|
Name |
Accession |
Description |
Interval |
E-value |
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-254 |
0e+00 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 536.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
250
....*....|....
gi 489958237 241 RNNPDVIRAYLGEA 254
Cdd:PRK11300 242 RNNPDVIKAYLGEA 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-254 |
1.74e-145 |
|
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: 407.12 E-value: 1.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....
gi 489958237 241 RNNPDVIRAYLGEA 254
Cdd:COG0411 241 RADPRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-246 |
8.51e-118 |
|
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: 336.33 E-value: 8.51e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLLVAQHQQLKTGLFSGllktpAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLA-----RARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
..
gi 489958237 245 DV 246
Cdd:cd03219 235 RV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-253 |
1.95e-78 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 236.94 E-value: 1.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAQHQqlKTGLFSGLLktpaFRRTQEEAlDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:COG4674 87 IGRKFQKPTVFEELTVFENLELALKG--DRGVFASLF----ARLTAEER-DRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdtTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
250
....*....|...
gi 489958237 241 RNNPDVIRAYLGE 253
Cdd:COG4674 238 QADPRVIEVYLGR 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-252 |
2.80e-60 |
|
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: 190.19 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVV 82
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 rtfqHV----RLFREMTVIENLLVAQHqqlktglfsgllkTPAFRRTQEEALDRAATWLDRigLLQHANRQASNLAYGDQ 158
Cdd:COG0410 82 ----YVpegrRIFPSLTVEENLLLGAY-------------ARRDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 159 RRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 238
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
250
....*....|....
gi 489958237 239 EIRNNPDVIRAYLG 252
Cdd:COG0410 222 ELLADPEVREAYLG 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-252 |
4.35e-60 |
|
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: 189.68 E-value: 4.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL---------------SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
....*...
gi 489958237 245 DVIRAYLG 252
Cdd:cd03218 225 LVRKVYLG 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-253 |
4.93e-60 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 189.47 E-value: 4.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVV 82
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RTFQHVRLFREMTVIENLL-VAQHQQLktglfsgllkTPAFRRTQEEALdraatwLDRIGLLQHANRQASNLAYGDQRRL 161
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILaVLELRKL----------SKKEREERLEEL------LEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 162 EIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 241
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
250
....*....|..
gi 489958237 242 NNPDVIRAYLGE 253
Cdd:COG1137 225 NNPLVRKVYLGE 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-251 |
5.30e-59 |
|
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: 187.11 E-value: 5.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI---- 76
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 ARMGVVrtFQHVRLFREMTVIENllVA----QHQQLktglfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASN 152
Cdd:COG1127 82 RRIGML--FQGGALFDSLTVFEN--VAfplrEHTDL----------------SEAEIRELVLEKLELVGLPGAADKMPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 153 LAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPL 232
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250 260
....*....|....*....|
gi 489958237 233 ANGTPEEIRNNPD-VIRAYL 251
Cdd:COG1127 222 AEGTPEELLASDDpWVRQFL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-254 |
4.91e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.80 E-value: 4.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVrt 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLLvaqhqqlktgLFSGLLKTPAfrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:COG1131 79 PQEPALYPDLTVRENLR----------FFARLYGLPR-----KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
250
....*....|..
gi 489958237 245 --DVIRAYLGEA 254
Cdd:COG1131 223 leDVFLELTGEE 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-243 |
1.84e-56 |
|
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: 179.94 E-value: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLLVAQHqqlktglfsgLLKTPAFRRTQEEALDRaatwLDRigLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAY----------ARRRAKRKARLERVYEL----FPR--LKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-253 |
2.98e-54 |
|
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: 174.77 E-value: 2.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLL-VAQHQQlktglfsgllKTPAFRRTQE-EALdraatwLDRIGLLQHANRQASNLAYGDQRRLE 162
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRK----------DLDRAEREERlEAL------LEEFQISHLRDNKAMSLSGGERRRVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 242
Cdd:TIGR04406 146 IARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
250
....*....|.
gi 489958237 243 NPDVIRAYLGE 253
Cdd:TIGR04406 225 NEKVRRVYLGE 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-246 |
1.33e-52 |
|
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: 170.38 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGL-PGQQIA---RMG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVrtFQHVRLFREMTVIENllVA----QHQQLKtglfsgllktpafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYG 156
Cdd:cd03261 81 ML--FQSGALFDSLTVFEN--VAfplrEHTRLS----------------EEEIREIVLEKLEAVGLRGAEDLYPAELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGT 236
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
250
....*....|..
gi 489958237 237 PEEIRN--NPDV 246
Cdd:cd03261 221 PEELRAsdDPLV 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-249 |
2.06e-49 |
|
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: 162.12 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM-GVVrtFQHVR--LF 91
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGLV--FQNPDdqLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 rEMTVIENllVAqhqqlktglFsGLLktpAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:COG1122 90 -APTVEED--VA---------F-GPE---NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIRA 249
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-250 |
7.28e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.02 E-value: 7.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLeGLPGQQIA--- 77
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-RRARRRIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 -RMGVVRTFQhvrlfreMTVIEnlLVAqhqqlkTGLFSgllKTPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYG 156
Cdd:COG1121 82 qRAEVDWDFP-------ITVRD--VVL------MGRYG---RRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNqGTPLANGT 236
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGP 221
|
250
....*....|....
gi 489958237 237 PEEIRNNPDVIRAY 250
Cdd:COG1121 222 PEEVLTPENLSRAY 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-243 |
1.11e-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: 158.10 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVr 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 tFQHVRLFREMTVIENLLvaqhqqlktgLFSgllktPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEI 163
Cdd:COG4555 80 -PDERGLYDRLTVRENIR----------YFA-----ELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
1.25e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.03 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiaR-M 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RnV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVrtFQHVRLFREMTVIENllVAqhqqlktglFsGL--LKTPAfrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGD 157
Cdd:COG3842 80 GMV--FQDYALFPHLTVAEN--VA---------F-GLrmRGVPK-----AEIRARVAELLELVGLEGLADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTP 237
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
....*..
gi 489958237 238 EEIRNNP 244
Cdd:COG3842 221 EEIYERP 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-241 |
3.15e-46 |
|
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: 153.68 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 7 VNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVrtFQ 86
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 87 HVRLFREMTVIENLLVaqhqqlktglFSGLLKTPAFRRTQeealdRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRC 166
Cdd:cd03265 81 DLSVDDELTGWENLYI----------HARLYGVPGAERRE-----RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 167 MVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 241
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-229 |
3.66e-46 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 160.58 E-value: 3.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQ--HLEGlPGQQIAR 78
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 -MGVVrtFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGD 157
Cdd:COG3845 81 gIGMV--HQHFMLVPNLTVAENIVL------------GLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-244 |
3.77e-45 |
|
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: 151.24 E-value: 3.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPgqqIARMGVVRT 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLlvaqhqqlktglfsgllktpAF----RRTQEEALDRAATW-LDRIGLLQHANRQASNLAYGDQR 159
Cdd:cd03300 78 FQNYALFPHLTVFENI--------------------AFglrlKKLPKAEIKERVAEaLDLVQLEGYANRKPSQLSGGQQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
....*
gi 489958237 240 IRNNP 244
Cdd:cd03300 218 IYEEP 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-241 |
6.89e-45 |
|
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: 150.35 E-value: 6.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGL--LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVV 82
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 rtFQHVRLFREMTVIENLlvaqhqqlktgLFSGLLKtpAFRRTQEEALdrAATWLDRIGLLQHANRQASNLAYGDQRRLE 162
Cdd:cd03263 81 --PQFDALFDELTVREHL-----------RFYARLK--GLPKSEIKEE--VELLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 241
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-229 |
1.30e-44 |
|
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: 149.56 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGG----LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-- 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 ---MGVVrtFQHVRLFREMTVIENLLVAQHqqlktglFSGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQASNLAY 155
Cdd:cd03255 81 rrhIGFV--FQSFNLLPDLTALENVELPLL-------LAGVPK--------KERRERAEELLERVGLGDRLNHYPSELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 156 GDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVmGISDRIYVVNQG 229
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDG 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-229 |
3.72e-44 |
|
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: 146.77 E-value: 3.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVrt 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLlvaqhqqlktgLFSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLEIV 164
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------KLSG----------------------------------------GMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-244 |
1.15e-43 |
|
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: 154.29 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF-----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI 76
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 A----RMGVVrtFQHVR--LFREMTVIENLLVAQHQQlktGLFSGllktpafrrtqEEALDRAATWLDRIGL-LQHANRQ 149
Cdd:COG1123 338 RelrrRVQMV--FQDPYssLNPRMTVGDIIAEPLRLH---GLLSR-----------AERRERVAELLERVGLpPDLADRY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 150 ASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:COG1123 402 PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
250
....*....|....*
gi 489958237 230 TPLANGTPEEIRNNP 244
Cdd:COG1123 482 RIVEDGPTEEVFANP 496
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-240 |
1.16e-43 |
|
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: 147.71 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFG-GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI----ARM 79
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVrtFQHVRLFREMTVIENLLVAQHQQlkTGLFSGLlktpaFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQR 159
Cdd:cd03256 81 GMI--FQQFNLIERLSVLENVLSGRLGR--RSTWRSL-----FGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 489958237 240 I 240
Cdd:cd03256 232 L 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-225 |
2.33e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.87 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAqhQQLKTGlfsGLLKTPAFRRtqeealdRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLG--REPRRG---GLIDWRAMRR-------RARELLARLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYV 225
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTV 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-240 |
4.35e-43 |
|
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: 146.73 E-value: 4.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVV 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 rtFQHVRLFREMTVIEnlLVAQ----HQqlktglfsgllktPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQ 158
Cdd:COG1120 81 --PQEPPAPFGLTVRE--LVALgrypHL-------------GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 159 RRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 238
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
..
gi 489958237 239 EI 240
Cdd:COG1120 224 EV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-229 |
5.82e-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: 144.98 E-value: 5.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 6 SVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGqqiaRMGVVRTF 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK----RIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 86 QHV-RLFReMTVIEnlLVAqhqqlkTGLFSGLLKTPAFRRTQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03235 77 RSIdRDFP-ISVRD--VVL------MGLYGHKGLFRRLSKADKAKVDEA---LERVGLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-242 |
3.26e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 145.64 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM----G 80
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLpeerG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 vvrtfqhvrLFREMTVIENLL-VAqhqQLKtGLfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQR 159
Cdd:COG4152 82 ---------LYPKMKVGEQLVyLA---RLK-GL------------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
...
gi 489958237 240 IRN 242
Cdd:COG4152 216 IRR 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-230 |
3.40e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 142.99 E-value: 3.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM-GVVrtFQHVR--LFREmT 95
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV--FQNPDdqFFGP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVA-QHQQLKtglfsgllktpafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:cd03225 93 VEEEVAFGlENLGLP----------------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 175 MLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-229 |
1.78e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFG----GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI 76
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 ARM-----GVVrtFQHVRLFREMTVIENLLVAQhqqlktgLFSGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQAS 151
Cdd:COG1136 81 ARLrrrhiGFV--FQFFNLLPELTALENVALPL-------LLAGVSR--------KERRERARELLERVGLGDRLDHRPS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 152 NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLvMGISDRIYVVNQG 229
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-244 |
3.10e-41 |
|
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: 141.32 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 7 VNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiARMGVVrtFQ 86
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNVGFV--FQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 87 HVRLFREMTVIENllVAqhqqlktglFsGLLKTPAFRRTQEEALD-RAATWLDRIGLLQHANRQASNLAYGDQRRLEIVR 165
Cdd:cd03296 82 HYALFRHMTVFDN--VA---------F-GLRVKPRSERPPEAEIRaKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 166 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-235 |
4.35e-41 |
|
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: 140.35 E-value: 4.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiARMGVVrt 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RNIGMV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLLVAqhqqlktglfsglLKTPAFRRTQEEAldRAATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03259 78 FQDYALFPHLTVAENIAFG-------------LKLRGVPKAEIRA--RVRELLELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-253 |
1.18e-40 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 140.03 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVR 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 TFQHVRLFREMTVIENLLVAqhQQLKTGLfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEI 163
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAV--LQIRDDL------------SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
250
....*....|
gi 489958237 244 PDVIRAYLGE 253
Cdd:PRK10895 228 EHVKRVYLGE 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-244 |
1.32e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.59 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLE-GLPGQQiARMGVVr 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE-RRVGFV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 tFQHVRLFREMTVIENllVAqhqqlktglFsGLLKTPAFRrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEI 163
Cdd:COG1118 81 -FQHYALFPHMTVAEN--IA---------F-GLRVRPPSK---AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKETKELDEliaELRDHHDT---TILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRR---WLRRLHDElggTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
....
gi 489958237 241 RNNP 244
Cdd:COG1118 222 YDRP 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-225 |
1.43e-39 |
|
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: 136.45 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGG----LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPgqqiARMG 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVrtFQHVRLFREMTVIENLLVAqhqqLKtglFSGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:cd03293 77 YV--FQQDALLPWLTVLDNVALG----LE---LQGVPK--------AEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYV 225
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVV 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-230 |
5.06e-39 |
|
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: 133.85 E-value: 5.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHL---EGLPGQQIARMGV 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VrtFQHVRLFREMTVIENLLVAqhqqlktglFSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRL 161
Cdd:cd03229 81 V--FQDFALFPHLTVLENIALG---------LSG----------------------------------------GQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 162 EIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-240 |
9.32e-39 |
|
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: 134.62 E-value: 9.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYK-----PTGGTIMLRDQHLEGLPGQQIA-- 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 -RMGVVrtFQHVRLFReMTVIENLLVAQHQQlktglfsGLLKTPAFRRTQEEALDRAATWlDRIGLLQHANRqasnLAYG 156
Cdd:cd03260 81 rRVGMV--FQKPNPFP-GSIYDNVAYGLRLH-------GIKLKEELDERVEEALRKAALW-DEVKDRLHALG----LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGT 236
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
....
gi 489958237 237 PEEI 240
Cdd:cd03260 224 TEQI 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-229 |
1.36e-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: 133.81 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGlPGQQI----ARMG 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNInelrQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVrtFQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:cd03262 80 MV--FQQFNLFPHLTVLENITLAPIKVKG--------------MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-249 |
2.45e-37 |
|
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: 136.96 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRF--GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTIMLRDQHLEGLPGQQ 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 76 IAR-MGVVrtFQHVrlfreMTVIENLLVAQhqQLKTGLFsgllktpAFRRTQEEALDRAATWLDRIGLLQHANRQASNLA 154
Cdd:COG1123 81 RGRrIGMV--FQDP-----MTQLNPVTVGD--QIAEALE-------NLGLSRAEARARVLELLEAVGLERRLDRYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 155 YGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLAN 234
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
250
....*....|....*
gi 489958237 235 GTPEEIRNNPDVIRA 249
Cdd:COG1123 225 GPPEEILAAPQALAA 239
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-181 |
3.20e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.15 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARMGVVrtFQHVRLFREMTVIE 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYV--FQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVAqhqqlktGLFSGLLKTPAFRRtqeeaLDRAATWLDRIGLL-QHANRQASNLAYGDQRRLEIVRCMVTQPEILMLD 177
Cdd:pfam00005 79 NLRLG-------LLLKGLSKREKDAR-----AEEALEKLGLGDLAdRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 489958237 178 EPAA 181
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-235 |
1.67e-36 |
|
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: 127.17 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 6 SVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVrt 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fqhvrlfremtvienllvaqhqqlktglfsgllktpafrrtqeealdraATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03214 79 -------------------------------------------------PQALELLGLAHLADRPFNELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-235 |
3.52e-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: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fqhvrLFREMTVIENLLVAqhQQLKtglfsGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03269 81 -----LYPKMKVIDQLVYL--AQLK-----GLKK--------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-211 |
4.74e-36 |
|
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: 128.28 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPT-GGTIMLRDQHLEGLPGQQI-ARMG 80
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVWELrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLvaqhqqlkTGLFS--GLlktpaFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQ 158
Cdd:COG1119 82 LVSPALQLRFPRDETVLDVVL--------SGFFDsiGL-----YREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489958237 159 RRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEH 211
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-244 |
6.90e-36 |
|
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: 128.53 E-value: 6.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 13 RFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-----ARMGVVrtFQH 87
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrrKKISMV--FQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 88 VRLFREMTVIENL---LVAQHQqlktglfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03294 111 FALLPHRTVLENVafgLEVQGV------------------PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-250 |
8.03e-36 |
|
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: 128.34 E-value: 8.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI----ARMGVVrtFQ---HvRLF 91
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrKKVGLV--FQfpeH-QLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 rEMTVIE-------NLlvaqhqqlktglfsGLlktpafrrTQEEALDRAATWLDRIGLLQH-ANRQASNLAYGDQRRLEI 163
Cdd:TIGR04521 97 -EETVYKdiafgpkNL--------------GL--------SEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
....*..
