|
Name |
Accession |
Description |
Interval |
E-value |
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-285 |
1.09e-135 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 383.96 E-value: 1.09e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQVLgqk 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH-----IEGL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqPGdwlnpaqlgqrlfykmfggtHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRNLLAGVLNTPAYRRSENDA 160
Cdd:PRK11300 73 --PG--------------------HQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLI 240
Cdd:PRK11300 131 LDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLGTD 285
Cdd:PRK11300 211 EHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYLGEA 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-288 |
1.70e-135 |
|
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: 383.23 E-value: 1.70e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 2 NATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqVLGQKf 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD-------ITGLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qpgdwlnpaqlgqrlfykmfggTHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRNLLAGVLNTPAYRRSENDAL 161
Cdd:COG0411 73 ----------------------PHRIARLGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 DRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIE 241
Cdd:COG0411 131 ERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1393793683 242 HDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLGTDESE 288
Cdd:COG0411 211 HDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEAYLGEEAAA 257
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-277 |
1.62e-108 |
|
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: 314.38 E-value: 1.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgd 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPaqlgqrlfykmfggtHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRNLLAGvlntpAYRRSENDALDRAF 165
Cdd:cd03219 67 -LPP---------------HEIARLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLA-----RARREEREARERAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMG 245
Cdd:cd03219 126 ELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMD 204
|
250 260 270
....*....|....*....|....*....|..
gi 1393793683 246 MVMGISDDIIVLDHGDVIARGKPAEIQHNEKV 277
Cdd:cd03219 205 VVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-284 |
7.77e-66 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 206.12 E-value: 7.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqk 80
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTG--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwLNPAQlgqrlfykmfggthlVNRAGLARTFQNIRLFREMSVVENLLVAqhMRVNRnllaGVLNTPAYRRS--EN 158
Cdd:COG4674 77 ------LDEHE---------------IARLGIGRKFQKPTVFEELTVFENLELA--LKGDR----GVFASLFARLTaeER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 159 DALDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVL 238
Cdd:COG4674 130 DRIEEV---LETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVV 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1393793683 239 LIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLGT 284
Cdd:COG4674 205 VVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPRVIEVYLGR 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-286 |
6.09e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.95 E-value: 6.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQKFqpgd 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR------------VLGEDV---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLNPAQLGQRLFYkmfggthlvnraglarTFQNIRLFREMSVVENLlvaqhmrvnrNLLAGvlntpAYRRSENDALDRAF 165
Cdd:COG1131 65 ARDPAEVRRRIGY----------------VPQEPALYPDLTVRENL----------RFFAR-----LYGLPRKEARERID 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMG 245
Cdd:COG1131 114 ELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLE 192
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 246 MVMGISDDIIVLDHGDVIARGKPAEIQHN--EKVIAAYLGTDE 286
Cdd:COG1131 193 EAERLCDRVAIIDKGRIVADGTPDELKARllEDVFLELTGEEA 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-283 |
1.51e-54 |
|
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: 176.71 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqVLGQKfq 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-------ITGLP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdwlnpaqlgqrlfykmfggTHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRnllagvlntpayrRSENDALD 162
Cdd:COG0410 72 ---------------------PHRIARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDR-------------AEVRADLE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAFYWLEVvdLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEH 242
Cdd:COG0410 118 RVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQ 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 243 DMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLG 283
Cdd:COG0410 195 NARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-274 |
4.44e-53 |
|
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: 172.62 E-value: 4.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfQPgd 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG----------LP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfykmfggTHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVnrnllagvlntpayRRSENDALDRAF 165
Cdd:cd03224 69 ------------------PHERARAGIGYVPEGRRIFPELTVEENLLLGAYARR--------------RAKRKARLERVY 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywlEVV-DLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDM 244
Cdd:cd03224 117 ---ELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNA 192
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEIQHN 274
Cdd:cd03224 193 RFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-275 |
1.23e-51 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 169.39 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL------------VDGQD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 FQPgdwLNPAQLgQRLFYKMfggthlvnraGLArtFQNIRLFREMSVVENllVAQHMRVNRNLlagvlntpayrrSENDA 160
Cdd:COG1127 69 ITG---LSEKEL-YELRRRI----------GML--FQGGALFDSLTVFEN--VAFPLREHTDL------------SEAEI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLI 240
Cdd:COG1127 119 RELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVV 198
|
250 260 270
....*....|....*....|....*....|....*
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNE 275
Cdd:COG1127 199 THDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-273 |
8.36e-49 |
|
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: 161.90 E-value: 8.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQKFQPgdwL 87
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL------------IDGEDISG---L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 NPAQLgQRLFYKMfggthlvnraGLArtFQNIRLFREMSVVENllVAQHMRVNRNLlagvlntpayrrSENDALDRAFYW 167
Cdd:cd03261 68 SEAEL-YRLRRRM----------GML--FQSGALFDSLTVFEN--VAFPLREHTRL------------SEEEIREIVLEK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMV 247
Cdd:cd03261 121 LEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTA 200
|
250 260
....*....|....*....|....*.
gi 1393793683 248 MGISDDIIVLDHGDVIARGKPAEIQH 273
Cdd:cd03261 201 FAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-281 |
3.64e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.94 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvlgqk 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnPAQLGQRLFYkmfggthLVNRAGLARTFQnirlfreMSVVEnlLVAQHMRVNRNLLAGvlntpaYRRSENDA 160
Cdd:COG1121 70 --------PRRARRRIGY-------VPQRAEVDWDFP-------ITVRD--VVLMGRYGRRGLFRR------PSRADREA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLI 240
Cdd:COG1121 120 VDEA---LERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVV 195
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGdVIARGKPAEIQHNEKVIAAY 281
Cdd:COG1121 196 THDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-283 |
4.13e-45 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 152.31 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgd 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfYKMfggtHLVNRAGLARTFQNIRLFREMSVVENLL-VAQHMRVNRnllagvlntpAYRRSENDALdra 164
Cdd:cd03218 67 ------------LPM----HKRARLGIGYLPQEASIFRKLTVEENILaVLEIRGLSK----------KEREEKLEEL--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 fywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDM 244
Cdd:cd03218 118 ---LEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNV 193
|
250 260 270
....*....|....*....|....*....|....*....
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLG 283
Cdd:cd03218 194 RETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-271 |
8.67e-45 |
|
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: 151.93 E-value: 8.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLgqkfqpgdwl 87
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 npaqlgQRLFYkMFGGTHLVNRaglartfqnirlfreMSVVENLlvaqhmrvnrNLLAgvlntPAYRRSENDALDRAFYW 167
Cdd:COG4555 74 ------RQIGV-LPDERGLYDR---------------LTVRENI----------RYFA-----ELYGLFDEELKKRIEEL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGMV 247
Cdd:COG4555 117 IELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEV 195
|
250 260
....*....|....*....|....
gi 1393793683 248 MGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG4555 196 EALCDRVVILHKGKVVAQGSLDEL 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-285 |
3.16e-44 |
|
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: 150.50 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIqvlgqkfqpg 84
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPM---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqlgqrlfykmfggtHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRnllagvlnTPAYRRSENDALdra 164
Cdd:TIGR04406 71 --------------------HERARLGIGYLPQEASIFRKLTVEENIMAVLEIRKDL--------DRAEREERLEAL--- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 fywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDM 244
Cdd:TIGR04406 120 ---LEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNV 195
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLGTD 285
Cdd:TIGR04406 196 RETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQ 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-285 |
5.48e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.79 E-value: 5.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqkfqpg 84
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 DWlnP----AQLGqrLFYkmfggthlvnragLArtfQNIRLFREMSVVENLL-VAQHMRVNRnllagvlntpAYRRSEND 159
Cdd:COG1137 69 HL--PmhkrARLG--IGY-------------LP---QEASIFRKLTVEDNILaVLELRKLSK----------KEREERLE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALdrafywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLL 239
Cdd:COG1137 119 EL------LEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIGVLI 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1393793683 240 IEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLGTD 285
Cdd:COG1137 192 TDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGED 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-272 |
1.53e-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: 148.48 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFG-GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpg 84
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwLNPAQLGQRlfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAqhmRVNR-NLLAGVLN--TPAYRRsendal 161
Cdd:cd03256 68 --LKGKALRQL-------------RRQIGMIFQQFNLIERLSVLENVLSG---RLGRrSTWRSLFGlfPKEEKQ------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 dRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIE 241
Cdd:cd03256 124 -RALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSL 202
|
250 260 270
....*....|....*....|....*....|.
gi 1393793683 242 HDMGMVMGISDDIIVLDHGDVIARGKPAEIQ 272
Cdd:cd03256 203 HQVDLAREYADRIVGLKDGRIVFDGPPAELT 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-272 |
8.14e-43 |
|
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: 145.98 E-value: 8.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIL---FNARNKTTNViqvlgqkfqpg 84
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvagHDVVREPREV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqlgqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVaqHMRvnrnlLAGVlntPAYRRSEndaldRA 164
Cdd:cd03265 72 ------------------------RRRIGIVFQDLSVDDELTGWENLYI--HAR-----LYGV---PGAERRE-----RI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDM 244
Cdd:cd03265 113 DELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYM 192
|
250 260
....*....|....*....|....*...
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEIQ 272
Cdd:cd03265 193 EEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-283 |
2.09e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 151.71 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 2 NATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKF 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD------------GEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 QpgdwlnpaqlgqrlfykmFGGTHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRvnrnlLAGVLNTPAYRRSENDAL 161
Cdd:COG1129 69 R------------------FRSPRDAQAAGIAIIHQELNLVPNLSVAENIFLGREPR-----RGGLIDWRAMRRRARELL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 DRafywLEV-VDLvdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLI 240
Cdd:COG1129 126 AR----LGLdIDP----DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYI 196
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHnEKVIAAYLG 283
Cdd:COG1129 197 SHRLDEVFEIADRVTVLRDGRLVGTGPVAELTE-DELVRLMVG 238
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-288 |
5.31e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.12 E-value: 5.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHF-GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfq 82
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTA----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdwLNPAQLgQRLfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAqhmRVNR-NLLAGVLNtpAYRRSEndaL 161
Cdd:COG3638 70 ----LRGRAL-RRL------------RRRIGMIFQQFNLVPRLSVLTNVLAG---RLGRtSTWRSLLG--LFPPED---R 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 DRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIE 241
Cdd:COG3638 125 ERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNL 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1393793683 242 HDMGMVMGISDDIIVLDHGDVIARGKPAEIqhNEKVIAAYLGTDESE 288
Cdd:COG3638 205 HQVDLARRYADRIIGLRDGRVVFDGPPAEL--TDAVLREIYGGEAEE 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-270 |
9.93e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.48 E-value: 9.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQK 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID------------GKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 FQPGdwlNPAQlgqrlfykmfggthlVNRAGLARTFQNIRLFREMSVVENLLVAqhmrvNRNLLAGVLNTPAYRRSENDA 160
Cdd:COG3845 69 VRIR---SPRD---------------AIALGIGMVHQHFMLVPNLTVAENIVLG-----LEPTKGGRLDRKAARARIREL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRafYWLEvVDLvdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLI 240
Cdd:COG3845 126 SER--YGLD-VDP----DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFI 197
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAE 270
Cdd:COG3845 198 THKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-271 |
1.67e-40 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 139.95 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGI--KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNviqvlgqkfqp 83
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwlnPAQLGQRLFYKMfggthlvnraglartfQNIRLFREMSVVENL-LVAQhmrvnrnlLAGVLNTPAYRRSENDald 162
Cdd:cd03263 70 -----RKAARQSLGYCP----------------QFDALFDELTVREHLrFYAR--------LKGLPKSEIKEEVELL--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 rafywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVLLIEH 242
Cdd:cd03263 118 -----LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTH 190
|
250 260
....*....|....*....|....*....
gi 1393793683 243 DMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:cd03263 191 SMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-271 |
2.40e-40 |
|
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: 139.78 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarNKTTNViqvlgqkfqpgdwLNPAQLGQr 95
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD--GKDITK-------------KNLRELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 lfykmfggthlvnRAGLarTFQNIR--LFrEMSVVENllVAQhmrvnrnllaGVLNtpaYRRSENDALDRAFYWLEVVDL 173
Cdd:COG1122 76 -------------KVGL--VFQNPDdqLF-APTVEED--VAF----------GPEN---LGLPREEIRERVEEALELVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHDMGMVMGISDD 253
Cdd:COG1122 125 EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADR 203
|
250
....*....|....*...
gi 1393793683 254 IIVLDHGDVIARGKPAEI 271
Cdd:COG1122 204 VIVLDDGRIVADGTPREV 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-271 |
2.58e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.98 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNViqvlgqkfqpgd 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnPAQlgQRlfykmfggthlvnRAGLarTFQNIRLFREMSVVENllVAQHMRVNRnllagvlntpayrRSENDALDRAF 165
Cdd:COG1118 71 ---PPR--ER-------------RVGF--VFQHYALFPHMTVAEN--IAFGLRVRP-------------PSKAEIRARVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLnpvETHKLSEIIRFLRDHHD---ITVLLIEH 242
Cdd:COG1118 116 ELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGAL---DAKVRKELRRWLRRLHDelgGTTVFVTH 192
|
250 260
....*....|....*....|....*....
gi 1393793683 243 DMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG1118 193 DQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-271 |
6.73e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.16 E-value: 6.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkTTNViqvlgqk 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-VTGL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnPAQlgQRlfykmfgGTHLVnraglartFQNIRLFREMSVVENllVAQHMRVNRnllagvlntpayrRSENDA 160
Cdd:COG3842 73 --------PPE--KR-------NVGMV--------FQDYALFPHLTVAEN--VAFGLRMRG-------------VPKAEI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvethKLSEIIRF-LRDHH---DIT 236
Cdd:COG3842 113 RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDA----KLREEMREeLRRLQrelGIT 188
|
250 260 270
....*....|....*....|....*....|....*
gi 1393793683 237 VLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG3842 189 FIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-271 |
1.07e-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: 138.08 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFY-----RASGGNILFNARNKTTNVIQVLgqkfq 82
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdWLnpaqlgqrlfykmfggthlvnRAGLARTFQNIRLFReMSVVENLLVAQHmrvnrnlLAGVLNTPAYRRSENDALD 162
Cdd:cd03260 78 ---EL---------------------RRRVGMVFQKPNPFP-GSIYDNVAYGLR-------LHGIKLKEELDERVEEALR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAFYWLEVvdlvdcANRL-AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhhDITVLLIE 241
Cdd:cd03260 126 KAALWDEV------KDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVT 197
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 242 HDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:cd03260 198 HNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-271 |
1.13e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 138.59 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFG-GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNArnktTNVIQVLGQKFQp 83
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEG----TDITKLRGKKLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwlnpaqlgqrlfyKMfggthlvnRAGLARTFQNIRLFREMSVVENLLVAqhmRVNR-NLLAGVLNTpaYRRSENDald 162
Cdd:TIGR02315 76 ---------------KL--------RRRIGMIFQHYNLIERLTVLENVLHG---RLGYkPTWRSLLGR--FSEEDKE--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEH 242
Cdd:TIGR02315 125 RALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLH 204
|
250 260
....*....|....*....|....*....
