK14258 208 SHNLHQVSRLSD 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-257 |
7.28e-22 |
|
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: 93.19 E-value: 7.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRA---TGGSIVlrarekvtdviqvl 77
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 78 gqklhpddflhpaqlgrriyykmFGGTHLVNRAGlaRTFQNIRLfREMSVIenllvAQ---------HTqVNRHLLAGIL 148
Cdd:COG0444 67 -----------------------FDGEDLLKLSE--KELRKIRG-REIQMI-----FQdpmtslnpvMT-VGDQIAEPLR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 149 NTRGYRQAEsqALDRAFYWLEVVEMVDCANRLA---GTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQA--Ls 223
Cdd:COG0444 115 IHGGLSKAE--ARERAIELLERVGLPDPERRLDrypHELSGGMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqiL- 190
|
250 260 270
....*....|....*....|....*....|....
gi 490250751 224 RIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVL 257
Cdd:COG0444 191 NLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-271 |
1.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI-----VLRAREKVTDVIQVlgqklhpddflhpaqlg 93
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtLITSTSKNKDIKQI----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 RRiyykmfggthlvnRAGLARTFQNIRLFREmSVIENllVAQHTQvnrhllagilnTRGYRQAESQALDRafywlEVVEM 173
Cdd:PRK13649 84 RK-------------KVGLVFQFPESQLFEE-TVLKD--VAFGPQ-----------NFGVSQEEAEALAR-----EKLAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 VDCANRLAGT----LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVME 249
Cdd:PRK13649 132 VGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVAN 210
|
250 260
....*....|....*....|..
gi 490250751 250 ISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK13649 211 YADFVYVLEKGKLVLSGKPKDI 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-271 |
1.34e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKL-HP 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD------------GVDLsHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 DDFLHPAQLgrriyykmfggthlvnraglarTFQNIRLFREMSVIENLLVaqhtqvnrhllagilntrGYRQ---AESQA 160
Cdd:PRK11607 87 PPYQRPINM----------------------MFQSYALFPHMTVEQNIAF------------------GLKQdklPKAEI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:PRK11607 127 ASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMV 206
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK11607 207 THDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-271 |
1.35e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL-------RARekvtdv 73
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsRAR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 74 iqvlgqklhpddflhpaqlgrriyykmfggtHLVNRAGLARTFQNirLFREMSVIENLLVAqhtqvnrhllagilnTRGY 153
Cdd:PRK13537 77 -------------------------------HARQRVGVVPQFDN--LDPDFTVRENLLVF---------------GRYF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 RQAESQALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvetQALSRIIRFLRQ-- 231
Cdd:PRK13537 109 GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP---QARHLMWERLRSll 185
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490250751 232 QHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK13537 186 ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-262 |
3.20e-21 |
|
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: 89.39 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKLHPddfLHpaqlGRR 95
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI------------RVNGQDVSD---LR----GRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 IYYkmfggthLVNRAGLArtFQNIRLFREMSVIENLLVAQH-TQVNRhllagilntRGYRQAESQALDRafywlevVEMV 174
Cdd:cd03292 73 IPY-------LRRKIGVV--FQDFRLLPDRNVYENVAFALEvTGVPP---------REIRKRVPAALEL-------VGLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETqalSRIIRFLRQQH--GITVLLIEHDMGMVMEISD 252
Cdd:cd03292 128 HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT---WEIMNLLKKINkaGTTVVVATHAKELVDTTRH 204
|
250
....*....|
gi 490250751 253 HIIVLDHGDV 262
Cdd:cd03292 205 RVIALERGKL 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-264 |
3.44e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 92.87 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 15 FGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvLGQKLHpddflhpaqlgr 94
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF------------QGKEID------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 95 riyykmFGGTHLVNRAGLARTFQNIRLFREMSVIENLLVAqhtqvnRHLLAGILNTRGYRQAESQALdraFYWLEVveMV 174
Cdd:PRK10982 64 ------FKSSKEALENGISMVHQELNLVLQRSVMDNMWLG------RYPTKGMFVDQDKMYRDTKAI---FDELDI--DI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 DCANRLAgTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDHI 254
Cdd:PRK10982 127 DPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEI 204
|
250
....*....|
gi 490250751 255 IVLDHGDVIA 264
Cdd:PRK10982 205 TILRDGQWIA 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-263 |
3.78e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.15 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDViqvlgqklhPDdflhpaqlgrriyY 98
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-VTKL---------PE-------------Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 KmfggthlvnRAGL-ARTFQNIRL--FREMSVIENLLVAQhtqvNRHllagilNTRGYRQAESQAlDRAFY--WLEVVEM 173
Cdd:COG1101 77 K---------RAKYiGRVFQDPMMgtAPSMTIEENLALAY----RRG------KRRGLRRGLTKK-RRELFreLLATLGL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 vDCANRL---AGTLSYGQqrRLEIARAMCT--RPEMICLDEPAAGLNPvETQAL-----SRIIRflrqQHGITVLLIEHD 243
Cdd:COG1101 137 -GLENRLdtkVGLLSGGQ--RQALSLLMATltKPKLLLLDEHTAALDP-KTAALvleltEKIVE----ENNLTTLMVTHN 208
|
250 260
....*....|....*....|
gi 490250751 244 MGMVMEISDHIIVLDHGDVI 263
Cdd:COG1101 209 MEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-278 |
3.91e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIV-------------LRAREKVTDVIQvlgqklHPDdfl 87
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldyskrglLALRQQVATVFQ------DPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 88 hpaqlgRRIYYkmfggTHLVNRAGLArtfqnirlFREMSVIENLLVaqhTQVNRHLLagILNTRGYRQAESQALdrafyw 167
Cdd:PRK13638 88 ------QQIFY-----TDIDSDIAFS--------LRNLGVPEAEIT---RRVDEALT--LVDAQHFRHQPIQCL------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 168 levvemvdcanrlagtlSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMV 247
Cdd:PRK13638 138 -----------------SHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLI 199
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 248 MEISDHIIVLDHGDVIARGAPQAIQANASVI 278
Cdd:PRK13638 200 YEISDAVYVLRQGQILTHGAPGEVFACTEAM 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-271 |
3.94e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.25 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRA----REKVTDVIQVLGQKL-HPDDFLHPA 90
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitKENIREVRKFVGLVFqNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 91 QLGRRIyykMFGGThlvnraglartfqnirlfremsvieNLLVAQHTQVNRhllagilntrgyrqaesqaLDRAFYWLEV 170
Cdd:PRK13652 95 TVEQDI---AFGPI-------------------------NLGLDEETVAHR-------------------VSSALHMLGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 171 VEMVDcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEI 250
Cdd:PRK13652 128 EELRD---RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEM 204
|
250 260
....*....|....*....|.
gi 490250751 251 SDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK13652 205 ADYIYVMDKGRIVAYGTVEEI 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
16-274 |
4.63e-21 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 90.54 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVF---NCLtgfYRATGGSIVLrAREKVTDviqvlgqklhpddfLHPAQL 92
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLrmiNRL---IEPTSGRILI-DGEDIRD--------------LDPVEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 93 GRRIYYKMfggthlvnraglartfQNIRLFREMSVIENL-LVAQhtqvnrhLLagilntrGYRQAESQAldRAfywLEVV 171
Cdd:COG1125 75 RRRIGYVI----------------QQIGLFPHMTVAENIaTVPR-------LL-------GWDKERIRA--RV---DELL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 172 EMVDC-----ANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGM 246
Cdd:COG1125 120 ELVGLdpeeyRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDE 199
|
250 260
....*....|....*....|....*...
gi 490250751 247 VMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG1125 200 ALKLGDRIAVMREGRIVQYDTPEEILAN 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-283 |
4.83e-21 |
|
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: 91.02 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 36 LIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvTDVIQVlgqklhpddflhPAQlgrriyykmfggthlvnRAGLART 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG----EDVTNV------------PPH-----------------LRHINMV 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 116 FQNIRLFREMSVIENLlvaqhtqvnrhllAGILNTRGYRQAESQAldRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIA 195
Cdd:TIGR01187 48 FQSYALFPHMTVEENV-------------AFGLKMRKVPRAEIKP--RVLEALRLVQLEEFADRKPHQLSGGQQQRVALA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 196 RAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQA-- 273
Cdd:TIGR01187 113 RALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEep 192
|
250
....*....|
gi 490250751 274 NASVIAAYLG 283
Cdd:TIGR01187 193 ANLFVARFIG 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-281 |
5.88e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrareKVTDVIQVLGQKLHPddfLHPAQlgrriyy 98
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVGDIVVSSTSKQKE---IKPVR------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 kmfggthlvNRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRHLLAGIlntrGYRQAESQALDRAFYWLEVVEmvdcan 178
Cdd:PRK13643 84 ---------KKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKI----AAEKLEMVGLADEFWEKSPFE------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 179 rlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDHIIVLD 258
Cdd:PRK13643 145 -----LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLE 218
|
250 260
....*....|....*....|...
gi 490250751 259 HGDVIARGAPQAIQANASVIAAY 281
Cdd:PRK13643 219 KGHIISCGTPSDVFQEVDFLKAH 241
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-274 |
7.63e-21 |
|
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: 89.24 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtDVIQVLGQKLhpddflhpaqlgRRIYYK 99
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ----DIAAMSRKEL------------RELRRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 MFGgthLVnraglartFQNIRLFREMSVIENLlvaqhtqvnrhllAGILNTRGYRQAESQAldRAFYWLEVVEMVDCANR 179
Cdd:cd03294 103 KIS---MV--------FQSFALLPHRTVLENV-------------AFGLEVQGVPRAEREE--RAAEALELVGLEGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPV---ETQALsriirFLRQQ--HGITVLLIEHDMGMVMEISDHI 254
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLirrEMQDE-----LLRLQaeLQKTIVFITHDLDEALRLGDRI 231
|
250 260
....*....|....*....|
gi 490250751 255 IVLDHGDVIARGAPQAIQAN 274
Cdd:cd03294 232 AIMKDGRLVQVGTPEEILTN 251
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-243 |
8.92e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.15 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIK----ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTdviqvlgq 79
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-VT-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 80 klHPDdflhpaqlgrriyykmfggthlvnrAGLARTFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGYRQAESQ 159
Cdd:COG4525 73 --GPG-------------------------ADRGVVFQKDALLPWLNVLDNVAFG-------------LRLRGVPKAERR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 AldRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpvetqALSR-----IIRFLRQQHG 234
Cdd:COG4525 113 A--RAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD-----ALTReqmqeLLLDVWQRTG 185
|
....*....
gi 490250751 235 ITVLLIEHD 243
Cdd:COG4525 186 KGVFLITHS 194
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-257 |
1.06e-20 |
|
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: 91.58 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFGG-IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQKL 81
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA------------VNGVPL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 HPDDflhPAQLGRRIYYkmfggthlvnraglarTFQNIRLFrEMSVIENLLVAQhtqvnrhllagilntRGYRQAE-SQA 160
Cdd:TIGR02857 387 ADAD---ADSWRDQIAW----------------VPQHPFLF-AGTIAENIRLAR---------------PDASDAEiREA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVEMVDCANRLAGT----LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiT 236
Cdd:TIGR02857 432 LERAGLDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--T 509
|
250 260
....*....|....*....|.
gi 490250751 237 VLLIEHDMGmVMEISDHIIVL 257
Cdd:TIGR02857 510 VLLVTHRLA-LAALADRIVVL 529
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-267 |
1.23e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.86 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtDVIQVLGQKLhpddflhpaQLGRR 95
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ----DLTALSEKEL---------RKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 IYYKMFGGTHLVNraglART-FQNIRLFREmsvienllvaqhtqvnrhlLAGIlntrgyRQAESQAldRAFYWLEVVEMV 174
Cdd:PRK11153 83 QIGMIFQHFNLLS----SRTvFDNVALPLE-------------------LAGT------PKAEIKA--RVTELLELVGLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHI 254
Cdd:PRK11153 132 DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRV 211
|
250
....*....|...
gi 490250751 255 IVLDHGDVIARGA 267
Cdd:PRK11153 212 AVIDAGRLVEQGT 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-274 |
1.42e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 89.37 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVLGQKLHPDDFLhpaqlGRRIY 97
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVI-----QKTRF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 YKMFGGTHLVNRAGLARTFQNIRLFRemSVIENLLvaqhtqvnrhllagILNTRGYRQAESQALDRAFYWLEVVEM-VDC 176
Cdd:PRK13651 95 KKIKKIKEIRRRVGVVFQFAEYQLFE--QTIEKDI--------------IFGPVSMGVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 177 ANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDHIIV 256
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*...
gi 490250751 257 LDHGDVIARGAPQAIQAN 274
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-270 |
1.46e-20 |
|
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: 87.87 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGG----IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqv 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 77 LGQKLHpddflhpaQLGRRiyykmfggthlvNRAGLAR-----TFQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTR 151
Cdd:COG4181 72 AGQDLF--------ALDED------------ARARLRArhvgfVFQSFQLLPTLTALENVMLP-------------LELA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 152 GYRQAESQALDrafyWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQ 231
Cdd:COG4181 119 GRRDARARARA----LLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR 194
|
250 260 270
....*....|....*....|....*....|....*....
gi 490250751 232 QHGITVLLIEHDMGMVmEISDHIIVLDHGDVIARGAPQA 270
Cdd:COG4181 195 ERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-271 |
2.49e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 7 RVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTD--------VIQVLG 78
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLD-VATtpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKLHpddflhpaqlgrriyykmfggthlvnraglartfQNIRLfremSVIEnlLVA----QHTQvnrhllaGILNtrgyr 154
Cdd:COG4604 82 QENH----------------------------------INSRL----TVRE--LVAfgrfPYSK-------GRLT----- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 155 QAESQALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHG 234
Cdd:COG4604 110 AEDREIIDEA---IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELG 186
|
250 260 270
....*....|....*....|....*....|....*..