gi 489958237 244 PDVIRAY 250
Cdd:TIGR04521 234 VDELEKI 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-229 |
9.74e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.71 E-value: 9.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 11 MMRF--------GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIA----R 78
Cdd:COG2884 1 MIRFenvskrypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 MGVVrtFQHVRLFREMTVIENLLVAqhqqLK-TGlfsgllktpafrRTQEEALDRAATWLDRIGLLQHANRQASNLAYGD 157
Cdd:COG2884 81 IGVV--FQDFRLLPDRTVYENVALP----LRvTG------------KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-252 |
6.32e-35 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 130.67 E-value: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAQHQQLKtglFSGlLKTPAFRRTQEealdRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKK---VCG-VNIIDWREMRV----RAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRK-EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
250
....*....|..
gi 489958237 241 RNNpDVIRAYLG 252
Cdd:PRK09700 233 SND-DIVRLMVG 243
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-252 |
7.14e-35 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 128.05 E-value: 7.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-----MLRDQHLEGLPGQQIARMGVVrtFQHVR 89
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIfidgeNIMKQSPVELREVRRKKIGMV--FQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 90 LFREMTVIENllvaqhqqlkTGLFSGLLKTPAFRRtQEEALDRaatwLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVT 169
Cdd:TIGR01186 82 LFPHMTILQN----------TSLGPELLGWPEQER-KEKALEL----LKLVGLEEYEHRYPDELSGGMQQRVGLARALAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 170 QPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVI 247
Cdd:TIGR01186 147 EPDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPanEYV 226
|
....*
gi 489958237 248 RAYLG 252
Cdd:TIGR01186 227 EEFIG 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-235 |
7.85e-35 |
|
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: 123.87 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLrDQHLEGLPGQQIARMGVVRT 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-DGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQhvRLFREMTVIENLLVAQhqqlktglfsgllktpAFRRTQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03268 80 AP--GFYPNLTARENLRLLA----------------RLLGIRKKRIDEV---LDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-244 |
1.87e-34 |
|
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: 123.46 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI----ARMGVVrtFQHVRLFREM 94
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkarRRIGMI--FQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 95 TVIENLLVAqhqqLKtglfsgLLKTPafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:cd03258 98 TVFENVALP----LE------IAGVP-----KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 175 MLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-252 |
8.12e-34 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 122.29 E-value: 8.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAqhqqlktGLFsgllktpAFRRTQEEALDRAATWLDRigLLQHANRQASNLAYGDQRR 160
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG-------GFF-------AERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
250
....*....|..
gi 489958237 241 RNNPDVIRAYLG 252
Cdd:PRK11614 225 LANEAVRSAYLG 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-244 |
2.87e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.18 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQ--IARMg 80
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpINMM- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 vvrtFQHVRLFREMTVIENLLVAQHQQlktglfsgllktpafRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK11607 97 ----FQSYALFPHMTVEQNIAFGLKQD---------------KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
....
gi 489958237 241 RNNP 244
Cdd:PRK11607 238 YEHP 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-244 |
2.93e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 120.52 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiARMGVVrtFQHVRLFREMTVIENLL 101
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RDISYV--PQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 102 VaqhqqlktglfsGLLKTPAFRRTQEEALDRAATWLDRIGLLqhaNRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAA 181
Cdd:cd03299 94 Y------------GLKKRKVDKKEIERKVLEIAEMLGIDHLL---NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 182 GLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-244 |
5.08e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiaR-MGVVr 83
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RnIAMV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 tFQHVRLFREMTVIENLLVAqhqqLKtglfsgLLKTPafRRTQEEALDRAAtwlDRIGLLQHANRQASNLAYGDQRRLEI 163
Cdd:COG3839 81 -FQSYALYPHMTVYENIAFP----LK------LRKVP--KAEIDRRVREAA---ELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKetkeL-DELIAELRDHH---DTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAK----LrVEMRAEIKRLHrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
....*
gi 489958237 240 IRNNP 244
Cdd:COG3839 221 LYDRP 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-229 |
8.46e-33 |
|
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: 119.15 E-value: 8.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GvvRTFQHVrlFRE--------MTVIEnllvaqhqQLKTGL-FSGLLKTPAFRRTQEEALdraatwLDRIGLL-QHANRQ 149
Cdd:cd03257 81 R--KEIQMV--FQDpmsslnprMTIGE--------QIAEPLrIHGKLSKKEARKEAVLLL------LVGVGLPeEVLNRY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 150 ASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03257 143 PHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-244 |
8.76e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.11 E-value: 8.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 7 VNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiARMGVVrtFQ 86
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKVGFV--FQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 87 HVRLFREMTVIENLLVaqhqqlktglfsGLLKTPAFRRTQEEALDRAATWLDRIGLLQH-ANRQASNLAYGDQRRLEIVR 165
Cdd:PRK10851 82 HYALFRHMTVFDNIAF------------GLTVLPRRERPNAAAIKAKVTQLLEMVQLAHlADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 166 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-244 |
1.03e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.36 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQiaRMgv 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllKTPAfrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK09452 88 VNTvFQSYALFPHMTVFEN--VAFGLRMQ--------KTPA-----AEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
....
gi 489958237 241 RNNP 244
Cdd:PRK09452 233 YEEP 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-212 |
1.31e-32 |
|
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: 117.97 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVV 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 rtFQHVRLFREMTVIENLlvAQHQQLKTGLFSGllktpafrrtqeealDRAATWLDRIGLLQHANRQASNLAYGDQRRLE 162
Cdd:COG4133 81 --GHADGLKPELTVRENL--RFWAALYGLRADR---------------EAIDEALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHD 212
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQ 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-250 |
1.43e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.45 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM-GVV 82
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RtfQHVRL---FremTVIEnlLVAqhqqlkTGLFSGLLKTPAFRRTQEEALDRAatwldriGLLQHANRQASNLAYGDQR 159
Cdd:COG4559 81 P--QHSSLafpF---TVEE--VVA------LGRAPHGSSAAQDRQIVREALALV-------GLAHLAGRSYQTLSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMV-------TQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPL 232
Cdd:COG4559 141 RVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
250
....*....|....*...
gi 489958237 233 ANGTPEEIRNNPDVIRAY 250
Cdd:COG4559 220 AQGTPEEVLTDELLERVY 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-230 |
2.36e-32 |
|
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: 115.99 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQhvrlfremtvienllvaqhqqlktglfsgllktpafrrtqeealdraatwldrigllqhanrqasnLAYGDQRRLEIV 164
Cdd:cd03216 81 YQ------------------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-253 |
3.35e-32 |
|
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: 118.17 E-value: 3.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVrtFQHVRLFRE 93
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRkIGYV--IQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 MTVIENllvaqhqqlkTGLFSGLLKTPafrrtQEEALDRAATWLDRIGL--LQHANRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:cd03295 90 MTVEEN----------IALVPKLLKWP-----KEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIRA 249
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPanDFVAE 234
|
....
gi 489958237 250 YLGE 253
Cdd:cd03295 235 FVGA 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-248 |
2.37e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.22 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGL---PGQ------- 74
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkDGQlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 75 --QIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLktglfsGLLKTpafrrtqeEALDRAATWLDRIGLLQHAN-RQAS 151
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL------GLSKQ--------EARERAVKYLAKVGIDERAQgKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 152 NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTP 231
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
250
....*....|....*..
gi 489958237 232 LANGTPEEIRNNPDVIR 248
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPR 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-253 |
4.60e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.85 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 8 NGLMMRFggllavnnvNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPgqqIARMGVVRTFQH 87
Cdd:COG3840 12 GDFPLRF---------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP---PAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 88 VRLFREMTVIENLlvaqhqqlktGLfsGLlkTPAFRRTQEEAlDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCM 167
Cdd:COG3840 80 NNLFPHLTVAQNI----------GL--GL--RPGLKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 168 VTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI--RNNPD 245
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldGEPPP 224
|
....*...
gi 489958237 246 VIRAYLGE 253
Cdd:COG3840 225 ALAAYLGI 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-251 |
6.51e-31 |
|
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: 119.87 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRF--GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARM 79
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVrtFQHVRLFReMTVIENLLV----AQHQQLktglfsgllktpafrrtqEEALDRA--ATWLDRI--GLLQHANRQAS 151
Cdd:COG4987 412 AVV--PQRPHLFD-TTLRENLRLarpdATDEEL------------------WAALERVglGDWLAALpdGLDTWLGEGGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 152 NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPkETKelDELIAELRDH-HDTTILLIEHDMkLVMGISDRIYVVNQGT 230
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDA-ATE--QALLADLLEAlAGRTVLLITHRL-AGLERMDRILVLEDGR 546
|
250 260
....*....|....*....|.
gi 489958237 231 PLANGTPEEIRNNPDVIRAYL 251
Cdd:COG4987 547 IVEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-230 |
1.73e-30 |
|
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: 111.18 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 6 SVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIaRMGVVRTF 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 86 QhvrlfremtvienllvaqhqqlktglFSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLEIVR 165
Cdd:cd00267 80 Q--------------------------LSG----------------------------------------GQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 166 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-244 |
4.74e-30 |
|
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: 112.59 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFG----GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR- 78
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 MGVVrtFQHVR--LFREMTVIEnllvaqhqqlktglfsgLLKTP--AFRRTQEEAldRAATWLDRIGL-LQHANRQASNL 153
Cdd:COG1124 81 VQMV--FQDPYasLHPRHTVDR-----------------ILAEPlrIHGLPDREE--RIAELLEQVGLpPSFLDRYPHQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 154 AYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLA 233
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
250
....*....|.
gi 489958237 234 NGTPEEIRNNP 244
Cdd:COG1124 220 ELTVADLLAGP 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-240 |
8.75e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 116.18 E-value: 8.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkPTG---GTIMLRDQHLEGLPGQQIA 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 RMGVVRTFQHVRLFREMTVIENllvaqhqqlktgLFSGLLKTPAFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGD 157
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLEN------------IFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQG-----TPL 232
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGrhigtRPA 227
|
....*...
gi 489958237 233 ANGTPEEI 240
Cdd:PRK13549 228 AGMTEDDI 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-239 |
1.06e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM-GV 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRtfQHVRLFREMTVIEnlLVAQhqqlktglfsGLLKTPAFRRTQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRRL 161
Cdd:PRK13548 81 LP--QHSSLSFPFTVEE--VVAM----------GRAPHGLSRAEDDALVAAA---LAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 162 EIVRCMV------TQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
....
gi 489958237 236 TPEE 239
Cdd:PRK13548 224 TPAE 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-239 |
1.25e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 116.40 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPG----QQIARMGvvrtfQHVRL 90
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPaswrRQIAWVP-----QNPYL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FrEMTVIENLLVAQHQqlktglfsgllktpAFRRTQEEALDRA--ATWLDRI--GLLQHANRQASNLAYGDQRRLEIVRC 166
Cdd:COG4988 423 F-AGTIRENLRLGRPD--------------ASDEELEAALEAAglDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 167 MVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdtTILLIEHDMKLVMgISDRIYVVNQGTPLANGTPEE 239
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-253 |
2.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.84 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-----ARMGVVRTFQHVRLFrEM 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrKKVSLVFQFPEAQLF-EN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 95 TVIENLLVAQHQqlktglfsgllktpaFRRTQEEALDRAATWLDRIGLLQH-ANRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK13641 102 TVLKDVEFGPKN---------------FGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 174 LMLDEPAAGLNPKETKELDELIAEL-RDHHdtTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD-VIRAYL 251
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYqKAGH--TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYL 244
|
..
gi 489958237 252 GE 253
Cdd:PRK13641 245 DE 246
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-229 |
2.12e-29 |
|
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: 108.62 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARMGVVrtFQHVRLFrEMTVI 97
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAYV--PQDPFLF-SGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENLLvaqhqqlktglfSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLEIVRCMVTQPEILMLD 177
Cdd:cd03228 94 ENIL------------SG----------------------------------------GQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489958237 178 EPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMgISDRIYVVNQG 229
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-248 |
2.25e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.32 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARMGVVRTFQHV--RLFR 92
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EmTVIENLLVAQhqqLKTGLfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PRK13639 94 P-TVEEDVAFGP---LNLGL------------SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIR 248
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-247 |
3.26e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHL--EGLPGQQI-ARMGVVRTFQHVRLFREmt 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIrKKVGLVFQYPEYQLFEE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVAQHQQLktglfsGLlktpafrrTQEEALDRAATWLDRIGL--LQHANRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK13637 100 TIEKDIAFGPINL------GL--------SEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 174 LMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVI 247
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-229 |
3.47e-29 |
|
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: 109.27 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGqqiARMGVVRT 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHVRLFREMTVIENLlvaqhqqlktglfsgllktpAF----RRTQEEALDRAATWLDRI-GLLQHANRQASNLAYGDQR 159
Cdd:cd03301 78 FQNYALYPHMTVYDNI--------------------AFglklRKVPKDEIDERVREVAELlQIEHLLDRKPKQLSGGQRQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-245 |
9.05e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 9.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-----MGVVRTFQHVRLFR 92
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKplrkkVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EmTVienllvaqhqqLKTGLFSGLlktpAFRRTQEEALDRAATWLDRIGLLQHA-NRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:PRK13634 101 E-TV-----------EKDICFGPM----NFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 245
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-252 |
9.44e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMgVV 82
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RTFQHVRLFREMTVIENLLVAQHQQLktGLFSGLlkTPAFRRTQEEALDRAatwldriGLLQHANRQASNLAYGDQRRLE 162
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHR--SRFDTW--TETDRAAVERAMERT-------GVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIeHDMKLVMGISDRIYVVNQGTPLANGTPEEIRn 242
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVL- 227
|
250
....*....|
gi 489958237 243 NPDVIRAYLG 252
Cdd:PRK09536 228 TADTLRAAFD 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-244 |
1.08e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI--AR--MGVVrtFQHVRL 90
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARrkIGMI--FQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMTVIEN----LLVAqhqqlktglfsgllKTPAfrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRC 166
Cdd:COG1135 94 LSSRTVAENvalpLEIA--------------GVPK-----AEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 167 MVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-229 |
1.19e-28 |
|
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: 107.88 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIA----RMGVVrtFQHVRL 90
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrrKIGVV--FQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMTVIENLLVAqhqqlktglfsgLLKTPAFRRtqeEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQ 170
Cdd:cd03292 90 LPDRNVYENVAFA------------LEVTGVPPR---EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 171 PEILMLDEPAAGLNPKETKELDELiaeLRDHHD--TTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNL---LKKINKagTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-247 |
1.31e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.33 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGG-----LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRD----QHLEGLPGQ 74
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 75 QIARMGVVRTFQhvRLFREMTVIenLLVAQHQQLKTGLFSGLLKTP-AFRRTQEEALDRAATWLDRIGL-LQHANRQASN 152
Cdd:PRK13631 101 TNPYSKKIKNFK--ELRRRVSMV--FQFPEYQLFKDTIEKDIMFGPvALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 153 LAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQGTPL 232
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 489958237 233 ANGTPEEIRNNPDVI 247
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-250 |
1.49e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.89 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHvrLFREMTVIENLLVaqhqqlkTGLFSGLlktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK13537 84 VVPQFDN--LDPDFTVRENLLV-------FGRYFGL--------SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKET----KELDELIAELRdhhdtTILLIEHDMKLVMGISDRIYVVNQGTPLANGT 236
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARhlmwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
250
....*....|....*..
gi 489958237 237 PEEIRNNP---DVIRAY 250
Cdd:PRK13537 222 PHALIESEigcDVIEIY 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-242 |
4.77e-28 |
|
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: 112.23 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVrtFQHVRLFrEMTV 96
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRqIGVV--LQDVFLF-SGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 IENLLVAQHQqlktglfsgllktpafrRTQEEALdRAAtwlDRIGLLQHANR-----------QASNLAYGDQRRLEIVR 165
Cdd:COG2274 566 RENITLGDPD-----------------ATDEEII-EAA---RLAGLHDFIEAlpmgydtvvgeGGSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 166 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRdhHDTTILLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEIRN 242
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLA 698
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-248 |
9.08e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 107.24 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEglpgqqIARMGVVRTFQHVRLFREMT 95
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID------YSRKGLMKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVAQHQQLKTGLFSglLKTPafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILM 175
Cdd:PRK13636 92 DNQLFSASVYQDVSFGAVN--LKLP-----EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIR 248
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-245 |
1.25e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.77 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI--ARMGV 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRTFQHVRLFREMTVIENllVAQHQQLKTGLFSGLLKTPAFRRtqeealdraatwLDRIGLLQHANRQASNLAYGDQRRL 161
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDN--VAYPLREHTQLPAPLLHSTVMMK------------LEAVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 162 EIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 241
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
....