gi 1393793683 243 DMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:TIGR02315 205 QVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-276 |
1.37e-39 |
|
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: 144.66 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHF-----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvl 77
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK------ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 78 gqkfqpgdwLNPAQLgqRLFYKMFGgthLVnraglartFQNIR--LFREMSVVEnlLVAQHMRVNRNLlagvlntpayrr 155
Cdd:COG1123 332 ---------LSRRSL--RELRRRVQ---MV--------FQDPYssLNPRMTVGD--IIAEPLRLHGLL------------ 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 156 SENDALDRAFYWLEVVDLV-DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHD 234
Cdd:COG1123 376 SRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELG 455
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1393793683 235 ITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEK 276
Cdd:COG1123 456 LTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-272 |
5.92e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 138.32 E-value: 5.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKFQPG 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD------------GEPLDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 DwlnpaqlgqrlfYKMFG------GthlvnraglartfqnirLFREMSVVENLL-VAQhmrvnrnlLAGVlntpayrrSE 157
Cdd:COG4152 69 D------------RRRIGylpeerG-----------------LYPKMKVGEQLVyLAR--------LKGL--------SK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 158 NDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITV 237
Cdd:COG4152 104 AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTV 182
|
250 260 270
....*....|....*....|....*....|....*
gi 1393793683 238 LLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQ 272
Cdd:COG4152 183 IFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-260 |
2.41e-38 |
|
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: 132.91 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQKFqpgd 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK------------VLGKDI---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLNPAQLGQRLFYkmfggthlvnraglarTFQNIRLFREMSVVENLlvaqhmrvnrnllagvlntpayrrsendaldraf 165
Cdd:cd03230 65 KKEPEEVKRRIGY----------------LPEEPSLYENLTVRENL---------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywlevvdlvdcanrlagEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMG 245
Cdd:cd03230 95 -----------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILE 156
|
250
....*....|....*
gi 1393793683 246 MVMGISDDIIVLDHG 260
Cdd:cd03230 157 EAERLCDRVAILNNG 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-260 |
4.99e-37 |
|
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: 129.61 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNviqvlgqkfqpgd 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfykmfGGTHLVNRAGLARTFQNIRLFREMSVVENLLVAqhmrvnrnlLAGvlntpayrrsendaldraf 165
Cdd:cd03229 68 ----------------EDELPPLRRRIGMVFQDFALFPHLTVLENIALG---------LSG------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywlevvdlvdcanrlagemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMG 245
Cdd:cd03229 104 ---------------------GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLD 162
|
250
....*....|....*
gi 1393793683 246 MVMGISDDIIVLDHG 260
Cdd:cd03229 163 EAARLADRVVVLRDG 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-271 |
5.34e-37 |
|
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: 131.69 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFqpgdwl 87
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 npaqlgqrlfykmfggthlvnraglarTFQNIRLFREMSVVENllVAQHMRVNRNllagvlntpAYRRSENDALDRAFYW 167
Cdd:cd03296 79 ---------------------------VFQHYALFRHMTVFDN--VAFGLRVKPR---------SERPPEAEIRAKVHEL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLnpvETHKLSEIIRFLRDHHD---ITVLLIEHDM 244
Cdd:cd03296 121 LKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL---DAKVRKELRRWLRRLHDelhVTTVFVTHDQ 197
|
250 260
....*....|....*....|....*..
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:cd03296 198 EEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-266 |
9.46e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.96 E-value: 9.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 7 HVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQKfqpgdw 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR------------VFGKP------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 87 lnPAQLGQRLFYkmfggthLVNRAGLARTFqNIRLFRemsVVENLLVAqHMRVNRNllagvlntpaYRRSENDALDRAfy 166
Cdd:cd03235 63 --LEKERKRIGY-------VPQRRSIDRDF-PISVRD---VVLMGLYG-HKGLFRR----------LSKADKAKVDEA-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 167 wLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGM 246
Cdd:cd03235 117 -LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGL 194
|
250 260
....*....|....*....|
gi 1393793683 247 VMGISDDIIVLDHGdVIARG 266
Cdd:cd03235 195 VLEYFDRVLLLNRT-VVASG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-271 |
1.41e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.50 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKFqpg 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD------------GEDL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dWLNPAQLGQRlfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAQhMRVNRnllagvlntpayrRSENDALDRA 164
Cdd:COG1126 66 -TDSKKDINKL-------------RRKVGMVFQQFNLFPHLTVLENVTLAP-IKVKK-------------MSKAEAEERA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNP--VethklSEIIRFLRD--HHDITVLLI 240
Cdd:COG1126 118 MELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPelV-----GEVLDVMRDlaKEGMTMVVV 192
|
250 260 270
....*....|....*....|....*....|.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG1126 193 THEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-260 |
2.11e-36 |
|
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: 129.12 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQK----FQpgdwlNPAQ 91
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglvFQ-----NPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 92 lgQrlfykmfggthlvnraglartFQNIRLFREmsvvenllVAQHMRvNRNLlagvlntpayrrSENDALDRAFYWLEVV 171
Cdd:cd03225 87 --Q---------------------FFGPTVEEE--------VAFGLE-NLGL------------PEEEIEERVEEALELV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 DLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHDMGMVMGIS 251
Cdd:cd03225 123 GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELA 201
|
....*....
gi 1393793683 252 DDIIVLDHG 260
Cdd:cd03225 202 DRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-266 |
2.54e-36 |
|
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: 129.18 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQvlgqkfqpgd 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENllVAQHMRVNRnllagvLNTPAYRRSENDALDRaf 165
Cdd:cd03259 71 -----------------------RRNIGMVFQDYALFPHLTVAEN--IAFGLKLRG------VPKAEIRARVRELLEL-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMG 245
Cdd:cd03259 118 -----VGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQE 192
|
250 260
....*....|....*....|.
gi 1393793683 246 MVMGISDDIIVLDHGDVIARG 266
Cdd:cd03259 193 EALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-260 |
4.35e-36 |
|
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: 128.42 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNAR---NKTTNVIQVlgqkfq 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltDDKKNINEL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdwlnpaqlgqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAQhMRVnrnllagvlntpaYRRSENDALD 162
Cdd:cd03262 75 --------------------------RQKVGMVFQQFNLFPHLTVLENITLAP-IKV-------------KGMSKAEAEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdHHDITVLLIEH 242
Cdd:cd03262 115 RALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTH 193
|
250
....*....|....*...
gi 1393793683 243 DMGMVMGISDDIIVLDHG 260
Cdd:cd03262 194 EMGFAREVADRVIFMDDG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-271 |
8.27e-36 |
|
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: 129.01 E-value: 8.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpg 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwLNPAQLGQRLFYkmfggthlvnragLArtfQNIRLFREMSVVEnlLVAQ----HMRVNRnllagvlntpayRRSEND- 159
Cdd:COG1120 68 --LSRRELARRIAY-------------VP---QEPPAPFGLTVRE--LVALgrypHLGLFG------------RPSAEDr 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 -ALDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVL 238
Cdd:COG1120 116 eAVEEA---LERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVV 192
|
250 260 270
....*....|....*....|....*....|...
gi 1393793683 239 LIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG1120 193 MVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-266 |
1.06e-35 |
|
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: 128.01 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNV------- 73
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 74 ---IQVLGQkfQPGDWLNPAqlgqrlfykmfggthlvnraglartfqnirlfreMSVVEnlLVAQHMRVNRNLlagvlnt 150
Cdd:cd03257 81 rkeIQMVFQ--DPMSSLNPR----------------------------------MTIGE--QIAEPLRIHGKL------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 151 payrRSENDALDRAFYWLEVVDLV-DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFL 229
Cdd:cd03257 116 ----SKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKL 191
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393793683 230 RDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARG 266
Cdd:cd03257 192 QEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-266 |
1.18e-34 |
|
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: 124.70 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGqkfqpgd 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLnPAQLGqrlfykmfggthlvnraglartfqnirLFREMSVVENLL-VAQhmrvnrnlLAGVlntpayrrSENDALDRA 164
Cdd:cd03269 74 YL-PEERG---------------------------LYPKMKVIDQLVyLAQ--------LKGL--------KKEEARRRI 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDM 244
Cdd:cd03269 110 DEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQM 188
|
250 260
....*....|....*....|..
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARG 266
Cdd:cd03269 189 ELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-266 |
1.58e-34 |
|
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: 124.25 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNArNKTTNVIQVLGqkfqpgd 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaQLGQrlfykmfggthLVNRAGlartfqnirLFREMSVVENLLVAQhmrvnrnLLAGVlntpayrrsENDALDRAf 165
Cdd:cd03268 73 -----RIGA-----------LIEAPG---------FYPNLTARENLRLLA-------RLLGI---------RKKRIDEV- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMG 245
Cdd:cd03268 111 --LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLS 187
|
250 260
....*....|....*....|.
gi 1393793683 246 MVMGISDDIIVLDHGDVIARG 266
Cdd:cd03268 188 EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-212 |
2.27e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.99 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLgqkfqpgdwlnpaqlgqrlfykm 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnRAGLARTFQNIRLFREMSVVENLLVAQHMRvnrnllagvlnTPAYRRSENDALDrafyWLEVVDLVDCANRL 180
Cdd:pfam00005 58 --------RKEIGYVFQDPQLFPRLTVRENLRLGLLLK-----------GLSKREKDARAEE----ALEKLGLGDLADRP 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 1393793683 181 AG----EMSYGQQRRLEIARAMCTSPEMICLDEPAA 212
Cdd:pfam00005 115 VGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-282 |
3.19e-34 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 124.17 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgd 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPAQLGqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAqhmrvnrnllagvlnTPAYRRSENDALDRAF 165
Cdd:TIGR03410 67 -LPPHERA---------------RAGIAYVPQGREIFPRLTVEENLLTG---------------LAALPRRSRKIPDEIY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVvdLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMG 245
Cdd:TIGR03410 116 ELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLD 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393793683 246 MVMGISDDIIVLDHGDVIARGKPAEIQHNEkvIAAYL 282
Cdd:TIGR03410 194 FARELADRYYVMERGRVVASGAGDELDEDK--VRRYL 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-260 |
3.91e-34 |
|
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: 123.37 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkf 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qpgdwLNPAQLgqrlfykmfggTHLVNR-AGLarTFQNIRLFREMSVVENLLVAQHmrvnrnlLAGVLNTpayrrsenDA 160
Cdd:cd03255 71 -----LSEKEL-----------AAFRRRhIGF--VFQSFNLLPDLTALENVELPLL-------LAGVPKK--------ER 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLI 240
Cdd:cd03255 118 RERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVV 197
|
250 260
....*....|....*....|
gi 1393793683 241 EHDMGMVmGISDDIIVLDHG 260
Cdd:cd03255 198 THDPELA-EYADRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-264 |
9.52e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.84 E-value: 9.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHFG----GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlg 78
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 79 qkfqpgdwLNPAQLGQ-RLfyKMFGgthLVnraglartFQNIRLFREMSVVENLLVAQhmrvnrnLLAGVlntpayrrSE 157
Cdd:COG1136 75 --------LSERELARlRR--RHIG---FV--------FQFFNLLPELTALENVALPL-------LLAGV--------SR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 158 NDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITV 237
Cdd:COG1136 119 KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTI 198
|
250 260
....*....|....*....|....*..
gi 1393793683 238 LLIEHDMGmVMGISDDIIVLDHGDVIA 264
Cdd:COG1136 199 VMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-280 |
1.06e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 128.48 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHF--GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASG---GNILFNARNKTTNVIQVL 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 78 GQK----FQ-PGDWLNPAQLGQRLfykmfggthlvnraglARTFQNIRLFREmsvvenllvaqhmrvnrnllagvlntpa 152
Cdd:COG1123 82 GRRigmvFQdPMTQLNPVTVGDQI----------------AEALENLGLSRA---------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 153 yrrsenDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDH 232
Cdd:COG1123 118 ------EARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRE 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1393793683 233 HDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAA 280
Cdd:COG1123 192 RGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-281 |
1.17e-33 |
|
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: 123.27 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNilfnarnkttnVIQVLGQKFqp 83
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-----------DVRLFGERR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 GDWlNPAQLGQRLfykmfgGthLVNrAGLARTFQnirlfREMSVVEnllvaqhmrVnrnLLAGVLNTPA-YRRSENDALD 162
Cdd:COG1119 69 GGE-DVWELRKRI------G--LVS-PALQLRFP-----RDETVLD---------V---VLSGFFDSIGlYREPTDEQRE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEH 242
Cdd:COG1119 122 RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 243 DMG-MVMGISdDIIVLDHGDVIARGKPAEIQHNEKVIAAY 281
Cdd:COG1119 202 HVEeIPPGIT-HVLLLKDGRVVAAGPKEEVLTSENLSEAF 240
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-277 |
5.15e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqv 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 77 lgqkfqpgdwlnpaqlGQRlfykmfggthlVNRAGLART--FQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayR 154
Cdd:COG1116 72 ----------------GKP-----------VTGPGPDRGvvFQEPALLPWLTVLDNVALGLELR---------------G 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 155 RSENDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHD 234
Cdd:COG1116 110 VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETG 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1393793683 235 ITVLLIEHDmgmvmgI------SDDIIVLDHGdviargkPAEIQHNEKV 277
Cdd:COG1116 190 KTVLFVTHD------VdeavflADRVVVLSAR-------PGRIVEEIDV 225
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-271 |
8.74e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 123.22 E-value: 8.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgd 85
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPAQLGqrlfykmFGgthLVnraglartFQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayRRSENDALDRAF 165
Cdd:TIGR03265 71 -LPPQKRD-------YG---IV--------FQSYALFPNLTVADNIAYGLKNR---------------GMGRAEVAERVA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMG 245
Cdd:TIGR03265 117 ELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQE 196
|
250 260
....*....|....*....|....*.
gi 1393793683 246 MVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:TIGR03265 197 EALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-271 |
8.91e-33 |
|
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: 120.38 E-value: 8.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqk 80
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwLNPAQLGQRlfykmfggthlvnRAGLARTFQNIRLFREMSVVENllVAQHMRvnrnlLAGVlntpayRRSENDA 160
Cdd:cd03258 72 ------LSGKELRKA-------------RRRIGMIFQHFNLLSSRTVFEN--VALPLE-----IAGV------PKAEIEE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 ldRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHklsEIIRFLRDHH---DITV 237
Cdd:cd03258 120 --RVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ---SILALLRDINrelGLTI 194
|
250 260 270
....*....|....*....|....*....|....
gi 1393793683 238 LLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:cd03258 195 VLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-285 |
1.33e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 120.00 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQVLGqkfqpg 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDED-----ISLLP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqlgqrlfykmfggTHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRNllagvlntpayrrsENDALDRA 164
Cdd:PRK10895 72 -------------------LHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLS--------------AEQREDRA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDM 244
Cdd:PRK10895 119 NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNV 197
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLGTD 285
Cdd:PRK10895 198 RETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGED 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-264 |
1.86e-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: 117.53 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKFQPgd 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------GKEVSF-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPAQlgqrlfykmfggthlVNRAGLARTFQnirlfremsvvenllvaqhmrvnrnllagvlntpayrrsendaldraf 165
Cdd:cd03216 67 -ASPRD---------------ARRAGIAMVYQ------------------------------------------------ 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywlevvdlvdcanrlageMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHDMG 245
Cdd:cd03216 83 ------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLD 143
|
250
....*....|....*....
gi 1393793683 246 MVMGISDDIIVLDHGDVIA 264
Cdd:cd03216 144 EVFEIADRVTVLRDGRVVG 162
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-283 |
2.16e-32 |
|
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: 120.63 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVL-------GQKFQpgdwlNP-A 90
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkvGLVFQ-----FPeH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 91 QLGQRLFYK--MFGgthlvnraglartfqnirlfremsvvenllvaqhmrvNRNLlaGVlntpayrrSENDALDRAFYWL 168
Cdd:TIGR04521 94 QLFEETVYKdiAFG-------------------------------------PKNL--GL--------SEEEAEERVKEAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 169 EVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMV 247
Cdd:TIGR04521 127 ELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDV 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393793683 248 MGISDDIIVLDHGDVIARGKPAEI-QHNEKVIAAYLG 283
Cdd:TIGR04521 207 AEYADRVIVMHKGKIVLDGTPREVfSDVDELEKIGLD 243
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-271 |
5.39e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.99 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNC------LTGFYRASGgNILFNARN---KTTNVI 74
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGARVEG-EILLDGEDiydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 75 QV---LGQKFQ-PgdwlNPaqlgqrlfykmfggthlvnraglartfqnirlFReMSVVENllVAQHMRVNrnllaGVLNt 150
Cdd:COG1117 89 ELrrrVGMVFQkP----NP--------------------------------FP-KSIYDN--VAYGLRLH-----GIKS- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 151 payrRSEND-----ALDRAFYWLEVVDlvdcanRL---AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKL 222
Cdd:COG1117 124 ----KSELDeiveeSLRKAALWDEVKD------RLkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1393793683 223 SEIIRFLRDHHdiTVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG1117 194 EELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-257 |
1.12e-31 |
|
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: 117.19 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkf 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qpgdwlnpaqlGQRlfykmfggthlVNRAGLART--FQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayRRSEND 159
Cdd:cd03293 65 -----------GEP-----------VTGPGPDRGyvFQQDALLPWLTVLDNVALGLELQ---------------GVPKAE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLL 239
Cdd:cd03293 108 ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLL 187
|
250
....*....|....*...