gi 490250751 235 ITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG4604 187 KTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-287 |
3.04e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 15 FGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQKLhPDDflhpAQLGR 94
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT------------VLGVPV-PAR----ARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 95 RiyykmfggthlvnRAGLARTFQNirLFREMSVIENLLVaqhtqVNRHLLagiLNTRgyrqaESQALDRAFywLEVVEMV 174
Cdd:PRK13536 114 A-------------RIGVVPQFDN--LDLEFTVRENLLV-----FGRYFG---MSTR-----EIEAVIPSL--LEFARLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDHI 254
Cdd:PRK13536 164 SKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRL 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250751 255 IVLDHGDVIARGAPQAI---QANASVIAAYLGAEEE 287
Cdd:PRK13536 243 CVLEAGRKIAEGRPHALideHIGCQVIEIYGGDPHE 278
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-260 |
3.25e-20 |
|
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: 86.72 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTdSILRVEHL-----MMHFGGIK--ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDV 73
Cdd:COG4778 1 MT-TLLEVENLsktftLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 74 iqvlgqklhpddflhpAQLG-RRIYYkmfggthlVNRAGLARTFQNIRLFREMSVIEnlLVAQHtqvnrhLLAgilntRG 152
Cdd:COG4778 80 ----------------AQASpREILA--------LRRRTIGYVSQFLRVIPRVSALD--VVAEP------LLE-----RG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 153 YRQAEsqALDRAFYWLE---VVEmvdcanRLAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRI 225
Cdd:COG4778 123 VDREE--ARARARELLArlnLPE------RLWDlppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVEL 194
|
250 260 270
....*....|....*....|....*....|....*
gi 490250751 226 IRFLRQQhGITVLLIEHDMGMVMEISDHIIVLDHG 260
Cdd:COG4778 195 IEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-285 |
3.39e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdviqvlgqklhPDD 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD---------------DVE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIyykmfggthlvnraglARTFQnirlfrEMSVIENLLVAQHTQVNRHLLAGILNTRGyrQAESQALDRAf 165
Cdd:PRK09536 69 ALSARAASRRV----------------ASVPQ------DTSLSFEFDVRQVVEMGRTPHRSRFDTWT--ETDRAAVERA- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLN---PVETQALSRIIrflrQQHGITVLLIEH 242
Cdd:PRK09536 124 --MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhQVRTLELVRRL----VDDGKTAVAAIH 197
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAIqANASVIAAYLGAE 285
Cdd:PRK09536 198 DLDLAARYCDELVLLADGRVRAAGPPADV-LTADTLRAAFDAR 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-271 |
4.93e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTgfyratggsivlrarekvtDVIQVLGQKLH 82
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN-------------------RLIEIYDSKIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 PDdflhpaqlGRRIYY--KMFGGTHLVNRAGLARTFQNIRLFREMSVIENLLVAQHTQvnrhllaGILNTRGYRQAESQA 160
Cdd:PRK14246 69 VD--------GKVLYFgkDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH-------GIKEKREIKKIVEEC 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLEVVemvDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhgITVLLI 240
Cdd:PRK14246 134 LRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIV 208
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK14246 209 SHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-262 |
5.42e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviqvlgqkLHPDD 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAGTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAQLGRRIyykmfggthlvnraglarTFQNIRLFREMSVIENLlvaqhtqvnrhllaGiLNTRG-YRQAESQALdra 164
Cdd:PRK11247 75 PLAEAREDTRL------------------MFQDARLLPWKKVIDNV--------------G-LGLKGqWRDAALQAL--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 fywlEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpvetqALSRI-----IRFLRQQHGITVLL 239
Cdd:PRK11247 119 ----AAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD-----ALTRIemqdlIESLWQQHGFTVLL 189
|
250 260
....*....|....*....|...
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDV 262
Cdd:PRK11247 190 VTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-273 |
6.29e-20 |
|
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: 89.42 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKA--LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDviqvlGQKLHP 83
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-------D-----GADLSQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 DDflhPAQLGRRIYYkmfggthlvnragLArtfQNIRLFrEMSVIENllVAQHTQVNRHllagilntrgyrqaesqaldr 163
Cdd:COG4618 399 WD---REELGRHIGY-------------LP---QDVELF-DGTIAEN--IARFGDADPE--------------------- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 afywlEVVEmvdcANRLAG---------------------TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQAL 222
Cdd:COG4618 436 -----KVVA----AAKLAGvhemilrlpdgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490250751 223 SRIIRFLRQQhGITVLLIEHDMGmVMEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:COG4618 507 AAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-271 |
9.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtdviqvlgqKLHPDDFlhPAQLGRRIYyk 99
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEG-------------------KVYVDGL--DTSDEENLW-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 mfggtHLVNRAGLarTFQNIrlfremsviENLLVAqhTQVNRHLLAGILNTrGYRQAESQAldRAFYWLEVVEMVDCANR 179
Cdd:PRK13633 82 -----DIRNKAGM--VFQNP---------DNQIVA--TIVEEDVAFGPENL-GIPPEEIRE--RVDESLKKVGMYEYRRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEiSDHIIVLDH 259
Cdd:PRK13633 141 APHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS 219
|
250
....*....|..
gi 490250751 260 GDVIARGAPQAI 271
Cdd:PRK13633 220 GKVVMEGTPKEI 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-271 |
1.00e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.22 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvtdviQVLGQklhp 83
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--------KPISM---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddfLHPAQLGRRIyykMFGGTHLVNRAGLArtfqnirlFREmsvienlLVAQHTqvNRHL-LAGILNtrgyrQAESQALD 162
Cdd:PRK11231 69 ---LSSRQLARRL---ALLPQHHLTPEGIT--------VRE-------LVAYGR--SPWLsLWGRLS-----AEDNARVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVEMvdcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEH 242
Cdd:PRK11231 121 QAMEQTRINHL---ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLH 196
|
250 260
....*....|....*....|....*....
gi 490250751 243 DMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK11231 197 DLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-266 |
1.38e-19 |
|
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: 84.85 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFggikalndvNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvTDVIqvlgqk 80
Cdd:cd03298 3 LDKIRFSYGEQPMHF---------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING----VDVT------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddFLHPAqlgrriyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAqhtqvnrhLLAGILNTRGYRQAESQA 160
Cdd:cd03298 64 -----AAPPA------------------DRPVSMLFQENNLFAHLTVEQNVGLG--------LSPGLKLTAEDRQAIEVA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRafywlevVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:cd03298 113 LAR-------VGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMV 185
|
250 260
....*....|....*....|....*.
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:cd03298 186 THQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-278 |
2.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.43 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHFGGIK--ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI-----------VLRAREK 69
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 70 VTDVIQvlgqklHPDDflhpaqlgrriyyKMFGGThlvNRAGLARTFQNIRLFR-EM-SVIENLlvAQHTQVNRHLlagi 147
Cdd:PRK13632 85 IGIIFQ------NPDN-------------QFIGAT---VEDDIAFGLENKKVPPkKMkDIIDDL--AKKVGMEDYL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 148 lntrgyrQAESQaldrafywlevvemvdcanrlagTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIR 227
Cdd:PRK13632 137 -------DKEPQ-----------------------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMV 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490250751 228 FLRQQHGITVLLIEHDMGMVMeISDHIIVLDHGDVIARGAPQAIQANASVI 278
Cdd:PRK13632 187 DLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-266 |
2.54e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviQVLGQKlhpddflhpaqlgrri 96
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI------------SILGQP---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 97 yykmfggthlVNRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRHLLAGILntRGYRQAESQALDRAfywLEVVEMVDC 176
Cdd:PRK15056 71 ----------TRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWL--RRAKKRDRQIVTAA---LARVDMVEF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 177 ANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQAlsRIIRFLRQ--QHGITVLLIEHDMGMVMEISDHI 254
Cdd:PRK15056 136 RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD-VKTEA--RIISLLRElrDEGKTMLVSTHNLGSVTEFCDYT 212
|
250
....*....|..
gi 490250751 255 IVLDhGDVIARG 266
Cdd:PRK15056 213 VMVK-GTVLASG 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-271 |
2.88e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.19 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGGIKA--LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlG 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN------------N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKLHPDDFlhpaqlgRRIyykmfggthlvnRAGLARTFQNIrlfremsviENLLVAqhTQVNRHLLAGILN----TRGYR 154
Cdd:PRK13648 71 QAITDDNF-------EKL------------RKHIGIVFQNP---------DNQFVG--SIVKYDVAFGLENhavpYDEMH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 155 QAESQALdrafywlEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHG 234
Cdd:PRK13648 121 RRVSEAL-------KQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 490250751 235 ITVLLIEHDMGMVMEiSDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK13648 194 ITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-271 |
3.60e-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: 87.17 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF-----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQvl 77
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTK-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 78 gqklhpddfLHPAQLGRRIYYkmfggthlvnragLARTFQNIRLFREMSVIENLLVAQHTQVNRHLlagilntrgyrqae 157
Cdd:TIGR03269 355 ---------PGPDGRGRAKRY-------------IGILHQEYDLYPHRTVLDNLTEAIGLELPDEL-------------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 158 sqALDRAFYWLEVV-----EMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQ 232
Cdd:TIGR03269 399 --ARMKAVITLKMVgfdeeKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREE 476
|
250 260 270
....*....|....*....|....*....|....*....
gi 490250751 233 HGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:TIGR03269 477 MEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-274 |
4.06e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.51 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVfncLTGFYRAtggsIVLRAREKVTDVIQVLGQKLHPDD 85
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTL---LRTFNRL----LELNEEARVEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 fLHPAQLGRRIyykmfggthlvnraglARTFQNIRLFREMSVIENllVAQHTQVNrhllaGILNTRGYRQAESQ-ALDRA 164
Cdd:PRK14267 78 -VDPIEVRREV----------------GMVFQYPNPFPHLTIYDN--VAIGVKLN-----GLVKSKKELDERVEwALKKA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 FYWLEVVemvDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHDM 244
Cdd:PRK14267 134 ALWDEVK---DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSP 208
|
250 260 270
....*....|....*....|....*....|
gi 490250751 245 GMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK14267 209 AQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-275 |
1.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF---GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYratggsivlrarEKVTDVIQVLGQ 79
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF------------EEFEGKVKIDGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 80 KLHPDDFLHpaqLGRRIyykmfggthlvnraglARTFQNIrlfremsviENLLVAqhTQVNRHLLAGILNTRGYRQAESQ 159
Cdd:PRK13642 70 LLTAENVWN---LRRKI----------------GMVFQNP---------DNQFVG--ATVEDDVAFGMENQGIPREEMIK 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLL 239
Cdd:PRK13642 120 RVDEA---LLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLS 196
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250751 240 IEHDMGMVMEiSDHIIVLDHGDVIARGAPQAIQANA 275
Cdd:PRK13642 197 ITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-271 |
1.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvtdviqVLGQKLHPDDFLHpaqlgrriyykm 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII------------IDGDLLTEENVWD------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvNRAGLARTFQNIrlfremsviENLLVAqhTQVNRHLLAGILNTRGYRQAESQALDRAfywLEVVEMVDCANRL 180
Cdd:PRK13650 79 -------IRHKIGMVFQNP---------DNQFVG--ATVEDDVAFGLENKGIPHEEMKERVNEA---LELVGMQDFKERE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVmEISDHIIVLDHG 260
Cdd:PRK13650 138 PARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
250
....*....|.
gi 490250751 261 DVIARGAPQAI 271
Cdd:PRK13650 217 QVESTSTPREL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-263 |
2.92e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 8 VEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqVLGQklhpDDFL 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIG----YLPQ----EPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 88 HPaqlGRRIYYKMFggthlvnrAGLARTFQnirLFREMSVIENLLVAQHTQVNRH-LLAGILNTRGYRQAESQA---LDR 163
Cdd:COG0488 73 DD---DLTVLDTVL--------DGDAELRA---LEAELEELEAKLAEPDEDLERLaELQEEFEALGGWEAEARAeeiLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 afywLEVVEmvDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPaaglnpveT-----QALSRIIRFLRQQHGiTVL 238
Cdd:COG0488 139 ----LGFPE--EDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP--------TnhldlESIEWLEEFLKNYPG-TVL 203
|
250 260
....*....|....*....|....*
gi 490250751 239 LIEHDMGMVMEISDHIIVLDHGDVI 263
Cdd:COG0488 204 VVSHDRYFLDRVATRILELDRGKLT 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-266 |
3.34e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.45 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDviqvlGQKLhpddflhpAQLGRR 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-------D-----GVDI--------RDLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 IYYKMFGgthLVnraglartFQNIRLFrEMSVIENLLVaqhtqvnrhllagilntrGYRQAESQALDRAfywLEVVEMVD 175
Cdd:COG1132 411 SLRRQIG---VV--------PQDTFLF-SGTIRENIRY------------------GRPDATDEEVEEA---AKAAQAHE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 CANRLAG-----------TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvET-----QALSRIIRflrqqhGITVLL 239
Cdd:COG1132 458 FIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDT-ETealiqEALERLMK------GRTTIV 530
|
250 260
....*....|....*....|....*..
gi 490250751 240 IEHDMGMVMEiSDHIIVLDHGDVIARG 266
Cdd:COG1132 531 IAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-279 |
3.40e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFY-RATGGSIVlrarekvtdviqvlgqklhpDDFLHPAQLGRRIY 97
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIV--------------------GDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 YKmfggtHLVNRAGLARTFQNIRLFREMsvienllvaqhtqVNRHLLAGILNTRGYRQaesQALDRAFYWLEVVEMV-DC 176
Cdd:PRK13645 85 VK-----RLRKEIGLVFQFPEYQLFQET-------------IEKDIAFGPVNLGENKQ---EAYKKVPELLKLVQLPeDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 177 ANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIV 256
Cdd:PRK13645 144 VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
250 260
....*....|....*....|...
gi 490250751 257 LDHGDVIARGAPQAIQANASVIA 279
Cdd:PRK13645 224 MHEGKVISIGSPFEIFSNQELLT 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-271 |
3.78e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSI--LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdvIQVLG 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH-----IQHYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKlhpddflhpaQLGRRIyykmfggthlvnraGLARtfQNIRLFREMSVIEnlLVAQHTQVNRHLLagilnTRgYRQAES 158
Cdd:PRK10253 76 SK----------EVARRI--------------GLLA--QNATTPGDITVQE--LVARGRYPHQPLF-----TR-WRKEDE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 159 QALDRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVL 238
Cdd:PRK10253 122 EAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLA 198
|
250 260 270
....*....|....*....|....*....|...
gi 490250751 239 LIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK10253 199 AVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-281 |
7.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGQKlhPDDFLHPAQlgrriyy 98
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-------DDITITHKT--KDKYIRPVR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 kmfggthlvNRAGLARTFQNIRLFREmsvienllvaqhtQVNRHLLAGILNtrgYRQAESQALDRAFYWL-EVVEMVDCA 177
Cdd:PRK13646 85 ---------KRIGMVFQFPESQLFED-------------TVEREIIFGPKN---FKMNLDEVKNYAHRLLmDLGFSRDVM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVL 257
Cdd:PRK13646 140 SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
250 260
....*....|....*....|....