gi 489958237 242 NNPD 245
Cdd:PRK11831 233 ANPD 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-242 |
1.65e-27 |
|
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: 110.87 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEglPGQQIARMGVVRTFQHVRLFREMT 95
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVaqHQQLKTglfsgllktpafrRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILM 175
Cdd:TIGR01257 1020 VAEHILF--YAQLKG-------------RSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHdtTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 242
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-215 |
1.72e-27 |
|
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: 105.21 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGG----LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR 78
Cdd:COG4181 7 PIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 -----MGVVrtFQHVRLFREMTVIENLLVaqhqqlktglfsgllktPAFRRTQEEALDRAATWLDRIGL---LQHANRQA 150
Cdd:COG4181 87 lrarhVGFV--FQSFQLLPTLTALENVML-----------------PLELAGRRDARARARALLERVGLghrLDHYPAQL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 151 SNlayGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKL 215
Cdd:COG4181 148 SG---GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-229 |
3.44e-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: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLhKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRt 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fQHVRLFREMTVIENLLvaqhqqlktglFSGLLKTPAFRRtQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRRLEIV 164
Cdd:cd03264 79 -QEFGVYPNFTVREFLD-----------YIAWLKGIPSKE-VKARVDEV---LELVNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-244 |
8.03e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.02 E-value: 8.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 13 RFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGlPGQQIARM----GVVrtFQHV 88
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIrqeaGMV--FQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 89 RLFREMTVIENLLVAQHQQLKTGlfsgllktpafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:PRK09493 87 YLFPHLTALENVMFGPLRVRGAS--------------KEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-229 |
8.86e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMgVVRTFQHVRL--FREMTV 96
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 IENLLVAQHQQLKTGLFSGLLKTpafRRTQ------------EEALDraatwlDRIGLLQHANRQAsnlaygdqrrLEIV 164
Cdd:COG1101 100 EENLALAYRRGKRRGLRRGLTKK---RRELfrellatlglglENRLD------TKVGLLSGGQRQA----------LSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPKETKELDELIAEL-RDHHDTTiLLIEHDMK--LVMGisDRIYVVNQG 229
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTT-LMVTHNMEqaLDYG--NRLIMMHEG 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-248 |
1.12e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglpGQQIARMGVvrtfQHVRLFREMtVIE 98
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR--------GEPITKENI----REVRKFVGL-VFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NllvAQHQQLKTGLFSGLLKTPAFRRTQEEALD-RAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLD 177
Cdd:PRK13652 86 N---PDDQIFSPTVEQDIAFGPINLGLDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 178 EPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIR 248
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-235 |
1.30e-26 |
|
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: 103.18 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIML--------RDQHLeglpgqqiARMGVVRTfQHVRL 90
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpwkrRKKFL--------RRIGVVFG-QKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMTVIENLLVAQH-QQLKTGlfsgllktpAFRRTqeeaLDRAATWLDRIGLLqhaNRQASNLAYGDQRRLEIVRCMVT 169
Cdd:cd03267 107 WWDLPVIDSFYLLAAiYDLPPA---------RFKKR----LDELSELLDLEELL---DTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 170 QPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
1.37e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.58 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCL-------TGFYkpTGGTIMLRDQHLEGlPG 73
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEDIYD-PD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 74 QQI----ARMGVVrtFQHVRLFReMTVIENllVA----QHQQLKTGLFSGLLktpafrrtqEEALDRAATW---LDRIgl 142
Cdd:COG1117 85 VDVvelrRRVGMV--FQKPNPFP-KSIYDN--VAyglrLHGIKSKSELDEIV---------EESLRKAALWdevKDRL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 143 lqhaNRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdtTILLIEHDMKLVMGISDR 222
Cdd:COG1117 149 ----KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|..
gi 489958237 223 IYVVNQGTPLANGTPEEIRNNP 244
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNP 244
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-244 |
7.32e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCL------------TG--------FYKPTGGT 60
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGsivynghnIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 61 IMLRDQhleglpgqqiarMGVVrtFQHVRLFrEMTVIENLLVaqhqqlktGL-FSGLLKTPAFRRTQEEALDRAATWlDR 139
Cdd:PRK14239 82 VDLRKE------------IGMV--FQQPNPF-PMSIYENVVY--------GLrLKGIKDKQVLDEAVEKSLKGASIW-DE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 140 IGLLQHANrqASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGI 219
Cdd:PRK14239 138 VKDRLHDS--ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRI 213
|
250 260
....*....|....*....|....*
gi 489958237 220 SDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK14239 214 SDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-251 |
1.69e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.19 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPG---QQIARMGV 81
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRTFQHVRLFREMTVIENllvaqhqqlkTGLFSGLLKTPAFRRtQEEALDRaatwLDRIGLLQHANRQASNLAYGDQRRL 161
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDN----------TAFGMELAGINAEER-REKALDA----LRQVGLENYAHSYPDELSGGMRQRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 162 EIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 241
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
250
....*....|..
gi 489958237 242 NNP--DVIRAYL 251
Cdd:PRK10070 254 NNPanDYVRTFF 265
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-250 |
1.79e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.35 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQ-----IARMGVVRTFQHVRLFRE 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 mTVIENLLVAQHQqlktglfsgllktpaFRRTQEEALDRAATWLDRIGLLQHA-NRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PRK13643 101 -TVLKDVAFGPQN---------------FGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELrdhHDT--TILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIRAY 250
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESI---HQSgqTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-252 |
1.94e-25 |
|
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: 104.14 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkPTG---GTIMLRDQHLEGLPGQQIARMG 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAQHQQLKtglfSGLLKTPAFRRTQEEALDRAATWLDRIgllqhaNRQASNLAYGDQRR 160
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLP----GGRMAYNAMYLRAKNLLRELQLDADNV------TRPVGDYGGGQQQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANgTPEEI 240
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMST 227
|
250
....*....|..
gi 489958237 241 RNNPDVIRAYLG 252
Cdd:TIGR02633 228 MSEDDIITMMVG 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-244 |
4.35e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 7 VNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEG---LPGQQIA----RM 79
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQQKGLirqlRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVRTFQHVRLFREMTVIENLLVAQHQqlktglfsgLLKTPafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYGDQR 159
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPVI---------VKGEP-----KEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
....*
gi 489958237 240 IRNNP 244
Cdd:PRK11264 231 LFADP 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-254 |
6.36e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 6.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI--ARMGVVRTFQHVRLFR 92
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EMTVIENLLVAqhqqLKtglfsgLLKTPAfrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PRK11153 96 SRTVFDNVALP----LE------LAGTPK-----AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIRAY 250
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhPLTREF 240
|
....
gi 489958237 251 LGEA 254
Cdd:PRK11153 241 IQST 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-248 |
6.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.68 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRFGG--LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-AR 78
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 MGVVrtFQHV-RLFREMTV-------IENLLVAqhqqlktglfsgllktpafRRTQEEALDRAATwldRIGLLQHANRQA 150
Cdd:PRK13632 85 IGII--FQNPdNQFIGATVeddiafgLENKKVP-------------------PKKMKDIIDDLAK---KVGMEDYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 151 SNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMgISDRIYVVNQGT 230
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGK 219
|
250
....*....|....*...
gi 489958237 231 PLANGTPEEIRNNPDVIR 248
Cdd:PRK13632 220 LIAQGKPKEILNNKEILE 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-239 |
6.42e-25 |
|
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: 98.45 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM-GVVrtFQHVRLFRE 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMiGVV--LQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 mTVIENLlvaqhqqlktglfsgLLKTPAFRRTQEEALDRAATWLDRI-----GLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:cd03254 92 -TIMENI---------------RLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRdhHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE 239
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-223 |
1.07e-24 |
|
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: 97.33 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEglPGQQIARMGVVrtFQHVR--LFR 92
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYV--MQDVDyqLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EmTVIENLLVaqhqqlktglfsGLLKTPAfrrtqeeALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:cd03226 87 D-SVREELLL------------GLKELDA-------GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRI 223
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRV 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-240 |
1.61e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGL--LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 M-GVVrtFQHV-RLFREMTVIENllVAqhqqlktglFSglLKTPAFRRtqEEALDRAATWLDRIGLLQHANRQASNLAYG 156
Cdd:PRK13635 82 QvGMV--FQNPdNQFVGATVQDD--VA---------FG--LENIGVPR--EEMVERVDQALRQVGMEDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGT 236
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
....
gi 489958237 237 PEEI 240
Cdd:PRK13635 224 PEEI 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-235 |
2.22e-24 |
|
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: 96.79 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 29 KKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPgqqIARMGVVRTFQHVRLFREMTVIENLlvaqhqql 108
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNV-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 109 ktglfsGLLKTPAFRRT--QEEALDRAATwldRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPK 186
Cdd:cd03298 92 ------GLGLSPGLKLTaeDRQAIEVALA---RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489958237 187 ETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-235 |
2.60e-24 |
|
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: 96.67 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM 79
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVrtFQHVRLFREMTVIENLlvaqhqqlktGLFSGL--LKtpafRRTQEEALDRAAtwlDRIGLLQHANRQASNLAYGD 157
Cdd:cd03266 81 GFV--SDSTGLYDRLTARENL----------EYFAGLygLK----GDELTARLEELA---DRLGMEELLDRRVGGFSTGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-229 |
2.98e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.76 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImlrdqHLEGLPgQQIARM- 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-----LIDGQE-MRFASTt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 -----GVVRTFQHVRLFREMTVIENLLVAqhqQLKTGLfsGLLKTPAFRRtqeealdRAATWLDRIGLLQHANRQASNLA 154
Cdd:PRK11288 75 aalaaGVAIIYQELHLVPEMTVAENLYLG---QLPHKG--GIVNRRLLNY-------EAREQLEHLGVDIDPDTPLKYLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 155 YGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRA-EGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-229 |
3.92e-24 |
|
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: 95.19 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLmmrfGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGV 81
Cdd:cd03215 2 EPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 V-----RtfQHVRLFREMTVIENLLVAQhqqlktgLFSGllktpafrrtqeealdraatwldrigllqhanrqasnlayG 156
Cdd:cd03215 78 AyvpedR--KREGLVLDLSVAENIALSS-------LLSG----------------------------------------G 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-249 |
4.67e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.13 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPAFRRTQEEALDRAATWLDrigllqhANRQASNLAYGDQRR 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILF------------GLPKRQASMQKMKQLLAALGCQLD-------LDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
....*....
gi 489958237 241 RNNpDVIRA 249
Cdd:PRK15439 228 STD-DIIQA 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-243 |
4.82e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.01 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkpTGGTIMlrDQHLEgLPGQQIARMG 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGDKSA--GSHIE-LLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVR------------TFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPAFRRT-----QEEALDRAATWLDRIGLL 143
Cdd:PRK09984 76 RLArdirksrantgyIFQQFNLVNRLSVLENVLI------------GALGSTPFWRTcfswfTREQKQRALQALTRVGMV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 144 QHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRI 223
Cdd:PRK09984 144 HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERI 223
|
250 260
....*....|....*....|
gi 489958237 224 YVVNQGTPLANGTPEEIRNN 243
Cdd:PRK09984 224 VALRQGHVFYDGSSQQFDNE 243
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
15-253 |
5.11e-24 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 97.85 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVF---NCLtgfYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVrtFQHVRL 90
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLrmiNRL---IEPTSGRILIDGEDIRDLDPVELRRrIGYV--IQQIGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMTVIENL-LVAQhqqlktglfsgLLKTPafrrtQEEALDRAATWLDRIGL--LQHANRQASNLAYGDQRRLEIVRCM 167
Cdd:COG1125 88 FPHMTVAENIaTVPR-----------LLGWD-----KERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 168 VTQPEILMLDEPAAGLNPKETKEL-DELI---AELRdhhdTTILLIEHDMK--LVMGisDRIYVVNQGTPLANGTPEEIR 241
Cdd:COG1125 152 AADPPILLMDEPFGALDPITREQLqDELLrlqRELG----KTIVFVTHDIDeaLKLG--DRIAVMREGRIVQYDTPEEIL 225
|
250
....*....|....
gi 489958237 242 NNP--DVIRAYLGE 253
Cdd:COG1125 226 ANPanDFVADFVGA 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-230 |
5.23e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQH--LEGLPG-QQIA--RM 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSdKAIRelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVRTFQHVRLFREMTVIENLLVAQHQQLktglfsGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQR 159
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVL------GLSK--------DQALARAEKLLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTIlLIEHDMKLVMGISDRI------YVVNQGT 230
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKTASRVvymengHIVEQGD 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
1.23e-23 |
|
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: 97.05 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKP---TGGTIMLRDQHLEGLPGQQI 76
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 -----ARMGVVrtFQH-------VrlfreMTV----IENLLVaqHQQLktglfsgllktpafrrTQEEALDRAATWLDRI 140
Cdd:COG0444 81 rkirgREIQMI--FQDpmtslnpV-----MTVgdqiAEPLRI--HGGL----------------SKAEARERAIELLERV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 141 GL---LQHANR---QASnlayGDQR-RLEIVRCMVTQPEILMLDEPaaglnpkeTKELD--------ELIAELRDHHDTT 205
Cdd:COG0444 136 GLpdpERRLDRyphELS----GGMRqRVMIARALALEPKLLIADEP--------TTALDvtiqaqilNLLKDLQRELGLA 203
|
250 260
....*....|....*....|
gi 489958237 206 ILLIEHDMKLVMGISDRIYV 225
Cdd:COG0444 204 ILFITHDLGVVAEIADRVAV 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-243 |
1.30e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIM--------LRDQHLeglpgqqiARMGVV---RTfqh 87
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkRRKEFA--------RRIGVVfgqRS--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 88 vRLFREMTVIENLLvaqhqqlktglfsgLLK------TPAFRRTqeeaLDRAATWLDRIGLLqhaNRQASNLAYGdQR-R 160
Cdd:COG4586 106 -QLWWDLPAIDSFR--------------LLKaiyripDAEYKKR----LDELVELLDLGELL---DTPVRQLSLG-QRmR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
...
gi 489958237 241 RNN 243
Cdd:COG4586 243 KER 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-254 |
1.39e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 13 RFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDqhlEGLPGQQIARMGVVRTFQHVRLFR 92
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EMTVIENLlvaqhqqlKTGLfsGLLKTPafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PRK11432 92 HMSLGENV--------GYGL--KMLGVP-----KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD--VIRAY 250
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAsrFMASF 236
|
....
gi 489958237 251 LGEA 254
Cdd:PRK11432 237 MGDA 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-244 |
1.57e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTT---VFNCLTGFYKptggtimlrDQHLEG---LPGQQIAR 78
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTllrVFNRLIELYP---------EARVSGevyLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 MGVVRTFQHVRL-FREMTVIENLLVAQHQQLKTGLfSGLLKTPA--FRRTQEeALDRAATW---LDRIgllqhaNRQASN 152
Cdd:PRK14247 75 MDVIELRRRVQMvFQIPNPIPNLSIFENVALGLKL-NRLVKSKKelQERVRW-ALEKAQLWdevKDRL------DAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 153 LAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVNQGTPL 232
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
250
....*....|..
gi 489958237 233 ANGTPEEIRNNP 244
Cdd:PRK14247 225 EWGPTREVFTNP 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
10-235 |
1.72e-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: 94.28 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 10 LMMRFGGLLAVNNVNLDLH-KKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEG------LPGQQiARMGVV 82
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQ-RKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 rtFQHVRLFREMTVIENLLvaqhqqlktglFSGLLKTPAFRRTQEEALdraatwLDRIGLLQHANRQASNLAYGDQRRLE 162
Cdd:cd03297 81 --FQQYALFPHLNVRENLA-----------FGLKRKRNREDRISVDEL------LDLLGLDHLLNRYPAQLSGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNpKETKelDELIAELRDHH---DTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALD-RALR--LQLLPELKQIKknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-253 |
2.21e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.82 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 9 GLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRTFQhv 88
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFD-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 89 RLFREMTVIENLLV-AQHQQLKTglfsgllktpafrRTQEEALdraATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCM 167
Cdd:PRK13536 124 NLDLEFTVRENLLVfGRYFGMST-------------REIEAVI---PSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 168 VTQPEILMLDEPAAGLNPKET----KELDELIAELRdhhdtTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARhliwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
250
....*....|...