gi 1393793683 240 IEHDMGMVMGISDDIIVL 257
Cdd:cd03293 188 VTHDIDEAVFLADRVVVL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-266 |
3.83e-31 |
|
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: 114.45 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwL 87
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS---------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 NPAQLGQRLFYkmfggthlvnraglartfqnirlfremsvvenllVAQhmrvnrnllagvlntpayrrsendaldrafyW 167
Cdd:cd03214 67 SPKELARKIAY----------------------------------VPQ-------------------------------A 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMV 247
Cdd:cd03214 82 LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLA 161
|
250
....*....|....*....
gi 1393793683 248 MGISDDIIVLDHGDVIARG 266
Cdd:cd03214 162 ARYADRVILLKDGRIVAQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-271 |
8.07e-31 |
|
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: 115.03 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkTTNViqvlgqkfqpgd 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-ITNL------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnPAqlgqrlfykmfggthlvNRAGLARTFQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayRRSENDALDRAF 165
Cdd:cd03300 68 ---PP-----------------HKRPVNTVFQNYALFPHLTVFENIAFGLRLK---------------KLPKAEIKERVA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpvetHKLSEIIRF-LRDHHD---ITVLLIE 241
Cdd:cd03300 113 EALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD----LKLRKDMQLeLKRLQKelgITFVFVT 188
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 242 HDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:cd03300 189 HDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-227 |
2.63e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.96 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgd 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlNPAQLGQRLFYkmfggthlvnraglarTFQNIRLFREMSVVENLlvaqhmrvnrNLLAGVLNTPAYRRSENDALDRaf 165
Cdd:COG4133 69 --AREDYRRRLAY----------------LGHADGLKPELTVRENL----------RFWAALYGLRADREAIDEALEA-- 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393793683 166 ywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIR 227
Cdd:COG4133 119 -----VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-284 |
1.01e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.16 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 9 EHLMMHFggikalndvNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLN 88
Cdd:COG3840 12 GDFPLRF---------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA---------------LP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 89 PAQlgqRLFykmfggTHLvnraglartFQNIRLFREMSVVENllVAQHMRVNRNLlagvlnTPAYRRSENDALDRafywl 168
Cdd:COG3840 68 PAE---RPV------SML---------FQENNLFPHLTVAQN--IGLGLRPGLKL------TAEQRAQVEQALER----- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 169 evVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVM 248
Cdd:COG3840 117 --VGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAA 194
|
250 260 270
....*....|....*....|....*....|....*...
gi 1393793683 249 GISDDIIVLDHGDVIARGKPAEIQ--HNEKVIAAYLGT 284
Cdd:COG3840 195 RIADRVLLVADGRIAADGPTAALLdgEPPPALAAYLGI 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-283 |
1.06e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 112.28 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqk 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgDWlnpaqlgqrlfykmfgGTHLVNRAGLARTFQNIRLFREMSVVENLLVAQHMrvnrnllagvlntpayrrsenda 160
Cdd:PRK11614 71 ----DW----------------QTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFF----------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRL-------AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhH 233
Cdd:PRK11614 108 AERDQFQERIKWVYELFPRLherriqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-Q 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1393793683 234 DITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLG 283
Cdd:PRK11614 187 GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-270 |
1.07e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.90 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvLGQkfqpgd 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP--------LAA------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPAQLGQRlfykmfggthlvnRAGLArtfQNIRL---FREMSVVEnllvaqhMrvnrnllaGVLNTPAYRRSENDALD 162
Cdd:COG4559 68 -WSPWELARR-------------RAVLP---QHSSLafpFTVEEVVA-------L--------GRAPHGSSAAQDRQIVR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMC-------TSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDI 235
Cdd:COG4559 116 EA---LALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGG 191
|
250 260 270
....*....|....*....|....*....|....*
gi 1393793683 236 TVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAE 270
Cdd:COG4559 192 GVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-276 |
2.00e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.00 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGnilfnarnkttnVIQVLGQKFQPgdwlnpaQLGQRLFY 98
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG------------TITIAGYHITP-------ETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 KmfggthLVNRAGLARTFQNIRLFrEMSVVENLLVaqhmrvnrnllaGVLNTPAyrrSENDALDRAFYWLEVVDL-VDCA 177
Cdd:PRK13641 82 K------LRKKVSLVFQFPEAQLF-ENTVLKDVEF------------GPKNFGF---SEDEAKEKALKWLKKVGLsEDLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIR-FLRDHHdiTVLLIEHDMGMVMGISDDIIV 256
Cdd:PRK13641 140 SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKdYQKAGH--TVILVTHNMDDVAEYADDVLV 217
|
250 260
....*....|....*....|
gi 1393793683 257 LDHGDVIARGKPAEIQHNEK 276
Cdd:PRK13641 218 LEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-287 |
2.85e-29 |
|
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: 111.24 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQR 95
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE---------------QDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFYkmfggthlvnraglarTFQNIRLFREMSVVENLlvaqhmrvnrNLLAGVLNTPAYRRSEndaldRAFYWLEVVDLVD 175
Cdd:cd03295 77 IGY----------------VIQQIGLFPHMTVEENI----------ALVPKLLKWPKEKIRE-----RADELLALVGLDP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 C--ANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEiiRFLRDHHDI--TVLLIEHDMGMVMGIS 251
Cdd:cd03295 126 AefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQE--EFKRLQQELgkTIVFVTHDIDEAFRLA 203
|
250 260 270
....*....|....*....|....*....|....*....
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI---QHNEKViAAYLGTDES 287
Cdd:cd03295 204 DRIAIMKNGEIVQVGTPDEIlrsPANDFV-AEFVGADRL 241
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-274 |
3.34e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 113.66 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkfqpGDWLNPAQLGQRLfykmfg 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG------------------GEVLQDSARGIFL------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 103 gthLVNRAGLARTFQNIRLFremsvvenllvaQHMRVNRNLLAGVLNTPAYRRseNDALDrafywlEVVDLVDCA---NR 179
Cdd:COG4148 73 ---PPHRRRIGYVFQEARLF------------PHLSVRGNLLYGRKRAPRAER--RISFD------EVVELLGIGhllDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpvETHKlSEIIRFL---RDHHDITVLLIEHDMGMVMGISDDIIV 256
Cdd:COG4148 130 RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD--LARK-AEILPYLerlRDELDIPILYVSHSLDEVARLADHVVL 206
|
250
....*....|....*...
gi 1393793683 257 LDHGDVIARGKPAEIQHN 274
Cdd:COG4148 207 LEQGRVVASGPLAEVLSR 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-278 |
4.13e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFG-GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFN------ARNKTTNV 73
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidySRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 74 IQVLGQKFQPGDwlnpaqlgQRLFYkmfggthlvnraglARTFQNIRLfremsvvenllvaqhmrvnrnllaGVLNTPAY 153
Cdd:PRK13636 81 RESVGMVFQDPD--------NQLFS--------------ASVYQDVSF------------------------GAVNLKLP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 154 RRSENDALDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHH 233
Cdd:PRK13636 115 EDEVRKRVDNA---LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKEL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 234 DITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVI 278
Cdd:PRK13636 192 GLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-266 |
4.80e-29 |
|
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: 109.98 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGsITALIGPNGAGKTTVFNCLTGFYRASGGNILFN---ARNKTTNVIQVLGqkFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdVLKQPQKLRRRIG--YL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 PgdwlnpaqlgqrlfykmfggthlvnraglartfQNIRLFREMSVVENLlvaQHMRVnrnlLAGVLNTPAYRRsendaLD 162
Cdd:cd03264 78 P---------------------------------QEFGVYPNFTVREFL---DYIAW----LKGIPSKEVKAR-----VD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhhDITVLLIEH 242
Cdd:cd03264 113 EV---LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTH 187
|
250 260
....*....|....*....|....
gi 1393793683 243 DMGMVMGISDDIIVLDHGDVIARG 266
Cdd:cd03264 188 IVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-260 |
1.25e-28 |
|
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: 107.33 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 7 HVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdw 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 87 LNPAQLGQRLFYkmfggthlvnraglarTFQnirlfremsvvenllvaqhmrvnrnllagvlntpayrrsendaldrafy 166
Cdd:cd00267 66 LPLEELRRRIGY----------------VPQ------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 167 wlevvdlvdcanrlageMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHDMGM 246
Cdd:cd00267 81 -----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPEL 142
|
250
....*....|....
gi 1393793683 247 VMGISDDIIVLDHG 260
Cdd:cd00267 143 AELAADRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-271 |
2.03e-28 |
|
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: 109.12 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFG----GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkf 81
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qpgdwlnpaqlGQRLFYKmfggthlvNRAGLARTFQnirlfremsvvenlLVAQH--------MRVNRnllagVLNTPAY 153
Cdd:COG1124 66 -----------GRPVTRR--------RRKAFRRRVQ--------------MVFQDpyaslhprHTVDR-----ILAEPLR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 154 RRSENDALDRAFYWLEVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVEThklSEIIRFLRD- 231
Cdd:COG1124 108 IHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQ---AEILNLLKDl 184
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1393793683 232 --HHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG1124 185 reERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-283 |
7.11e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.94 E-value: 7.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYrASG---GNILFNarnkttnviqvl 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFE------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 78 GQKFQpgdwlnpaqlgqrlfykmFGGTHLVNRAGLARTFQNIRLFREMSVVENLLVAqhmrvNRNLLAGVLNTPA-YRRS 156
Cdd:PRK13549 68 GEELQ------------------ASNIRDTERAGIAIIHQELALVKELSVLENIFLG-----NEITPGGIMDYDAmYLRA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 157 ENdaldrafyWLEVVDL-VDCANRLaGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdHHDI 235
Cdd:PRK13549 125 QK--------LLAQLKLdINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGI 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1393793683 236 TVLLIEHDMGMVMGISDDIIVLDHGDVIARgKPAEIQHNEKVIAAYLG 283
Cdd:PRK13549 195 ACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTEDDIITMMVG 241
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-263 |
1.03e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQVLGQKFQPgdwlnpaQLGQR 95
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-----LSRLKRREIP-------YLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LfykmfgGthLVnraglartFQNIRLFREMSVVENLLVAqhMRVnrnllAGvlntpayrRSENDALDRAFYWLEVVDLVD 175
Cdd:COG2884 81 I------G--VV--------FQDFRLLPDRTVYENVALP--LRV-----TG--------KSRKEIRRRVREVLDLVGLSD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvethKLS-EIIRFLRDHHD--ITVLLIEHDMGMVMGISD 252
Cdd:COG2884 130 KAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP----ETSwEIMELLEEINRrgTTVLIATHDLELVDRMPK 205
|
250
....*....|.
gi 1393793683 253 DIIVLDHGDVI 263
Cdd:COG2884 206 RVLELEDGRLV 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-266 |
1.39e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 106.30 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVlgqk 80
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnpaqlgqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAQHmrvnrnlLAGVlntpaYRRSENDA 160
Cdd:cd03266 77 ----------------------------RRRLGFVSDSTGLYDRLTARENLEYFAG-------LYGL-----KGDELTAR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDcanRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLI 240
Cdd:cd03266 117 LEELADRLGMEELLD---RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFS 192
|
250 260
....*....|....*....|....*.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARG 266
Cdd:cd03266 193 THIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-266 |
1.44e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 106.65 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviQVLGqkFQPgdWLNPAQLGQRLF 97
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV------------RVAG--LVP--WKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 98 YkMFGgthlvnraglartfQNIRLFREMSVVENLlvaqhmrvnrNLLAGVLNTPAYRRSENdaLDRAFYWLEVVDLVDCA 177
Cdd:cd03267 98 V-VFG--------------QKTQLWWDLPVIDSF----------YLLAAIYDLPPARFKKR--LDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRlagEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVL 257
Cdd:cd03267 151 VR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
....*....
gi 1393793683 258 DHGDVIARG 266
Cdd:cd03267 228 DKGRLLYDG 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-275 |
1.56e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.54 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKttnviqvlgqkfqpgdwlnPAQLGQRLFykmfg 102
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-------------------PAMSRSRLY----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 103 gthlVNRAGLARTFQNIRLFREMSVVENllVAQHMRVNRNLLAGVLNTPAYRRsendaldrafywLEVVDLVDCANRLAG 182
Cdd:PRK11831 81 ----TVRKRMSMLFQSGALFTDMNVFDN--VAYPLREHTQLPAPLLHSTVMMK------------LEAVGLRGAAKLMPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 183 EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDV 262
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
250
....*....|...
gi 1393793683 263 IARGKPAEIQHNE 275
Cdd:PRK11831 223 VAHGSAQALQANP 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-271 |
1.56e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.01 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkTTNViqvlgqkfQPGD 85
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-VTDL--------PPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfykmfggthlvnRaGLARTFQNIRLFREMSVVENLlvAQHMRVNRnllagvlntpaYRRSENDAldRAF 165
Cdd:COG3839 75 -----------------------R-NIAMVFQSYALYPHMTVYENI--AFPLKLRK-----------VPKAEIDR--RVR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvethKL-----SEIIRFLRDhHDITVLLI 240
Cdd:COG3839 116 EAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA----KLrvemrAEIKRLHRR-LGTTTIYV 190
|
250 260 270
....*....|....*....|....*....|.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG3839 191 THDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-276 |
3.32e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCL------------TGFYRASGGNIlFNARN 68
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNI-YSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 69 KTTNVIQVLGQKFQ-PgdwlNPAqlgqrlfykmfggthlvnraglartfqnirlfrEMSVVENllVAQHMRVNrnllaGV 147
Cdd:PRK14239 80 DTVDLRKEIGMVFQqP----NPF---------------------------------PMSIYEN--VVYGLRLK-----GI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 148 LNTPAYRRSENDALDRAFYWLEVVD-LVDCANRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEII 226
Cdd:PRK14239 116 KDKQVLDEAVEKSLKGASIWDEVKDrLHDSALGLSG----GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1393793683 227 RFLRDhhDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEK 276
Cdd:PRK14239 192 LGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-271 |
3.75e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.86 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLgqR 95
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA---------------LSEREL--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFykmfggthlvnRAGLARTFQNIRLFREMSVVENllVAQHMRvnrnlLAGVlnTPAYRRSENDALdrafywLEVVDLVD 175
Cdd:COG1135 79 AA-----------RRKIGMIFQHFNLLSSRTVAEN--VALPLE-----IAGV--PKAEIRKRVAEL------LELVGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDII 255
Cdd:COG1135 133 KADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVA 212
|
250
....*....|....*.