gi 490250751 258 DHGDVIARGAPQAIQANASVIAAY 281
Cdd:PRK13646 220 KEGSIVSQTSPKELFKDKKKLADW 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
9.90e-18 |
|
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: 82.81 E-value: 9.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFGG----IKALNDVNLEVERGSITALIGPNGAGKT----TVFNCLTGFYRATGGSIVLRAREkvtd 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 73 viqVLGqklhpddfLHPAQL----GRRIyykmfggthlvnraglARTFQnirlfrE-MS-----------VIENLLVaqH 136
Cdd:COG4172 78 ---LLG--------LSERELrrirGNRI----------------AMIFQ------EpMTslnplhtigkqIAEVLRL--H 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 137 TQVNRhllagilntrgyRQAESQALDrafyWLEVVEMVDCANRLAG---TLSYGQQRRLEIARAMCTRPEMICLDEPAAG 213
Cdd:COG4172 123 RGLSG------------AAARARALE----LLERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTA 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250751 214 LNpVETQAlsRI---IRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:COG4172 187 LD-VTVQA--QIldlLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-270 |
1.71e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.06 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRA---TGGSIVLRAREkVTDViqvlgqklh 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRR-LTAL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 pddflhPAQLgRRIyykmfggthlvnraGLarTFQNIRLFREMSVIENLLVAQHTQVNRhllagilNTRgyRQAESQALD 162
Cdd:COG4136 72 ------PAEQ-RRI--------------GI--LFQDDLLFPHLSVGENLAFALPPTIGR-------AQR--RARVEQALE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAfywlevvEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNP-----VETQALSRIirflrQQHGITV 237
Cdd:COG4136 120 EA-------GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAalraqFREFVFEQI-----RQRGIPA 187
|
250 260 270
....*....|....*....|....*....|...
gi 490250751 238 LLIEHDMgmvmeiSDhiiVLDHGDVIARGAPQA 270
Cdd:COG4136 188 LLVTHDE------ED---APAAGRVLDLGNWQH 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-284 |
1.98e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 14 HFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdVIQVLGqklhpddflhpaqLG 93
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----VSALLE-------------LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 rriyykmfggthlvnrAGlartFQNirlfrEMSVIENLlvaqhtqvnrHLLAGILntrGYRQAESQA-LDrafywlEVVE 172
Cdd:COG1134 97 ----------------AG----FHP-----ELTGRENI----------YLNGRLL---GLSRKEIDEkFD------EIVE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 173 MVDCANRL---AGTLSYGQQRRLEIARAMCTRPEMICLDEpaaglnpvetqALS------------RIIRFLRQqhGITV 237
Cdd:COG1134 133 FAELGDFIdqpVKTYSSGMRARLAFAVATAVDPDILLVDE-----------VLAvgdaafqkkclaRIRELRES--GRTV 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490250751 238 LLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAiqanasVIAAYLGA 284
Cdd:COG1134 200 IFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE------VIAAYEAL 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-266 |
2.09e-17 |
|
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: 78.79 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvTDVIQvlgqklhpddfLHPAQLGRRIY 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----TDIRQ-----------LDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 YKMfggthlvnraglartfQNIRLFREmSVIENLlvaqhtqvnrhllagilnTRGYRQAESQALdrafywLEVVEMVdCA 177
Cdd:cd03245 82 YVP----------------QDVTLFYG-TLRDNI------------------TLGAPLADDERI------LRAAELA-GV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGT---------------LSYGQQRRLEIARAMCTRPEMICLDEPAAGL-NPVETQALSRIIRFLRqqhGITVLLIE 241
Cdd:cd03245 120 TDFVNKhpngldlqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMdMNSEERLKERLRQLLG---DKTLIIIT 196
|
250 260
....*....|....*....|....*
gi 490250751 242 HDMGMvMEISDHIIVLDHGDVIARG 266
Cdd:cd03245 197 HRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-271 |
2.41e-17 |
|
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: 81.65 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF-----------GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGgsivlrarekvtdV 73
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEG-------------E 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 74 IQVLGQKLHPddfLHPAQLgRRIyykmfggthlvnRAGLARTFQ------NIRLFREMSVIENLLVaQHTQVNRhllagi 147
Cdd:COG4172 342 IRFDGQDLDG---LSRRAL-RPL------------RRRMQVVFQdpfgslSPRMTVGQIIAEGLRV-HGPGLSA------ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 148 lntrgyrqaeSQALDRAFYWLEVVEM-VDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPaaglnpveTQALSRII 226
Cdd:COG4172 399 ----------AERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP--------TSALDVSV 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490250751 227 RF--------LRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:COG4172 461 QAqildllrdLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-244 |
3.14e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.36 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlgqklhpd 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dflhpaqlGRRiyykmfggthlVNRAGLAR--TFQNIRLFREMSVIENllVAQHTQvnrhlLAGIlntrgyrqAESQALD 162
Cdd:PRK11248 62 --------GKP-----------VEGPGAERgvVFQNEGLLPWRNVQDN--VAFGLQ-----LAGV--------EKMQRLE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEH 242
Cdd:PRK11248 108 IAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
..
gi 490250751 243 DM 244
Cdd:PRK11248 188 DI 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-263 |
3.29e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviqVLGQKLhpd 84
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dflhpaQLGrriYYKmfggthlvnraglartfQNIRLFR-EMSVIENL--LVAQHTQVN-RHLLAGILNTRgyrqaesqa 160
Cdd:COG0488 379 ------KIG---YFD-----------------QHQEELDpDKTVLDELrdGAPGGTEQEvRGYLGRFLFSG--------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 lDRAFywlevvemvdcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAaglNPVETQALSRIIRFLRQQHGiTVLLI 240
Cdd:COG0488 424 -DDAF-------------KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT---NHLDIETLEALEEALDDFPG-TVLLV 485
|
250 260
....*....|....*....|...
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVI 263
Cdd:COG0488 486 SHDRYFLDRVATRILEFEDGGVR 508
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-266 |
8.04e-17 |
|
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: 80.15 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGG--IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvtdviqvlgqklHP 83
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG---------------HD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 DDFLHPAQLgrriyykmfggthlvnRAGLARTFQNIRLFREmSVIENLLVAQHTQVNRhllagilntrgyrqAESQALDR 163
Cdd:TIGR02203 396 LADYTLASL----------------RRQVALVSQDVVLFND-TIANNIAYGRTEQADR--------------AEIERALA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 AFYWLEVVemvdcaNRL-----------AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGL-NPVETQ---ALSRIIRf 228
Cdd:TIGR02203 445 AAYAQDFV------DKLplgldtpigenGVLLSGGQRQRLAIARALLKDAPILILDEATSALdNESERLvqaALERLMQ- 517
|
250 260 270
....*....|....*....|....*....|....*...
gi 490250751 229 lrqqhGITVLLIEHDMGMVmEISDHIIVLDHGDVIARG 266
Cdd:TIGR02203 518 -----GRTTLVIAHRLSTI-EKADRIVVMDDGRIVERG 549
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-271 |
1.06e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 10 HLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTgfyratggsivlRAREKVTdviqvlGQKLHPDdflhp 89
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLN------------RMNDKVS------GYRYSGD----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 90 AQLGRRIYYKMFGGTHLVNRAGLarTFQNIRLFrEMSVIENLLVAqhtqVNRHLLAGILNTRGYRQAEsqaLDRAFYWLE 169
Cdd:PRK14271 83 VLLGGRSIFNYRDVLEFRRRVGM--LFQRPNPF-PMSIMDNVLAG----VRAHKLVPRKEFRGVAQAR---LTEVGLWDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 170 VVE-MVDCANRLAGtlsyGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhgITVLLIEHDMGMVM 248
Cdd:PRK14271 153 VKDrLSDSPFRLSG----GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAA 226
|
250 260
....*....|....*....|...
gi 490250751 249 EISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK14271 227 RISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-266 |
1.34e-16 |
|
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: 76.89 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGQKLhpddflhpAQLGRRI 96
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-------DGHDVRDYTL--------ASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 97 yykmfggtHLVNraglartfQNIRLFREmSVIENLLVAqhtqvnrhllagilnTRGYRQAESQALDRAFYWLEVV-EMVD 175
Cdd:cd03251 79 --------GLVS--------QDVFLFND-TVAENIAYG---------------RPGATREEVEEAARAANAHEFImELPE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 CANRLAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQqhGITVLLIEHDMGMVMEiS 251
Cdd:cd03251 127 GYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-A 203
|
250
....*....|....*
gi 490250751 252 DHIIVLDHGDVIARG 266
Cdd:cd03251 204 DRIVVLEDGKIVERG 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-286 |
1.36e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.76 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdviqVL---GQKLhpddFLHPAQlgRRIYYk 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR--------VLfdaEKGI----CLPPEK--RRIGY- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 mfggthlvnraglarTFQNIRLFREMSVIENLLvaqhtqvnrhllagilntrgYRQAESqalDRAfYWLEVVEMVDCA-- 177
Cdd:PRK11144 81 ---------------VFQDARLFPHYKVRGNLR--------------------YGMAKS---MVA-QFDKIVALLGIEpl 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 -NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIV 256
Cdd:PRK11144 122 lDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVV 201
|
250 260 270
....*....|....*....|....*....|
gi 490250751 257 LDHGDVIARGAPQAIQANaSVIAAYLGAEE 286
Cdd:PRK11144 202 LEQGKVKAFGPLEEVWAS-SAMRPWLPKEE 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-273 |
1.46e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 9 EHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSivlrARekvtdviqVLGQKLHPDDFlh 88
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE----AW--------LFGQPVDAGDI-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 89 paQLGRRIYYkMfggthlvnraglartFQNIRLFREMSVIENLLvaqhtqvnrhllagiLNTRGYRQAESQALDRafywl 168
Cdd:NF033858 336 --ATRRRVGY-M---------------SQAFSLYGELTVRQNLE---------------LHARLFHLPAAEIAAR----- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 169 eVVEMV------DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEH 242
Cdd:NF033858 378 -VAEMLerfdlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 243 DMGMVmEISDHIIVLDHGDVIARGAPQAIQA 273
Cdd:NF033858 457 FMNEA-ERCDRISLMHAGRVLASDTPAALVA 486
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-266 |
1.99e-16 |
|
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: 76.54 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyRATGGSIVlrarekvTDVIQVLGQKLHPDDFLhpaqlgRRIYY 98
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTT-------SGQILFNGQPRKPDQFQ------KCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 kmfggthlvnraglarTFQNIRLFREMSVIENLlvaqhtqvnrHLLAGILNTRGYRQAESQALDrafywlEVVEMVDCAN 178
Cdd:cd03234 86 ----------------VRQDDILLPGLTVRETL----------TYTAILRLPRKSSDAIRKKRV------EDVLLRDLAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 179 -RLAGT----LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVetQALSrIIRFLRQ--QHGITVLLIEHDMGM-VMEI 250
Cdd:cd03234 134 tRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF--TALN-LVSTLSQlaRRNRIVILTIHQPRSdLFRL 210
|
250
....*....|....*.
gi 490250751 251 SDHIIVLDHGDVIARG 266
Cdd:cd03234 211 FDRILLLSSGEIVYSG 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-271 |
3.97e-16 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 75.48 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFY----RATGGSIVLRAREkvtdviqVLGQKLHpddflhpaqlGRRIYY 98
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLppglTQTSGEILLDGRP-------LLPLSIR----------GRHIAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 KMfggthlvnraglartfQNirlfrEMSVIENLLVAQHTQVNRHLLAGILntrgyrqaESQALDRAFYWLEVVEMVDCAN 178
Cdd:TIGR02770 67 IM----------------QN-----PRTAFNPLFTMGNHAIETLRSLGKL--------SKQARALILEALEAVGLPDPEE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 179 RL---AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHII 255
Cdd:TIGR02770 118 VLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVA 197
|
250
....*....|....*.
gi 490250751 256 VLDHGDVIARGAPQAI 271
Cdd:TIGR02770 198 VMDDGRIVERGTVKEI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-264 |
5.68e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLmmhfGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPD 84
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD------------GKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dflHPAQ-LGRRIYYkmfggthlV--NRAGLArtfqnirLFREMSVIENLLVAQHTQVNRHllaGILNtrgyRQAESQAL 161
Cdd:COG1129 320 ---SPRDaIRAGIAY--------VpeDRKGEG-------LVLDLSIRENITLASLDRLSRG---GLLD----RRRERALA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAFYWLEVVemVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVET-QALSRIIRFLRQQhGITVLLI 240
Cdd:COG1129 375 EEYIKRLRIK--TPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGAkAEIYRLIRELAAE-GKAVIVI 450
|
250 260
....*....|....*....|....
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIA 264
Cdd:COG1129 451 SSELPELLGLSDRILVMREGRIVG 474
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-271 |
9.95e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvtdviQVLGQkl 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA--------QPLES-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 hpddfLHPAQLGRRIYYkmfggthlvnraglartfqnirLFREMSVIENLLVAQHTQVNRHLLAGILNTrgYRQAESQAL 161
Cdd:PRK10575 78 -----WSSKAFARKVAY----------------------LPQQLPAAEGMTVRELVAIGRYPWHGALGR--FGAADREKV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 162 DRAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLN---PVETQALsriIRFLRQQHGITVL 238
Cdd:PRK10575 129 EEA---ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahQVDVLAL---VHRLSQERGLTVI 202
|
250 260 270
....*....|....*....|....*....|...
gi 490250751 239 LIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK10575 203 AVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-283 |
1.10e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHFggikalndvNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDViqvlgqk 80
Cdd:PRK10771 4 LTDITWLYHHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhPAQlgRRIyyKMFggthlvnraglartFQNIRLFREMSVIENLLVAQH-----TQVNRHLLAGIlntrgyrq 155
Cdd:PRK10771 68 --------PSR--RPV--SML--------------FQENNLFSHLTVAQNIGLGLNpglklNAAQREKLHAI-------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 156 AESQALDrafywlevvemvDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGI 235
Cdd:PRK10771 114 ARQMGIE------------DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQL 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490250751 236 TVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAYLG 283
Cdd:PRK10771 182 TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-262 |
1.15e-15 |
|
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: 73.02 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPddfLHPAQLGRRIYYKM 100
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD------------GADISQ---WDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnraglartfQNIRLFrEMSVIENLLvaqhtqvnrhllagilntrgyrqaesqaldrafywlevvemvdcanrl 180
Cdd:cd03246 83 ----------------QDDELF-SGSIAENIL------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 agtlSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGmVMEISDHIIVLDHG 260
Cdd:cd03246 98 ----SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPE-TLASADRILVLEDG 171
|
..
gi 490250751 261 DV 262
Cdd:cd03246 172 RV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-260 |
1.24e-15 |
|
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: 73.24 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLmmhfGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdviqvlgqklhPD 84
Cdd:cd03215 4 VLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK---------------PV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DFLHPAQLgrriyykmfggthlvNRAGLA-----RtfQNIRLFREMSVIENLLVAQHtqvnrhllagilntrgyrqaesq 159
Cdd:cd03215 65 TRRSPRDA---------------IRAGIAyvpedR--KREGLVLDLSVAENIALSSL----------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 aldrafywlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLL 239
Cdd:cd03215 105 ------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLL 159
|
250 260
....*....|....*....|.