gi 489958237 244 P---DVIRAYLGE 253
Cdd:PRK13536 263 HigcQVIEIYGGD 275
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
10-240 |
8.40e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.11 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 10 LMMRFggllavnnvNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQ-HLEGLPGQQIARMgvvrTFQHV 88
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPSRRPVSM----LFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 89 RLFREMTVIENLLVaqhqqlktGLFSGLLKTPAFRRTQEEALDRaatwldrIGLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:PRK10771 81 NLFSHLTVAQNIGL--------GLNPGLKLNAAQREKLHAIARQ-------MGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-244 |
1.33e-22 |
|
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: 95.91 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF---GGLL--------AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkPTGGTIMLRDQHLEG 70
Cdd:COG4172 273 PPLLEARDLKVWFpikRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 71 LPGQQI----ARMGVVrtFQ------HVRLFREMTVIENLLVaqHQqlktglfsgllktPAFRRTQEEAldRAATWLDRI 140
Cdd:COG4172 352 LSRRALrplrRRMQVV--FQdpfgslSPRMTVGQIIAEGLRV--HG-------------PGLSAAERRA--RVAEALEEV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 141 GLL-QHANRqasnlaY-----GDQR-RLEIVRCMVTQPEILMLDEPaaglnpkeTKELD--------ELIAELRDHHDTT 205
Cdd:COG4172 413 GLDpAARHR------YphefsGGQRqRIAIARALILEPKLLVLDEP--------TSALDvsvqaqilDLLRDLQREHGLA 478
|
250 260 270
....*....|....*....|....*....|....*....
gi 489958237 206 ILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-241 |
1.47e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 91.43 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTIMLRDQHLEGLPGQQIARMGVV 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RTFQHVRLFREMTVIENLlvaqhQQLKTGlFSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLE 162
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL-----RYVNEG-FSG----------------------------------------GEKKRNE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGI-SDRIYVVNQGTPLANGTPEEIR 241
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELAL 193
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-240 |
2.36e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPG----QQI-ARMGVVRTFQHVRLFRE 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIrKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 mTVIENllVAQHQQlktglfsgllktpAFRRTQEEALDRAATWLDRIGLLQHA-NRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PRK13649 102 -TVLKD--VAFGPQ-------------NFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELrdHHD-TTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKL--HQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-240 |
2.42e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLE-GLPGQQIARMGVV 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RTFQHVRLFREMTVIENLLVAQHQQLktglfsGLLKTPAFRRtqeeaLDRAATWLDRigllQHANRQASN-LAYGDQRRL 161
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSLRNL------GVPEAEITRR-----VDEALTLVDA----QHFRHQPIQcLSHGQKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 162 EIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAEL--RDHHdttILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNH---VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
.
gi 489958237 240 I 240
Cdd:PRK13638 223 V 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-212 |
3.63e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 7 VNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglPGqqiARMGVVRtfQ 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-------KG---LRIGYLP--Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 87 HVRLFREMTVIENLLVAqhqqlktglFSGLLKTPAFRRTQEEALDRAATWLDRIGLLQHA-------------------- 146
Cdd:COG0488 69 EPPLDDDLTVLDTVLDG---------DAELRALEAELEELEAKLAEPDEDLERLAELQEEfealggweaearaeeilsgl 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 147 -------NRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPaaglnpkeTKELD-ELIAELRDH---HDTTILLIEHD 212
Cdd:COG0488 140 gfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEP--------TNHLDlESIEWLEEFlknYPGTVLVVSHD 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-213 |
4.65e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGlPGqqiARMGVVr 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PG---AERGVV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 tFQHVRLFREMTVIENllVAQHQQLktglfSGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEI 163
Cdd:PRK11248 76 -FQNEGLLPWRNVQDN--VAFGLQL-----AGVEK--------MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKETKELDELIaeLRDHHDT--TILLIEHDM 213
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLL--LKLWQETgkQVLLITHDI 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-229 |
5.76e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 94.30 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQ--HLEGLPGQQIAR 78
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 MGVVRtfQHVRLFREMTVIENllvaqhqqlktgLFSGLLKTPAFRRTQ-EEALDRAATWLDRIGLLQHANRQASNLAYGD 157
Cdd:PRK10762 81 IGIIH--QELNLIPQLTIAEN------------IFLGREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQG-RGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-250 |
6.53e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIML---------RDQHLEglPGQQiaRMGVVRTFQHVR 89
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditithktKDKYIR--PVRK--RIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 90 LFrEMTVIENLLVAQHQqlktglfsgllktpaFRRTQEEALDRAATWLDRIG----LLQHANRQASNlayGDQRRLEIVR 165
Cdd:PRK13646 98 LF-EDTVEREIIFGPKN---------------FKMNLDEVKNYAHRLLMDLGfsrdVMSQSPFQMSG---GQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 166 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 245
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
....*
gi 489958237 246 VIRAY 250
Cdd:PRK13646 239 KLADW 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-229 |
7.56e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRfgglLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGL-PGQQIARmG 80
Cdd:COG1129 254 EVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsPRDAIRA-G 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VV-----RtfQHVRLFREMTVIENLLVAQHQQLKTGLFsgllktpaFRRTQEEALdrAATWLDRIGL-LQHANRQASNLA 154
Cdd:COG1129 329 IAyvpedR--KGEGLVLDLSIRENITLASLDRLSRGGL--------LDRRRERAL--AEEYIKRLRIkTPSPEQPVGNLS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 155 YGDQRRLEIVRCMVTQPEILMLDEPaaglnpkeTKELD--------ELIAELRDhHDTTILLIEHDMKLVMGISDRIYVV 226
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEP--------TRGIDvgakaeiyRLIRELAA-EGKAVIVISSELPELLGLSDRILVM 467
|
...
gi 489958237 227 NQG 229
Cdd:COG1129 468 REG 470
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-243 |
8.64e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 17 LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI--MLRDQHLEGLPG--------------------- 73
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKekekvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 74 -QQI-ARMGVVRTFQHVRLFrEMTVIENLlvaqhqqlktgLFSGLlktpAFRRTQEEALDRAATWLDRIGL-LQHANRQA 150
Cdd:PRK13651 100 iKEIrRRVGVVFQFAEYQLF-EQTIEKDI-----------IFGPV----SMGVSKEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 151 SNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250
....*....|...
gi 489958237 231 PLANGTPEEIRNN 243
Cdd:PRK13651 243 IIKDGDTYDILSD 255
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-241 |
1.10e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.65 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 9 GLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEglPGQQIARMGVVRTFQHV 88
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--AGDIATRRRVGYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 89 RLFREMTVIENLLVaqHQQLktglfsgllktpaFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:NF033858 349 SLYGELTVRQNLEL--HARL-------------FHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIR 241
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALV 485
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-230 |
1.65e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.93 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 10 LMMR-----FGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkPTG---GTImlrdqHLEGLPGQ-----QI 76
Cdd:NF040905 2 LEMRgitktFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEI-----LFDGEVCRfkdirDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 ARMGVVRTFQHVRLFREMTVIENLLVAqHQQLKTGLFSgllktpafrrtQEEALDRAATWLDRIGLLQHANRQASNLAYG 156
Cdd:NF040905 76 EALGIVIIHQELALIPYLSIAENIFLG-NERAKRGVID-----------WNETNRRARELLAKVGLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTIlLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSI-IISHKLNEIRRVADSITVLRDGR 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-239 |
1.77e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 92.92 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARMGVVrtFQHVRLFrEMTVI 97
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLrRQIGVV--PQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENLLVAQHQqlktglfsgllktpafrRTQEE---ALDRAATWlDRI-----GLLQHANRQASNLAyGDQR-RLEIVRCMV 168
Cdd:COG1132 432 ENIRYGRPD-----------------ATDEEveeAAKAAQAH-EFIealpdGYDTVVGERGVNLS-GGQRqRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRdhHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE 239
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-226 |
2.08e-21 |
|
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: 92.73 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGG-LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLP----GQQIARM 79
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADadswRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GvvrtfQHVRLFrEMTVIENLLVAQHQQLKTGLfsgllktpafrrtqEEALDRAAtwLDRI------GLLQHANRQASNL 153
Cdd:TIGR02857 402 P-----QHPFLF-AGTIAENIRLARPDASDAEI--------------REALERAG--LDEFvaalpqGLDTPIGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 154 AYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdtTILLIEHDMKLvMGISDRIYVV 226
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLAL-AALADRIVVL 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-240 |
2.85e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVrtFQHVrlfremtv 96
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKhIGIV--FQNP-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 iENLLVAQHQQLKT--GLFSGLLKTPAFRRTQEEALDRaatwldrIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:PRK13648 93 -DNQFVGSIVKYDVafGLENHAVPYDEMHRRVSEALKQ-------VDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 175 MLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-249 |
9.07e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.25 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGG--TIMLRDQHLEglpGQQIARMGVVRTFQHV--RLF 91
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvKVMGREVNAE---NEKWVRSKVGLVFQDPddQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 rEMTVIENLLVAQHQQlktGLfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:PRK13647 94 -SSTVWDDVAFGPVNM---GL------------DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAELrDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPeEIRNNPDVIRA 249
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQ 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-245 |
1.00e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.30 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNC-------LTGFYkpTGGTIMLRDQHLEGL---PG 73
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR--VEGKVTFHGKNLYAPdvdPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 74 QQIARMGVVrtFQHVRLFREmTVIENLLVAQHQQLKTGLFSGLLktpafrrtqEEALDRAATWlDRIGllQHANRQASNL 153
Cdd:PRK14243 88 EVRRRIGMV--FQKPNPFPK-SIYDNIAYGARINGYKGDMDELV---------ERSLRQAALW-DEVK--DKLKQSGLSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 154 AYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdtTILLIEHDMKLVMGISDRIYVVN------ 227
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNvelteg 230
|
250 260
....*....|....*....|.
gi 489958237 228 ---QGTPLANGTPEEIRNNPD 245
Cdd:PRK14243 231 ggrYGYLVEFDRTEKIFNSPQ 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-247 |
1.08e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.86 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImLRDQHLeglpgqqiaRMG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKL---------RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTfqhvRLFREMTVieNLLVAQHQQLKTGLFSGLLkTPAFRRTQEEALDRAAtwldriglLQhanrqasNLAYGDQRR 160
Cdd:PRK09544 71 YVPQ----KLYLDTTL--PLTVNRFLRLRPGTKKEDI-LPALKRVQAGHLIDAP--------MQ-------KLSGGETQR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTpLANGTPEEI 240
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHI-CCSGTPEVV 207
|
....*..
gi 489958237 241 RNNPDVI 247
Cdd:PRK09544 208 SLHPEFI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-215 |
3.75e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF--GGLLA--VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIA 77
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 -----RMGVVRTFQHvrLFREMTVIEN----LLVAQhqqlktglfsgllKTPAfrrtqeEALDRAATWLDRIGLLQHANR 148
Cdd:PRK11629 83 elrnqKLGFIYQFHH--LLPDFTALENvampLLIGK-------------KKPA------EINSRALEMLAAVGLEHRANH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 149 QASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKL 215
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-197 |
5.40e-20 |
|
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: 84.72 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHL---EGLPGQQIARMGv 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 vrtfqHVR-LFREMTVIENLLVAQHqqlktglFSGllktpAFRRTQEEAldraatwLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:TIGR01189 80 -----HLPgLKPELSALENLHFWAA-------IHG-----GAQRTIEDA-------LAAVGLTGFEDLPAAQLSAGQQRR 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAE 197
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-240 |
5.86e-20 |
|
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: 88.32 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF-----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLR------DQHLEG 70
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 71 LPGQQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSG----LLKTPAFrrtqEEalDRAATWLDRIgllqha 146
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMkaviTLKMVGF----DE--EKAEEILDKY------ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 147 nrqASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVV 226
Cdd:TIGR03269 425 ---PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
250
....*....|....
gi 489958237 227 NQGTPLANGTPEEI 240
Cdd:TIGR03269 502 RDGKIVKIGDPEEI 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-230 |
7.79e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLR--------DQHLEGLPG 73
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGetvkigyfDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 74 qqiarmgvvrtfqhvrlfrEMTVIENLlvaqhQQLKTGLfsgllktpafrrTQEEALDRAATWL---DRigllqhANRQA 150
Cdd:COG0488 393 -------------------DKTVLDEL-----RDGAPGG------------TEQEVRGYLGRFLfsgDD------AFKPV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 151 SNLAYGDQRRLEIVRCMVTQPEILMLDEPaaglnpkeTKELD----ELIAELRDHHDTTILLIEHDMKLVMGISDRIYVV 226
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEP--------TNHLDietlEALEEALDDFPGTVLLVSHDRYFLDRVATRILEF 502
|
....
gi 489958237 227 NQGT 230
Cdd:COG0488 503 EDGG 506
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-244 |
8.91e-20 |
|
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: 87.82 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGG----LLAVNNVNLDLHKKEIVSLIGPNGAGKT----TVFNCLTGFYKPTGGTIMLRDQHLEGLP 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 73 GQQI-----ARMGVVrtFQhvrlfrE-MT-----------VIENLLVaqHQQLktglfsgllktpafrrTQEEALDRAAT 135
Cdd:COG4172 83 ERELrrirgNRIAMI--FQ------EpMTslnplhtigkqIAEVLRL--HRGL----------------SGAAARARALE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 136 WLDRIGLLQHANRQAsnlAY-----GDQR-RLEIVRCMVTQPEILMLDEPaaglnpkeTKELD--------ELIAELRDH 201
Cdd:COG4172 137 LLERVGIPDPERRLD---AYphqlsGGQRqRVMIAMALANEPDLLIADEP--------TTALDvtvqaqilDLLKDLQRE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489958237 202 HDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:COG4172 206 LGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-229 |
1.49e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQH-----LEGLPGQQ 75
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 76 IARM-----GVVRtfQHVRLFREMTVI------ENLLV--AQHqqlktglfsgllktpaFRRTQEEALDraatWLDRIGL 142
Cdd:PRK11701 83 RRRLlrtewGFVH--QHPRDGLRMQVSaggnigERLMAvgARH----------------YGDIRATAGD----WLERVEI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 143 lqHANR---QASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGI 219
Cdd:PRK11701 141 --DAARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLL 218
|
250
....*....|
gi 489958237 220 SDRIYVVNQG 229
Cdd:PRK11701 219 AHRLLVMKQG 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-244 |
1.68e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTG-----GTIMLRDQHL-EGLPGQQI 76
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 ARMGVVRTFQHVRLFrEMTVIENL-----LVAQHQQLKtglFSGLLktpafrrtqEEALDRAATWlDRIGLLQHanRQAS 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLF-PMSVYDNVaygvkIVGWRPKLE---IDDIV---------ESALKDADLW-DEIKHKIH--KSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 152 NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISD--RIYVVNQ- 228
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDftAFFKGNEn 229
|
250
....*....|....*...
gi 489958237 229 --GTPLANGTPEEIRNNP 244
Cdd:PRK14258 230 riGQLVEFGLTKKIFNSP 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-249 |
2.53e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 6 SVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVRT 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHV--RLfremTVIEnlLVA----QHQQlktGlfsgllktpafRRTQE--EALDRAatwLDRIGLLQHANRQASNLAyG 156
Cdd:COG4604 83 ENHInsRL----TVRE--LVAfgrfPYSK---G-----------RLTAEdrEIIDEA---IAYLDLEDLADRYLDELS-G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 157 DQR-RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:COG4604 139 GQRqRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
250
....*....|....