gi 1393793683 256 VLDHGDVIARGKPAEI 271
Cdd:COG1135 213 VLENGRIVEQGPVLDV 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-275 |
4.22e-27 |
|
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: 110.23 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQR 95
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD---------------LDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFYkmfggthlVNraglartfQNIRLFrEMSVVENLLVAQhmrvnrnllagvlntPAYRRSE-NDALDRAFYWLEVVDLV 174
Cdd:COG4988 413 IAW--------VP--------QNPYLF-AGTIRENLRLGR---------------PDASDEElEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 175 DCANRLAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVLLIEHDMGMVMgI 250
Cdd:COG4988 461 DGLDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-Q 537
|
250 260
....*....|....*....|....*
gi 1393793683 251 SDDIIVLDHGDVIARGKPAEIQHNE 275
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-284 |
5.09e-27 |
|
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: 105.11 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKaLNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgd 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPaqlgqrlfykmfggthlvNRAGLARTFQNIRLFREMSVVENLlvAQHMRVNRnllagvlntpaYRRSENDAldRAF 165
Cdd:cd03299 66 -LPP------------------EKRDISYVPQNYALFPHMTVYKNI--AYGLKKRK-----------VDKKEIER--KVL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMG 245
Cdd:cd03299 112 EIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFE 191
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1393793683 246 MVMGISDDIIVLDHGDVIARGKPAEI---QHNEKViAAYLGT 284
Cdd:cd03299 192 EAWALADKVAIMLNGKLIQVGKPEEVfkkPKNEFV-AEFLGF 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-283 |
6.79e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.50 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQvlgqk 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnpaqlgQRlfykmfggthlvnraGLARTFQNIRLFREMSVVENLLVAQHMrvnrnllagvLNTPAYRRSEnda 160
Cdd:PRK11432 77 -------------QR---------------DICMVFQSYALFPHMSLGENVGYGLKM----------LGVPKEERKQ--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 ldRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLI 240
Cdd:PRK11432 116 --RVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYV 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEI--QHNEKVIAAYLG 283
Cdd:PRK11432 194 THDQSEAFAVSDTVIVMNKGKIMQIGSPQELyrQPASRFMASFMG 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-287 |
1.86e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMH---FGGiKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnVIQvl 77
Cdd:PRK13634 1 MDITFQKVEHRYQYktpFER-RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGER-----VIT-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 78 GQKfqpgdwlNPAQLGQrlfykmfggthLVNRAGLARTFQNIRLFREMsvvenllvaqhmrVNRNLLAGVLNtpaYRRSE 157
Cdd:PRK13634 73 AGK-------KNKKLKP-----------LRKKVGIVFQFPEHQLFEET-------------VEKDICFGPMN---FGVSE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 158 NDALDRAFYWLEVVDLV-DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDIT 236
Cdd:PRK13634 119 EDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLT 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1393793683 237 VLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI-QHNEKVIAAYLGTDES 287
Cdd:PRK13634 199 TVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfADPDELEAIGLDLPET 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-274 |
3.10e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 14 HFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQKfqpgdwLNPAQLG 93
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI------------VDGLK------VNDPKVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 QRLFYKmfggthlvnRAGLarTFQNIRLFREMSVVENllvaqhmrvnrnllagVLNTPAYRR--SENDALDRAFYWLEVV 171
Cdd:PRK09493 72 ERLIRQ---------EAGM--VFQQFYLFPHLTALEN----------------VMFGPLRVRgaSKEEAEKQARELLAKV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 DLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHklsEIIRFLRDHHD--ITVLLIEHDMGMVMG 249
Cdd:PRK09493 125 GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH---EVLKVMQDLAEegMTMVIVTHEIGFAEK 201
|
250 260
....*....|....*....|....*
gi 1393793683 250 ISDDIIVLDHGDVIARGKPAEIQHN 274
Cdd:PRK09493 202 VASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-270 |
3.27e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqkfqp 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gDWlNPAQLGQRlfykmfggthlvnRAGLArtfQNIRL---FREMSVVEnllvaqhMrvnrnllaGVLNTPAYRRSENDA 160
Cdd:PRK13548 68 -DW-SPAELARR-------------RAVLP---QHSSLsfpFTVEEVVA-------M--------GRAPHGLSRAEDDAL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMC------TSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHD 234
Cdd:PRK13548 115 VAAA---LAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERG 191
|
250 260 270
....*....|....*....|....*....|....*.
gi 1393793683 235 ITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAE 270
Cdd:PRK13548 192 LAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-271 |
3.30e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.55 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 15 FGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNArnktTNVIQVLGQKFQPGdwlnpaqlgq 94
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHARDRKVG---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 rlfykmFggthlvnraglarTFQNIRLFREMSVVENllVAQHMRVnrnllagvlnTPAYRRSENDALD-RAFYWLEVVDL 173
Cdd:PRK10851 78 ------F-------------VFQHYALFRHMTVFDN--IAFGLTV----------LPRRERPNAAAIKaKVTQLLEMVQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLnpvETHKLSEIIRFLRDHHD---ITVLLIEHDMGMVMGI 250
Cdd:PRK10851 127 AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL---DAQVRKELRRWLRQLHEelkFTSVFVTHDQEEAMEV 203
|
250 260
....*....|....*....|.
gi 1393793683 251 SDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK10851 204 ADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-276 |
4.06e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTT---VFNCLTGFYRAS--GGNILFNarnkttnviqvlgqk 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTllrVFNRLIELYPEArvSGEVYLD--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnpaqlGQRLFyKMfggTHLVNRAGLARTFQNIRLFREMSVVENllVAQHMRVNRNllagVLNTPAYRRSENDA 160
Cdd:PRK14247 69 ------------GQDIF-KM---DVIELRRRVQMVFQIPNPIPNLSIFEN--VALGLKLNRL----VKSKKELQERVRWA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCAnrlAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIirFLRDHHDITVLLI 240
Cdd:PRK14247 127 LEKAQLWDEVKDRLDAP---AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESL--FLELKKDMTIVLV 201
|
250 260 270
....*....|....*....|....*....|....*.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEK 276
Cdd:PRK14247 202 THFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-271 |
4.88e-26 |
|
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: 107.61 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGG--IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvLGQkfqp 83
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID--------LRQ---- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwLNPAQLGQRLFYKMfggthlvnraglartfQNIRLFrEMSVVENLLVAqhmrvnrnllagvlntpayrrSENDALDR 163
Cdd:COG2274 542 ---IDPASLRRQIGVVL----------------QDVFLF-SGTIRENITLG---------------------DPDATDEE 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AFYWLEVVDLVDCANRLA-------GEM----SYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKlseIIRFLRDH 232
Cdd:COG2274 581 IIEAARLAGLHDFIEALPmgydtvvGEGgsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI---ILENLRRL 657
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 233 -HDITVLLIEHDMGMVMgISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG2274 658 lKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-260 |
5.42e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 100.54 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviQVLGQKFQPGDWlnpaqlgqrlfY 98
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID---------GVDLRDLDLESL-----------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 KMFGgthLVnraglartFQNIRLFrEMSVVENLLvaqhmrvnrnllagvlntpayrrsendaldrafywlevvdlvdcan 178
Cdd:cd03228 76 KNIA---YV--------PQDPFLF-SGTIRENIL---------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 179 rlagemSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVLLIEHDMGMVMgISDDIIVLD 258
Cdd:cd03228 98 ------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLD 168
|
..
gi 1393793683 259 HG 260
Cdd:cd03228 169 DG 170
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-271 |
6.44e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 6.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARN------KTTNVIQVLGQKFQPGDWlnpaQL 92
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvKLSDIRKKVGLVFQYPEY----QL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 GQRLFYK--MFGGTHLvnraGLARTFQNIRLFREMSVVenllvaqhmrvnrnllagvlntpayrrsendALDRAFYwlev 170
Cdd:PRK13637 97 FEETIEKdiAFGPINL----GLSEEEIENRVKRAMNIV-------------------------------GLDYEDY---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 171 vdlvdcANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGI 250
Cdd:PRK13637 138 ------KDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKL 211
|
250 260
....*....|....*....|.
gi 1393793683 251 SDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13637 212 ADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-271 |
1.72e-25 |
|
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: 101.95 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQrlfyk 99
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA---------------MSRKELRE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 mfggthlVNRAGLARTFQNIRLFREMSVVENllVAQHMRVnrnllAGVlntpayrrSENDALDRAFYWLEVVDLVDCANR 179
Cdd:cd03294 99 -------LRRKKISMVFQSFALLPHRTVLEN--VAFGLEV-----QGV--------PRAEREERAAEALELVGLEGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDH 259
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
250
....*....|..
gi 1393793683 260 GDVIARGKPAEI 271
Cdd:cd03294 237 GRLVQVGTPEEI 248
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-275 |
3.85e-25 |
|
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: 104.46 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHF--GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqp 83
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD------------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwLNPAQLgqrlfykmfggthlvnRAGLARTFQNIRLFReMSVVENLLVA------QHMRvnrnllagvlntpayrrse 157
Cdd:COG4987 402 ---LDEDDL----------------RRRIAVVPQRPHLFD-TTLRENLRLArpdatdEELW------------------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 158 nDALDRA--FYWLEvvDLVDCANRLAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPV-ETHKLSEIIRFLR 230
Cdd:COG4987 443 -AALERVglGDWLA--ALPDGLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAAtEQALLADLLEALA 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 231 DHhdiTVLLIEHDMgMVMGISDDIIVLDHGDVIARGKPAEIQHNE 275
Cdd:COG4987 520 GR---TVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-283 |
5.47e-24 |
|
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: 101.05 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASG--GNILFNarnkttnviqvlgqkfq 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWS----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdwlnpaqlGQRLFYKMFGGTHlvnRAGLARTFQNIRLFREMSVVENLLVAQHMRVNrnllAGVLNTPA-YRRSENdal 161
Cdd:TIGR02633 64 ----------GSPLKASNIRDTE---RAGIVIIHQELTLVPELSVAENIFLGNEITLP----GGRMAYNAmYLRAKN--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 drafyWLEVVDLVDCAN-RLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdHHDITVLLI 240
Cdd:TIGR02633 124 -----LLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYI 197
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARgKPAEIQHNEKVIAAYLG 283
Cdd:TIGR02633 198 SHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSEDDIITMMVG 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-291 |
1.83e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFN----ARNKTTNVIQ---VLGQKFQpgdwlnpa 90
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpFKRRKEFARRigvVFGQRSQ-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 91 qlgqrlfykmfggthlvnraglartfqnirLFREMSVVENLLVAQHMrvnrnllagvlntpaYRRSENDALDRAFYWLEV 170
Cdd:COG4586 107 ------------------------------LWWDLPAIDSFRLLKAI---------------YRIPDAEYKKRLDELVEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 171 VDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGI 250
Cdd:COG4586 142 LDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1393793683 251 SDDIIVLDHGDVIARGKPAEIQH---NEKVIAAYLGTDESEVNL 291
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKErfgPYKTIVLELAEPVPPLEL 265
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-262 |
1.93e-23 |
|
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: 95.01 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqKFQPGD 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT---------DLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfykmfggthlvnrAGLARTFQNIRLFREMSVVENLlvAQHMRVnrnllagvlntpayRRSENDALDRAF 165
Cdd:cd03301 72 ------------------------RDIAMVFQNYALYPHMTVYDNI--AFGLKL--------------RKVPKDEIDERV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWL-EVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvethKL-----SEIIRFLRDhHDITVLL 239
Cdd:cd03301 112 REVaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA----KLrvqmrAELKRLQQR-LGTTTIY 186
|
250 260
....*....|....*....|...
gi 1393793683 240 IEHDMGMVMGISDDIIVLDHGDV 262
Cdd:cd03301 187 VTHDQVEAMTMADRIAVMNDGQI 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-271 |
2.37e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLgqR 95
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA---------------LSEKEL--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFykmfggthlvnRAGLARTFQNIRLFREMSVVENllVAQHMRvnrnlLAGVlntpayrrSENDALDRAFYWLEVVDLVD 175
Cdd:PRK11153 79 KA-----------RRQIGMIFQHFNLLSSRTVFDN--VALPLE-----LAGT--------PKAEIKARVTELLELVGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHK----LSEIIRFLrdhhDITVLLIEHDMGMVMGIS 251
Cdd:PRK11153 133 KADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSilelLKDINREL----GLTIVLITHEMDVVKRIC 208
|
250 260
....*....|....*....|
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI 271
Cdd:PRK11153 209 DRVAVIDAGRLVEQGTVSEV 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-266 |
3.43e-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: 94.67 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQ---RGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvlgqkfqpgdWLNPAQlgqr 95
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----------------LFDSRK---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 lfyKMFGGTHlvnRAGLARTFQNIRLFREMSVVENLLVAqhMRVNRNllagvlntpayrrseNDALDRAFYWLEVVDLVD 175
Cdd:cd03297 67 ---KINLPPQ---QRKIGLVFQQYALFPHLNVRENLAFG--LKRKRN---------------REDRISVDELLDLLGLDH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLnpvETHKLSEIIRFLRDHH---DITVLLIEHDMGMVMGISD 252
Cdd:cd03297 124 LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL---DRALRLQLLPELKQIKknlNIPVIFVTHDLSEAEYLAD 200
|
250
....*....|....
gi 1393793683 253 DIIVLDHGDVIARG 266
Cdd:cd03297 201 RIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-263 |
5.53e-23 |
|
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: 93.86 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 7 HVEHLMMHFG-GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkfqpGD 85
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN------------------GK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLNPAQLGQRLFYKMfggthlvnraglartfQNIR--LFREmSVVENLLVaqhmrvnrnllaGVLNTPAYRRSENDALDR 163
Cdd:cd03226 63 PIKAKERRKSIGYVM----------------QDVDyqLFTD-SVREELLL------------GLKELDAGNEQAETVLKD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 afywLEVVDLVDcanRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHD 243
Cdd:cd03226 114 ----LDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHD 185
|
250 260
....*....|....*....|
gi 1393793683 244 MGMVMGISDDIIVLDHGDVI 263
Cdd:cd03226 186 YEFLAKVCDRVLLLANGAIV 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-282 |
5.78e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 94.69 E-value: 5.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLtgfyrasggNILFNARNKTtnvIQVLGQKFQPGD 85
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL---------NLLETPDSGQ---LNIAGHQFDFSQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLNPAQlGQRLfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAQhMRVnrnllAGVlntpayrrSENDALDRAF 165
Cdd:COG4161 71 KPSEKA-IRLL------------RQKVGMVFQQYNLWPHLTVMENLIEAP-CKV-----LGL--------SKEQAREKAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 YWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdHHDITVLLIEHDMG 245
Cdd:COG4161 124 KLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVE 202
|
250 260 270
....*....|....*....|....*....|....*...
gi 1393793683 246 MVMGISDDIIVLDHGDVIARGKPAEIQHNE-KVIAAYL 282
Cdd:COG4161 203 FARKVASQVVYMEKGRIIEQGDASHFTQPQtEAFAHYL 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-276 |
5.92e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.04 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQVLGQK 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT-----INLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnPAQLgqrlfyKMFGGTHL-VNRAGLARTFQNIRLFREMSVVENLLVAQhmrvnrnllAGVLNTpayrrSEND 159
Cdd:PRK10619 76 --------DGQL------KVADKNQLrLLRTRLTMVFQHFNLWSHMTVLENVMEAP---------IQVLGL-----SKQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALDRAFYWLEVVDLVDCAN-RLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvetHKLSEIIRFLRD--HHDIT 236
Cdd:PRK10619 128 ARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQlaEEGKT 204
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 237 VLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEK 276
Cdd:PRK10619 205 MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-264 |
7.33e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 7.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 14 HFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvlgQKFQ-PGDWLNpaql 92
Cdd:PRK11288 13 TFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE----------MRFAsTTAALA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 gqrlfykmfggthlvnrAGLARTFQNIRLFREMSVVENLLVAQhmRVNRnllAGVLNTPAYRRSENDALDRafywleVVD 172
Cdd:PRK11288 79 -----------------AGVAIIYQELHLVPEMTVAENLYLGQ--LPHK---GGIVNRRLLNYEAREQLEH------LGV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 LVDCANRLaGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDItVLLIEHDMGMVMGISD 252
Cdd:PRK11288 131 DIDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCD 208
|
250
....*....|..
gi 1393793683 253 DIIVLDHGDVIA 264
Cdd:PRK11288 209 AITVFKDGRYVA 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-272 |
8.09e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.77 E-value: 8.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqkfqp 83
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwlnpaqlgqrlfykmFGGTHLVNRAGLARTFQNIRLFREMSVVENLLVAqhmRVNRNLLAGVLNTPAYRrsENDALdr 163
Cdd:PRK10762 70 -----------------FNGPKSSQEAGIGIIHQELNLIPQLTIAENIFLG---REFVNRFGRIDWKKMYA--EADKL-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 afywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHD 243
Cdd:PRK10762 126 ----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQG-RGIVYISHR 200
|
250 260
....*....|....*....|....*....