gi 490250751 240 IEHDMGMVMEISDHIIVLDHG 260
Cdd:cd03215 160 ISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-262 |
1.36e-15 |
|
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: 74.04 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAR-------EKVTDVIQVLGQKlhpddflhPAqlg 93
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehKYLHSKVSLVGQE--------PV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 rriyykMFGGTHLVNRA-GLARTfqnirlfrEMSVIENLLVAQHTQVNRHLLAgilntrgyrqaesqaldrAFYWLEVVE 172
Cdd:cd03248 99 ------LFARSLQDNIAyGLQSC--------SFECVKEAAQKAHAHSFISELA------------------SGYDTEVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 173 MvdcanrlAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHDMGMVmEISD 252
Cdd:cd03248 147 K-------GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERAD 216
|
250
....*....|
gi 490250751 253 HIIVLDHGDV 262
Cdd:cd03248 217 QILVLDGGRI 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-266 |
1.36e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 73.35 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyratggsivLRAREKVTDVIQVLGQKLHPDDFlhpaqlGRRIYYKM 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG----------RRTGLGVSGEVLINGRPLDKRSF------RKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnraglartfQNIRLFREMSVIENLLVAqhtqvnrhllagiLNTRGyrqaesqaldrafywlevvemvdcanrl 180
Cdd:cd03213 89 ----------------QDDILHPTLTVRETLMFA-------------AKLRG---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 agtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDM-GMVMEISDHIIVLDH 259
Cdd:cd03213 112 ---LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQ 187
|
....*..
gi 490250751 260 GDVIARG 266
Cdd:cd03213 188 GRVIYFG 194
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-266 |
1.54e-15 |
|
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: 73.33 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGF--YRATGGSIVLRArEKVTDviqvlgqkLHP 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG-EDITD--------LPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 DDflhpaqlgrRIyykmfggthlvnRAGLARTFQNIRLFREMSVIENLlvaqhtqvnRHLLAGilntrgyrqaesqaldr 163
Cdd:cd03217 72 EE---------RA------------RLGIFLAFQYPPEIPGVKNADFL---------RYVNEG----------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 afywlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHd 243
Cdd:cd03217 105 --------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH- 162
|
250 260
....*....|....*....|....*...
gi 490250751 244 mgmVMEISDHII-----VLDHGDVIARG 266
Cdd:cd03217 163 ---YQRLLDYIKpdrvhVLYDGRIVKSG 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-266 |
1.79e-15 |
|
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: 73.72 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekVTDVIqvlgqklhpddflhpaqlgrr 95
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSSLL--------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 iyykmfggthlvnraGLARTFQNirlfrEMSVIENLlvaqhtqvnrHLLAGILntrGYRQAESQALDRAFYwlEVVEMVD 175
Cdd:cd03220 90 ---------------GLGGGFNP-----ELTGRENI----------YLNGRLL---GLSRKEIDEKIDEII--EFSELGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 CANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEP-AAGLNPVETQALSRIIRFLRQqhGITVLLIEHDMGMVMEISDHI 254
Cdd:cd03220 135 FIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVGDAAFQEKCQRRLRELLKQ--GKTVILVSHDPSSIKRLCDRA 212
|
250
....*....|..
gi 490250751 255 IVLDHGDVIARG 266
Cdd:cd03220 213 LVLEKGKIRFDG 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-276 |
1.82e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvTDVIQVLGQKLHPdd 85
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----VDIAKISDAELRE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmfggthlVNRAGLARTFQNIRLFREMSVIENLLVAQHtqvnrhlLAGIlntrgyrqAESQALDRAF 165
Cdd:PRK10070 103 ---------------------VRRKKIAMVFQSFALMPHMTVLDNTAFGME-------LAGI--------NAEERREKAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNP-VETQALSRIIRfLRQQHGITVLLIEHDM 244
Cdd:PRK10070 147 DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELVK-LQAKHQRTIVFISHDL 225
|
250 260 270
....*....|....*....|....*....|..
gi 490250751 245 GMVMEISDHIIVLDHGDVIARGAPQAIQANAS 276
Cdd:PRK10070 226 DEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-281 |
2.13e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqVLGQKLHPD 84
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVT----LNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DflhPAQLGRRiyykmfggthlvnRAGLARTFQNIRLFremSVIENLLVAQHTQVNRhllAGILNTRGyRQAESQALDRA 164
Cdd:PRK13547 77 D---APRLARL-------------RAVLPQAAQPAFAF---SAREIVLLGRYPHARR---AGALTHRD-GEIAWQALALA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 fywlevvEMVDCANRLAGTLSYGQQRRLEIARAMC---------TRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGI 235
Cdd:PRK13547 134 -------GATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490250751 236 TVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQANASVIAAY 281
Cdd:PRK13547 207 GVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-288 |
2.21e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGF--YRatgGSIvlrarekvtdviQVLGQKLHPddfLHPAQLgr 94
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSL------------KINGIELRE---LDPESW-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 95 riyykmfggthlvnRAGLARTFQNIRLFrEMSVIENLLVAQH----TQVNrhllagilntrgyrqaesQALDRAFYWlEV 170
Cdd:PRK11174 422 --------------RKHLSWVGQNPQLP-HGTLRDNVLLGNPdasdEQLQ------------------QALENAWVS-EF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 171 VEMVdcANRL-------AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHD 243
Cdd:PRK11174 468 LPLL--PQGLdtpigdqAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQ 543
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490250751 244 MGMVMEIsDHIIVLDHGDVIARGAPQAIQANASVIAAYLGAEEEE 288
Cdd:PRK11174 544 LEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-280 |
2.41e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtdVIQVLGQKLHPd 84
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG------------TLEIGGNPCAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 dfLHPA---QLGrrIYykmfggthLVNraglartfQNIRLFREMSVIENLLVA-QHTQVNRHLLAGILntrgyRQAESQa 160
Cdd:PRK15439 78 --LTPAkahQLG--IY--------LVP--------QEPLLFPNLSVKENILFGlPKRQASMQKMKQLL-----AALGCQ- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDrafywLEVvemvdcanrLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLI 240
Cdd:PRK15439 132 LD-----LDS---------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFI 196
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490250751 241 EHDMGMVMEISDHIIVLDHGdVIARGAPQAIQANASVIAA 280
Cdd:PRK15439 197 SHKLPEIRQLADRISVMRDG-TIALSGKTADLSTDDIIQA 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-286 |
2.97e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSIlRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDViqvlGQK 80
Cdd:PRK09544 1 MTSLV-SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYV----PQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 LHPDDFLhPAQLGRriyykmfggtHLVNRAGLARtfqnirlfremsviENLLVAQHTQVNRHLLagilntrgyrQAESQa 160
Cdd:PRK09544 76 LYLDTTL-PLTVNR----------FLRLRPGTKK--------------EDILPALKRVQAGHLI----------DAPMQ- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 ldrafywlevvemvdcanrlagTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:PRK09544 120 ----------------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMV 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490250751 241 EHDMGMVMEISDHIIVLDHgDVIARGAPQAIQANASVIA--AYLGAEE 286
Cdd:PRK09544 178 SHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPEFISmfGPRGAEQ 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-268 |
3.71e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRveHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrAREKVTDViqvlgqk 80
Cdd:PRK11000 1 MASVTLR--NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDV------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflHPAQlgrriyykmfggthlvnrAGLARTFQNIRLFREMSVIENLLVAQHtqvnrhlLAGILNTRGYRQAESQA 160
Cdd:PRK11000 71 -------PPAE------------------RGVGMVFQSYALYPHLSVAENMSFGLK-------LAGAKKEEINQRVNQVA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 ldrafywlEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNP-VETQALSRIIRfLRQQHGITVLL 239
Cdd:PRK11000 119 --------EVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAaLRVQMRIEISR-LHKRLGRTMIY 189
|
250 260
....*....|....*....|....*....
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDVIARGAP 268
Cdd:PRK11000 190 VTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-243 |
4.16e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHFGG----IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvL 77
Cdd:PRK10584 3 AENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 78 GQKLHPDDFLHPAQLgrriyykmfggthlvnRA-GLARTFQNIRLFREMSVIENLLvaqhtqvnrhlLAGILntRGyrQA 156
Cdd:PRK10584 71 GQPLHQMDEEARAKL----------------RAkHVGFVFQSFMLIPTLNALENVE-----------LPALL--RG--ES 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 157 ESQALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGIT 236
Cdd:PRK10584 120 SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTT 199
|
....*..
gi 490250751 237 VLLIEHD 243
Cdd:PRK10584 200 LILVTHD 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-273 |
1.10e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVLGQklhpddflhpaqlgrriyykm 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ--------------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fgGTHLVNR--AGLARTF-QNIRLFREMS---VIENLLVAQHTQVNRHLLAGIlNTRGYRQAEsqaldrafywlevvemv 174
Cdd:PRK10790 416 --GVAMVQQdpVVLADTFlANVTLGRDISeeqVWQALETVQLAELARSLPDGL-YTPLGEQGN----------------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 dcanrlagTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhgITVLLIEHDMGMVMEiSDHI 254
Cdd:PRK10790 476 --------NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTI 544
|
250
....*....|....*....
gi 490250751 255 IVLDHGDVIARGAPQAIQA 273
Cdd:PRK10790 545 LVLHRGQAVEQGTHQQLLA 563
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-238 |
1.49e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARE----KVTDVIQVLGQKl 81
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiddpDVAEACHYLGHR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 82 hpdDFLHPAqlgrriyykmfggthlvnraglartfqnirlfreMSVIENLLvaqhtqvnrhLLAGILNTRGYRQAESqal 161
Cdd:PRK13539 82 ---NAMKPA----------------------------------LTVAENLE----------FWAAFLGGEELDIAAA--- 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250751 162 drafywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCT-RPEMIcLDEPAAGLNpVETQAL-SRIIRFLRQQHGITVL 238
Cdd:PRK13539 112 ------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSnRPIWI-LDEPTAALD-AAAVALfAELIRAHLAQGGIVIA 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-269 |
1.54e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTgFYRATG----GSIVLRarekvtdviqvlgqklhpddflhpaqlGRRI 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLN---------------------------GMPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 97 YYKMFggthlvnRAGLARTFQNIRLFREMSVIENLLVAQHTQVNRHLlagilNTRGYRQAESQALDRafywlevVEMVDC 176
Cdd:TIGR00955 93 DAKEM-------RAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRV-----TKKEKRERVDEVLQA-------LGLRKC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 177 ANRLAGT------LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEI 250
Cdd:TIGR00955 154 ANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFEL 233
|
250
....*....|....*....
gi 490250751 251 SDHIIVLDHGDVIARGAPQ 269
Cdd:TIGR00955 234 FDKIILMAEGRVAYLGSPD 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-291 |
1.64e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.74 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPDDFLHPAQLGRRIY 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID------------DHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 YKmfGGTHLVNRAGLARTFQ-NIRLFREMSVIEnllvaQHTQVNRHL-LAGILNtrgyrqaesqalDRAFYWLEVvemvd 175
Cdd:PRK15112 94 QD--PSTSLNPRQRISQILDfPLRLNTDLEPEQ-----REKQIIETLrQVGLLP------------DHASYYPHM----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 canrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHII 255
Cdd:PRK15112 150 --------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVL 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250751 256 VLDHGDVIARGapqaiqANASVIAAYLgaeEEETRR 291
Cdd:PRK15112 222 VMHQGEVVERG------STADVLASPL---HELTKR 248
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-263 |
1.68e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 7 RVEHLMMHFG----GIK--ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlgqk 80
Cdd:COG2401 26 RVAIVLEAFGvelrVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhpaqlgrriyykmfggthlvnraglartFQNIRLFREMSVIENLLVAQHTqvnrHLLAGILNTRGyrqaesqa 160
Cdd:COG2401 91 -----------------------------------VPDNQFGREASLIDAIGRKGDF----KDAVELLNAVG-------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYWLevvemvdcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLI 240
Cdd:COG2401 124 LSDAVLWL----------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVA 193
|
250 260
....*....|....*....|....
gi 490250751 241 EHDMGMVMEIS-DHIIVLDHGDVI 263
Cdd:COG2401 194 THHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-266 |
1.93e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.46 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAgkttvfncltgfyratggsivlrAREKVTDVIQVLGqklhPDd 85
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA-----------------------A**RGALPAHV*G----PD- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqLGRRIYYKMfggTHLVNRAGLARTFQNIRLFR-----EMSVIENL-LVAQHTQVNRhllagilntrgyrqaeSQ 159
Cdd:NF000106 66 ------AGRRPWRF*---TWCANRRALRRTIG*HRPVR*grreSFSGRENLyMIGR*LDLSR----------------KD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLL 239
Cdd:NF000106 121 ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLL 199
|
250 260
....*....|....*....|....*..
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDVIARG 266
Cdd:NF000106 200 TTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-247 |
3.05e-14 |
|
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: 69.69 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqvlgQKLHPDD 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-------QRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHpaqlgrriyykmfggtHLVNRAGLARtfqnirlfrEMSVIENLlvaqhtqvnrHLLAGILntrgyrQAESQALDRAf 165
Cdd:TIGR01189 74 NIL----------------YLGHLPGLKP---------ELSALENL----------HFWAAIH------GGAQRTIEDA- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:TIGR01189 112 --LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLG 189
|
..
gi 490250751 246 MV 247
Cdd:TIGR01189 190 LV 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-268 |
4.07e-14 |
|
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: 72.74 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVlgqklhpddflhpaqlgrri 96
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-------------------- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 97 yykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVaqHTQVnrhllagilntRGYRQAESQALDRAFywLEVVEMVDC 176
Cdd:TIGR01257 1002 ------------RQSLGMCPQHNILFHHLTVAEHILF--YAQL-----------KGRSWEEAQLEMEAM--LEDTGLHHK 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 177 ANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIrfLRQQHGITVLLIEHDMGMVMEISDHIIV 256
Cdd:TIGR01257 1055 RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAI 1132
|
250
....*....|..
gi 490250751 257 LDHGDVIARGAP 268
Cdd:TIGR01257 1133 ISQGRLYCSGTP 1144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-266 |
5.91e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.59 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGQKLhpddflhpaqlgrriyyk 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-------DGHDLRDYTL------------------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 mfggTHLVNRAGLARtfQNIRLFREmSVIENLLVAQHTQvnrhllagilntrgYRQAESQALDRAFYWLEVVE-MVDCAN 178
Cdd:PRK11176 413 ----ASLRNQVALVS--QNVHLFND-TIANNIAYARTEQ--------------YSREQIEEAARMAYAMDFINkMDNGLD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 179 RLAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHgiTVLLIEHDMGMVmEISDHI 254
Cdd:PRK11176 472 TVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTI-EKADEI 548
|
250
....*....|..