gi 489958237 236 TPEEIRnNPDVIRA 249
Cdd:COG4604 219 TPEEII-TPEVLSD 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-229 |
2.79e-19 |
|
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: 83.29 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMlrdqhLEGLPGQQiarmgvvrtFQHVRLFREMTVI 97
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL-----LDGKPISQ---------YEHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENLLVAQHQQLKTGLFSGLLKTPAFRRTqeEALDRAATWlDRIGLLQH-----ANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQSCSFECVK--EAAQKAHAH-SFISELASgydteVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAElrDHHDTTILLIEHDMKLVMGiSDRIYVVNQG 229
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
3.09e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 86.26 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF-GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARmg 80
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTF-QHVRLFrEMTVIENLLVAqhqqlktglfsgllktpafrrtQEEALDRAATW-LDRIGLLQHANR---------- 148
Cdd:TIGR02868 410 RVSVCaQDAHLF-DTTVRENLRLA----------------------RPDATDEELWAaLERVGLADWLRAlpdgldtvlg 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 149 -QASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETkelDELIAELRDHHD-TTILLIEHD 212
Cdd:TIGR02868 467 eGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA---DELLEDLLAALSgRTVVLITHH 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-229 |
4.68e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLsVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImlrdqhLEGLPGQQIARMGVV 82
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RTFQHVRLFREMTVIENLlvaqhqqlktglfsGLLKTPAFRRTQEEALDRaatwldrIGLLQHANRQASNLAYGDQRRLE 162
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNV--------------GLGLKGQWRDAALQALAA-------VGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-249 |
5.16e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMlrdqhLEGLPgqqiarmgvVRTFQHVRLFREMTvienlL 101
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL-----LDGVP---------LVQYDHHYLHRQVA-----L 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 102 VAQHQQLKTGLFS-----GLLKTPafrRTQEEALDRAATWLDRIGLLQHA-----NRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:TIGR00958 560 VGQEPVLFSGSVReniayGLTDTP---DEEIMAAAKAANAHDFIMEFPNGydtevGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 172 EILMLDEPAAGLNpketKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVIRA 249
Cdd:TIGR00958 637 RVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-247 |
8.40e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFY-KPTGGTIMLRDQHLEGLPG-QQIARM----GVVRTFQHVRLFR 92
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIVGDYAIPANLKKiKEVKRLrkeiGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EmtVIENLLVAQHQQLKTglfsgllktpafrrTQEEALDRAATWLDRIGLLQ-HANRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGE--------------NKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVI 247
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-239 |
9.79e-19 |
|
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: 82.28 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVRtfQHVRLFREmTVI 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRqIGLVS--QDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENLLVAQHqqlktglfsgllktpafRRTQEEALD--RAATWLDRI-----GLLQHANRQASNLAYGDQRRLEIVRCMVTQ 170
Cdd:cd03251 94 ENIAYGRP-----------------GATREEVEEaaRAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 171 PEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE 239
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
1.05e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF--GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-AR 78
Cdd:PRK11160 336 QVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALrQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 79 MGVVRtfQHVRLFREmTVIENLLVAQHQ----QL-----KTGLfSGLLktpafrrTQEEALDraaTWLDRIGllqhanRQ 149
Cdd:PRK11160 416 ISVVS--QRVHLFSA-TLRDNLLLAAPNasdeALievlqQVGL-EKLL-------EDDKGLN---AWLGEGG------RQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 150 ASNlayGDQRRLEIVRCMVTQPEILMLDEPAAGLNpKETKEldELIAELRDH-HDTTILLIEHDMKLvMGISDRIYVVNQ 228
Cdd:PRK11160 476 LSG---GEQRRLGIARALLHDAPLLLLDEPTEGLD-AETER--QILELLAEHaQNKTVLMITHRLTG-LEQFDRICVMDN 548
|
250
....*....|.
gi 489958237 229 GTPLANGTPEE 239
Cdd:PRK11160 549 GQIIEQGTHQE 559
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-245 |
1.24e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTV---FNCL---------TGFYKPTGGTIMLRDQHl 68
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLlelneearvEGEVRLFGRNIYSPDVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 69 eglPGQQIARMGVVrtFQHVRLFREMTVIENLLVAqhqqLKtglFSGLLKTPA-FRRTQEEALDRAATW---LDRIgllq 144
Cdd:PRK14267 80 ---PIEVRREVGMV--FQYPNPFPHLTIYDNVAIG----VK---LNGLVKSKKeLDERVEWALKKAALWdevKDRL---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 145 haNRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGISDRIY 224
Cdd:PRK14267 144 --NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVA 219
|
250 260
....*....|....*....|.
gi 489958237 225 VVNQGTPLANGTPEEIRNNPD 245
Cdd:PRK14267 220 FLYLGKLIEVGPTRKVFENPE 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-240 |
1.87e-18 |
|
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: 84.08 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTIMLRDQHLE-----GLP---GQ 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEkcgyvERPskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 75 Q-----------------------------IARMgVVRTFQhvrLFREMTVIENLLVAQHQQLKTGlfsgllktpafrrt 125
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsdklrrrirkrIAIM-LQRTFA---LYGDDTVLDNVLEALEEIGYEG-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 126 qEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTT 205
Cdd:TIGR03269 143 -KEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS 221
|
250 260 270
....*....|....*....|....*....|....*
gi 489958237 206 ILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:TIGR03269 222 MVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-252 |
3.19e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 10 LMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVRtfQHV 88
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARrIGLLA--QNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 89 RLFREMTVIEnlLVAQHQQLKTGLFSgllktpAFRRTQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:PRK10253 91 TTPGDITVQE--LVARGRYPHQPLFT------RWRKEDEEAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRnNPDVIR 248
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-TAELIE 238
|
....
gi 489958237 249 AYLG 252
Cdd:PRK10253 239 RIYG 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-235 |
4.80e-18 |
|
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: 79.94 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMlrdqhLEGLPGQQI------ARMGVVRtfQHVRLFR 92
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-----LDGTDIRQLdpadlrRNIGYVP--QDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EmTVIENLlvaqhqqlktglfsgLLKTPAfrrTQEEALDRAATwldRIGLLQHANRQASNLAY----------GDQRRL- 161
Cdd:cd03245 92 G-TLRDNI---------------TLGAPL---ADDERILRAAE---LAGVTDFVNKHPNGLDLqigergrglsGGQRQAv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 162 EIVRCMVTQPEILMLDEPAAGL-NPKETKELDELIAELRdhhDTTILLIEHDMKLvMGISDRIYVVNQGTPLANG 235
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMdMNSEERLKERLRQLLG---DKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-244 |
5.19e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 14 FGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGqqiARMGVVRTFQHVRLFRE 93
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 MTVIENLLVAqhqqLKtglFSGLLKTPAFRRTQEealdrAATWLDRIGLLQhanRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK11000 90 LSVAENMSFG----LK---LAGAKKEEINQRVNQ-----VAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 174 LMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-244 |
5.34e-18 |
|
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: 80.11 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKP----TGGTIMLRDQHLEGLPGQQIArmgVVRTFQHvrlfrEM 94
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRH---IATIMQN-----PR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 95 TVIENLLVAQHQQLKTGLFSGllktpafrRTQEEALDRAATWLDRIGLLQHA---NRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:TIGR02770 73 TAFNPLFTMGNHAIETLRSLG--------KLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEP 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:TIGR02770 145 PFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-244 |
6.12e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.68 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRFG-------------GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHL 68
Cdd:PRK15079 6 KVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 69 EGLPGQQI--ARMGVVRTFQH--VRLFREMTVIEnlLVAQHqqlktglfsglLKTPAFRRTQEEALDRAATWLDRIGLLQ 144
Cdd:PRK15079 86 LGMKDDEWraVRSDIQMIFQDplASLNPRMTIGE--IIAEP-----------LRTYHPKLSRQEVKDRVKAMMLKVGLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 145 HA-NRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRI 223
Cdd:PRK15079 153 NLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 232
|
250 260
....*....|....*....|.
gi 489958237 224 YVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHNP 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-240 |
7.75e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRT 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 FQHvrLFRE-MTVIEnlLVAQHQQLKTGLFSGLlktpafRRTQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRRLEI 163
Cdd:PRK11231 83 QHH--LTPEgITVRE--LVAYGRSPWLSLWGRL------SAEDNARVNQA---MEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 164 VRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIeHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL-HDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-229 |
8.09e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 11 MMRF--------GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIA--RMG 80
Cdd:PRK10908 1 MIRFehvskaylGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVRTFQHVRLFREMTVIENLLVAqhqqlktglfsgLLKTPAfrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIP------------LIIAGA---SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELrDHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-240 |
8.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.52 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLR--DQHLEGLPGQQIARMGVVrtFQH-----VRL 90
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENLWDIRNKAGMV--FQNpdnqiVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMTVI---ENLLVAQHQqlktglfsgllktpaFRRTQEEALDRAATWLDRigllqhanRQASNLAYGDQR-RLEIVRC 166
Cdd:PRK13633 102 IVEEDVAfgpENLGIPPEE---------------IRERVDESLKKVGMYEYR--------RHAPHLLSGGQKqRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 167 MVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-244 |
1.69e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRF---GGLL--------AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEG 70
Cdd:PRK10261 311 EPILQVRNLVTRFplrSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 71 LPGQQIA--RMGVVRTFQ--HVRLFREMTV----IENLLVAqhqqlktGLFSGllktpafrrtqEEALDRAATWLDRIGL 142
Cdd:PRK10261 391 LSPGKLQalRRDIQFIFQdpYASLDPRQTVgdsiMEPLRVH-------GLLPG-----------KAAAARVAWLLERVGL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 143 L-QHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISD 221
Cdd:PRK10261 453 LpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISH 532
|
250 260
....*....|....*....|...
gi 489958237 222 RIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK10261 533 RVAVMYLGQIVEIGPRRAVFENP 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-240 |
1.71e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMR-FGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMG 80
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 81 VVrtfqHV---RLFR----EMTVIENLLVAQHqqlKTGLFS--GLLKTPAFRRTQEEALD----RAATwldrigllqhAN 147
Cdd:COG3845 335 VA----YIpedRLGRglvpDMSVAENLILGRY---RRPPFSrgGFLDRKAIRAFAEELIEefdvRTPG----------PD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 148 RQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVN 227
Cdd:COG3845 398 TPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMY 476
|
250
....*....|....*...
gi 489958237 228 QG-----TPLANGTPEEI 240
Cdd:COG3845 477 EGrivgeVPAAEATREEI 494
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-202 |
2.82e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLE-GLPGQQIARMGv 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 vrtfqHVR-LFREMTVIENLLVAQhqqlktglfsgllktpAFRRTQEEALDRAatwLDRIGLLQHANRQASNLAYGDQRR 160
Cdd:PRK13539 80 -----HRNaMKPALTVAENLEFWA----------------AFLGGEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNpketKELDELIAELRDHH 202
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALD----AAAVALFAELIRAH 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-244 |
2.92e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.98 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFY-KPTG----GTIMLRDQHLEGLPGQQIA 77
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 RMGVVRTFQHVRLFrEMTVIENLL--VAQHQQLKTGLFSGLlktpafrrtqeealdrAATWLDRIGLLQHANRQASN--- 152
Cdd:PRK14271 100 RRRVGMLFQRPNPF-PMSIMDNVLagVRAHKLVPRKEFRGV----------------AQARLTEVGLWDAVKDRLSDspf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 153 -LAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHhdTTILLIEHDMKLVMGISDRIYVVNQGTP 231
Cdd:PRK14271 163 rLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRL 240
|
250
....*....|...
gi 489958237 232 LANGTPEEIRNNP 244
Cdd:PRK14271 241 VEEGPTEQLFSSP 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-240 |
3.27e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRF---GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIA 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 R-MGVVrtFQHV-RLFREMTVIENLLVAQHQQlktGLfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAY 155
Cdd:PRK13642 81 RkIGMV--FQNPdNQFVGATVEDDVAFGMENQ---GI------------PREEMIKRVDEALLAVNMLDFKTREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 156 GDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANG 235
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
....*
gi 489958237 236 TPEEI 240
Cdd:PRK13642 223 APSEL 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-229 |
6.35e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.39 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 14 FGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRTFQHVRLFRE 93
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 MTVIENLLVAQHQqlKTGLFSgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK10982 88 RSVMDNMWLGRYP--TKGMFV----------DQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 174 LMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-242 |
6.58e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI 76
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 77 ARM-----GVVrtFQHVRLFREMTVIENLLVAqhqqlktGLFSGLLKtpafrrtqEEALDRAATWLDRIGLLQHANRQAS 151
Cdd:PRK10535 81 AQLrrehfGFI--FQRYHLLSHLTAAQNVEVP-------AVYAGLER--------KQRLLRAQELLQRLGLEDRVEYQPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 152 NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTIlLIEHDmKLVMGISDRIYVVNQGTP 231
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVI-IVTHD-PQVAAQAERVIEIRDGEI 221
|
250
....*....|.
gi 489958237 232 LANGTPEEIRN 242
Cdd:PRK10535 222 VRNPPAQEKVN 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-244 |
1.74e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.46 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKT-TVFnCLTGFYKPTG---GTIMLRDQHLEGLP 72
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 73 GQQIARMgvvRTFQHVRLFRE--------MTVIENLL-VAQhqqlktgLFSGLLKTPAFrrtqEEA---LD--RAATWLD 138
Cdd:PRK09473 88 EKELNKL---RAEQISMIFQDpmtslnpyMRVGEQLMeVLM-------LHKGMSKAEAF----EESvrmLDavKMPEARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 139 RIGLLQHanrqasNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMG 218
Cdd:PRK09473 154 RMKMYPH------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAG 227
|
250 260
....*....|....*....|....*.
gi 489958237 219 ISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK09473 228 ICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-248 |
2.96e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPtggtimlrdqhlEGLPGQQIARMGVVRTFQHVRLFREMTVIe 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP------------DDNPNSKITVDGITLTAKTVWDIREKVGI- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 nllVAQHQQLKtglFSGL---------LKTPAFRRTQEEALDRAAtwLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVT 169
Cdd:PRK13640 89 ---VFQNPDNQ---FVGAtvgddvafgLENRAVPRPEMIKIVRDV--LADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 170 QPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVIR 248
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-229 |
3.46e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRF--GGLLA-------VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPG 73
Cdd:PRK10419 2 TLLNVSGLSHHYahGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 74 QQIarmgvvRTFQH-VRLfremtVIENLLVAQHQQLKTGlfsGLLKTPAFRRT---QEEALDRAATWLDRIGL-LQHANR 148
Cdd:PRK10419 82 AQR------KAFRRdIQM-----VFQDSISAVNPRKTVR---EIIREPLRHLLsldKAERLARASEMLRAVDLdDSVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 149 QASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQ 228
Cdd:PRK10419 148 RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
.
gi 489958237 229 G 229
Cdd:PRK10419 228 G 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-244 |
4.25e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.47 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLegLPGQQIARMGVVR-------TFQHVRLFR 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQIDAIKlrkevgmVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EMTVIENLLVAqhqqLKTglfSGLLKTPAFRRTQEEALDRAATWLDrigLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PRK14246 104 HLSIYDNIAYP----LKS---HGIKEKREIKKIVEECLRKVGLWKE---VYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-254 |
5.80e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRF---GGLL------AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLE-- 69
Cdd:PRK15112 1 VETLLEVRNLSKTFryrTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 70 --GLPGQQIaRMgvvrtfqhvrLFREMTVIENllvaQHQQLktglfSGLLKTPAFRRTQEEALDRAA---TWLDRIGLL- 143
Cdd:PRK15112 81 dySYRSQRI-RM----------IFQDPSTSLN----PRQRI-----SQILDFPLRLNTDLEPEQREKqiiETLRQVGLLp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 144 QHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRI 223
Cdd:PRK15112 141 DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQV 220
|
250 260 270
....*....|....*....|....*....|....*..
gi 489958237 224 YVVNQGTPLANGTPEEIRNNP------DVIRAYLGEA 254
Cdd:PRK15112 221 LVMHQGEVVERGSTADVLASPlheltkRLIAGHFGEA 257
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-239 |
8.85e-16 |
|
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: 74.11 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 21 NNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARMGVVRtfQHVRLFrEMTVIEN 99
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrSQIGLVS--QEPVLF-DGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 100 LLVAqhqqlktglfsgllktpAFRRTQEEALD--RAATWLDRI-----GLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:cd03249 97 IRYG-----------------KPDATDEEVEEaaKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 173 ILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE 239
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-229 |
1.02e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRTFQHVR---LFREMT 95
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVAQHQQLKTGLfsGLLKTPAFRRTQEEALDRAatwldRIGLLQHANRQASnLAYGDQRRLEIVRCMVTQPEILM 175
Cdd:PRK10982 343 IGFNSLISNIRNYKNKV--GLLDNSRMKSDTQWVIDSM-----RVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-252 |
1.85e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 1 MKPLLSVNGLMMRF-GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleGLPGQQIARM 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIL-----GQPTRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVrtfQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLktpafRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQR 159
Cdd:PRK15056 78 NLV---AYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWL-----RRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 160 RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVnQGTPLANGTPEE 239
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTET 227
|
250
....*....|...