gi 1393793683 244 MGMVMGISDDIIVLDHGDVIARGKPAEIQ 272
Cdd:PRK10762 201 LKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-266 |
9.46e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLtgfyrasggNILFNARNKTTNVIqvlGQKFQPGDWL 87
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL---------NLLEMPRSGTLNIA---GNHFDFSKTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 NPAQlGQRLfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAQhMRVnrnllAGVlntpayrrSENDALDRAFYW 167
Cdd:PRK11124 73 SDKA-IREL------------RRNVGMVFQQYNLWPHLTVQQNLIEAP-CRV-----LGL--------SKDQALARAEKL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHDMGMV 247
Cdd:PRK11124 126 LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVA 204
|
250
....*....|....*....
gi 1393793683 248 MGISDDIIVLDHGDVIARG 266
Cdd:PRK11124 205 RKTASRVVYMENGHIVEQG 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-243 |
1.10e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.16 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIK----ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviQVLGqkf 81
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-------PVTG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qPGdwlnpaqlgqrlfykmfggthlvnrAGLARTFQNIRLFREMSVVENllVAQHMRvnrnlLAGVlnTPAYRRsendal 161
Cdd:COG4525 74 -PG-------------------------ADRGVVFQKDALLPWLNVLDN--VAFGLR-----LRGV--PKAERR------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 DRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIE 241
Cdd:COG4525 113 ARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLIT 192
|
..
gi 1393793683 242 HD 243
Cdd:COG4525 193 HS 194
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-276 |
1.45e-22 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.71 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarNKTTNVIQVLGQKFQPGD 85
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVG--GEEIRLKPDRDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnPAQLgQRLfykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVA-QHmrvnrnllagVLntpayRRSENDALDRA 164
Cdd:COG4598 87 ---RRQL-QRI------------RTRLGMVFQSFNLWSHMTVLENVIEApVH----------VL-----GRPKAEAIERA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNP--VethklSEIIRFLRDHHD--ITVLLI 240
Cdd:COG4598 136 EALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPelV-----GEVLKVMRDLAEegRTMLVV 210
|
250 260 270
....*....|....*....|....*....|....*.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEK 276
Cdd:COG4598 211 THEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-285 |
1.72e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfNARNKTTNviqvlgqk 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI--TINNINYN-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnpaQLGQRLFYKMfggthlvnraGLARTFQNIRLFREMSVVENLLVAQHmrvnrnLLAGVLNTPAYRRSEndA 160
Cdd:PRK09700 71 ----------KLDHKLAAQL----------GIGIIYQELSVIDELTVLENLYIGRH------LTKKVCGVNIIDWRE--M 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLI 240
Cdd:PRK09700 123 RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYI 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQhNEKVIAAYLGTD 285
Cdd:PRK09700 202 SHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS-NDDIVRLMVGRE 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-262 |
2.39e-22 |
|
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: 92.09 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQkfqpgdwlNPAQLGQR 95
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN------------GQ--------DVSDLRGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFYKMfggthlvnRAGLARTFQNIRLFREMSVVENllVAQHMRVnrnllagvlnTPAYRRsenDALDRAFYWLEVVDLVD 175
Cdd:cd03292 72 AIPYL--------RRKIGVVFQDFRLLPDRNVYEN--VAFALEV----------TGVPPR---EIRKRVPAALELVGLSH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVEThklSEIIRFLRDHHD--ITVLLIEHDMGMVMGISDD 253
Cdd:cd03292 129 KHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT---WEIMNLLKKINKagTTVVVATHAKELVDTTRHR 205
|
....*....
gi 1393793683 254 IIVLDHGDV 262
Cdd:cd03292 206 VIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-266 |
2.41e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfNARNKTTNVIQVLGQKfqpgdwl 87
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITIDTARSLSQQ------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 npaqlgQRLFYKMfggthlvnRAGLARTFQNIRLFREMSVVENLLvaqhmrvnrnllAGVLNTPAYRRSENDALDRAFyw 167
Cdd:PRK11264 77 ------KGLIRQL--------RQHVGFVFQNFNLFPHRTVLENII------------EGPVIVKGEPKEEATARAREL-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMV 247
Cdd:PRK11264 129 LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFA 207
|
250
....*....|....*....
gi 1393793683 248 MGISDDIIVLDHGDVIARG 266
Cdd:PRK11264 208 RDVADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-280 |
4.70e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.88 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHF-GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviQVLGQKF 81
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV------------KVMGREV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 QPGD--WLNpaqlgqrlfykmfggthlvNRAGLarTFQNI--RLFrEMSVVENLLVAQhmrVNRNLLAGVLNtpayRRSE 157
Cdd:PRK13647 70 NAENekWVR-------------------SKVGL--VFQDPddQVF-SSTVWDDVAFGP---VNMGLDKDEVE----RRVE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 158 nDALDrafywleVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLrDHHDITV 237
Cdd:PRK13647 121 -EALK-------AVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTV 191
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 238 LLIEHDMGMVMGISDDIIVLDHGDVIARGKPaEIQHNEKVIAA 280
Cdd:PRK13647 192 IVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQ 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-271 |
5.40e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.24 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkTTNViqvlgqk 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-ITHV------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwlnPAQlgQRlfykmfggtHlVNRaglarTFQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayRRSENDA 160
Cdd:PRK09452 82 --------PAE--NR---------H-VNT-----VFQSYALFPHMTVFENVAFGLRMQ---------------KTPAAEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpvetHKL-----SEiIRFLRDHHDI 235
Cdd:PRK09452 122 TPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD----YKLrkqmqNE-LKALQRKLGI 196
|
250 260 270
....*....|....*....|....*....|....*.
gi 1393793683 236 TVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK09452 197 TFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-276 |
5.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFQPGDWLNPAQlgqrlF 97
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTR-----F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 98 YKMFGGTHLVNRAGLARTFQNIRLFREMsvvenllvaqhmrVNRNLLAGVLntpAYRRSENDALDRAFYWLEVVDL-VDC 176
Cdd:PRK13651 95 KKIKKIKEIRRRVGVVFQFAEYQLFEQT-------------IEKDIIFGPV---SMGVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMVMGISDDIIV 256
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIF 237
|
250 260
....*....|....*....|
gi 1393793683 257 LDHGDVIARGKPAEIQHNEK 276
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSDNK 257
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-252 |
5.87e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCltgfyrasggnilFNARNKTTNVIQVLGQKFQP 83
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRC-------------FNRLNDLIPGFRVEGKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 GdwlnpaqlgQRLFYKMFGGTHLVNRAGLarTFQNIRLFREmSVVENllVAQHMRVNRnlLAGVLNTPAYRrsendALDR 163
Cdd:PRK14243 76 G---------KNLYAPDVDPVEVRRRIGM--VFQKPNPFPK-SIYDN--IAYGARING--YKGDMDELVER-----SLRQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AFYWLEVVD-LVDCANRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVLLIEH 242
Cdd:PRK14243 135 AALWDEVKDkLKQSGLSLSG----GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTH 208
|
250
....*....|
gi 1393793683 243 DMGMVMGISD 252
Cdd:PRK14243 209 NMQQAARVSD 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-278 |
7.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIK--ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFyrasggnILFNARNKTtnVIQVLG 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL-------LLPDDNPNS--KITVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 79 QKfqpgdwlnpaqLGQRLFYKMfggthlvnRAGLARTFQNirlfremsvVENLLVAQhmRVNRNLLAGVLNTPAYRRSEN 158
Cdd:PRK13640 72 IT-----------LTAKTVWDI--------REKVGIVFQN---------PDNQFVGA--TVGDDVAFGLENRAVPRPEMI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 159 DALDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVL 238
Cdd:PRK13640 122 KIVRDV---LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVI 198
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 239 LIEHDMGMVMGiSDDIIVLDHGDVIARGKPAEIQHNEKVI 278
Cdd:PRK13640 199 SITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-256 |
9.90e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.87 E-value: 9.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHF---GGI--------KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNK 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 70 TTnviqvlgqkfqpgdwLNPAQLGQRlfykmfggthlvnRAGLARTFQ------NIRlfreMSVVEnlLVAQHMRVNRnl 143
Cdd:COG4608 83 TG---------------LSGRELRPL-------------RRRMQMVFQdpyaslNPR----MTVGD--IIAEPLRIHG-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 144 lagvLNTPAYRRsendalDRAFYWLEVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpvethkL 222
Cdd:COG4608 127 ----LASKAERR------ERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD------V 190
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 223 S---EIIRFLRD---HHDITVLLIEHDMGMVMGISDDIIV 256
Cdd:COG4608 191 SiqaQVLNLLEDlqdELGLTYLFISHDLSVVRHISDRVAV 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-279 |
1.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.61 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGG-----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqVLGQ 79
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI--------YIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 80 KFQPGDWLNPAQlgQRlfyKMFGGTHLVNRAGLARTFQNIRLFREMsvvenllvaqhmrVNRNLLAGVLntpAYRRSEND 159
Cdd:PRK13631 93 KKNNHELITNPY--SK---KIKNFKELRRRVSMVFQFPEYQLFKDT-------------IEKDIMFGPV---ALGVKKSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALDRAFYWLEVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVL 238
Cdd:PRK13631 152 AKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVF 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 239 LIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIA 279
Cdd:PRK13631 231 VITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-290 |
1.14e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.61 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGfyrasggniLFNARNKTTNVIQVLGqkfqp 83
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---------LITGDKSAGSHIELLG----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwlNPAQLGQRLfykmfGGTHLVNRAGLARTFQNIRLFREMSVVENLLVaqhmrvnrnllaGVL-NTPAYRRS----EN 158
Cdd:PRK09984 69 ----RTVQREGRL-----ARDIRKSRANTGYIFQQFNLVNRLSVLENVLI------------GALgSTPFWRTCfswfTR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 159 DALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVL 238
Cdd:PRK09984 128 EQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1393793683 239 LIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQhNEKVIAAYLGTDESEVN 290
Cdd:PRK09984 208 VTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD-NERFDHLYRSINRVEEN 258
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-278 |
1.37e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.59 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI-----------LFNARNKttnviqvLGQKFQpgdwlN 88
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenLKEIRKK-------IGIIFQ-----N 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 89 PAQlgqrlfyKMFGGThlvNRAGLARTFQNIRLFR-EM-SVVENLLVAQHMRvnrnllagvlntpayrrsenDALDRAFY 166
Cdd:PRK13632 92 PDN-------QFIGAT---VEDDIAFGLENKKVPPkKMkDIIDDLAKKVGME--------------------DYLDKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 167 WLevvdlvdcanrlagemSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGM 246
Cdd:PRK13632 142 NL----------------SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDE 205
|
250 260 270
....*....|....*....|....*....|..
gi 1393793683 247 VMgISDDIIVLDHGDVIARGKPAEIQHNEKVI 278
Cdd:PRK13632 206 AI-LADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-271 |
1.67e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.91 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFqpgdwl 87
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 npAQLGQRlfykmfggTHLvnraglartfqNIRLfremSVVEnlLVA----QHMRvnrnllaGVLnTPAYRRsendALDR 163
Cdd:COG4604 78 --AILRQE--------NHI-----------NSRL----TVRE--LVAfgrfPYSK-------GRL-TAEDRE----IIDE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPaagLNPVETHKLSEIIRFLR---DHHDITVLLI 240
Cdd:COG4604 119 A---IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP---LNNLDMKHSVQMMKLLRrlaDELGKTVVIV 192
|
250 260 270
....*....|....*....|....*....|.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG4604 193 LHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-278 |
1.70e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.29 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkfqpgdwlnpaqlGQRL 96
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK---------------------------GEPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 97 FYKMFGgthLVN-RAGLARTFQNirlfremsvVENLLVAQhmRVNRNLLAGVLNtpaYRRSENDALDRAFYWLEVVDLVD 175
Cdd:PRK13639 67 KYDKKS---LLEvRKTVGIVFQN---------PDDQLFAP--TVEEDVAFGPLN---LGLSKEEVEKRVKEALKAVGMEG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVEThklSEIIRFLRDHHD--ITVLLIEHDMGMVMGISDD 253
Cdd:PRK13639 130 FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA---SQIMKLLYDLNKegITIIISTHDVDLVPVYADK 206
|
250 260
....*....|....*....|....*
gi 1393793683 254 IIVLDHGDVIARGKPAEIQHNEKVI 278
Cdd:PRK13639 207 VYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-285 |
2.24e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.23 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIK--ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKT-TNVIQV- 76
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 77 --LGQKFQpgdwlNPAQlgqrlfykMFGGTHLvnRAGLARTFQNIRLFREmSVVEnllvaqhmRVNrnllagvlntpayr 154
Cdd:PRK13635 81 rqVGMVFQ-----NPDN--------QFVGATV--QDDVAFGLENIGVPRE-EMVE--------RVD-------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 155 rsenDALDRafywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHD 234
Cdd:PRK13635 123 ----QALRQ-------VGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKG 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1393793683 235 ITVLLIEHDMGMVMGiSDDIIVLDHGDVIARGKPAEI-QHNEKVIAayLGTD 285
Cdd:PRK13635 192 ITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfKSGHMLQE--IGLD 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-289 |
4.43e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviQVLGQK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI------------SLCGEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 FqPGDwlnpaqlgqrlfykmfgGTHLVNRAGLARTFQNirLFREMSVVENLLVAQHMrvnrnllagvlntpaYRRSENDA 160
Cdd:PRK13537 71 V-PSR-----------------ARHARQRVGVVPQFDN--LDPDFTVRENLLVFGRY---------------FGLSAAAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLI 240
Cdd:PRK13537 116 RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLT 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIqhnekvIAAYLGTDESEV 289
Cdd:PRK13537 195 THFMEEAERLCDRLCVIEEGRKIAEGAPHAL------IESEIGCDVIEI 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-263 |
4.80e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.55 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 15 FGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRAS--GGNILFNarnkttnviqvlGQKFQpgdwlnpaql 92
Cdd:NF040905 11 FPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFD------------GEVCR---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 gqrlfykmFGGTHLVNRAGLARTFQNIRLFREMSVVENLLVAqhmrvNRNLLAGVLNTpayrrseNDALDRAFYWLEVVD 172
Cdd:NF040905 69 --------FKDIRDSEALGIVIIHQELALIPYLSIAENIFLG-----NERAKRGVIDW-------NETNRRARELLAKVG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 LVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGMVMGISD 252
Cdd:NF040905 129 LDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVAD 207
|
250
....*....|.
gi 1393793683 253 DIIVLDHGDVI 263
Cdd:NF040905 208 SITVLRDGRTI 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
5.37e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLtgfyrasggnilfNARNKTTNVIQVLGQ-KFqpg 84
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-------------NRMNELESEVRVEGRvEF--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqLGQRLFYKMFGGTHLvnRAGLARTFQNIRLFrEMSVVENL-----LVAQHMRVNrnlLAGVLNTpayrrsend 159
Cdd:PRK14258 72 -------FNQNIYERRVNLNRL--RRQVSMVHPKPNLF-PMSVYDNVaygvkIVGWRPKLE---IDDIVES--------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALDRAFYWLEVVDLVdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLL 239
Cdd:PRK14258 130 ALKDADLWDEIKHKI---HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVI 206
|
250
....*....|...