gi 490250751 255 IVLDHGDVIARG 266
Cdd:PRK11176 549 LVVEDGEIVERG 560
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-274 |
8.70e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.01 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAR-------EKVTDVIQVLGQKLHpddflhpaq 91
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseAALRQAISVVSQRVH--------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 92 lgrriyykMFGGThlvnraglartfqnIRlfremsviENLLVAQHTQVNRHLLAgILNTRGYRQ--AESQALDRafyWLe 169
Cdd:PRK11160 425 --------LFSAT--------------LR--------DNLLLAAPNASDEALIE-VLQQVGLEKllEDDKGLNA---WL- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 170 vvemvdcanrlaG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvETQalSRIIRFLRqQH--GITVLLIEHD 243
Cdd:PRK11160 470 ------------GeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA-ETE--RQILELLA-EHaqNKTVLMITHR 533
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 244 MgMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK11160 534 L-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-280 |
1.32e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.91 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtDVIQVLGQKLHPddflHPAQLGRRIYykM 100
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV----PLVQYDHHYLHR----QVALVGQEPV--L 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 FGGTHLVNRA-GLARTfqnirlfrEMSVIENllVAQhtQVNRHLLAGILnTRGYRQaesqaldrafywlEVVEmvdcanr 179
Cdd:TIGR00958 567 FSGSVRENIAyGLTDT--------PDEEIMA--AAK--AANAHDFIMEF-PNGYDT-------------EVGE------- 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 lAGT-LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRiirfLRQQHGITVLLIEHDMGMVmEISDHIIVLD 258
Cdd:TIGR00958 614 -KGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTV-ERADQILVLK 687
|
250 260
....*....|....*....|..
gi 490250751 259 HGDVIARGAPQAIQANASVIAA 280
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-260 |
1.49e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHL-MMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdvIQVLGQKLHP 83
Cdd:PRK10908 1 MIRFEHVsKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD-----ITRLKNREVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddFLhpaqlgrriyykmfggthlvnRAGLARTFQNIRLFREMSVIENLLVAqhtqvnrhLLAGILNTRGYRQAESQALDR 163
Cdd:PRK10908 76 --FL---------------------RRQIGMIFQDHHLLMDRTVYDNVAIP--------LIIAGASGDDIRRRVSAALDK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 164 afywlevVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpvetQALSR-IIRFLRQ--QHGITVLLI 240
Cdd:PRK10908 125 -------VGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEgILRLFEEfnRVGVTVLMA 193
|
250 260
....*....|....*....|
gi 490250751 241 EHDMGMVMEISDHIIVLDHG 260
Cdd:PRK10908 194 THDIGLISRRSYRMLTLSDG 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-271 |
1.83e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIK-----------ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtdv 73
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE------------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 74 IQVLGQKLHpddflhpaQLGRRiyyKMfggthLVNRAGLARTFQ------NIRLFREMSVIENLLVAQhtqvnRHLLAGI 147
Cdd:PRK15134 342 IWFDGQPLH--------NLNRR---QL-----LPVRHRIQVVFQdpnsslNPRLNVLQIIEEGLRVHQ-----PTLSAAQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 148 LNTRGYRQAESQALDRAfywlevvemvdCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLN-PVETQALSrII 226
Cdd:PRK15134 401 REQQVIAVMEEVGLDPE-----------TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDkTVQAQILA-LL 468
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490250751 227 RFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK15134 469 KSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-260 |
1.96e-13 |
|
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: 66.32 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarekvtdviqvlgqKLHPdd 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------------TWGS-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlGRRIYYkmfggthlvnraglartfqnirlfremsvienllVAQhtqvnrhllagilntrgyrqaesqaldraf 165
Cdd:cd03221 62 -------TVKIGY----------------------------------FEQ------------------------------ 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPaagLNPVETQALSRIIRFLRQQHGiTVLLIEHDMG 245
Cdd:cd03221 71 ------------------LSGGEKMRLALAKLLLENPNLLLLDEP---TNHLDLESIEALEEALKEYPG-TVILVSHDRY 128
|
250
....*....|....*
gi 490250751 246 MVMEISDHIIVLDHG 260
Cdd:cd03221 129 FLDQVATKIIELEDG 143
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-263 |
4.89e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLhpddflhpAQLGRRiyykm 100
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR------------GEPL--------AKLNRA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvNRAGLARTFQNIrlFREMSVIENllvAQHT------QVNRHLLAgiLNTRGyRQAESQALdrafywLEVVEMV 174
Cdd:PRK10419 83 -------QRKAFRRDIQMV--FQDSISAVN---PRKTvreiirEPLRHLLS--LDKAE-RLARASEM------LRAVDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 D-CANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPV-ETQALsRIIRFLRQQHGITVLLIEHDMGMVMEISD 252
Cdd:PRK10419 142 DsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlQAGVI-RLLKKLQQQFGTACLFITHDLRLVERFCQ 220
|
250
....*....|.
gi 490250751 253 HIIVLDHGDVI 263
Cdd:PRK10419 221 RVMVMDNGQIV 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-266 |
2.80e-12 |
|
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: 64.81 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqvlgqklhpddfLHPAQLGRRIYYK 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL---------------ADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 MFGGThLVNRaglartfqnirlfremSVIENLLVAQHTQVNRHLLAgilntrgyrqAESQALDRAFywleVVEMVDCANR 179
Cdd:cd03252 82 LQENV-LFNR----------------SIRDNIALADPGMSMERVIE----------AAKLAGAHDF----ISELPEGYDT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRQ-QHGITVLLIEHDMGMVMEiSDHI 254
Cdd:cd03252 131 IVGeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL---DYESEHAIMRNMHDiCAGRTVIIIAHRLSTVKN-ADRI 206
|
250
....*....|..
gi 490250751 255 IVLDHGDVIARG 266
Cdd:cd03252 207 IVMEKGRIVEQG 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-266 |
5.77e-12 |
|
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: 63.10 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL------RAREKVTDVIQVLGQKLHpddflhpaql 92
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvpvsDLEKALSSLISVLNQRPY---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 93 grriyykMFGGThlvnraglartfqnirlfremsvienllvaqhtqvnrhllagILNTRGYRqaesqaldrafywlevve 172
Cdd:cd03247 86 -------LFDTT------------------------------------------LRNNLGRR------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 173 mvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPV-ETQALSRIIRFLRQQhgiTVLLIEHDMgMVMEIS 251
Cdd:cd03247 99 -----------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPItERQLLSLIFEVLKDK---TLIWITHHL-TGIEHM 163
|
250
....*....|....*
gi 490250751 252 DHIIVLDHGDVIARG 266
Cdd:cd03247 164 DKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-268 |
7.04e-12 |
|
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: 63.79 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 14 HFG---GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDVIQvlgqklhpddflhpA 90
Cdd:cd03253 7 TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD-IREVTL--------------D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 91 QLGRRIyykmfgG-----THLVNraglARTFQNIRLFR----EMSVIENLLVAQHTQVnrhllagILNTR-GYrqaESQA 160
Cdd:cd03253 72 SLRRAI------GvvpqdTVLFN----DTIGYNIRYGRpdatDEEVIEAAKAAQIHDK-------IMRFPdGY---DTIV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 161 LDRAFYwlevvemvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQqhGITVLLI 240
Cdd:cd03253 132 GERGLK-----------------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVI 192
|
250 260
....*....|....*....|....*...
gi 490250751 241 EHDMGMVMEiSDHIIVLDHGDVIARGAP 268
Cdd:cd03253 193 AHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-291 |
7.35e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyratggsivlrAREKVTDVIQVLGQKLhpD 84
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG------------ARKIQQGRVEVLGGDM--A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DFLHPAQLGRRIYYkMfggthlvnRAGLARtfqNirLFREMSVIENL-----LVAQhtqvnrhllagilnTRGYRQAESQ 159
Cdd:NF033858 67 DARHRRAVCPRIAY-M--------PQGLGK---N--LYPTLSVFENLdffgrLFGQ--------------DAAERRRRID 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRA-----FywlevvemvdcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvetqaLSR-----IIRFL 229
Cdd:NF033858 119 ELLRAtglapF-----------ADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP-----LSRrqfweLIDRI 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250751 230 RQQH-GITVLliehdmgmV----MEIS---DHIIVLDHGDVIARGAPQAIQAN---ASVIAAYLGAEEEETRR 291
Cdd:NF033858 183 RAERpGMSVL--------VatayMEEAerfDWLVAMDAGRVLATGTPAELLARtgaDTLEAAFIALLPEEKRR 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-244 |
1.07e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.42 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFGGIK--ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVlgqklh 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV------ 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 83 pddflhpaqlgrriyykmfggthlvnraglartFQNIRLFREMSVIENLLVAQHtqvnrHLLagiLNTRgYRQAESQALD 162
Cdd:TIGR01257 2011 ---------------------------------HQNMGYCPQFDAIDDLLTGRE-----HLY---LYAR-LRGVPAEEIE 2048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYW-LEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQAL-SRIIRFLRQqhGITVLLI 240
Cdd:TIGR01257 2049 KVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIRE--GRAVVLT 2126
|
....
gi 490250751 241 EHDM 244
Cdd:TIGR01257 2127 SHSM 2130
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
178-287 |
1.11e-11 |
|
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: 65.03 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPE--MICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMvMEISDHII 255
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHDEDT-IRAADYVI 560
|
90 100 110
....*....|....*....|....*....|....*....
gi 490250751 256 VL-----DH-GDVIARGAPQAIQAN-ASVIAAYLGAEEE 287
Cdd:TIGR00630 561 DIgpgagEHgGEVVASGTPEEILANpDSLTGQYLSGRKK 599
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
178-285 |
1.22e-11 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 65.24 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPEMIC--LDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVmEISDHII 255
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMI-SLADRII 548
|
90 100 110
....*....|....*....|....*....|....*..
gi 490250751 256 VLD------HGDVIARGAPQAIQANA-SVIAAYLGAE 285
Cdd:PRK00635 549 DIGpgagifGGEVLFNGSPREFLAKSdSLTAKYLRQE 585
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-260 |
1.30e-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: 62.26 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyRATGGSIvlrarekvTDVIQVLGQKLhPDDFLhpaqlgRRIYYKM 100
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--------TGEILINGRPL-DKNFQ------RSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnraglartfQNIRLFREMSVIENLLVAqhtqvnrhllagilntrgyrqaesqALDRAfywlevvemvdcanrl 180
Cdd:cd03232 86 ----------------QQDVHSPNLTVREALRFS-------------------------ALLRG---------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 agtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRQ--QHGITVLL-IEHDMGMVMEISDHIIVL 257
Cdd:cd03232 109 ---LSVEQRKRLTIGVELAAKPSILFLDEPTSGL---DSQAAYNIVRFLKKlaDSGQAILCtIHQPSASIFEKFDRLLLL 182
|
...
gi 490250751 258 DHG 260
Cdd:cd03232 183 KRG 185
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-274 |
1.84e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHFG-------------GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvt 71
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 72 dviqvLGQKLhpddflhpaqlgrriyYKMFGGTHLVNRAGLARTFQN--IRLFREMSVIEnllvaqhtqvnrhLLAGILN 149
Cdd:PRK15079 81 -----LGKDL----------------LGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGE-------------IIAEPLR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 150 TRGYRQAESQALDRafywleVVEMV-------DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQAl 222
Cdd:PRK15079 127 TYHPKLSRQEVKDR------VKAMMlkvgllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD-VSIQA- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490250751 223 sRIIRFLRQ---QHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK15079 199 -QVVNLLQQlqrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-274 |
1.98e-11 |
|
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: 62.56 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHpddFLHPAQLGRRI 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD------------GVDIR---DLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 97 YY-----KMFGGTHLvnraglartfQNIRLFREmSVIENLLVAQHTQVNRH-LLAGILNtrGYrqaESQALDRAFywlev 170
Cdd:cd03249 80 GLvsqepVLFDGTIA----------ENIRYGKP-DATDEEVEEAAKKANIHdFIMSLPD--GY---DTLVGERGS----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 171 vemvdcanrlagTLSYGQQRRLEIARAMCTRPEMICLDEPAAGL-NPVETQ---ALSRIIRflrqqhGITVLLIEHDMGM 246
Cdd:cd03249 139 ------------QLSGGQKQRIAIARALLRNPKILLLDEATSALdAESEKLvqeALDRAMK------GRTTIVIAHRLST 200
|
250 260
....*....|....*....|....*...
gi 490250751 247 VMEiSDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:cd03249 201 IRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-247 |
2.57e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRARekvtdviqvlgqklhPDD 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---------------PLD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 FLHPAqLGRRIYYkmfggthLVNRAGLARTfqnirlfreMSVIENLlvaqhtqvnrHLLAGILNTRGYRQAESQALDRAF 165
Cdd:cd03231 66 FQRDS-IARGLLY-------LGHAPGIKTT---------LSVLENL----------RFWHADHSDEQVEEALARVGLNGF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 ywlevvemvdcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:cd03231 119 -----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLG 187
|
..
gi 490250751 246 MV 247
Cdd:cd03231 188 LS 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-243 |
2.61e-11 |
|
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: 63.53 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHF-GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtdviqvlgqklhpd 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL-------------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DFLHPAQLgrriyykmfGGTHLVNRAGLarTFQNIRLFrEMSVIENLLVAQHTQVNRHLLAgilntrgyrqaesqALDRA 164
Cdd:TIGR02868 395 DGVPVSSL---------DQDEVRRRVSV--CAQDAHLF-DTTVRENLRLARPDATDEELWA--------------ALERV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 FY--WLEvvEMVDCANRLAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvetQALSRIIRFLRQ-QHGITV 237
Cdd:TIGR02868 449 GLadWLR--ALPDGLDTVLGeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDA---ETADELLEDLLAaLSGRTV 523
|
....*.
gi 490250751 238 LLIEHD 243
Cdd:TIGR02868 524 VLITHH 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-271 |
2.71e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI-----VLRAREKvtD 72
Cdd:PRK10261 9 ARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSR--Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 73 VIQVLGQKlhpddflhPAQLGRriyykmfggthlVNRAGLARTFQnirlfREMSVIENLL-VAQHTQVNRHLLAGILNTR 151
Cdd:PRK10261 87 VIELSEQS--------AAQMRH------------VRGADMAMIFQ-----EPMTSLNPVFtVGEQIAESIRLHQGASREE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 152 GYRQAEsqaldRAFYWLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQA-LSRIIRFLR 230
Cdd:PRK10261 142 AMVEAK-----RMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD-VTIQAqILQLIKVLQ 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490250751 231 QQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK10261 216 KEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-280 |
3.43e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqvlgqkLHPDDFlhpAQLgRRIY 97
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT---------LDADAL---AQL-RREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 YKMFggthlvnraglartFQNIRLFREMSVIENLLVAQhtqvnrhLLAGIlnTRGYRQAESQALdrafywLEVVEMVDCA 177
Cdd:PRK10535 88 FGFI--------------FQRYHLLSHLTAAQNVEVPA-------VYAGL--ERKQRLLRAQEL------LQRLGLEDRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGM------VMEIS 251
Cdd:PRK10535 139 EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVaaqaerVIEIR 217
|
250 260
....*....|....*....|....*....