gi 489958237 240 IRNNPDVIRAYLG 252
Cdd:PRK15056 228 TFTAENLELAFSG 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-229 |
2.09e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRTFQHVR---LFREMTV 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 IENL-LVA-----------QHQ--QLKTGLFSGL--LKTPAfrRTQeealdraatwldRIGllqhanrqasNLAYGDQRR 160
Cdd:PRK10762 348 KENMsLTAlryfsraggslKHAdeQQAVSDFIRLfnIKTPS--MEQ------------AIG----------LLSGGNQQK 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-237 |
2.84e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 72.53 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRF--GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQI-ARMGV 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRtfQHVRLFrEMTVIENLlvaqhqqlktglfsgllktPAFRRTQEEALDRAatwLDRIGLLQHANRQA----------- 150
Cdd:cd03244 83 IP--QDPVLF-SGTIRSNL-------------------DPFGEYSDEELWQA---LERVGLKEFVESLPggldtvveegg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 151 SNLAYGdQRRL-EIVRCMVTQPEILMLDEPAAGLNPketkELDELIAE-LRDH-HDTTILLIEHDMKLVMGiSDRIYVVN 227
Cdd:cd03244 138 ENLSVG-QRQLlCLARALLRKSKILVLDEATASVDP----ETDALIQKtIREAfKDCTVLTIAHRLDTIID-SDRILVLD 211
|
250
....*....|
gi 489958237 228 QGTPLANGTP 237
Cdd:cd03244 212 KGRVVEFDSP 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-241 |
3.03e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.00 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTtvfncltgfykptggtimlRDQHLEGLPGQQIARmgvvrt 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------------RGALPAHV*GPDAGR------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fqhvRLFREMTVIENL-----LVAQHQQLKTGL---FSGLLKTPAFRR----TQEEALDRAATWLDRIGLLQHANRQASN 152
Cdd:NF000106 69 ----RPWRF*TWCANRralrrTIG*HRPVR*GRresFSGRENLYMIGR*ldlSRKDARARADELLERFSLTEAAGRAAAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 153 LAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKEL-DELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVNQGTP 231
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRD--GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
250
....*....|
gi 489958237 232 LANGTPEEIR 241
Cdd:NF000106 223 IADGKVDELK 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-185 |
3.44e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.30 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 17 LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTG---FYKPTGGTIMLRDQHLEglPGQQIARMGVVRtfQHVRLFRE 93
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRK--PDQFQKCVAYVR--QDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 MTVIENLLVAQHqqlktglFSGLLKTPAFRRTQEEALDRaatwLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:cd03234 96 LTVRETLTYTAI-------LRLPRKSSDAIRKKRVEDVL----LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170
....*....|..
gi 489958237 174 LMLDEPAAGLNP 185
Cdd:cd03234 165 LILDEPTSGLDS 176
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-227 |
4.57e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 23 VNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM---GVVRTFQHVRLFREMTVIEN 99
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 100 LlvaqhqQLktglfsgllktPAFRR--TQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLD 177
Cdd:PRK10584 109 V------EL-----------PALLRgeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489958237 178 EPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVN 227
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-244 |
8.25e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI----ML---RDQHLEGLP 72
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLlrrRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 73 GQQIARMGVVRTFQHVRLFRE-MTVIENLL-----VAQHQQLKTGLfsgllktpafrrTQEEALDRAATWLDRIGLLQHA 146
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEpMTSLNPVFtvgeqIAESIRLHQGA------------SREEAMVEAKRMLDQVRIPEAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 147 ---NRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRI 223
Cdd:PRK10261 160 tilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
250 260
....*....|....*....|.
gi 489958237 224 YVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIFHAP 260
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-240 |
9.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.07 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIAR-MGVVrtFQHV-RLFREMTV- 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHkIGMV--FQNPdNQFVGATVe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 ------IENLLVAqHQQLKtglfsgllktpafRRTQEEaldraatwLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQ 170
Cdd:PRK13650 101 ddvafgLENKGIP-HEEMK-------------ERVNEA--------LELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 171 PEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-252 |
9.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRTFQHVRL-FREM 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 95 TVIENLLVAQHQqlktglfsgLLKTPAFRRTQeeaLDRAatwLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:PRK13644 94 TVEEDLAFGPEN---------LCLPPIEIRKR---VDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 175 MLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKlVMGISDRIYVVNQGTPLANGTPEEIRNNPDVirAYLG 252
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSL--QTLG 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-253 |
1.25e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.21 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHL------EGLPGQQiARMGVVrtFQHVRLFREMT 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgICLPPEK-RRIGYV--FQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLlvaqhqqlKTGLfsgllktpafRRTQEEALDRAATWLDRIGLLqhaNRQASNLAYGDQRRLEIVRCMVTQPEILM 175
Cdd:PRK11144 93 VRGNL--------RYGM----------AKSMVAQFDKIVALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPdVIRAYLGE 253
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS-AMRPWLPK 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-229 |
1.38e-14 |
|
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: 69.65 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRtfQHVRLFrEMTVI 97
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLN--QRPYLF-DTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENLlvaqhqqlktGL-FSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLEIVRCMVTQPEILML 176
Cdd:cd03247 93 NNL----------GRrFSG----------------------------------------GERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 177 DEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKlvmGIS--DRIYVVNQG 229
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT---GIEhmDKILFLENG 172
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-230 |
1.41e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImlrdqhleglpgqqiarmgvvrt 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fqhvrlfremTVIENLLVAQHQQLktglfSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLEIV 164
Cdd:cd03221 58 ----------TWGSTVKIGYFEQL-----SG----------------------------------------GEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 165 RCMVTQPEILMLDEPAAGLNPkETKELdeLIAELRDHHDtTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDL-ESIEA--LEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-240 |
2.60e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIML-----RDQHLEGLPgQQIArmgVVRtfQHVRLFR 92
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlRDYTLASLR-NQVA---LVS--QNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 93 EmTVIENLLVAQHQQlktglfsgllktpaFRRTQEEALDRAATWLDRIGLLQHA-----NRQASNLAYGDQRRLEIVRCM 167
Cdd:PRK11176 431 D-TIANNIAYARTEQ--------------YSREQIEEAARMAYAMDFINKMDNGldtviGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 168 VTQPEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-229 |
3.23e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVV---RTFQHVRLFREMTVIE 98
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpEDRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVAQHQQLktglfsGLLKTPAFRRTQEEALDRAatwldrIGL-LQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLD 177
Cdd:PRK15439 361 NVCALTHNRR------GFWIKPARENAVLERYRRA------LNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489958237 178 EPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-229 |
4.03e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKptG---GTIMLRDQHLE-GLPGQQIA-----------RMGVVRt 84
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKiRNPQQAIAqgiamvpedrkRDGIVP- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fqhvrlfrEMTVIENLLVAQHQQLKTGlfsGLLKTPAFRRTQEEALDR----AATWLDRIGLLQHANRQASNLAygdqrr 160
Cdd:PRK13549 355 --------VMGVGKNITLAALDRFTGG---SRIDDAAELKTILESIQRlkvkTASPELAIARLSGGNQQKAVLA------ 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 161 leivRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK13549 418 ----KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-250 |
5.91e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 31 EIVSLIGPNGAGKTTVFNCLTGFYkPTGGTIMLRDQHLEGLPGQQIARMgvvRTF--QHVRLFREMTVIENLlvAQHQql 108
Cdd:PRK03695 23 EILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARH---RAYlsQQQTPPFAMPVFQYL--TLHQ-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 109 ktglfsgllktPAFRRTQ--EEALDRAAtwlDRIGLLQHANRQASNLAYGD-QR-RLEIVrCMVTQPEI------LMLDE 178
Cdd:PRK03695 95 -----------PDKTRTEavASALNEVA---EALGLDDKLGRSVNQLSGGEwQRvRLAAV-VLQVWPDInpagqlLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 179 PAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIRAY 250
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-241 |
6.58e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.97 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 26 DLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImlrdqhleGLPGQQIARMGvvrtfQHVRLFREMTVienllvaqh 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDTVSYKP-----QYIKADYEGTV--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 106 QQLKTGLFSGLLKTPAFRrtqeealdraATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNP 185
Cdd:cd03237 79 RDLLSSITKDFYTHPYFK----------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 186 KETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIyVVNQGTPLANG---TPEEIR 241
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGvanPPQSLR 206
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-240 |
6.76e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.10 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 31 EIVSLIGPNGAGKTTVFNCLTGFYkPTGGTIMLRDQHLEGLPGQQIARMgvvRTF--QHVRLFREMTVIENLlvAQHQQL 108
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARH---RAYlsQQQSPPFAMPVFQYL--ALHQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 109 KTglfsgllktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVT-------QPEILMLDEPAA 181
Cdd:COG4138 97 GA--------------SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 182 GLNPKETKELDELIAELRDHHDTTILLIeHDMKLVMGISDRIYVVNQGTPLANGTPEEI 240
Cdd:COG4138 163 SLDVAQQAALDRLLRELCQQGITVVMSS-HDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-241 |
7.95e-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: 70.81 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLrdqhleglPGQQIArMGVVRTFQHVRLFREMTVIE 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--------AGKSIL-TNISDVHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVAQHQQLktgLFSGLLKTPAfrrtqeEALDRAATW-LDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLD 177
Cdd:TIGR01257 2025 DLLTGREHLY---LYARLRGVPA------EEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 178 EPAAGLNPKETKEL-DELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 241
Cdd:TIGR01257 2096 EPTTGMDPQARRMLwNTIVSIIRE--GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-212 |
1.19e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIaRMGV 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-RQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRTFQHVRLFREmTVIENLLVaqhqqlktglfsgllktPAFRRTQEEALDRAATWLDRIGLLQHANRQASN-LAYGDQRR 160
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIF-----------------PWQIRNQQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHD 212
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-252 |
1.63e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 31 EIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMgVVRTFQHVRLFREMTVIEnlLVA-----QH 105
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRE--LVAigrypWH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 106 QQLktGLFSGllktpAFRRTQEEALDRaatwldrIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNP 185
Cdd:PRK10575 115 GAL--GRFGA-----ADREKVEEAISL-------VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 186 KETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRnNPDVIRAYLG 252
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM-RGETLEQIYG 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-229 |
1.65e-13 |
|
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: 66.47 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGL--LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMlrdqhLEGLPGQQIARMGVV 82
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----LDGADISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 RTF----QHVRLFrEMTVIENLLvaqhqqlktglfSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQ 158
Cdd:cd03246 76 DHVgylpQDDELF-SGSIAENIL------------SG----------------------------------------GQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958237 159 RRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVmGISDRIYVVNQG 229
Cdd:cd03246 103 QRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDG 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-244 |
1.78e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRF---GGLL--------AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkPTGGTIMLRDQHLEGL 71
Cdd:PRK15134 274 PLLDVEQLQVAFpirKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 72 PGQQI----ARMGVVrtFQ------HVRLFREMTVIENLLVaqHQqlktglfsgllktPAFRRTQEEAldRAATWLDRIG 141
Cdd:PRK15134 353 NRRQLlpvrHRIQVV--FQdpnsslNPRLNVLQIIEEGLRV--HQ-------------PTLSAAQREQ--QVIAVMEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 142 L---LQHanRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMG 218
Cdd:PRK15134 414 LdpeTRH--RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRA 491
|
250 260
....*....|....*....|....*.
gi 489958237 219 ISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK15134 492 LCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-229 |
2.11e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRF--GGLL--AVNNVNLDLHKKEIVSLIGPNGAGKT-TVFNCLTGFYKP----TGGTIMLR--------D 65
Cdd:PRK15134 4 PLLAIENLSVAFrqQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHgesllhasE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 66 QHLEGLPGQQIARmgvvrtfqhvrLFREMTVIENLLVAQHQQLKT--GLFSGLLKTPAfrrtQEEALDraatWLDRIGLL 143
Cdd:PRK15134 84 QTLRGVRGNKIAM-----------IFQEPMVSLNPLHTLEKQLYEvlSLHRGMRREAA----RGEILN----CLDRVGIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 144 QHANRQAS---NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGIS 220
Cdd:PRK15134 145 QAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLA 224
|
....*....
gi 489958237 221 DRIYVVNQG 229
Cdd:PRK15134 225 DRVAVMQNG 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-196 |
2.12e-13 |
|
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: 66.75 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEglpgqqiarmgvvrt 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fqhvrlFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRTQeealDRAATW--LDRIGLLQHANRQASNLAYGDQRRLE 162
Cdd:cd03231 66 ------FQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADH----SDEQVEeaLARVGLNGFEDRPVAQLSAGQQRRVA 135
|
170 180 190
....*....|....*....|....*....|....
gi 489958237 163 IVRCMVTQPEILMLDEPAAGLNPKETKELDELIA 196
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-251 |
2.91e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglpGQQIARMGVVRTFQHvrlfrEMTVIE 98
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN--------GRVSALLELGAGFHP-----ELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVAqhqqlktGLFSGLlktpafrrTQEEALDRaatwLDRI----GLLQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:COG1134 108 NIYLN-------GRLLGL--------SRKEIDEK----FDEIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 175 MLDEP-AAGlnpketkelD--------ELIAELRDHHdTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEirnnpd 245
Cdd:COG1134 169 LVDEVlAVG---------DaafqkkclARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE------ 232
|
....*.
gi 489958237 246 VIRAYL 251
Cdd:COG1134 233 VIAAYE 238
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-238 |
4.29e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 2 KPLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTIMLRDQHLEGLPGQQIARM 79
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 GVVRTFQHVRLFREMTVIENLLVAQHQQLKtglFSGLLKTPAFrrtqeEALDRAATWLDRIGLLQHANRQASNLAY--GD 157
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLRLAYNSKRK---FQGLPELDPL-----EFLEIINEKLKLVGMDPSFLSRNVNEGFsgGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGIS-DRIYVVNQGTPLANGT 236
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMT-SENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGD 235
|
..
gi 489958237 237 PE 238
Cdd:CHL00131 236 AE 237
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-244 |
4.64e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKP----TGGTIMLRDQHLEGLPGQQiaRMGVVRtfqhvrl 90
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRE--RRKIIG------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 fREMTVIenllvAQH------------QQLKTGLFSGLLKTPAFRRTQEEALdRAATWLDRIGLLQHANRQAS---NLAY 155
Cdd:COG4170 89 -REIAMI-----FQEpsscldpsakigDQLIEAIPSWTFKGKWWQRFKWRKK-RAIELLHRVGIKDHKDIMNSyphELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 156 GDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
....*....
gi 489958237 236 TPEEIRNNP 244
Cdd:COG4170 242 PTEQILKSP 250
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-240 |
5.42e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLpGQQIARMGVVRT-----------FQHVRL 90
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAMVqqdpvvladtfLANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMT---VIENLLVAQHQQLKTGLFSGLLKtpafrrtqeealdraatwldRIGllqhanRQASNLAYGDQRRLEIVRCM 167
Cdd:PRK10790 438 GRDISeeqVWQALETVQLAELARSLPDGLYT--------------------PLG------EQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 168 VTQPEILMLDEPAAGLNPKETKELDELIAELRDHhdTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-244 |
7.20e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRF----GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKP----TGGTIMLRDQHLEGLPGQ 74
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 75 QiaRMGVVRtfQHVRL-FREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRTQEEaLDRAATWLDRIGLLQHANRQAS-- 151
Cdd:PRK15093 82 E--RRKLVG--HNVSMiFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWR-KRRAIELLHRVGIKDHKDAMRSfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 152 -NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGT 230
Cdd:PRK15093 157 yELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250
....*....|....