gi 1393793683 240 IEHDMGMVMGISD 252
Cdd:PRK14258 207 VSHNLHQVSRLSD 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-260 |
7.20e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.68 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqkfQPGdwlnPAQLgqrlfykm 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-----------EPG----PDRM-------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnraglaRTFQNIRLFREMSVVENLLVAqhmrVNRNLlagvlntPAYRRSENDALDRAFywLEVVDLVDCANRL 180
Cdd:TIGR01184 58 -------------VVFQNYSLLPWLTVRENIALA----VDRVL-------PDLSKSERRAIVEEH--IALVGLTEAADKR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDHG 260
Cdd:TIGR01184 112 PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-270 |
7.22e-21 |
|
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: 88.44 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFqpgdwlnpAQLGQR 95
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI--------GVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFykMFGGThlvnraglarTFQNIRLFREMSVVENLLVAQHmRVNRNLLAgvlntpayRRSENDaldrafYWLEVVDlvd 175
Cdd:cd03254 86 TF--LFSGT----------IMENIRLGRPNATDEEVIEAAK-EAGAHDFI--------MKLPNG------YDTVLGE--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 canrLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdhHDITVLLIEHDMGMVMGiSDDII 255
Cdd:cd03254 136 ----NGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKIL 208
|
250
....*....|....*
gi 1393793683 256 VLDHGDVIARGKPAE 270
Cdd:cd03254 209 VLDDGKIIEEGTHDE 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-271 |
1.43e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 15 FGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviQVLGQKFqpgdwlnPAQlgQ 94
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI------------TVLGVPV-------PAR--A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 RLFYKmfggthlvnRAGLARTFQNirLFREMSVVENLLV-AQHMRVNRNLLAGVLNTpayrrsendaldrafyWLEVVDL 173
Cdd:PRK13536 110 RLARA---------RIGVVPQFDN--LDLEFTVRENLLVfGRYFGMSTREIEAVIPS----------------LLEFARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMVMGISDD 253
Cdd:PRK13536 163 ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDR 241
|
250
....*....|....*...
gi 1393793683 254 IIVLDHGDVIARGKPAEI 271
Cdd:PRK13536 242 LCVLEAGRKIAEGRPHAL 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-271 |
2.41e-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: 90.63 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGF--YRASGGNILFN-ARNKTTNVIQ------- 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvALCEKCGYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 76 ---VLGQKFQP--GDWLNPAQLGQRLFYKMfggthlvNRAGLARTFQnirLFREMSVVENLLVAqhmrvnrnllagvLNT 150
Cdd:TIGR03269 81 pcpVCGGTLEPeeVDFWNLSDKLRRRIRKR-------IAIMLQRTFA---LYGDDTVLDNVLEA-------------LEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 151 PAYrrSENDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLR 230
Cdd:TIGR03269 138 IGY--EGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAV 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 231 DHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:TIGR03269 216 KASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-271 |
4.12e-20 |
|
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: 88.19 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRA---SGGNILFNARN----KTTNV 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 74 IQVLGQK----FQ-PGDWLNPaqlgqrlfykmfggthlVNRAGlartfqniRLFREMsvvenllvaqhMRVNRNLlagvl 148
Cdd:COG0444 81 RKIRGREiqmiFQdPMTSLNP-----------------VMTVG--------DQIAEP-----------LRIHGGL----- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 149 ntpayrrSENDALDRAFYWLEVVDLVDCANRLA---GEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEI 225
Cdd:COG0444 120 -------SKAEARERAIELLERVGLPDPERRLDrypHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNL 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1393793683 226 IRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG0444 193 LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-283 |
4.42e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 88.32 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 36 LIGPNGAGKTTVFNCLTGFYRASGGNILFNArnktTNVIQVlgqkfqpgdwlnPAQlgqrlfykmfggthlvnRAGLART 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG----EDVTNV------------PPH-----------------LRHINMV 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 116 FQNIRLFREMSVVENLLVAQHMRvnrnllagvlNTPayrRSENDAldRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIA 195
Cdd:TIGR01187 48 FQSYALFPHMTVEENVAFGLKMR----------KVP---RAEIKP--RVLEALRLVQLEEFADRKPHQLSGGQQQRVALA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 196 RAMCTSPEMICLDEPAAGLNpvetHKLSEIIRF-LRDHHD---ITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:TIGR01187 113 RALVFKPKILLLDEPLSALD----KKLRDQMQLeLKTIQEqlgITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
250
....*....|....
gi 1393793683 272 --QHNEKVIAAYLG 283
Cdd:TIGR01187 189 yeEPANLFVARFIG 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-285 |
4.95e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFncltgfyRASGGNIlfnarNKTTNVIQVLGqkfQPGD 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLL-------RAINGTL-----TPTAGTVLVAG---DDVE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLNPAQLGQRlfykmfggthlvnragLARTFQnirlfrEMSVVENLLVAQHMRVNRNLLAGVLN--TPAYRRSENDALDR 163
Cdd:PRK09536 69 ALSARAASRR----------------VASVPQ------DTSLSFEFDVRQVVEMGRTPHRSRFDtwTETDRAAVERAMER 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 afywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHD 243
Cdd:PRK09536 127 -------TGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHD 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1393793683 244 MGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAY-----LGTD 285
Cdd:PRK09536 199 LDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFdartaVGTD 245
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-283 |
5.84e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 89.40 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 15 FGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFnarnkttnviqvLGQKFQpgdwlnpaqlgq 94
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF------------QGKEID------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 rlfykmFGGTHLVNRAGLARTFQNIRLFREMSVVENllvaqhMRVNRNLLAG--VLNTPAYRRSEN--DALDrafywlev 170
Cdd:PRK10982 64 ------FKSSKEALENGISMVHQELNLVLQRSVMDN------MWLGRYPTKGmfVDQDKMYRDTKAifDELD-------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 171 VDlVDCANRLAgEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGMVMGI 250
Cdd:PRK10982 124 ID-IDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQL 200
|
250 260 270
....*....|....*....|....*....|...
gi 1393793683 251 SDDIIVLDHGDVIARgKPAEIQHNEKVIAAYLG 283
Cdd:PRK10982 201 CDEITILRDGQWIAT-QPLAGLTMDKIIAMMVG 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-283 |
6.50e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.43 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVfncLTGFYRAsggnILFNARNKTTNVIQVLGQKFQPGD 85
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTL---LRTFNRL----LELNEEARVEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wLNPAQLgqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENllVAQHMRVNrNLLAGvlntpayrRSEND-----A 160
Cdd:PRK14267 78 -VDPIEV----------------RREVGMVFQYPNPFPHLTIYDN--VAIGVKLN-GLVKS--------KKELDervewA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRAFYWLEVVDLVdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhhDITVLLI 240
Cdd:PRK14267 130 LKKAALWDEVKDRL---NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLV 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHN------EKVIAAYLG 283
Cdd:PRK14267 205 THSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENpeheltEKYVTGALG 253
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-244 |
1.59e-19 |
|
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: 85.18 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviQV 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV------------RL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 77 LGQKFqpgdwlnpAQLGQRlfykmfggthlvNRAGLAR-----TFQNIRLFREMSVVENLLVaqhmrvnrnllagvlntP 151
Cdd:COG4181 72 AGQDL--------FALDED------------ARARLRArhvgfVFQSFQLLPTLTALENVML-----------------P 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 152 AYRRSENDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRD 231
Cdd:COG4181 115 LELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR 194
|
250
....*....|...
gi 1393793683 232 HHDITVLLIEHDM 244
Cdd:COG4181 195 ERGTTLVLVTHDP 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-279 |
1.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFyrasggnilfnarnkttnVIQVLGQKFQpGDWLNPAQLGqrlfy 98
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------------------IISETGQTIV-GDYAIPANLK----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 KMFGGTHLVNRAGLARTFQNIRLFREMsvvenllvaqhmrVNRNLLAGVLNTPAyrrSENDALDRAFYWLEVVDLV-DCA 177
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQFPEYQLFQET-------------IEKDIAFGPVNLGE---NKQEAYKKVPELLKLVQLPeDYV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVL 257
Cdd:PRK13645 145 KRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
250 260
....*....|....*....|..
gi 1393793683 258 DHGDVIARGKPAEIQHNEKVIA 279
Cdd:PRK13645 225 HEGKVISIGSPFEIFSNQELLT 246
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-276 |
2.21e-19 |
|
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: 84.73 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRAsggnilfnarnkttNVIQVLGQKFQPGDWLNPAQLGQRLFykmfg 102
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPP--------------GLTQTSGEILLDGRPLLPLSIRGRHI----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 103 gthlvnraglARTFQNirlfrEMSVVENLL-VAQHMRvNRNLLAGVLntpayrrsENDALDRAFYWLEVVDLVDCANRL- 180
Cdd:TIGR02770 65 ----------ATIMQN-----PRTAFNPLFtMGNHAI-ETLRSLGKL--------SKQARALILEALEAVGLPDPEEVLk 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 --AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLD 258
Cdd:TIGR02770 121 kyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMD 200
|
250
....*....|....*...
gi 1393793683 259 HGDVIARGKPAEIQHNEK 276
Cdd:TIGR02770 201 DGRIVERGTVKEIFYNPK 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-271 |
4.68e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNAR--NKTTNVIQVLGQK----FQPGDwlnpaqlgQ 94
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQvatvFQDPE--------Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 RLFYKMFGgthlvnrAGLARTFQNI-----RLFREMSVVENLLVAQHMRvnrnllagvlNTPayrrsendaldrafywle 169
Cdd:PRK13638 89 QIFYTDID-------SDIAFSLRNLgvpeaEITRRVDEALTLVDAQHFR----------HQP------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 170 vvdlVDCanrlageMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFL--RDHHditVLLIEHDMGMV 247
Cdd:PRK13638 134 ----IQC-------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNH---VIISSHDIDLI 199
|
250 260
....*....|....*....|....
gi 1393793683 248 MGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13638 200 YEISDAVYVLRQGQILTHGAPGEV 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-257 |
7.30e-19 |
|
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: 86.19 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGnilfnarnkttnVIQVLGQKFQPGDwlnPAQLGQR 95
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG------------SIAVNGVPLADAD---ADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 LFYkmfggthlvnraglarTFQNIRLFrEMSVVENLLVAQhmrvnrnllagvlntPAYRRSE-NDALDRAFYWLEVVDLV 174
Cdd:TIGR02857 398 IAW----------------VPQHPFLF-AGTIAENIRLAR---------------PDASDAEiREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 175 DCANRLAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVLLIEHDMGmVMGI 250
Cdd:TIGR02857 446 QGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLA-LAAL 522
|
....*..
gi 1393793683 251 SDDIIVL 257
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-266 |
1.25e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvlgqk 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpGDWLNPAQLGQRlfykmfggthlvNRAGLART-----FQNIRLFREMSV-----VENLLVAQHMRvnrnllagvlnt 150
Cdd:PRK11701 70 ---GQLRDLYALSEA------------ERRRLLRTewgfvHQHPRDGLRMQVsaggnIGERLMAVGAR------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 151 pAYRRSENDALDrafyWLEVVDLVdcANR---LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIR 227
Cdd:PRK11701 123 -HYGDIRATAGD----WLERVEID--AARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLR 195
|
250 260 270
....*....|....*....|....*....|....*....
gi 1393793683 228 FLRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARG 266
Cdd:PRK11701 196 GLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-270 |
1.27e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 10 HLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLtgfyrasggnilfnarNKTTNviQVLGQKFQpGDWLnp 89
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL----------------NRMND--KVSGYRYS-GDVL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 90 aqLGQRLFYKMFGGTHLVNRAGLarTFQNIRLFrEMSVVENLL--VAQHMRVNRNLLAGVLNTpayrrsendALDRAFYW 167
Cdd:PRK14271 85 --LGGRSIFNYRDVLEFRRRVGM--LFQRPNPF-PMSIMDNVLagVRAHKLVPRKEFRGVAQA---------RLTEVGLW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVD-LVDCANRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHhdITVLLIEHDMGM 246
Cdd:PRK14271 151 DAVKDrLSDSPFRLSG----GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQ 224
|
250 260
....*....|....*....|....
gi 1393793683 247 VMGISDDIIVLDHGDVIARGkPAE 270
Cdd:PRK14271 225 AARISDRAALFFDGRLVEEG-PTE 247
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-263 |
1.33e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.21 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTtnviqvlgqkFQPGdwlnpaqlgqrlfY 98
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT----------KLPE-------------Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 KmfggthlvnRAGL-ARTFQNIRL--FREMSVVENLLVAQHMRVNRNLLAGVLNTpayrrsendalDRAFY--WLEVVDL 173
Cdd:COG1101 77 K---------RAKYiGRVFQDPMMgtAPSMTIEENLALAYRRGKRRGLRRGLTKK-----------RRELFreLLATLGL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 vDCANRL---AGEMSYGQqrRLEIARAMCT--SPEMICLDEPAAGLNPvethKLSEII-----RFLRDHHdITVLLIEHD 243
Cdd:COG1101 137 -GLENRLdtkVGLLSGGQ--RQALSLLMATltKPKLLLLDEHTAALDP----KTAALVlelteKIVEENN-LTTLMVTHN 208
|
250 260
....*....|....*....|
gi 1393793683 244 MGMVMGISDDIIVLDHGDVI 263
Cdd:COG1101 209 MEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-271 |
1.47e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQvlgQKFQPgdwlnpaqlgqrlfy 98
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQ---KEIKP--------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 kmfggthLVNRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRNLLAGVlntpAYRRSENDALDRAFYwlevvdlvdcaN 178
Cdd:PRK13643 82 -------VRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKI----AAEKLEMVGLADEFW-----------E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 179 RLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNP---VETHKLSEIIRflrdHHDITVLLIEHDMGMVMGISDDII 255
Cdd:PRK13643 140 KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkarIEMMQLFESIH----QSGQTVVLVTHLMDDVADYADYVY 215
|
250
....*....|....*.
gi 1393793683 256 VLDHGDVIARGKPAEI 271
Cdd:PRK13643 216 LLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-271 |
1.88e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFN----ARNKTTNVIQVLGQKFQpgdwlNPAQ--LG 93
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaiTDDNFEKLRKHIGIVFQ-----NPDNqfVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 QRLFYKM-FGgthlvnraglartfqnirlfremsvVENLLVA---QHMRVNRNLlagvlntpayrrsendaldrafywlE 169
Cdd:PRK13648 99 SIVKYDVaFG-------------------------LENHAVPydeMHRRVSEAL-------------------------K 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 170 VVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMG 249
Cdd:PRK13648 129 QVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME 208
|
250 260
....*....|....*....|..
gi 1393793683 250 iSDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13648 209 -ADHVIVMNKGTVYKEGTPTEI 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-284 |
1.94e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.12 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvlgqkfqpg 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwLNPAQLGQRLFYKMFggthlvnraglartfQNIRLFremsvvenllvaQHMRVNRNLLAGVLNTpayRRSENDALDRA 164
Cdd:PRK11607 83 --LSHVPPYQRPINMMF---------------QSYALF------------PHMTVEQNIAFGLKQD---KLPKAEIASRV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLS-EIIRFLrDHHDITVLLIEHD 243
Cdd:PRK11607 131 NEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDIL-ERVGVTCVMVTHD 209
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 244 MGMVMGISDDIIVLDHGDVIARGKPAEI-QH-NEKVIAAYLGT 284
Cdd:PRK11607 210 QEEAMTMAGRIAIMNRGKFVQIGEPEEIyEHpTTRYSAEFIGS 252
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-289 |
4.12e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQrlfyk 99
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK---------------ISDAELRE----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 mfggthlVNRAGLARTFQNIRLFREMSVVENLLVAQHmrvnrnlLAGVlntPAYRRSENdALDRafywLEVVDLVDCANR 179
Cdd:PRK10070 103 -------VRRKKIAMVFQSFALMPHMTVLDNTAFGME-------LAGI---NAEERREK-ALDA----LRQVGLENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDH 259
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250 260 270
....*....|....*....|....*....|...