gi 490250751 252 DHIIVLDHGdviARGAPQAIQANASVIAA 280
Cdd:PRK10535 218 DGEIVRNPP---AQEKVNVAGGTEPVVNT 243
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-260 |
4.32e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyRATGGSIVlrarekvtdviqvlgqklhpddflhpaqlgrriyykm 100
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVIT------------------------------------- 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fGGTHLVNRAGLARTFQNIRLFREMSVI--ENLLVAQHTQVNRHLlagilntrgyRQAES----QALDRAFYWLEVVEMV 174
Cdd:TIGR00956 820 -GGDRLVNGRPLDSSFQRSIGYVQQQDLhlPTSTVRESLRFSAYL----------RQPKSvsksEKMEYVEEVIKLLEME 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 DCANRLAGT----LSYGQQRRLEIARAMCTRPEMIC-LDEPAAGLnpvETQALSRIIRFLRQ--QHGITVL-LIEHDMGM 246
Cdd:TIGR00956 889 SYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL---DSQTAWSICKLMRKlaDHGQAILcTIHQPSAI 965
|
250
....*....|....
gi 490250751 247 VMEISDHIIVLDHG 260
Cdd:TIGR00956 966 LFEEFDRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-239 |
4.97e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyratggsivlrarekvtDviqvlgqklHPDDFLHPAQLgrriyykm 100
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------------D---------HPQGYSNDLTL-------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 FGgthlvNRAGLARTFQNIRlfREMSVIENLLvaqH------TQVNRHLLAGILNTRGYRQAESQALDR-AFYWLEVVEM 173
Cdd:PRK10938 321 FG-----RRRGSGETIWDIK--KHIGYVSSSL---HldyrvsTSVRNVILSGFFDSIGIYQAVSDRQQKlAQQWLDILGI 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 vdcANRLAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLL 239
Cdd:PRK10938 391 ---DKRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISE-GETQLL 456
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-268 |
6.29e-11 |
|
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: 60.97 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL-----------RAREKVTDVIQvlgqklhpDDFLh 88
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdiskiglhDLRSRISIIPQ--------DPVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 89 paqlgrriyykmFGGThlvnraglARtfQNIRLFREMSVIENLLVAQHTQVNRHL--LAGILNTRgyrqaesqaldrafy 166
Cdd:cd03244 90 ------------FSGT--------IR--SNLDPFGEYSDEELWQALERVGLKEFVesLPGGLDTV--------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 167 wlevVEMVDCanrlagTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRflRQQHGITVLLIEHDMGM 246
Cdd:cd03244 133 ----VEEGGE------NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDT 200
|
250 260
....*....|....*....|..
gi 490250751 247 VMEiSDHIIVLDHGDVIARGAP 268
Cdd:cd03244 201 IID-SDRILVLDKGRVVEFDSP 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-244 |
6.32e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.98 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPDDFLHPAQLGRRiyykm 100
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN------------GQPMSKLSSAAKAELRNQ----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnraGLARTFQNIRLFREMSVIENllvaqhtqVNRHLLAGilntrgyRQAESQALDRAFYWLEVVEMVDCANRL 180
Cdd:PRK11629 88 ----------KLGFIYQFHHLLPDFTALEN--------VAMPLLIG-------KKKPAEINSRALEMLAAVGLEHRANHR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250751 181 AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDM 244
Cdd:PRK11629 143 PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-260 |
7.66e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDviqvlgqklHPDDFLhpaqlgrriyykm 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR---------SPQDGL------------- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnRAGLARTFQNIR---LFREMSVIENLLVAQHTQVNRhlLAGILNtrgyRQAESQALD---RAFYwLEVVEMv 174
Cdd:PRK10762 326 --------ANGIVYISEDRKrdgLVLGMSVKENMSLTALRYFSR--AGGSLK----HADEQQAVSdfiRLFN-IKTPSM- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 dcaNRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGlnpVETQALSRIIRFLRQ--QHGITVLLIEHDMGMVMEISD 252
Cdd:PRK10762 390 ---EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG---VDVGAKKEIYQLINQfkAEGLSIILVSSEMPEVLGMSD 463
|
....*...
gi 490250751 253 HIIVLDHG 260
Cdd:PRK10762 464 RILVMHEG 471
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-258 |
8.60e-11 |
|
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: 60.88 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSIT-----ALIGPNGAGKTTVFNCLTGFYRATGGSIvlrarEKVTDVIQVLGQKLHPDdflhpaqlg 93
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTVSYKPQYIKAD--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 rriyykmfggthlvnraglartfqnirlfREMSVienllvaqhtqvnRHLLAGILNTRGyrqaesqalDRAFYWLEVV-- 171
Cdd:cd03237 74 -----------------------------YEGTV-------------RDLLSSITKDFY---------THPYFKTEIAkp 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 172 -EMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEI 250
Cdd:cd03237 103 lQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYL 182
|
....*...
gi 490250751 251 SDHIIVLD 258
Cdd:cd03237 183 ADRLIVFE 190
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-271 |
9.03e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.62 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGgsivlrarekvtdVIQVLGQKLhpdDFLHPAQLGRRiyykm 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQG-------------EILLNGRPL---SDWSAAELARH----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 fggthlvnRAGLArtfQNIRLFREMSVIENLLVAQHtqvnrhllagilntrgyRQAESQALDRAFYWL-EVVEMVDCANR 179
Cdd:COG4138 71 --------RAYLS---QQQSPPFAMPVFQYLALHQP-----------------AGASSEAVEQLLAQLaEALGLEDKLSR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAGTLSYGQQRRLEIArAMC------TRPE--MICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEIS 251
Cdd:COG4138 123 PLTQLSGGEWQRVRLA-AVLlqvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHA 200
|
250 260
....*....|....*....|
gi 490250751 252 DHIIVLDHGDVIARGAPQAI 271
Cdd:COG4138 201 DRVWLLKQGKLVASGETAEV 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-271 |
1.08e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.30 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 4 SILRVEHLMMHFGG----IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGgsivlrarekvtdviQVLGQ 79
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPG---------------RVMAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 80 KLHPD--DFLHPAQLGRRiyyKMFGgthlvnrAGLARTFQ------NIRLFREMSVIENLLVAQHtqvnrhllagilntr 151
Cdd:PRK11022 67 KLEFNgqDLQRISEKERR---NLVG-------AEVAMIFQdpmtslNPCYTVGFQIMEAIKVHQG--------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 152 GYRQAESQaldRAFYWLEVVEMVDCANRL---AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQAlsRIIRF 228
Cdd:PRK11022 122 GNKKTRRQ---RAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD-VTIQA--QIIEL 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490250751 229 L---RQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK11022 196 LlelQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-266 |
1.14e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrarekvtDVIQVLGqklhpddflhpaqlgrriyyk 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-------DGTDIRT--------------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 mfggthlVNRAGLART----FQNIRLFREmSVIENLLVAQHTQVNRHLLAgilntrgyrqaesqALDRAFYWLEVVEMVD 175
Cdd:PRK13657 402 -------VTRASLRRNiavvFQDAGLFNR-SIEDNIRVGRPDATDEEMRA--------------AAERAQAHDFIERKPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 176 CANRLAG----TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQA-LSRIIRFLRqqHGITVLLIEHDMGMVMEi 250
Cdd:PRK13657 460 GYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALD-VETEAkVKAALDELM--KGRTTFIIAHRLSTVRN- 535
|
250
....*....|....*.
gi 490250751 251 SDHIIVLDHGDVIARG 266
Cdd:PRK13657 536 ADRILVFDNGRVVESG 551
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-269 |
1.52e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 24 VNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGsivlrarekvtdvIQVLGQKLhpdDFLHPAQLGRRiyykmfgg 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGS-------------IQFAGQPL---EAWSAAELARH-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 104 thlvnRAGLArtfQNIRLFREMSVIENLLVAQHTQVNRHLLAGILNtrgyrqaesqaldrafywlEVVEMV---DCANRL 180
Cdd:PRK03695 71 -----RAYLS---QQQTPPFAMPVFQYLTLHQPDKTRTEAVASALN-------------------EVAEALgldDKLGRS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 AGTLSYGQQRR-------LEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDH 253
Cdd:PRK03695 124 VNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADR 202
|
250
....*....|....*.
gi 490250751 254 IIVLDHGDVIARGAPQ 269
Cdd:PRK03695 203 VWLLKQGKLLASGRRD 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-264 |
1.54e-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: 61.38 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF---GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYR-ATGGSIVLRArekvtdviqvlg 78
Cdd:TIGR02633 255 DVILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING------------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 qklHPDDFLHPAQlgrriyykmfggthlVNRAGLA-----RTFQNIrlFREMSVIENLLVAQhtqVNRHLLAGILNTrgy 153
Cdd:TIGR02633 323 ---KPVDIRNPAQ---------------AIRAGIAmvpedRKRHGI--VPILGVGKNITLSV---LKSFCFKMRIDA--- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 rQAESQALDRAFYWLEVveMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQh 233
Cdd:TIGR02633 377 -AAELQIIGSAIQRLKV--KTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE- 452
|
250 260 270
....*....|....*....|....*....|.
gi 490250751 234 GITVLLIEHDMGMVMEISDHIIVLDHGDVIA 264
Cdd:TIGR02633 453 GVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-243 |
2.33e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMMHFGGIK-ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPD 84
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD------------GKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 85 DflhpaqlgRRIYYKMFggthlvnraglARTFQNIRLFREMsvienllvaqhtqvnrhllagiLNTRGYrQAESQALDRa 164
Cdd:PRK10522 391 Q--------PEDYRKLF-----------SAVFTDFHLFDQL----------------------LGPEGK-PANPALVEK- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 165 fyWLEVVEMVD----CANRLAGT-LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLL 239
Cdd:PRK10522 428 --WLERLKMAHklelEDGRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFA 505
|
....
gi 490250751 240 IEHD 243
Cdd:PRK10522 506 ISHD 509
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-283 |
4.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.23 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHLMMHF-GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRArekvtdviqvlgqkLHP 83
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--------------IDT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 DDFlhpaqlgrriyYKMFGGTHLVnraGLarTFQNIRL-FREMSVIENLLVAQHtqvnrHLLAGILNTRgyrqaesQALD 162
Cdd:PRK13644 67 GDF-----------SKLQGIRKLV---GI--VFQNPETqFVGRTVEEDLAFGPE-----NLCLPPIEIR-------KRVD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAfywLEVVEMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEH 242
Cdd:PRK13644 119 RA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITH 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490250751 243 DMGMvMEISDHIIVLDHGDVIARGAPQAIQANASViaAYLG 283
Cdd:PRK13644 195 NLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL--QTLG 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-258 |
4.22e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSI-----TALIGPNGAGKTTVFNCLTGFYRATGGSIvlraREKVtdviqvlgqklhpddflhpaqlg 93
Cdd:COG1245 349 KSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV----DEDL----------------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 rRIYYKMfggthlvnraglartfQNIRLFREMSVIENLlvaqhtqvnrhllagilntrgyRQAESQALDRAFYWLEVVE- 172
Cdd:COG1245 402 -KISYKP----------------QYISPDYDGTVEEFL----------------------RSANTDDFGSSYYKTEIIKp 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 173 -----MVDcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQ-ALSRIIRFLRQQHGITVLLIEHDMGM 246
Cdd:COG1245 443 lglekLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRlAVAKAIRRFAENRGKTAMVVDHDIYL 518
|
250
....*....|..
gi 490250751 247 VMEISDHIIVLD 258
Cdd:COG1245 519 IDYISDRLMVFE 530
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
178-260 |
4.42e-10 |
|
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: 57.72 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPE--MICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMvMEISDHII 255
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDV-LSSADWII 159
|
....*
gi 490250751 256 VLDHG 260
Cdd:cd03238 160 DFGPG 164
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-271 |
4.71e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHF--GGI--KALNDVNLEVERGSITALIGPNGAGKTTvfncltgfyraTGGSiVLRArekvtdviqv 76
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSV-----------TALS-ILRL---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 77 lgqkLHPDDFLHPAQLGRriyykmFGGTHLVNRAglARTFQNIR------LFREMSVIENLLvaqHTqVNRHLLAGILNT 150
Cdd:PRK15134 59 ----LPSPPVVYPSGDIR------FHGESLLHAS--EQTLRGVRgnkiamIFQEPMVSLNPL---HT-LEKQLYEVLSLH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 151 RGYRQ--AESQALDrafyWLEVVEMVDCANRLAG---TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLN-PVETQALSr 224
Cdd:PRK15134 123 RGMRReaARGEILN----CLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQ- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490250751 225 IIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK15134 198 LLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-274 |
6.70e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQklhpdDFLHP-----AQL 92
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQ------------GQ-----DLLKAdpeaqKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 93 GRRIyykmfggtHLVnraglartFQNirlfremsvienllvaQHTQVN-RHLLAGIL------NTrgyrqaESQALDRAF 165
Cdd:PRK11308 91 RQKI--------QIV--------FQN----------------PYGSLNpRKKVGQILeeplliNT------SLSAAERRE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 166 YWLEVVEMV----DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLN-PVETQALSRIIRfLRQQHGITVLLI 240
Cdd:PRK11308 133 KALAMMAKVglrpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVLNLMMD-LQQELGLSYVFI 211
|
250 260 270
....*....|....*....|....*....|....
gi 490250751 241 EHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK11308 212 SHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-258 |
2.16e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLH--PDDFLH-PAQLGrriyyk 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ------------GEPIRrqRDEYHQdLLYLG------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 100 mfggtHLvnrAGLARtfqnirlfrEMSVIENLLVAQHtqvnrhlLAGILNtrgyRQAESQALDRAfyWLEVVEMVdcanr 179
Cdd:PRK13538 81 -----HQ---PGIKT---------ELTALENLRFYQR-------LHGPGD----DEALWEALAQV--GLAGFEDV----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAGTLSYGQQRRLEIARAMCTRPEMICLDEPaagLNPVETQALSRIIRFLRQ---QHGITVLLIEHDMGMvmeISDHIIV 256
Cdd:PRK13538 126 PVRQLSAGQQRRVALARLWLTRAPLWILDEP---FTAIDKQGVARLEALLAQhaeQGGMVILTTHQDLPV---ASDKVRK 199
|
..
gi 490250751 257 LD 258
Cdd:PRK13538 200 LR 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-260 |
2.23e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 5 ILRVEHL-MMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDviqvlgqklhp 83
Cdd:COG3845 257 VLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED-ITG----------- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 84 ddfLHPAQlgRRiyykmfggthlvnRAGLARtfqnI---RLFR----EMSVIENLLVAQHTQ--VNRHllaGILNtRGYR 154
Cdd:COG3845 325 ---LSPRE--RR-------------RLGVAY----IpedRLGRglvpDMSVAENLILGRYRRppFSRG---GFLD-RKAI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 155 QAESQALDRAFywlEVVemVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhG 234
Cdd:COG3845 379 RAFAEELIEEF---DVR--TPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-G 452
|
250 260
....*....|....*....|....*.
gi 490250751 235 ITVLLIEHDMGMVMEISDHIIVLDHG 260
Cdd:COG3845 453 AAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
178-266 |
3.54e-09 |
|
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: 55.73 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQQRRLEIARAMCTRPEMIC--LDEPAAGLNPVETQALSRIIRFLRqQHGITVLLIEHDMGMvMEISDHII 255
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDEDT-IRAADHVI 209
|
90
....*....|....*..