gi 489958237 231 PLANGTPEEIRNNP 244
Cdd:PRK15093 237 TVETAPSKELVTTP 250
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-240 |
9.97e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.29 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIML-----RDQHLEGLPgQQIarmGVVrtFQHVRLFRE 93
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdiRTVTRASLR-RNI---AVV--FQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 mTVIENLLVAqhqqlktglfsgllKTPAFRRTQEEALDRAATwLDRI-----GLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:PRK13657 424 -SIEDNIRVG--------------RPDATDEEMRAAAERAQA-HDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958237 169 TQPEILMLDEPAAGLNPKETKELDELIAELRdhHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 240
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-239 |
1.50e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 21 NNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTgFYKPTG----GTIMLRDQHLEGlpGQQIARMGVVRtfQHVRLFREMTV 96
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPIDA--KEMRAISAYVQ--QDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 IENLlvaqhqqlktgLFSGLLKTPAfRRTQEEALDRAATWLDRIGLLQHAN------RQASNLAYGDQRRLEIVRCMVTQ 170
Cdd:TIGR00955 117 REHL-----------MFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 171 PEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-212 |
7.47e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGlPGQQIARMGVVRTFQHVRLFremtviE 98
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKLFSAVFTDFHLF------D 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVAQHQQLKTGLfsgllktpafrrtqeealdrAATWLDRIGL---LQHANRQASN--LAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK10522 411 QLLGPEGKPANPAL--------------------VEKWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489958237 174 LMLDEPAAGLNPKETKEL-DELIAELRDhHDTTILLIEHD 212
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFyQVLLPLLQE-MGKTIFAISHD 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-229 |
8.03e-12 |
|
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: 62.94 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglpGQQIARMGVVRTFQhvrlfREMTVIE 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR--------GRVSSLLGLGGGFN-----PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVaqhqqlkTGLFSGLlktpafrrTQEEALDRaatwLDRI----GLLQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:cd03220 104 NIYL-------NGRLLGL--------SRKEIDEK----IDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 175 MLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-240 |
9.43e-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: 62.89 E-value: 9.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLrDQHLEGL--PGQQIARMGVVrtFQHVRLFRE 93
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALadPAWLRRQVGVV--LQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 mTVIENLLVAQhqqlktglfsgllktPAFRRTQEEALDRAATWLDRI-----GLLQHANRQASNLAYGDQRRLEIVRCMV 168
Cdd:cd03252 91 -SIRDNIALAD---------------PGMSMERVIEAAKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 169 TQPEILMLDEPAAGLNpketKELDELIaeLRDHHDT----TILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 240
Cdd:cd03252 155 HNPRILIFDEATSALD----YESEHAI--MRNMHDIcagrTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-229 |
9.95e-12 |
|
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: 64.08 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPT-GGTIMLRDQHLEGLPGQQIARMGVVRTFQHVR---LFREMT 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVAQHQQlktglFSGLLKTPAfrRTQEEALDRAatwLDRIGL-LQHANRQASNLAYGDQRRLEIVRCMVTQPEIL 174
Cdd:TIGR02633 356 VGKNITLSVLKS-----FCFKMRIDA--AAELQIIGSA---IQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 175 MLDEPAAGLNPKETKELDELIAELRdHHDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-235 |
1.22e-11 |
|
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: 61.80 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTG--FYKPTGGTIML--RDQHLEGLPgqqiARMGVVRtfQHVRLFREMT 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLIngRPLDKRSFR----KIIGYVP--QDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 96 VIENLLVAQHqqLKtGLfSGllktpafrrtqeealdraatwldrigllqhanrqasnlayGDQRRLEIVRCMVTQPEILM 175
Cdd:cd03213 99 VRETLMFAAK--LR-GL-SG----------------------------------------GERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-197 |
1.43e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglpGQQIARMGVvrTFQHVRLF--------RE 93
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--------GEPIRRQRD--EYHQDLLYlghqpgikTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 MTVIENLLVAQHQQlktglfsgllktpafrrtqeEALDRAATW--LDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQP 171
Cdd:PRK13538 89 LTALENLRFYQRLH--------------------GPGDDEALWeaLAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRA 148
|
170 180
....*....|....*....|....*.
gi 489958237 172 EILMLDEPAAGLNPKETKELDELIAE 197
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-253 |
1.74e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.71 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 16 GLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYkPTGGTIMLRDQHLEGLP----GQQIARMGvvrtfQHVRLF 91
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDpeswRKHLSWVG-----QNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 rEMTVIENLLVAQHQQLKTGLFSGLLKTPA--FRRTQEEALDRAatwldrIGllqhanRQASNLAYGDQRRLEIVRCMVT 169
Cdd:PRK11174 436 -HGTLRDNVLLGNPDASDEQLQQALENAWVseFLPLLPQGLDTP------IG------DQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 170 QPEILMLDEPAAGLNPK-ETKELDELIAELRDHhdtTILLIEH---DMKLVmgisDRIYVVNQGTPLANGTPEEIRNNPD 245
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHsEQLVMQALNAASRRQ---TTLMVTHqleDLAQW----DQIWVMQDGQIVQQGDYAELSQAGG 575
|
....*...
gi 489958237 246 VIRAYLGE 253
Cdd:PRK11174 576 LFATLLAH 583
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-244 |
1.94e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQ---HLEglPgqqiARMGVVRTFQHVRLF 91
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELE--P----ADRDIAMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 REMTVIENLLVAqhqqLKTglfSGLLKTPAFRRTQEealdrAATWLDRIGLLQHANRQASnlayGDQR-RLEIVRCMVTQ 170
Cdd:PRK11650 89 PHMSVRENMAYG----LKI---RGMPKAEIEERVAE-----AARILELEPLLDRKPRELS----GGQRqRVAMGRAIVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 171 PEILMLDEPAAGLNPK-------ETKELDeliAELRdhhdTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKlrvqmrlEIQRLH---RRLK----TTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
.
gi 489958237 244 P 244
Cdd:PRK11650 226 P 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-235 |
9.22e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 31 EIVSLIGPNGAGKTTVFNCLTGFYKPTG--GTIMLRDQHLEglpGQQIARMGVVRtfQHVRLFREMTVIENLlvaqhqql 108
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT---KQILKRTGFVT--QDDILYPHLTVRETL-------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 109 ktgLFSGLLKTPAfRRTQEEALDRAATWLDRIGLLQHANRQASN-----LAYGDQRRLEIVRCMVTQPEILMLDEPAAGL 183
Cdd:PLN03211 162 ---VFCSLLRLPK-SLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489958237 184 NPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANG 235
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-240 |
9.79e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVRTFQHVR---LFREMTV 96
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 97 IENLLVAqhQQLKTGLFS---GLLKTPAFRRTQEEALDRAATWLDRIgllqhaNRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK09700 359 AQNMAIS--RSLKDGGYKgamGLFHEVDEQRTAENQRELLALKCHSV------NQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 174 LMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVNQG------TPLANGTPEEI 240
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGrltqilTNRDDMSEEEI 502
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-244 |
1.60e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIA--RMGVVRTFQ------HVRL 90
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVFQnpygslNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 91 FREMTVIENLLVaqhqqlKTGLfsgllkTPAFRRtqeealDRAATWLDRIGLL-QHANRQASNLAYGDQRRLEIVRCMVT 169
Cdd:PRK11308 110 KVGQILEEPLLI------NTSL------SAAERR------EKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 170 QPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-237 |
1.64e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.96 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLL--AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMlrdqhlegLPGQQIARMGVv 82
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--------IDGIDISTIPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 rtfqhVRLFREMTVIEnllvaqhqQLKTgLFSGLLKTpafrrtqeeALDRAATWLDR--IGLLQhANRQASNLAYGDQRR 160
Cdd:cd03369 78 -----EDLRSSLTIIP--------QDPT-LFSGTIRS---------NLDPFDEYSDEeiYGALR-VSEGGLNLSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 161 LEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELrdHHDTTILLIEHDMKLVMGIsDRIYVVNQGTPLANGTP 237
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-251 |
1.71e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 61.00 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 147 NRQASNLAYGDQRRLEIVRCMVTQPEILM--LDEPAAGLNPKETKELDELIAELRDHHDtTILLIEHDMKLVmGISDRIY 224
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRII 548
|
90 100 110
....*....|....*....|....*....|....
gi 489958237 225 VVNQGTP------LANGTPEEIRNNPDVIRA-YL 251
Cdd:PRK00635 549 DIGPGAGifggevLFNGSPREFLAKSDSLTAkYL 582
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-252 |
1.93e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNC----LTGFYKPTG----GTIMLRDQHLEGLPGQQIARMGVVRTFQHVRLF 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 rEMTVIENLLVAQHqqlktglfsgllktPAFRRTQEEAL-DRAATW--LDRIGLLQHANRQASNLAYGDQRRLEIVRCM- 167
Cdd:PRK13547 97 -AFSAREIVLLGRY--------------PHARRAGALTHrDGEIAWqaLALAGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 168 --------VTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 239
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250
....*....|...
gi 489958237 240 IRnNPDVIRAYLG 252
Cdd:PRK13547 242 VL-TPAHIARCYG 253
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-235 |
2.12e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTIMLRDQHLEGLPGQQIARMGV 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRTFQHvrlfremtVIENLLVAQHQQLKTGLfsgllktPAFRR-TQEEALDR---AATWLDRIGLLQHAN---RQASNLA 154
Cdd:PRK09580 81 FMAFQY--------PVEIPGVSNQFFLQTAL-------NAVRSyRGQEPLDRfdfQDLMEEKIALLKMPEdllTRSVNVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 155 Y--GDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPL 232
Cdd:PRK09580 146 FsgGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIV 225
|
...
gi 489958237 233 ANG 235
Cdd:PRK09580 226 KSG 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-241 |
3.22e-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: 59.80 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 26 DLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImlrdqhLEGL-----PgqqiarmgvvrtfQHVRLFREMTVIENL 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLkisykP-------------QYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 101 lvaqHQQLKTGLFSGLLKTPAFRRTQeealdraatwLDRIgllqhANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPA 180
Cdd:COG1245 423 ----RSANTDDFGSSYYKTEIIKPLG----------LEKL-----LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 181 AGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNqGTPLANGT---PEEIR 241
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGHasgPMDMR 546
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-240 |
3.76e-10 |
|
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: 59.38 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGG--LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARM-GV 81
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHiGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 82 VRtfQHVRLFrEMTVIENllVAQhqqlktglfsgllktpaFRRTQEEALDRAA-----------------TWLDRIGllq 144
Cdd:COG4618 411 LP--QDVELF-DGTIAEN--IAR-----------------FGDADPEKVVAAAklagvhemilrlpdgydTRIGEGG--- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 145 hanrqaSNLAyGDQR-RLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHdTTILLIEHDMKLvMGISDRI 223
Cdd:COG4618 466 ------ARLS-GGQRqRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARG-ATVVVITHRPSL-LAAVDKL 536
|
250
....*....|....*..
gi 489958237 224 YVVNQGTPLANGTPEEI 240
Cdd:COG4618 537 LVLRDGRVQAFGPRDEV 553
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-61 |
1.21e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 1.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 61
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-241 |
2.53e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 27 LHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLrDQHLEGLPgqqiarmgvvrtfQHVRLFREMTVIENLlvaqhQ 106
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKP-------------QYIKPDYDGTVEDLL-----R 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 107 QLKTGLFSGLLKTPAFRRTQeealdraatwLDRIgllqhANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPK 186
Cdd:PRK13409 423 SITDDLGSSYYKSEIIKPLQ----------LERL-----LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 187 ETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIyVVNQGTPLANGT---PEEIR 241
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL-MVFEGEPGKHGHasgPMDMR 544
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-61 |
2.58e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 2.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 7 VNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 61
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-232 |
2.81e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 21 NNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYK--PTGGTIMLRDQHLEglpgqqiarmgvvrtfqhvrlfREMTVIE 98
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG----------------------REASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 99 NLLVAQHQQLKTGLFS--GLLKTPAFRRTQEEaldraatwldrigllqhanrqasnLAYGDQRRLEIVRCMVTQPEILML 176
Cdd:COG2401 105 AIGRKGDFKDAVELLNavGLSDAVLWLRRFKE------------------------LSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 177 DEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGIS-DRIYVVNQGTPL 232
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
232-254 |
3.26e-09 |
|
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: 51.10 E-value: 3.26e-09
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-211 |
3.95e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFY--------------KPTGGTIMLRDQHL 68
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysndltlfgrrRGSGETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 69 eglpgqqiarmGVVRTFQHVRlFREMTVIENLLVaqhqqlkTGLFS--GLLKTPAFRRTQeealdRAATWLDRIGLlqhA 146
Cdd:PRK10938 339 -----------GYVSSSLHLD-YRVSTSVRNVIL-------SGFFDsiGIYQAVSDRQQK-----LAQQWLDILGI---D 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 147 NRQAS----NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEH 211
Cdd:PRK10938 392 KRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-242 |
7.70e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 31 EIVSLIGPNGAGKTTVFNCLTGFYKPTGGtimlrdqHLEGLPGQQiarmGVVRTFQHVRLFREMTVIEN--LLVAQHQQL 108
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFDDPPDWD----EILDEFRGSELQNYFTKLLEgdVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 109 K-------TGLFSGLLKTPAFRRTQEEALDRaatwLDRIGLLqhaNRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAA 181
Cdd:cd03236 96 VdlipkavKGKVGELLKKKDERGKLDELVDQ----LELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 182 GLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVVnQGTPLANGT---PEEIRN 242
Cdd:cd03236 169 YLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYLSDYIHCL-YGEPGAYGVvtlPKSVRE 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-251 |
1.54e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 152 NLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGiSDRIYVVNQ--- 228
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdr 1436
|
90 100
....*....|....*....|....*.
gi 489958237 229 -GTPL-ANGTPEEIRNNPD-VIRAYL 251
Cdd:PTZ00265 1437 tGSFVqAHGTHEELLSVQDgVYKKYV 1462
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-229 |
2.60e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMmrfGGLLAvNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLE-GLPGQQIaRMGVV- 82
Cdd:PRK11288 258 LRLDGLK---GPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAI-RAGIMl 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 83 ----RTFQHVRLFRemTVIENL-LVAQHQQLKTGLFSGllktpafRRTQEEALDRaatwldRIGLLQ----HANRQASNL 153
Cdd:PRK11288 333 cpedRKAEGIIPVH--SVADNInISARRHHLRAGCLIN-------NRWEAENADR------FIRSLNiktpSREQLIMNL 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958237 154 AYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHhDTTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-223 |
8.75e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 5 LSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQqiarmgvvrt 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ---------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 85 fQHVRLFRE-MTVIEnlLVAQHQQLKTG-----------LFSGllktpafrrtqeealdraatwlDRIgllqhaNRQASN 152
Cdd:PRK15064 390 -DHAYDFENdLTLFD--WMSQWRQEGDDeqavrgtlgrlLFSQ----------------------DDI------KKSVKV 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 153 LAYGDQRRLEIVRCMVTQPEILMLDEPaaglnpkeTKELD-ELIAELR---DHHDTTILLIEHDMKLVMGISDRI 223
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEP--------TNHMDmESIESLNmalEKYEGTLIFVSHDREFVSSLATRI 505
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-243 |
1.29e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 31 EIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQhleglpgqQIARMGVVRtfqhvrLFREMTVIENLLVaqhqqlkt 110
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--------DVAKFGLTD------LRRVLSIIPQSPV-------- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 111 gLFSGLLK--TPAFRRTQE----EALDRA----ATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPA 180
Cdd:PLN03232 1321 -LFSGTVRfnIDPFSEHNDadlwEALERAhikdVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 181 AGLNPKETKELDELIAElrDHHDTTILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-241 |
1.32e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 6 SVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIM-----LRD-QHLEGLpGQQIARM 79
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADaRHRRAV-CPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 80 --GVVRTfqhvrLFREMTVIENLlvaqhqqlktgLFSGLLktpaFRRTQEEALDRAATWLDRIGLLQHANRQASNLAYGD 157
Cdd:NF033858 82 pqGLGKN-----LYPTLSVFENL-----------DFFGRL----FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 158 QRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDttilliehdmklvmGIS--------------DRI 223
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERP--------------GMSvlvataymeeaerfDWL 207
|
250
....*....|....*...
gi 489958237 224 YVVNQGTPLANGTPEEIR 241
Cdd:NF033858 208 VAMDAGRVLATGTPAELL 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-242 |
1.36e-07 |
|
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: 50.26 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 26 DLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglpgqqiarmgvvrtfqhvrlfremtvienllvaqh 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD----------------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 106 qqlktglfsglLKTPAFRRtqeealdraatwldrigllqhanrQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNP 185
Cdd:cd03222 60 -----------GITPVYKP------------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 186 KETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVnQGTPLANGT---PEEIRN 242
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIasqPKGTRE 163
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
19-66 |
2.43e-07 |
|
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: 50.95 E-value: 2.43e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQ 66
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-240 |
2.87e-07 |
|
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: 51.10 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 18 LAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLrdqhleglPGQQIARMGVvrtfqHvRLFREMTVI 97
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII--------DGLNIAKIGL-----H-DLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENLLVaqhqqlktgLFSGLLKT---PAFRRTQEE---ALDRA--ATWLDRI--GLLQHANRQASNLAYGDQRRLEIVRCM 167
Cdd:TIGR00957 1366 PQDPV---------LFSGSLRMnldPFSQYSDEEvwwALELAhlKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 168 VTQPEILMLDEPAAGLNpketKELDELI-AELRDHHDT-TILLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 240
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVD----LETDNLIqSTIRTQFEDcTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-229 |
1.25e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 15 GGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI---------MLRDQHLEGLPGQQIARMGVVRTF 85
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 86 QHVrlfremtvienllvaQHQQLKTGLFSgllktpaFRRTQEEALDRAATwldrigllqhanrqasnLAYGDQRRLEIVR 165
Cdd:PLN03073 600 PGV---------------PEQKLRAHLGS-------FGVTGNLALQPMYT-----------------LSGGQKSRVAFAK 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958237 166 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhdtTILLIEHDMKLVMGISDRIYVVNQG 229
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEG 700
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
147-223 |
1.52e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 147 NRQASNLAYGDQRRLEivrcMVTQPE------ILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKlVMGIS 220
Cdd:cd03270 132 SRSAPTLSGGEAQRIR----LATQIGsgltgvLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDED-TIRAA 205
|
...