gi 1393793683 260 GDVIARGKPAEIQH---NEKVIAAYLGTDESEV 289
Cdd:PRK10070 241 GEVVQVGTPDEILNnpaNDYVRTFFRGVDISQV 273
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
9-283 |
5.02e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 9 EHLMMHFggikalndvNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNViqvlgqkfqpgdwln 88
Cdd:PRK10771 12 HHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 89 PAQlgqrlfykmfggthlvnRAgLARTFQNIRLFREMSVVENLLVAQHmrvnrnllAGVLNTPAYRRSENDALDRafywl 168
Cdd:PRK10771 68 PSR-----------------RP-VSMLFQENNLFSHLTVAQNIGLGLN--------PGLKLNAAQREKLHAIARQ----- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 169 evVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVM 248
Cdd:PRK10771 117 --MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAA 194
|
250 260 270
....*....|....*....|....*....|....*
gi 1393793683 249 GISDDIIVLDHGDVIARGKPAEIQHNEKVIAAYLG 283
Cdd:PRK10771 195 RIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-266 |
6.18e-18 |
|
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: 80.23 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFggikalndvNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqk 80
Cdd:cd03298 3 LDKIRFSYGEQPMHF---------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqpgdwLNPAqlgqrlfykmfggthlvnRAGLARTFQNIRLFREMSVVENllvaqhmrVNRNLLAGVLNTPAYRRSENDA 160
Cdd:cd03298 65 ------APPA------------------DRPVSMLFQENNLFAHLTVEQN--------VGLGLSPGLKLTAEDRQAIEVA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 161 LDRafywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLI 240
Cdd:cd03298 113 LAR-------VGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMV 185
|
250 260
....*....|....*....|....*.
gi 1393793683 241 EHDMGMVMGISDDIIVLDHGDVIARG 266
Cdd:cd03298 186 THQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-271 |
6.31e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGG-----NILFNARNKTTNVIQVLGQkfqpgdwlnpaqlg 93
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvdDTLITSTSKNKDIKQIRKK-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrlfykmfggthlvnrAGLARTFQNIRLFREMSVVENLLVAQHMRVnrnllagvlntpayrrSENDALDRAFYWLEVVDL 173
Cdd:PRK13649 87 ----------------VGLVFQFPESQLFEETVLKDVAFGPQNFGV----------------SQEEAEALAREKLALVGI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 V-DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLrdHHD-ITVLLIEHDMGMVMGIS 251
Cdd:PRK13649 135 SeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQSgMTIVLVTHLMDDVANYA 212
|
250 260
....*....|....*....|
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13649 213 DFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-271 |
8.58e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.00 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKT-TNVIQV---LGQKFQ-PGDWLNPA 90
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVrkfVGLVFQnPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 91 QLGQRLfykMFGGTHLvnraGLARtfqnirlfremsvvenllvaqhmrvnrnllagvlNTPAYRRSENdaldrafywLEV 170
Cdd:PRK13652 95 TVEQDI---AFGPINL----GLDE----------------------------------ETVAHRVSSA---------LHM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 171 VDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvetHKLSEIIRFLRD---HHDITVLLIEHDMGMV 247
Cdd:PRK13652 125 LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP---QGVKELIDFLNDlpeTYGMTVIFSTHQLDLV 201
|
250 260
....*....|....*....|....
gi 1393793683 248 MGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13652 202 PEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-271 |
1.02e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.81 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHF-----------GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRaSGGNILFNarnktt 71
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFD------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 72 nviqvlGQKFQPgdwLNPAQLgQRLfykmfggthlvnRAGLARTFQ------NIRlfreMSVVEnlLVAQHMRVNRnlla 145
Cdd:COG4172 346 ------GQDLDG---LSRRAL-RPL------------RRRMQVVFQdpfgslSPR----MTVGQ--IIAEGLRVHG---- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 146 gvlntPAYRRSENDAldRAFYWLEVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHKlsE 224
Cdd:COG4172 394 -----PGLSAAERRA--RVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQA--Q 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1393793683 225 IIRFLRD---HHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG4172 464 ILDLLRDlqrEHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-271 |
1.68e-17 |
|
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: 82.16 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF-----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvLGQ 79
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR-----------VGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 80 kfqpgDWLNPAQLGqrlfykmFGGTHLVNRAgLARTFQNIRLFREMSVVENLLVAQHMRVNRNLlagvlntpayrrsend 159
Cdd:TIGR03269 348 -----EWVDMTKPG-------PDGRGRAKRY-IGILHQEYDLYPHRTVLDNLTEAIGLELPDEL---------------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALDRAFYWLEVVDL-----VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHD 234
Cdd:TIGR03269 399 ARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEME 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393793683 235 ITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:TIGR03269 479 QTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-270 |
2.09e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI--LFNARNKT--TNVIQVLGQKfQPGDWLNPAQL 92
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsiLGQPTRQAlqKNLVAYVPQS-EEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 GQRLFYKMFGGTHLVNRAglartfqnirlfremsvvenllvaqhmrvnrnllagvlnTPAYRRSENDALDRafywlevVD 172
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRA---------------------------------------KKRDRQIVTAALAR-------VD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 LVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMVMGISd 252
Cdd:PRK15056 132 MVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFC- 209
|
250
....*....|....*...
gi 1393793683 253 DIIVLDHGDVIARGkPAE 270
Cdd:PRK15056 210 DYTVMVKGTVLASG-PTE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-260 |
2.11e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.02 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNaTILHVEHL-----MMHFGGIK--ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnv 73
Cdd:COG4778 1 MT-TLLEVENLsktftLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 74 iqvlgqkfqpGDWLNPAQLGQRlfykmfggthlvnraglartfQNIRLFR-EMSvvenlLVAQHMRV-----NRNLLAGv 147
Cdd:COG4778 74 ----------GGWVDLAQASPR---------------------EILALRRrTIG-----YVSQFLRViprvsALDVVAE- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 148 lntPAYRR--SENDALDRAFYWLEVVDLvdcANRLAG----EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHK 221
Cdd:COG4778 117 ---PLLERgvDREEARARARELLARLNL---PERLWDlppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAV 190
|
250 260 270
....*....|....*....|....*....|....*....
gi 1393793683 222 LSEIIRFLRDhHDITVLLIEHDMGMVMGISDDIIVLDHG 260
Cdd:COG4778 191 VVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-260 |
2.60e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.36 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviQVLGqkfqPG 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-------PVEG----PG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqlgqrlfykmfggthlvnrAGLARTFQNIRLFREMSVVENllVAQHMRvnrnlLAGVlntPAYRRsendaLDRA 164
Cdd:PRK11248 70 -------------------------AERGVVFQNEGLLPWRNVQDN--VAFGLQ-----LAGV---EKMQR-----LEIA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIrfLRDHHDI--TVLLIEH 242
Cdd:PRK11248 110 HQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL--LKLWQETgkQVLLITH 187
|
250
....*....|....*...
gi 1393793683 243 DMGMVMGISDDIIVLDHG 260
Cdd:PRK11248 188 DIEEAVFMATELVLLSPG 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-270 |
2.98e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 81.36 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLgqr 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD---------------LTLESL--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 96 lfYKMFGgthLVnraglartFQNIRLFrEMSVVENLlvaqhmrvnrnllagvlntpAYRRSE--NDALDRAfywLEVVDL 173
Cdd:COG1132 413 --RRQIG---VV--------PQDTFLF-SGTIRENI--------------------RYGRPDatDEEVEEA---AKAAQA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 VDCANRLA-------GE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdhHDITVLLIEH 242
Cdd:COG1132 456 HEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAH 533
|
250 260
....*....|....*....|....*...
gi 1393793683 243 DMGMVMGiSDDIIVLDHGDVIARGKPAE 270
Cdd:COG1132 534 RLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-281 |
3.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.44 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFN---ARNKTTN-VIQvlgqkfqpgdwlnpaqlgq 94
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditITHKTKDkYIR------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 rlfykmfggtHLVNRAGLARTFQNIRLFREmsvvenllvaqhmRVNRNLLAGVLNtpaYRRSENDALDRAFYWLevVDL- 173
Cdd:PRK13646 82 ----------PVRKRIGMVFQFPESQLFED-------------TVEREIIFGPKN---FKMNLDEVKNYAHRLL--MDLg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 --VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGIS 251
Cdd:PRK13646 134 fsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYA 213
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 252 DDIIVLDHGDVIARGKPAEIQHNEKVIAAY 281
Cdd:PRK13646 214 DEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-266 |
1.41e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 79.38 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGG--IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFqp 83
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwlnpAQLGQRLFykMFGGThlvnraglarTFQNIRLFREMSVVENllvaqhmRVNRNLLAgvlntpAYRRSENDALDR 163
Cdd:TIGR02203 409 ------ALVSQDVV--LFNDT----------IANNIAYGRTEQADRA-------EIERALAA------AYAQDFVDKLPL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AFYwlevVDLVDCANRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGL-NPVETHKLSEIIRFLRDHhdiTVLLIEH 242
Cdd:TIGR02203 458 GLD----TPIGENGVLLSG----GQRQRLAIARALLKDAPILILDEATSALdNESERLVQAALERLMQGR---TTLVIAH 526
|
250 260
....*....|....*....|....
gi 1393793683 243 DMGMVMGiSDDIIVLDHGDVIARG 266
Cdd:TIGR02203 527 RLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-284 |
1.89e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 14 HFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarNKTTNVIQvlgqkfqpgdwlnPAQlg 93
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVP-------------PAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrlfykmfggthlvnrAGLARTFQNIRLFREMSVVENLlvAQHMRvnrnlLAGVLNTPAYRRSENDAldrafywlEVVDL 173
Cdd:PRK11000 75 ----------------RGVGMVFQSYALYPHLSVAENM--SFGLK-----LAGAKKEEINQRVNQVA--------EVLQL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNP-------VETHKLSEIIRflrdhhdITVLLIEHDMGM 246
Cdd:PRK11000 124 AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmrIEISRLHKRLG-------RTMIYVTHDQVE 196
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 247 VMGISDDIIVLDHGDVIARGKPAEIQH--NEKVIAAYLGT 284
Cdd:PRK11000 197 AMTLADKIVVLDAGRVAQVGKPLELYHypANRFVAGFIGS 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-271 |
2.04e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNArnkttnviqvlgqkfQP 83
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD---------------KP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 GDWLNPAQLGQRLfykMFGGTHLVNRAGLartfqnirlfremSVVEnlLVAqHMRVNRNLLAGvlntpayRRSEND--AL 161
Cdd:PRK11231 66 ISMLSSRQLARRL---ALLPQHHLTPEGI-------------TVRE--LVA-YGRSPWLSLWG-------RLSAEDnaRV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 DRAFYWLEVVDLvdcANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIE 241
Cdd:PRK11231 120 NQAMEQTRINHL---ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVL 195
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 242 HDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK11231 196 HDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-288 |
3.15e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLmmhfGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKFQ 82
Cdd:COG1129 254 EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD------------GKPVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 PGdwlNPAQ-LGQRLFYkmfggthlV--NRAGLArtfqnirLFREMSVVENLLVAQHMRVNRNllaGVLNtpayRRSEND 159
Cdd:COG1129 318 IR---SPRDaIRAGIAY--------VpeDRKGEG-------LVLDLSIRENITLASLDRLSRG---GLLD----RRRERA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 160 ALDRAFYWLEVVdlVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHklSEIIRFLRD--HHDITV 237
Cdd:COG1129 373 LAEEYIKRLRIK--TPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGAK--AEIYRLIRElaAEGKAV 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1393793683 238 LLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHnEKVIAAYLGTDESE 288
Cdd:COG1129 448 IVISSELPELLGLSDRILVMREGRIVGELDREEATE-EAIMAAATGGAAAA 497
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-266 |
3.29e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.77 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGfyRASGGNIlfnarnkTTNVIQVLGQKfqpgdwLNPAQLGQRLFY 98
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGT-------TSGQILFNGQP------RKPDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 kmfggthlvnraglarTFQNIRLFREMSVVENLLVAQHMRVNRNllagvlnTPAYRRSENDaldrafywlEVVDLVDCAN 178
Cdd:cd03234 86 ----------------VRQDDILLPGLTVRETLTYTAILRLPRK-------SSDAIRKKRV---------EDVLLRDLAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 179 RLAGEM-----SYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLseiIRFLRD--HHDITVLLIEHDMGM-VMGI 250
Cdd:cd03234 134 TRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL---VSTLSQlaRRNRIVILTIHQPRSdLFRL 210
|
250
....*....|....*.
gi 1393793683 251 SDDIIVLDHGDVIARG 266
Cdd:cd03234 211 FDRILLLSSGEIVYSG 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-272 |
3.70e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.47 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAgkttvfncltgfyrasggnilfnARNKTTNVIQVLGQKFQPGD 85
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA-----------------------A**RGALPAHV*GPDAGRRP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WLNPAQLGQRLFYKMFGGTHLVNRAGLARTFqnirlfremSVVENL-LVAQHMRVNRNllagvlntpayrrsenDALDRA 164
Cdd:NF000106 71 WRF*TWCANRRALRRTIG*HRPVR*GRRESF---------SGRENLyMIGR*LDLSRK----------------DARARA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIR-FLRDhhDITVLLIEHD 243
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRsMVRD--GATVLLTTQY 203
|
250 260
....*....|....*....|....*....
gi 1393793683 244 MGMVMGISDDIIVLDHGDVIARGKPAEIQ 272
Cdd:NF000106 204 MEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-271 |
5.51e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF---GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGnilfnarnkttnVIQVLGQKF 81
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG------------KVKIDGELL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 QPGDWLNPaqlgqrlfykmfggthlvnRAGLARTFQNirlfremsvVENLLVAQhmRVNRNLLAGVLNTPAYRRSENDAL 161
Cdd:PRK13642 72 TAENVWNL-------------------RRKIGMVFQN---------PDNQFVGA--TVEDDVAFGMENQGIPREEMIKRV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 DRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIE 241
Cdd:PRK13642 122 DEA---LLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSIT 198
|
250 260 270
....*....|....*....|....*....|
gi 1393793683 242 HDMGMVMGiSDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13642 199 HDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-262 |
6.36e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.48 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNArnkttnviqvlgqkfQP 83
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---------------AP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwLNPAQLGQRLFykmfggthlvnraglartFQNIRLFREMSVVENllVAQHMRVNrnllagvlntpaYRrsendalDR 163
Cdd:PRK11247 76 ---LAEAREDTRLM------------------FQDARLLPWKKVIDN--VGLGLKGQ------------WR-------DA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHD 243
Cdd:PRK11247 114 ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD 193
|
250
....*....|....*....
gi 1393793683 244 MGMVMGISDDIIVLDHGDV 262
Cdd:PRK11247 194 VSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-270 |
8.49e-16 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 74.96 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFqpgdwlnpAQLGQRL 96
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI--------GLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 97 FykMFGGThlvnraglarTFQNIRLFREMSVVENLLVAQHMrvnRNLLAGVLNTPayrrsenDALDrafywlevVDLVDC 176
Cdd:cd03251 86 F--LFNDT----------VAENIAYGRPGATREEVEEAARA---ANAHEFIMELP-------EGYD--------TVIGER 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVLLIEHDMGMVMGiSDDIIV 256
Cdd:cd03251 136 GVKLSG----GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVV 208
|
250
....*....|....
gi 1393793683 257 LDHGDVIARGKPAE 270
Cdd:cd03251 209 LEDGKIVERGTHEE 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-271 |
1.52e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRasggniLFNARNKTTNVIQVLGQKfqpg 84
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIE------IYDSKIKVDGKVLYFGKD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqlgqrlfykMFGGTHLVNRAGLARTFQNIRLFREMSVVENllVAQHMRVNrnllaGVLNTPAYRRSENDALDRA 164
Cdd:PRK14246 80 ---------------IFQIDAIKLRKEVGMVFQQPNPFPHLSIYDN--IAYPLKSH-----GIKEKREIKKIVEECLRKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYWLEVVDLVdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhhDITVLLIEHDM 244
Cdd:PRK14246 138 GLWKEVYDRL---NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNP 212
|
250 260
....*....|....*....|....*..
gi 1393793683 245 GMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK14246 213 QQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-271 |
3.83e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviqvlgqkfq 82
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdWLNPAQLGQrlfykmFGGTHLVNRAGLARtfQNIRLFREMSVVEnlLVAQHMRVNRNLLAgvlntpAYRRSENDALD 162
Cdd:PRK10253 65 ---WLDGEHIQH------YASKEVARRIGLLA--QNATTPGDITVQE--LVARGRYPHQPLFT------RWRKEDEEAVT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEH 242
Cdd:PRK10253 126 KA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLH 202
|
250 260
....*....|....*....|....*....