gi 490250751 256 VL-----DH-GDVIARG 266
Cdd:cd03270 210 DIgpgagVHgGEIVAQG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-262 |
3.62e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 19 KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPddflhpaqlgRRIYY 98
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN------------GKDISP----------RSPLD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 KMFGGTHLV--NRaglartfqnirlfREMSVIENLLVAQHTQVNRHL-------LAGILNTRGYRQ-AESQALDRAfywl 168
Cdd:PRK09700 335 AVKKGMAYIteSR-------------RDNGFFPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQRtAENQRELLA---- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 169 evvemVDCA--NRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGlnpVETQALSRIIRFLRQ--QHGITVLLIEHDM 244
Cdd:PRK09700 398 -----LKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG---IDVGAKAEIYKVMRQlaDDGKVILMVSSEL 469
|
250
....*....|....*...
gi 490250751 245 GMVMEISDHIIVLDHGDV 262
Cdd:PRK09700 470 PEIITVCDRIAVFCEGRL 487
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
184-257 |
6.80e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 6.80e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVeTQAlsRIIRFL---RQQHGITVLLIEHDMGMVMEISDHIIVL 257
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMEST-TQA--QIFRLLarlNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-258 |
7.09e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 18 IKALNDVNLEVE-----RGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVlrarekvTDViqvlgqklhpddflhpaql 92
Cdd:PRK13409 347 TKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-------PEL------------------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 93 grRIYYKMfggthlvnraglartfQNIRLFREMSVienllvaqhtqvnRHLLAGIlntrgyrqaeSQALDRAFYWLEVVE 172
Cdd:PRK13409 401 --KISYKP----------------QYIKPDYDGTV-------------EDLLRSI----------TDDLGSSYYKSEIIK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 173 ------MVDcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQ-ALSRIIRFLRQQHGITVLLIEHDMG 245
Cdd:PRK13409 440 plqlerLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRlAVAKAIRRIAEEREATALVVDHDIY 515
|
250
....*....|...
gi 490250751 246 MVMEISDHIIVLD 258
Cdd:PRK13409 516 MIDYISDRLMVFE 528
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
184-268 |
8.36e-09 |
|
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: 54.34 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRflRQQHGITVLLIEHDMGMVMEIsDHIIVLDHGDVI 263
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
....*
gi 490250751 264 ARGAP 268
Cdd:cd03369 203 EYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-269 |
8.50e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF---GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYR-ATGGSIVLRarekvtdviqvlG 78
Cdd:PRK13549 257 EVILEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFID------------G 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 79 QKLhpdDFLHPAQlgrriyykmfggthlVNRAGLA-----RTFQNIRLfrEMSVIENLLVAQHTQVNRHllaGILNTrgy 153
Cdd:PRK13549 325 KPV---KIRNPQQ---------------AIAQGIAmvpedRKRDGIVP--VMGVGKNITLAALDRFTGG---SRIDD--- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 rQAESQALDRAFYWLEVvemvDCAN-RLA-GTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQ 231
Cdd:PRK13549 379 -AAELKTILESIQRLKV----KTASpELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490250751 232 QhGITVLLIEHDMGMVMEISDHIIVLDHG----DVIARGAPQ 269
Cdd:PRK13549 454 Q-GVAIIVISSELPEVLGLSDRVLVMHEGklkgDLINHNLTQ 494
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-261 |
1.05e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVI----------QVLGQKlHPDDFLHPAQL 92
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTneqdyqgdeeQNVGMK-NVNEFSLTKEG 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 93 GRRIYYKMFGGTHLVNRAGLARTFQNIRLFREMSVIenllVAQHTQV-NRHLLAGIlnTRGYRQAESQALDRAFYWLEVV 171
Cdd:PTZ00265 1265 GSGEDSTVFKNSGKILLDGVDICDYNLKDLRNLFSI----VSQEPMLfNMSIYENI--KFGKEDATREDVKRACKFAAID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 172 EMVDC-ANRL-------AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHD 243
Cdd:PTZ00265 1339 EFIESlPNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1418
|
250
....*....|....*...
gi 490250751 244 MGMVMEiSDHIIVLDHGD 261
Cdd:PTZ00265 1419 IASIKR-SDKIVVFNNPD 1435
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-266 |
1.08e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKT----TVFNCLTGFYRATGGSIVLRAREkvtdviqvlgqklhpddfLHPAQL-GRRIy 97
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKP------------------VAPCALrGRKI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 98 ykmfggthlvnraglARTFQNIRL----FREMS--VIENLLVAQHTQVNRHLLAgilntrgyrqaesqALDRAfyWLEVV 171
Cdd:PRK10418 82 ---------------ATIMQNPRSafnpLHTMHthARETCLALGKPADDATLTA--------------ALEAV--GLENA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 172 EMVdcANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVeTQAlsRIIRFLR---QQHGITVLLIEHDMGMVM 248
Cdd:PRK10418 131 ARV--LKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV-AQA--RILDLLEsivQKRALGMLLVTHDMGVVA 205
|
250
....*....|....*...
gi 490250751 249 EISDHIIVLDHGDVIARG 266
Cdd:PRK10418 206 RLADDVAVMSHGRIVEQG 223
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
178-291 |
2.19e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 55.03 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 NRLAGTLSYGQ-QR-RLeiARAmctrpemI---------CLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGM 246
Cdd:COG0178 480 DRSAGTLSGGEaQRiRL--ATQ-------IgsglvgvlyVLDEPSIGLHQRDNDRLIETLKRLRDL-GNTVIVVEHDEDT 549
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250751 247 vMEISDHIIvlD-------H-GDVIARGAPQAIQAN-ASVIAAYLGAEEE----ETRR 291
Cdd:COG0178 550 -IRAADYII--DigpgageHgGEVVAQGTPEEILKNpDSLTGQYLSGRKRipvpKKRR 604
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-260 |
2.90e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATG--GSIVLRAREKVTDVIQVLGqKLHPDDFLHPaqlgrriyy 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTG-FVTQDDILYP--------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 99 kmfggtHLVNRAGLarTFQN-IRLFREMSVIENLLVAQhtqvnrhllaGILNTRGYRQAESQALDRAFywlevvemvdca 177
Cdd:PLN03211 154 ------HLTVRETL--VFCSlLRLPKSLTKQEKILVAE----------SVISELGLTKCENTIIGNSF------------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 178 nrLAGtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVL 257
Cdd:PLN03211 204 --IRG-ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVL 280
|
...
gi 490250751 258 DHG 260
Cdd:PLN03211 281 SEG 283
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-64 |
3.11e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 3.11e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250751 3 DSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL 64
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-271 |
3.76e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 1 MTDSILRVEHLMMHF----GGIKALNDVNLEVERGSITALIGPNGAGKT-TVFnCLTGFYRATG---GSIVLRAREKVTd 72
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 73 viqvlgqklhpddfLHPAQLGRRiyykmfggthlvnRA-GLARTFQN--IRLFREMSVIENLL--VAQHTQVNRhllagi 147
Cdd:PRK09473 86 --------------LPEKELNKL-------------RAeQISMIFQDpmTSLNPYMRVGEQLMevLMLHKGMSK------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 148 lntrgyrqaeSQALDRAFYWLEVVEMVDCANRLA---GTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQA-LS 223
Cdd:PRK09473 133 ----------AEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD-VTVQAqIM 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490250751 224 RIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAI 271
Cdd:PRK09473 202 TLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-65 |
3.90e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 3.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250751 1 MTDSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGF--YRATGGSIVLR 65
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFK 69
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-226 |
5.49e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 35 ALI--GPNGAGKTTVFNCLTGFYRATGGSIVLRArekvtdviqvlgqklhpddflHPAQLGRRIYYKMFGGtHLVNragl 112
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDG---------------------KTATRGDRSRFMAYLG-HLPG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 113 artfqnirLFREMSVIENLlvaqhtqvnrHLLAGiLNTRGYRQAESQALdrafywlEVVEMVDCANRLAGTLSYGQQRRL 192
Cdd:PRK13543 93 --------LKADLSTLENL----------HFLCG-LHGRRAKQMPGSAL-------AIVGLAGYEDTLVRQLSAGQKKRL 146
|
170 180 190
....*....|....*....|....*....|....
gi 490250751 193 EIARAMCTRPEMICLDEPAAGLNPVETQALSRII 226
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-243 |
9.06e-08 |
|
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: 51.45 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 33 ITALIGPNGAGKTTVFNCLtgFYRATG-GSIVLRAREKVTDVIQ---VLGQ-KLHpddFLHPAqlgrriyykmfGGTHLV 107
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAL--KYALTGeLPPNSKGGAHDPKLIRegeVRAQvKLA---FENAN-----------GKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 108 NRaglartfqnirlfrEMSVIENLLVAqhtqvnrhllagilntrgyRQAESQALdrafywleVVEMVdcanrlaGTLSYG 187
Cdd:cd03240 88 TR--------------SLAILENVIFC-------------------HQGESNWP--------LLDMR-------GRCSGG 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250751 188 QQR------RLEIARAMCTRPEMICLDEPAAGLNP--VEtQALSRIIRFLRQQHGITVLLIEHD 243
Cdd:cd03240 120 EKVlasliiRLALAETFGSNCGILALDEPTTNLDEenIE-ESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-64 |
1.34e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250751 3 DSILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL 64
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-64 |
1.70e-07 |
|
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: 50.55 E-value: 1.70e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL 64
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV 64
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-62 |
2.26e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 2.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490250751 6 LRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
183-257 |
2.35e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 2.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250751 183 TLSYGQQRRLEIAR---AMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVmEISDHIIVL 257
Cdd:PRK00635 809 SLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV-KVADYVLEL 884
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
184-271 |
8.35e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVI 263
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*...
gi 490250751 264 ARGAPQAI 271
Cdd:PRK15093 239 ETAPSKEL 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
181-271 |
1.19e-06 |
|
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: 49.63 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 AGTLSYGQQRRLEIARAMCTR---PEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGmVMEISDHIIVL 257
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIEHNLD-VIKTADYIIDL 904
|
90 100
....*....|....*....|
gi 490250751 258 -----DH-GDVIARGAPQAI 271
Cdd:TIGR00630 905 gpeggDGgGTVVASGTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
181-268 |
1.35e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 181 AGTLSYGQQRRLEIARAM---CTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGmVMEISDHIIVL 257
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLD-VIKCADWIIDL 244
|
90
....*....|....*..
gi 490250751 258 -----DH-GDVIARGAP 268
Cdd:cd03271 245 gpeggDGgGQVVASGTP 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-260 |
1.47e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkvtdvIQVLGQKlhpddflhpAQLGRRIYYkmfg 102
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKE-----INALSTA---------QRLARGLVY---- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 103 gthlvnragLARTFQNIRLFREMSVIENLLVAQHtqvnrhllagilNTRGY---RQAESQALDRAFYWLEVveMVDCANR 179
Cdd:PRK15439 343 ---------LPEDRQSSGLYLDAPLAWNVCALTH------------NRRGFwikPARENAVLERYRRALNI--KFNHAEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 180 LAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDHIIVLDH 259
Cdd:PRK15439 400 AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQ 478
|
.
gi 490250751 260 G 260
Cdd:PRK15439 479 G 479
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
184-258 |
1.52e-06 |
|
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: 47.57 E-value: 1.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEHDMGMVMEISDHIIVLD 258
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
183-274 |
1.56e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 183 TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQALsrIIRFLRQQ-HGITVLLIEHDMGMVMEiSDHIIVLDHGD 261
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSL--IQRTIREEfKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
90
....*....|...
gi 490250751 262 VIARGAPQAIQAN 274
Cdd:PLN03232 1447 VLEYDSPQELLSR 1459
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-274 |
1.58e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 3 DSILRVEHLMMHF---GGI--------KALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvt 71
Cdd:PRK10261 311 EPILQVRNLVTRFplrSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 72 dviqvlGQKLhpdDFLHPAQLG--RRIYYKMFGGTHlvnrAGLartfqNIRLFREMSVIENLLVaqhtqvnRHLLAGiln 149
Cdd:PRK10261 385 ------GQRI---DTLSPGKLQalRRDIQFIFQDPY----ASL-----DPRQTVGDSIMEPLRV-------HGLLPG--- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 150 trgyrqaeSQALDRAFYWLEVVEMV-DCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRF 228
Cdd:PRK10261 437 --------KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490250751 229 LRQQHGITVLLIEHDMGMVMEISDHIIVLDHGDVIARGAPQAIQAN 274
Cdd:PRK10261 509 LQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
184-255 |
1.63e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 1.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490250751 184 LSYGQQRRLEIARAM----CTRPEMICLDEPAAGLNPVETQALSRIIRFLRqQHGITVLLIEHDMgMVMEISDHII 255
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLP-ELAELADKLI 151
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
183-242 |
1.95e-06 |
|
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: 46.76 E-value: 1.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 183 TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRqQHGITVLLIEH 242
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSAL---DEESEDRLYQLLK-ELGITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-64 |
2.42e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.64 E-value: 2.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490250751 24 VNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL 64
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
16-268 |
2.54e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.30 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 16 GGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLrAREKVTDviqvlgqklhpddfLHPAqlgrr 95
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI-GGRVVNE--------------LEPA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 iyykmfggthlvNRaGLARTFQNIRLFREMSVIENllvaqhtqvnrhlLAGILNTRGYRQAE-SQALDRAFYWLEVVEMV 174
Cdd:PRK11650 75 ------------DR-DIAMVFQNYALYPHMSVREN-------------MAYGLKIRGMPKAEiEERVAEAARILELEPLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 175 DcanRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpvetqALSRI-----IRFLRQQHGITVLLIEHDMGMVME 249
Cdd:PRK11650 129 D---RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-----AKLRVqmrleIQRLHRRLKTTSLYVTHDQVEAMT 200
|
250
....*....|....*....
gi 490250751 250 ISDHIIVLDHGDVIARGAP 268
Cdd:PRK11650 201 LADRVVVMNGGVAEQIGTP 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
184-273 |
3.61e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEpaaGLNPVETQALSRIIRFLRQ-QHGITVLLIEHDMGMVMEiSDHIIVLDHGDV 262
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDD---ALSAVDGRTEHQILHNLRQwGEGRTVIISAHRLSALTE-ASEILVMQHGHI 527
|
90
....*....|.
gi 490250751 263 IARGAPQAIQA 273
Cdd:PRK10789 528 AQRGNHDQLAQ 538
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
185-274 |
3.71e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 185 SYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQALsrIIRFLRQQ-HGITVLLIEHDMGMVMEiSDHIIVLDHGDVI 263
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVD-VRTDAL--IQKTIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
90
....*....|.
gi 490250751 264 ARGAPQAIQAN 274
Cdd:PLN03130 1452 EFDTPENLLSN 1462
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
17-52 |
4.57e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 46.34 E-value: 4.57e-06
10 20 30
....*....|....*....|....*....|....*.