gi 489958237 221 DRI 223
Cdd:cd03270 206 DHV 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
149-240 |
2.09e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 149 QASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHhDTTILLIEHDMKLVMGISDRIYVVNQ 228
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNE 479
|
90
....*....|....*..
gi 489958237 229 GT-----PLANGTPEEI 240
Cdd:NF040905 480 GRitgelPREEASQERI 496
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
176-252 |
2.19e-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: 48.47 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHDtTILLIEHDmKLVMGISDriYVVNQGtP---------LANGTPEEIRNNPDV 246
Cdd:TIGR00630 514 LDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHD-EDTIRAAD--YVIDIG-PgagehggevVASGTPEEILANPDS 588
|
....*..
gi 489958237 247 IR-AYLG 252
Cdd:TIGR00630 589 LTgQYLS 595
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-244 |
3.87e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGG----LLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFY----KPTGGTIMLRDQHLEGLPG-- 73
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 74 -QQIARMGVVRTFQHvrlfrEMT-----------VIENLLVAQHQQLKTglfsgllktpafRRtqeealDRAATWLDRIG 141
Cdd:PRK11022 83 rRNLVGAEVAMIFQD-----PMTslnpcytvgfqIMEAIKVHQGGNKKT------------RR------QRAIDLLNQVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 142 LLQHANR---QASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMG 218
Cdd:PRK11022 140 IPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAE 219
|
250 260
....*....|....*....|....*.
gi 489958237 219 ISDRIYVVNQGTPLANGTPEEIRNNP 244
Cdd:PRK11022 220 AAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-221 |
4.99e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHleglpgqqiarmgvvr 83
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 tfqhvrlfremtvIENLLVAQHQQL-----KTGLFSGL-LKTPAFRRTQEEALDRAATWLDRIGLLQH-ANRQASNLAYG 156
Cdd:PRK13540 65 -------------IKKDLCTYQKQLcfvghRSGINPYLtLRENCLYDIHFSPGAVGITELCRLFSLEHlIDYPCGLLSSG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 157 DQRRLEIVRCMVTQPEILMLDEPAAGLnpkETKELDELIAELRDHHDT--TILLIEHDmKLVMGISD 221
Cdd:PRK13540 132 QKRQVALLRLWMSKAKLWLLDEPLVAL---DELSLLTIITKIQEHRAKggAVLLTSHQ-DLPLNKAD 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-226 |
6.99e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 29 KKEIVSLIGPNGAGKTTVFNCLTGFYKPT-G----------------GTIMLrdQHLEGLPGQQIArmgVVRTFQHVRLF 91
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlGdydeepswdevlkrfrGTELQ--DYFKKLANGEIK---VAHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 92 REM---TVIEnllvaqhqqlktglfsgLLKtpafrRTQEE-ALDRAAtwlDRIGLLQHANRQASNLAYGDQRRLEIVRCM 167
Cdd:COG1245 173 PKVfkgTVRE-----------------LLE-----KVDERgKLDELA---EKLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 168 VTQPEILMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLVMGISDRIYVV 226
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-216 |
9.17e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHL-----EGLPGQqiarmgvvrtfqhvrlfre 93
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNGQ------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 MTVIENLlvaqhqQLKtGLFSGLlktpafrrTQEEALDRAATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPEI 173
Cdd:PRK13545 100 LTGIENI------ELK-GLMMGL--------TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489958237 174 LMLDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDMKLV 216
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLSQV 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-223 |
1.38e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 1.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 147 NRQASNLAYGDQRRLEIVRCMVTQPE--ILMLDEPAAGLNPKETKELDELIAELRDHHDTTIlLIEHDMKlVMGISDRI 223
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVI-LIEHNLD-VLSSADWI 158
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
176-245 |
1.44e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDhHDTTILLIEHDmKLVMGISDRI------------YVVnqgtplANGTPEEIRNN 243
Cdd:COG0178 511 LDEPSIGLHQRDNDRLIETLKRLRD-LGNTVIVVEHD-EDTIRAADYIidigpgagehggEVV------AQGTPEEILKN 582
|
..
gi 489958237 244 PD 245
Cdd:COG0178 583 PD 584
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-216 |
1.44e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 30 KEIVSLIGPNGAGKTTVFNCLtgFYKPTGGTIMLRDQhleGLPGQQIARMGVVR-----TFQHVRlFREMTVIENLLVaq 104
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEAL--KYALTGELPPNSKG---GAHDPKLIREGEVRaqvklAFENAN-GKKYTITRSLAI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 105 hqqlktglfsglLKTPAFRRtQEEALdraatWL--DRIGLLQHANRQASNLAYgdqrRLEIVRCMVTQPEILMLDEPAAG 182
Cdd:cd03240 94 ------------LENVIFCH-QGESN-----WPllDMRGRCSGGEKVLASLII----RLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|....*
gi 489958237 183 LNP-KETKELDELIAELRDHHDTTILLIEHDMKLV 216
Cdd:cd03240 152 LDEeNIEESLAEIIEERKSQKNFQLIVITHDEELV 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-216 |
1.74e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVS-------------LIGPNGAGKTTVFNCLTGFYKPTGGTIMLR--------DQHLEGL-Pgqqia 77
Cdd:PRK11147 322 MENVNYQIDGKQLVKdfsaqvqrgdkiaLIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklevayfDQHRAELdP----- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 78 rmgvvrtfqhvrlfrEMTVIENLlvAQHQQ--------------LKTGLFSgllktPAFRRTQEEAldraatwldrigll 143
Cdd:PRK11147 397 ---------------EKTVMDNL--AEGKQevmvngrprhvlgyLQDFLFH-----PKRAMTPVKA-------------- 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958237 144 qhanrqasnLAYGDQRRLEIVRCMVTQPEILMLDEPaaglnpkeTKELD----ELIAELRDHHDTTILLIEHDMKLV 216
Cdd:PRK11147 441 ---------LSGGERNRLLLARLFLKPSNLLILDEP--------TNDLDvetlELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-211 |
1.93e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTImlrdqhleGLPgqQIARMgvvrtfqhvrlfremtvien 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARP--AGARV-------------------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 100 LLVAQHQQLKTGLFSGLLKTPAfrrtQEEALDRAA--TWLDRIGLLQHANR--QASN----LAYGDQRRLEIVRCMVTQP 171
Cdd:COG4178 429 LFLPQRPYLPLGTLREALLYPA----TAEAFSDAElrEALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489958237 172 EILMLDEPAAGLNPketKELDELIAELRDH-HDTTILLIEH 211
Cdd:COG4178 505 DWLFLDEATSALDE---ENEAALYQLLREElPGTTVISVGH 542
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-186 |
2.39e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 32 IVSLIGPNGAGKTTVFNCLTGfyKPTGGTIMlRDQHLEGLPGQQiarmgvvRTFQHVRLFREMTVIENLLVAQHQQLktg 111
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKKQ-------ETFARISGYCEQNDIHSPQVTVRESL--- 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 112 LFSGLLKTPAfRRTQEEALdraaTWLDRIGLLQHAN--RQA-------SNLAYGDQRRLEIVRCMVTQPEILMLDEPAAG 182
Cdd:PLN03140 975 IYSAFLRLPK-EVSKEEKM----MFVDEVMELVELDnlKDAivglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
....
gi 489958237 183 LNPK 186
Cdd:PLN03140 1050 LDAR 1053
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-216 |
2.81e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHleGLPGQQI----ARMGVVRtfQHVRLFREmTVI 97
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLkwwrSKIGVVS--QDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 98 ENL------------LVAQHQQLKTGLFSGLLKTPAFRRTQEEALDRAATWLDRIGLLQ--------------------- 144
Cdd:PTZ00265 478 NNIkyslyslkdleaLSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEmrknyqtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 145 -H-------------ANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIE 210
Cdd:PTZ00265 558 iHdfvsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
....*.
gi 489958237 211 HDMKLV 216
Cdd:PTZ00265 638 HRLSTI 643
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-235 |
3.04e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 32 IVSLIGPNGAGKTTVFNCLTGFYKPT-----------------GGTIMLrdQHLEGLPGQQIArmgVVRTFQHVRLFREM 94
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQ--NYFKKLYNGEIK---VVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 95 ---TVIEnllvaqhqqlktglfsgLLKtpafrRTQEE-ALDRAAtwlDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQ 170
Cdd:PRK13409 176 fkgKVRE-----------------LLK-----KVDERgKLDEVV---ERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 171 PEILMLDEPAAGLNPKETKELDELIAELRDhhDTTILLIEHDMKLVMGISDRIYVVnQGTPLANG 235
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA-YGEPGAYG 292
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-212 |
3.12e-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: 44.54 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 35 LIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglPGQQIARMGvvrtfQHVRLFREMTVIENLL--VAQHQQLKTGL 112
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIKVGYLP-----QEPQLDPTKTVRENVEegVAEIKDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 113 -------------FSGLLKTPAfrrTQEEALDRAATW-LDR-IGLLQHANR------QASNLAYGDQRRLEIVRCMVTQP 171
Cdd:TIGR03719 104 neisakyaepdadFDKLAAEQA---ELQEIIDAADAWdLDSqLEIAMDALRcppwdaDVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489958237 172 EILMLDEPaaglnpkeTKELD-ELIAELRDH-HD--TTILLIEHD 212
Cdd:TIGR03719 181 DMLLLDEP--------TNHLDaESVAWLERHlQEypGTVVAVTHD 217
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-196 |
5.08e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRDQHLEGLPGQQIARMGvvrtfQHVRLFREMTVIENLl 101
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-----HNLGLKLEMTVFENL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 102 vaqhqqlktglfsgllKTPAFRRTQEEALDRAATWLDRIGLLqhaNRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAA 181
Cdd:PRK13541 92 ----------------KFWSEIYNSAETLYAAIHYFKLHDLL---DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170
....*....|....*
gi 489958237 182 GLNPKETKELDELIA 196
Cdd:PRK13541 153 NLSKENRDLLNNLIV 167
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-243 |
5.80e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 23 VNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLrdqhleglPGQQIARMGVVRtfqhvrLFREMTVIENLLV 102
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI--------DGCDISKFGLMD------LRKVLGIIPQAPV 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 103 aqhqqlktgLFSGLLK--TPAFRRTQE----EALDRA----ATWLDRIGLLQHANRQASNLAYGDQRRLEIVRCMVTQPE 172
Cdd:PLN03130 1324 ---------LFSGTVRfnLDPFNEHNDadlwESLERAhlkdVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958237 173 ILMLDEPAAGLNPKEtkelDELIAE-LRDHHDT-TILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 243
Cdd:PLN03130 1395 ILVLDEATAAVDVRT----DALIQKtIREEFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-240 |
7.87e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 143 LQHA--NRQASNLAYGDQRRLEIVRCM---VTQPEILMLDEPAAGLNPKETKELDELIAELrDHHDTTILLIEHDMKLVM 217
Cdd:PRK00635 798 LDYLplGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVVK 876
|
90 100 110
....*....|....*....|....*....|.
gi 489958237 218 gISDriYVVNQGTP--------LANGTPEEI 240
Cdd:PRK00635 877 -VAD--YVLELGPEggnlggylLASCSPEEL 904
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-229 |
9.52e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 3 PLLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRD--------QH-LEGL-- 71
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklgyfaQHqLEFLra 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 72 ---PGQQIARMGVVRTFQHVRL------FREMTVIENllvaqhqqlkTGLFSGllktpafrrtqeealdraatwldrigl 142
Cdd:PRK10636 391 desPLQHLARLAPQELEQKLRDylggfgFQGDKVTEE----------TRRFSG--------------------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 143 lqhanrqasnlayGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELrdhhDTTILLIEHDMKLVMGISDR 222
Cdd:PRK10636 434 -------------GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLLRSTTDD 496
|
....*..
gi 489958237 223 IYVVNQG 229
Cdd:PRK10636 497 LYLVHDG 503
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-245 |
1.15e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 20 VNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKP----TGGTIML--RDQHLEGLPGQQIArmgvvrtfqhvrlfre 93
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLdgKPVAPCALRGRKIA---------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 94 mTVIEN-------LLVAQHQQLKTGLFSGLlktPAFRRTQEEALDrAATWLDRIGLLQhanRQASNLAYGDQRRLEIVRC 166
Cdd:PRK10418 83 -TIMQNprsafnpLHTMHTHARETCLALGK---PADDATLTAALE-AVGLENAARVLK---LYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958237 167 MVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 245
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-240 |
1.21e-04 |
|
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: 43.08 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 153 LAYGDQRRleivrcmVTQPEILMLDEPAAGLNPKETKELDELIAELRDHHDtTILLIEHDMKlVMGISDriYVV------ 226
Cdd:TIGR00630 840 LAKELSKR-------STGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKTAD--YIIdlgpeg 908
|
90
....*....|....*.
gi 489958237 227 --NQGTPLANGTPEEI 240
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-153 |
2.27e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 14 FGGLLAVNNVNLDlhkKEIVSLIGPNGAGKTTVFNCLT-GFYKPTGGTIMLRDQHLEglpgQQIARMGVVRTFQH----V 88
Cdd:COG0419 10 FRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLIN----VGSEEASVELEFEHggkrY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 89 RLFREMTVIENLLVAQHQQLKTgLFSGLLKTPAFRRTQEEALDRAATWLDRIGLLQHANRQASNL 153
Cdd:COG0419 83 RIERRQGEFAEFLEAKPSERKE-ALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEI 146
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
21-110 |
2.48e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.94 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 21 NNVNLDLHKKeIVSLIGPNGAGKTTVFNC----LTGFYKPTGGTIMLRDQHLEGLPGQQIARMGVVR-TFQHVRLFREMT 95
Cdd:pfam13476 10 RDQTIDFSKG-LTLITGPNGSGKTTILDAiklaLYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEiTFENNDGRYTYA 88
|
90
....*....|....*
gi 489958237 96 VIENLLVAQHQQLKT 110
Cdd:pfam13476 89 IERSRELSKKKGKTK 103
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-223 |
3.63e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLtgfykptGGTIMLRDQHLeglpgqQIARMGVVR 83
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRI------IYEQDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 84 TFQ-----HVrlfrEMTV----------IENLLVAQHQ---QLKTGLFSGLLKTPAfrRTQEEaLDRAATW--------- 136
Cdd:PRK11147 70 RLQqdpprNV----EGTVydfvaegieeQAEYLKRYHDishLVETDPSEKNLNELA--KLQEQ-LDHHNLWqlenrinev 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 137 LDRIGLlqHANRQASNLAYGDQRRLEIVRCMVTQPEILMLDEPAAGLNPKETKELDELIAELRDhhdtTILLIEHDMKLV 216
Cdd:PRK11147 143 LAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFI 216
|
....*..
gi 489958237 217 MGISDRI 223
Cdd:PRK11147 217 RNMATRI 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-61 |
4.60e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 4.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489958237 19 AVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 61
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-97 |
6.63e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958237 4 LLSVNGLMMRFGGLLAVNNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIMLRdqhleglPGQqiaRMGVVR 83
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNE---RLGKLR 70
|
90
....*....|....
gi 489958237 84 TFQHVrlFREMTVI 97
Cdd:PRK15064 71 QDQFA--FEEFTVL 82
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
176-245 |
1.48e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHDTtILLIEHDMKlVMGISDriYVV--------NQGTPLANGTPEEIRNNPD 245
Cdd:PRK00349 857 LDEPTTGLHFEDIRKLLEVLHRLVDKGNT-VVVIEHNLD-VIKTAD--WIIdlgpeggdGGGEIVATGTPEEVAKVEA 930
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
176-245 |
2.35e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958237 176 LDEPAAGLNPKETKELDELIAELRDHHDTtILLIEHDMKlVMGISDriYVV--------NQGTPLANGTPEEIRNNPD 245
Cdd:COG0178 853 LDEPTTGLHFHDIRKLLEVLHRLVDKGNT-VVVIEHNLD-VIKTAD--WIIdlgpeggdGGGEIVAEGTPEEVAKVKA 926
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-206 |
2.45e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958237 135 TWLDRIGLLQ-HANRQASNLAYGDQRRLEIVRCMVTQPE--ILMLDEPAAGLNPKETKELDELIAELRDHHDTTI 206
Cdd:PRK00635 1369 TFIDKVGLSYiTLGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI 1443
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-61 |
4.56e-03 |
|
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: 37.06 E-value: 4.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489958237 21 NNVNLDLHKKEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 61
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV 62
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-50 |
8.35e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.90 E-value: 8.35e-03
10 20 30
....*....|....*....|....*....|
gi 489958237 22 NVNLDLHKKEIVS-LIGPNGAGKTTVFNCL 50
Cdd:COG3950 16 DLEIDFDNPPRLTvLVGENGSGKTTLLEAI 45
|
|
| |