gi 490250751 17 GIKALNDVNLEVERGsITALIGPNGAGKTTVFNCLT 52
Cdd:pfam13476 5 NFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAIK 39
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-257 |
5.35e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 23 DVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDV--------IQVLGQklhpDDFLHPAQLGR 94
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInlkwwrskIGVVSQ----DPLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 95 RIYYKMFGGTHL------VNRAGLA-RTFQNIRLFREMSVIENLLVAQHTQVNRHLLAGILNTRGYRQAESQALDRAFYW 167
Cdd:PTZ00265 479 NIKYSLYSLKDLealsnyYNEDGNDsQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 168 LEVVEMV-DCANRLAGT----LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGITVLLIEH 242
Cdd:PTZ00265 559 HDFVSALpDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
250
....*....|....*
gi 490250751 243 DMGMVmEISDHIIVL 257
Cdd:PTZ00265 639 RLSTI-RYANTIFVL 652
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-285 |
5.80e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 17 GIKALNDVNLEVERGsITALIGPNGAGKTTVFNCLTGFYRATGgsivlrarekvtdviqvlGQKLHPDDFLHPAQLG--- 93
Cdd:COG3593 10 NFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSS------------------SRKFDEEDFYLGDDPDlpe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 -----------RRIYYKMFGGTHlvnRAGLARTFQNIRlfremSVIENLLVAQHTQVNRHLLAGILNTRGYRQAESQALD 162
Cdd:COG3593 71 ieieltfgsllSRLLRLLLKEED---KEELEEALEELN-----EELKEALKALNELLSEYLKELLDGLDLELELSLDELE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVeMVDCANRLAGTLSYGQQRRL------EIARAMCTRPE-MICLDEPAAGLNPvetQALSRIIRFLRQ--QH 233
Cdd:COG3593 143 DLLKSLSLR-IEDGKELPLDRLGSGFQRLIllallsALAELKRAPANpILLIEEPEAHLHP---QAQRRLLKLLKElsEK 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490250751 234 GITVLLIEHDMGMVMEIS-DHIIVL--DHGDVIARGAPQAIQANASVIAAYLGAE 285
Cdd:COG3593 219 PNQVIITTHSPHLLSEVPlENIRRLrrDSGGTTSTKLIDLDDEDLRKLLRYLGVT 273
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
262-285 |
7.68e-06 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 41.85 E-value: 7.68e-06
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-242 |
9.05e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.72 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTdviqvlgqklhpddFLhPaqlgRRIYykM 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL--------------FL-P----QRPY--L 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 FGGThLvnRAGLARTfqnirlfremsvienllvAQHTQVNRHLLAGILntrgyRQAESQALdrafywlevVEMVDCANRL 180
Cdd:COG4178 438 PLGT-L--REALLYP------------------ATAEAFSDAELREAL-----EAVGLGHL---------AERLDEEADW 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250751 181 AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPvETQAlsRIIRFLRQQ-HGITVLLIEH 242
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE-ENEA--ALYQLLREElPGTTVISVGH 542
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
184-277 |
1.13e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGMVMEISDHIIVLDHGDVI 263
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
90
....*....|....
gi 490250751 264 ARGAPQAIQANASV 277
Cdd:PRK10938 215 ETGEREEILQQALV 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
184-268 |
1.78e-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: 46.09 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpVETQALsrIIRFLRQQ-HGITVLLIEHDMGMVMEISdHIIVLDHGDV 262
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVD-LETDNL--IQSTIRTQfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
....*.
gi 490250751 263 IARGAP 268
Cdd:TIGR00957 1498 AEFGAP 1503
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-68 |
3.23e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 3.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490250751 5 ILRVEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGF--YRATGGSIVLRARE 68
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD 66
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-62 |
3.36e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 3.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490250751 8 VEHLMMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI 62
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-227 |
3.89e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGfyRATGGSIVLRAR----EKVTDVIQVLGQKLHPDDfLHPAQLGRR- 95
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRisgfPKKQETFARISGYCEQND-IHSPQVTVRe 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 96 -IYYKMFggthlvnraglartfqnIRLFREMSVIENLLVAQhtQVnrhllagilntrgyrqaesqaldrafywLEVVEMV 174
Cdd:PLN03140 973 sLIYSAF-----------------LRLPKEVSKEEKMMFVD--EV----------------------------MELVELD 1005
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250751 175 DCANRLAGT-----LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIR 227
Cdd:PLN03140 1006 NLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-242 |
5.48e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.40 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSivlrarekvtdvIQVLGQKLHPDDFLHPAQLgrriyykM 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE------------ILFERQSIKKDLCTYQKQL-------C 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 101 FGGthlvNRAGLARTfqnirlfreMSVIENLLVAQHTqvnrhllagilntrgyrQAESQALDRAFYWLEVVEMVDCAnrl 180
Cdd:PRK13540 78 FVG----HRSGINPY---------LTLRENCLYDIHF-----------------SPGAVGITELCRLFSLEHLIDYP--- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250751 181 AGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQHGiTVLLIEH 242
Cdd:PRK13540 125 CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGG-AVLLTSH 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
184-262 |
8.31e-05 |
|
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: 43.30 E-value: 8.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRflRQQHGITVLLIEHDMGMVMEiSDHIIVLDHGDV 262
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
154-268 |
9.71e-05 |
|
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: 43.77 E-value: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 154 RQAESQA-LDRAFYW-LEV-VEMVDCANRL------AGTLSYGQQRRLEIARAMCTRPEMICLDEPAaglNPVETQALSR 224
Cdd:TIGR03719 123 EQAELQEiIDAADAWdLDSqLEIAMDALRCppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPT---NHLDAESVAW 199
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490250751 225 IIRFLRQQHGiTVLLIEHDMGMVMEISDHIIVLDHGdviaRGAP 268
Cdd:TIGR03719 200 LERHLQEYPG-TVVAVTHDRYFLDNVAGWILELDRG----RGIP 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-262 |
1.45e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.98 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 6 LRVEHLMmhfgGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRarekvtdviqvlGQKLHPDD 85
Cdd:PRK11288 258 LRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD------------GKPIDIRS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 86 flhpaqlgrriyykmfggTHLVNRAGLA-----RTFQNIRLFRemSVIENLLVAQHtqvNRHLLAG-ILNtrgyRQAESQ 159
Cdd:PRK11288 322 ------------------PRDAIRAGIMlcpedRKAEGIIPVH--SVADNINISAR---RHHLRAGcLIN----NRWEAE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 160 ALDRAFYWLEVveMVDCANRLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQQhGITVLL 239
Cdd:PRK11288 375 NADRFIRSLNI--KTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLF 451
|
250 260
....*....|....*....|...
gi 490250751 240 IEHDMGMVMEISDHIIVLDHGDV 262
Cdd:PRK11288 452 VSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
182-262 |
1.63e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 182 GTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLN---PVETQALsrIIRFLRQQHGItvLLIEHDMGMVMEISDHIIVLD 258
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgaKFEIYQL--IAELAKKDKGI--IIISSEMPELLGITDRILVMS 465
|
....
gi 490250751 259 HGDV 262
Cdd:PRK10982 466 NGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
168-263 |
4.42e-04 |
|
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: 40.32 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 168 LEVVEMVDCANRLAGT-----LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNpvETQALsRIIRFLRQqhgitvllIEH 242
Cdd:cd03233 98 LTVRETLDFALRCKGNefvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTAL-EILKCIRT--------MAD 166
|
90 100 110
....*....|....*....|....*....|...
gi 490250751 243 DMGMVMEIS------------DHIIVLDHGDVI 263
Cdd:cd03233 167 VLKTTTFVSlyqasdeiydlfDKVLVLYEGRQI 199
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
14-69 |
4.61e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 4.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250751 14 HFGGIKALnDVNLEVERGsITALIGPNGAGKTTVFNCL--------TGFYRATGGSIVLRAREK 69
Cdd:COG3950 10 NFRGFEDL-EIDFDNPPR-LTVLVGENGSGKTTLLEAIalalsgllSRLDDVKFRKLLIRNGEF 71
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-62 |
4.69e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 4.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI 62
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-92 |
5.17e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 5.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 33 ITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQVLGQKLHPDDFLHPAQL 92
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEF 60
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
185-278 |
5.61e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 185 SYGQQRRLEIARAMCTRPE-MICLDEPAAGLNPvetqALSRIIR--FLRQQHGITVLLIEHDMGMVMEIsDHIIVLDHGD 261
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSgFILMDEATANIDP----ALDRQIQatVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGA 1521
|
90
....*....|....*..
gi 490250751 262 VIARGAPQAIQANASVI 278
Cdd:PTZ00243 1522 VAEMGSPRELVMNRQSI 1538
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
184-256 |
8.50e-04 |
|
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: 41.05 E-value: 8.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIirfLRQQHG-ITVLLIEHDMGMVMEISDHIIV 256
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKT---LKQSFSnCTVILSEHRVEALLECQQFLVI 1424
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-242 |
9.70e-04 |
|
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: 40.50 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 2 TDSILRVEHL-MMHFGGIKALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREKVTDVIQvlgqk 80
Cdd:TIGR00954 448 QDNGIKFENIpLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ----- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 81 lhpddflhpaqlgrriyykmfggthlvnraglaRTFQNIRLFRE-----MSVIEnllvaqhtqvnrhllagiLNTRGYRQ 155
Cdd:TIGR00954 523 ---------------------------------RPYMTLGTLRDqiiypDSSED------------------MKRRGLSD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 156 AESQALdrafywLEVVEMVDCANRLAG---------TLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRii 226
Cdd:TIGR00954 552 KDLEQI------LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR-- 623
|
250
....*....|....*.
gi 490250751 227 rfLRQQHGITVLLIEH 242
Cdd:TIGR00954 624 --LCREFGITLFSVSH 637
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-266 |
1.28e-03 |
|
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: 40.19 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVLRAREkVTDVIQvlgQKLH------PDD-FLHPAQLG 93
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-IRDVTQ---ASLRaaigivPQDtVLFNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 94 RRIYYKMFGGTHL-VNRAglARTFQnIRLFremsvIENLLVAQHTQVNRhllagilntRGYRqaesqaldrafywlevve 172
Cdd:COG5265 450 YNIAYGRPDASEEeVEAA--ARAAQ-IHDF-----IESLPDGYDTRVGE---------RGLK------------------ 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 173 mvdcanrlagtLSYGQQRRLEIARAMCTRPEMICLDEPAAGLnpvETQALSRIIRFLRQ-QHGITVLLIEHDMGMVMEiS 251
Cdd:COG5265 495 -----------LSGGEKQRVAIARTLLKNPPILIFDEATSAL---DSRTERAIQAALREvARGRTTLVIAHRLSTIVD-A 559
|
250
....*....|....*
gi 490250751 252 DHIIVLDHGDVIARG 266
Cdd:COG5265 560 DEILVLEAGRIVERG 574
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-257 |
1.49e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 28 VERGSITALIGPNGAGKTTVFNCLTGfyratggsivlrarekvtDVIQVLGQKLHP---DDFLhpaqlgrriyyKMFGGT 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSG------------------ELIPNLGDYEEEpswDEVL-----------KRFRGT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 105 HLvnraglartfQNirLFREMSViENLLVAQHTQ-VN----------RHLLAGIlNTRGyrqaesqALDrafywlEVVEM 173
Cdd:PRK13409 147 EL----------QN--YFKKLYN-GEIKVVHKPQyVDlipkvfkgkvRELLKKV-DERG-------KLD------EVVER 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 174 VDCAN---RLAGTLSYGQQRRLEIARAMCTRPEMICLDEPAAGLNPVETQALSRIIRFLRQqhGITVLLIEHDMGMVMEI 250
Cdd:PRK13409 200 LGLENildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYL 277
|
....*..
gi 490250751 251 SDHIIVL 257
Cdd:PRK13409 278 ADNVHIA 284
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-51 |
1.50e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 490250751 17 GIKALNDVNLEVERgsITALIGPNGAGKTTVFNCL 51
Cdd:COG4637 9 NFKSLRDLELPLGP--LTVLIGANGSGKSNLLDAL 41
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
163-247 |
1.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 163 RAFYWLEVVEMVDCANRLAGTLSYGQQR------RLEIARAMCTRPEMICLDEPAAGLN--PVETQA--LSRIIRFLRQQ 232
Cdd:TIGR00606 1179 RNYNYRVVMLKGDTALDMRGRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDreNIESLAhaLVEIIKSRSQQ 1258
|
90
....*....|....*
gi 490250751 233 HGITVLLIEHDMGMV 247
Cdd:TIGR00606 1259 RNFQLLVITHDEDFV 1273
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-76 |
2.17e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 2.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRA-TGGSIVLRARekVTDVIQV 76
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT--VAYVPQV 687
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-53 |
2.38e-03 |
|
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: 39.38 E-value: 2.38e-03
10 20
....*....|....*....|....*
gi 490250751 29 ERGSITALIGPNGAGKTTVFNCLTG 53
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSG 121
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-62 |
2.40e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490250751 20 ALNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI 62
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-65 |
2.90e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250751 5 ILRVEhlMMHFGGIKALNDVNLEverGSITALIGPNGAGKTTVFNCLT-GFYRATGGSIVLR 65
Cdd:COG0419 2 LLRLR--LENFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLR 58
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
30-82 |
3.34e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.15 E-value: 3.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250751 30 RGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL-----RAREKVTDVIQVLGQKLH 82
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLaaptgKAAKRLSESTGIEASTIH 68
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
207-282 |
4.34e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 207 LDEPAAGLNPVETQALSRIIRFLRQQhGITVLLIEHDMGmVMEISDHIIVL-----DH-GDVIARGAPQAIQAN-ASVIA 279
Cdd:COG0178 853 LDEPTTGLHFHDIRKLLEVLHRLVDK-GNTVVVIEHNLD-VIKTADWIIDLgpeggDGgGEIVAEGTPEEVAKVkASYTG 930
|
...
gi 490250751 280 AYL 282
Cdd:COG0178 931 RYL 933
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-64 |
5.27e-03 |
|
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: 36.58 E-value: 5.27e-03
10 20 30
....*....|....*....|....*....|....*
gi 490250751 30 RGSITALIGPNGAGKTTVFNCLTGFYRATGGSIVL 64
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
184-282 |
5.69e-03 |
|
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: 38.39 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250751 184 LSYGQQRRLEIARAMCTRPEMICLDEPaagLNPVETQALSRIIRFLRQQHGI----TVLLIEHDMGMVMEIsDHIIVLDH 259
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDP---LSAVDAHVGKHIFEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSG 836
|
90 100
....*....|....*....|...
gi 490250751 260 GDVIARGAPQAIQANASVIAAYL 282
Cdd:TIGR00957 837 GKISEMGSYQELLQRDGAFAEFL 859
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-62 |
7.18e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 37.84 E-value: 7.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490250751 21 LNDVNLEVERGSITALIGPNGAGKTTVFNCLTGFYRATGGSI 62
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV 717
|
|
| |