gi 1393793683 243 DMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK10253 203 DLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-266 |
4.47e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.81 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGfYRASG---GNILFNARNkttnviqvlgqkfqpgdwlnpaqLGQRLF 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG-RRTGLgvsGEVLINGRP-----------------------LDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 98 YKMFGgthLVNraglartfQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayrrsendaldrafywlevvdlvdca 177
Cdd:cd03213 81 RKIIG---YVP--------QDDILHPTLTVRETLMFAAKLR--------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 nRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdITVLLIEHD-MGMVMGISDDIIV 256
Cdd:cd03213 111 -GLSG----GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIICSIHQpSSEIFELFDKLLL 184
|
250
....*....|
gi 1393793683 257 LDHGDVIARG 266
Cdd:cd03213 185 LSQGRVIYFG 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-271 |
6.52e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnVIQVLGQKFQPGDWlnpaqlgqrlfyk 99
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV----------YVDGLDTSDEENLW------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 mfggtHLVNRAGLarTFQNirlfremsvVENLLVAQhmRVNRNLLAGVLN---TPAYRRSendaldRAFYWLEVVDLVDC 176
Cdd:PRK13633 82 -----DIRNKAGM--VFQN---------PDNQIVAT--IVEEDVAFGPENlgiPPEEIRE------RVDESLKKVGMYEY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGiSDDIIV 256
Cdd:PRK13633 138 RRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIV 216
|
250
....*....|....*
gi 1393793683 257 LDHGDVIARGKPAEI 271
Cdd:PRK13633 217 MDSGKVVMEGTPKEI 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-280 |
6.84e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 15 FGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQ 94
Cdd:PRK15439 21 YSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR---------------LTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 RlfykmfgGTHLVNraglartfQNIRLFREMSVVENLLV--AQHMRVNR---NLLAGV---LNtpayrrsendaLDRAFY 166
Cdd:PRK15439 86 L-------GIYLVP--------QEPLLFPNLSVKENILFglPKRQASMQkmkQLLAALgcqLD-----------LDSSAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 167 WLEVVDlvdcanrlagemsygqQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGM 246
Cdd:PRK15439 140 SLEVAD----------------RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPE 202
|
250 260 270
....*....|....*....|....*....|....
gi 1393793683 247 VMGISDDIIVLDHGDVIARGKPAEIQHNEkVIAA 280
Cdd:PRK15439 203 IRQLADRISVMRDGTIALSGKTADLSTDD-IIQA 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-275 |
7.08e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqVLGQKFQpGDWLNPAQlgQRLFYkmfg 102
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR--------VLFDAEK-GICLPPEK--RRIGY---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 103 gthlvnraglarTFQNIRLFremsvvenllvaQHMRVNRNLLAGVlntpayRRSENDALDRafywleVVDLVDCA---NR 179
Cdd:PRK11144 81 ------------VFQDARLF------------PHYKVRGNLRYGM------AKSMVAQFDK------IVALLGIEpllDR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDH 259
Cdd:PRK11144 125 YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
250
....*....|....*.
gi 1393793683 260 GDVIARGKPAEIQHNE 275
Cdd:PRK11144 205 GKVKAFGPLEEVWASS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-267 |
7.40e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQvlgqkfqpgDWlNPAQLgqrlfy 98
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-----IA---------DY-SEAAL------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 kmfggthlvnRAGLARTFQNIRLFREmSVVENLLVAQHmRVNRNLLAGVLNTP--AYRRSENDALDRafyWLevvdlvdc 176
Cdd:PRK11160 413 ----------RQAISVVSQRVHLFSA-TLRDNLLLAAP-NASDEALIEVLQQVglEKLLEDDKGLNA---WL-------- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 anrlaGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvETHKlsEIIRFLRDH-HDITVLLIEHDM-GMV-Mg 249
Cdd:PRK11160 470 -----GEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA-ETER--QILELLAEHaQNKTVLMITHRLtGLEqF- 540
|
250
....*....|....*...
gi 1393793683 250 isDDIIVLDHGDVIARGK 267
Cdd:PRK11160 541 --DRICVMDNGQIIEQGT 556
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-283 |
7.64e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQK----FQ-PGDWLNPAQ- 91
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRirmiFQdPSTSLNPRQr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 92 LGQRLFYKMFGGTHLVNRAGLARTFQNIRLfremsvvenllvaqhmrvnrnllAGVLNtpayrrsendalDRAFYWLEVv 171
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQIIETLRQ-----------------------VGLLP------------DHASYYPHM- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 dlvdcanrlageMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGIS 251
Cdd:PRK15112 150 ------------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIS 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI----QHN--EKVIAAYLG 283
Cdd:PRK15112 218 DQVLVMHQGEVVERGSTADVlaspLHEltKRLIAGHFG 255
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-271 |
8.32e-15 |
|
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: 74.40 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKA--LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvLGQkfqp 83
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD--------LSQ---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdWlNPAQLGQRLFYkmfggthlvnragLArtfQNIRLFrEMSVVENllVAqhmrvnrnllagvlntpayrRSEnDALDR 163
Cdd:COG4618 399 --W-DREELGRHIGY-------------LP---QDVELF-DGTIAEN--IA--------------------RFG-DADPE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AfywleVVDlvdcANRLAG--EM-------------------SYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKL 222
Cdd:COG4618 436 K-----VVA----AAKLAGvhEMilrlpdgydtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1393793683 223 SEIIRFLRDHHdITVLLIEHDMGmVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG4618 507 AAAIRALKARG-ATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-260 |
2.31e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 14 HFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQVLGQKFQPgdwlnpaqlg 93
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD-----ITRLKNREVP---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrlfykmfggthlVNRAGLARTFQNIRLFREMSVVENLLVAQhmrvnrnLLAGVlNTPAYRRSENDALDRafywlevVDL 173
Cdd:PRK10908 76 -------------FLRRQIGMIFQDHHLLMDRTVYDNVAIPL-------IIAGA-SGDDIRRRVSAALDK-------VGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpvetHKLSE-IIRFLRDHH--DITVLLIEHDMGMVMGI 250
Cdd:PRK10908 128 LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEgILRLFEEFNrvGVTVLMATHDIGLISRR 203
|
250
....*....|
gi 1393793683 251 SDDIIVLDHG 260
Cdd:PRK10908 204 SYRMLTLSDG 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-262 |
2.99e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 70.19 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTT-------NVIQVLGQKFQpgdwlnpaqlg 93
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylhSKVSLVGQEPV----------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrlfykMFGGTHLVNRA-GLARTfqnirlfrEMSVVENLLVAQHMRVNRNLLAgvlntpayrrsendaldrAFYWLEVvd 172
Cdd:cd03248 99 ------LFARSLQDNIAyGLQSC--------SFECVKEAAQKAHAHSFISELA------------------SGYDTEV-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 lvdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRflRDHHDITVLLIEHDMGMVMGiSD 252
Cdd:cd03248 145 -----GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTVER-AD 216
|
250
....*....|
gi 1393793683 253 DIIVLDHGDV 262
Cdd:cd03248 217 QILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-282 |
3.14e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGF--YRasgGNILFNarnkttnviqvlGQKFQPgdwLNPAQLgq 94
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKIN------------GIELRE---LDPESW-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 rlfykmfggthlvnRAGLARTFQNIRLFrEMSVVENLLVAQHMRVNRNLlagvlntpayrrseNDALDRAFYWLEVVDLV 174
Cdd:PRK11174 422 --------------RKHLSWVGQNPQLP-HGTLRDNVLLGNPDASDEQL--------------QQALENAWVSEFLPLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 175 DCANRLAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpvethKLSE--IIRFLRD-HHDITVLLIEH----- 242
Cdd:PRK11174 473 QGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD-----AHSEqlVMQALNAaSRRQTTLMVTHqledl 547
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393793683 243 -DMgmvmgisDDIIVLDHGDVIARGKPAEIQHNEKVIAAYL 282
Cdd:PRK11174 548 aQW-------DQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-271 |
3.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqVLGQKFQPGD-WLNPAQLGQrlfyk 99
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII------------IDGDLLTEENvWDIRHKIGM----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 mfggthlvnraglarTFQNirlfremsvVENLLVAQhmRVNRNLLAGVLNTPAYRRSENDALDRAfywLEVVDLVDCANR 179
Cdd:PRK13650 86 ---------------VFQN---------PDNQFVGA--TVEDDVAFGLENKGIPHEEMKERVNEA---LELVGMQDFKER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVmGISDDIIVLDH 259
Cdd:PRK13650 137 EPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKN 215
|
250
....*....|..
gi 1393793683 260 GDVIARGKPAEI 271
Cdd:PRK13650 216 GQVESTSTPREL 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-281 |
3.38e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASG--------GNILFNARnkttnviqv 76
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 77 lgqkfqPGDWLNPAQLGQRlfykmfggthlvnRAGLARTFQNIRLFremSVVENLLVAQHMRVNRnllAGvlntpAYRRS 156
Cdd:PRK13547 72 ------PLAAIDAPRLARL-------------RAVLPQAAQPAFAF---SAREIVLLGRYPHARR---AG-----ALTHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 157 ENDALDRAfywLEVVDLVDCANRLAGEMSYGQQRRLEIARAMC---------TSPEMICLDEPAAGLNPVETHKLSEIIR 227
Cdd:PRK13547 122 DGEIAWQA---LALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVR 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1393793683 228 FLRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEKVIAAY 281
Cdd:PRK13547 199 RLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-271 |
3.97e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.36 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnviqvlgqkfqpgdwLNPAQLgqrlfyk 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD------------------LRDYTL------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 mfggTHLVNRAGLARtfQNIRLFREmSVVENLLVAQHMRvnrnllagvlntpaYRRSENDALDRAFYWLEVVD-LVDCAN 178
Cdd:PRK11176 413 ----ASLRNQVALVS--QNVHLFND-TIANNIAYARTEQ--------------YSREQIEEAARMAYAMDFINkMDNGLD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 179 RLAGE----MSYGQQRRLEIARAMC-TSPEMIcLDEPAAGLNPVETHKLSEIIRFLRDhhDITVLLIEHDMGMVMGiSDD 253
Cdd:PRK11176 472 TVIGEngvlLSGGQRQRIAIARALLrDSPILI-LDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADE 547
|
250
....*....|....*...
gi 1393793683 254 IIVLDHGDVIARGKPAEI 271
Cdd:PRK11176 548 ILVVEDGEIVERGTHAEL 565
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-266 |
6.04e-14 |
|
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: 69.54 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkTTNVIQvlgqkfqpgdwLNPAQLGQRLF 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD----GTDIRQ-----------LDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 98 YKMfggthlvnraglartfQNIRLFREmSVVENLLVA-------QHMRVNRnlLAGVLntpAYRRSENDALDrafywLEV 170
Cdd:cd03245 82 YVP----------------QDVTLFYG-TLRDNITLGapladdeRILRAAE--LAGVT---DFVNKHPNGLD-----LQI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 171 vdlvdcanrlaGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGL-NPVETHKLSEIIRFLRdhhDITVLLIEHDMG 245
Cdd:cd03245 135 -----------GErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMdMNSEERLKERLRQLLG---DKTLIIITHRPS 200
|
250 260
....*....|....*....|.
gi 1393793683 246 MvMGISDDIIVLDHGDVIARG 266
Cdd:cd03245 201 L-LDLVDRIIVMDSGRIVADG 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-273 |
6.30e-14 |
|
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: 71.64 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKT----TVFNCLTGFYRASGGNILFNARN---- 68
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 69 --KTTNviQVLGQK----FQ-PGDWLNPaqlgqrlfykmfggthlvnraglartfqnirLFR-EMSVVENLLVAQHMrvn 140
Cdd:COG4172 82 seRELR--RIRGNRiamiFQePMTSLNP-------------------------------LHTiGKQIAEVLRLHRGL--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 141 rnllagvlntpayrrSENDALDRAFYWLEVVDLVDCANRLAG---EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpV 217
Cdd:COG4172 126 ---------------SGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALD-V 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393793683 218 ETHKlsEIIRFLRD---HHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI----QH 273
Cdd:COG4172 190 TVQA--QILDLLKDlqrELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELfaapQH 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-243 |
1.16e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNilfnarnkttnvIQVLGQK 80
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGE------------VSLVGQP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 FQPGDWLNPAQLgqrlfykmfggthlvnRA-GLARTFQNIRLFREMSVVENllvaqhmrvnrnllagvLNTPAYRR--SE 157
Cdd:PRK10584 74 LHQMDEEARAKL----------------RAkHVGFVFQSFMLIPTLNALEN-----------------VELPALLRgeSS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 158 NDALDRAFYWLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITV 237
Cdd:PRK10584 121 RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTL 200
|
....*.
gi 1393793683 238 LLIEHD 243
Cdd:PRK10584 201 ILVTHD 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-217 |
1.18e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 9 EHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGnilfNARnkttnviqVLGQKFQPGDwln 88
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEG----EAW--------LFGQPVDAGD--- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 89 pAQLGQRLFYkMfggthlvnraglartFQNIRLFREMSVVENLLVaqHMRVnrnllagvlntpaYRRSENDALDRAFYWL 168
Cdd:NF033858 335 -IATRRRVGY-M---------------SQAFSLYGELTVRQNLEL--HARL-------------FHLPAAEIAARVAEML 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1393793683 169 EVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPV 217
Cdd:NF033858 383 ERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-270 |
1.27e-13 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 68.80 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 14 HFG---GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKFQpgdwlnpa 90
Cdd:cd03253 7 TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID------------GQDIR-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 91 QLGQRLFYKMFG----GTHLVNraglARTFQNIRLFR----EMSVVENLLVAQHMRVnrnllagVLNTPayrrsenDALD 162
Cdd:cd03253 67 EVTLDSLRRAIGvvpqDTVLFN----DTIGYNIRYGRpdatDEEVIEAAKAAQIHDK-------IMRFP-------DGYD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 rafywlEVVdlvdcanrlaGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHdiTVL 238
Cdd:cd03253 129 ------TIV----------GErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTI 190
|
250 260 270
....*....|....*....|....*....|..
gi 1393793683 239 LIEHDMGMVMGiSDDIIVLDHGDVIARGKPAE 270
Cdd:cd03253 191 VIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-270 |
1.54e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTgFYRASG----GNILFNARNKTTNVIQVLGQKFQPGDwlnpaqlgqrl 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPIDAKEMRAISAYVQQDD----------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 97 fykMFGGThlvnraglartfqnirlfreMSVVENLLVAQHMRVNRNLlagvlnTPAYRRSENDALdrafywLEVVDLVDC 176
Cdd:TIGR00955 109 ---LFIPT--------------------LTVREHLMFQAHLRMPRRV------TKKEKRERVDEV------LQALGLRKC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLAGE------MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGI 250
Cdd:TIGR00955 154 ANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFEL 233
|
250 260
....*....|....*....|
gi 1393793683 251 SDDIIVLDHGDVIARGKPAE 270
Cdd:TIGR00955 234 FDKIILMAEGRVAYLGSPDQ 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-268 |
1.73e-13 |
|
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: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVlgqkfqpgdwlnpaqlgqrl 96
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-------------------- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 97 fykmfggthlvnRAGLARTFQNIRLFREMSVVENLLVAQHMRvnrnllagvlntpayRRSENDALDRAFYWLEVVDLVDC 176
Cdd:TIGR01257 1002 ------------RQSLGMCPQHNILFHHLTVAEHILFYAQLK---------------GRSWEEAQLEMEAMLEDTGLHHK 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIrfLRDHHDITVLLIEHDMGMVMGISDDIIV 256
Cdd:TIGR01257 1055 RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAI 1132
|
250
....*....|..
gi 1393793683 257 LDHGDVIARGKP 268
Cdd:TIGR01257 1133 ISQGRLYCSGTP 1144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-263 |
2.66e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviqVLGQKFQP 83
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 G------DWLNPaqlgqrlfykmfggthlvnraglartfqnirlfrEMSVVENLL-VAQHMRVN--RNLLAGVLNTPayr 154
Cdd:COG0488 381 GyfdqhqEELDP----------------------------------DKTVLDELRdGAPGGTEQevRGYLGRFLFSG--- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 155 rsendalDRAFywlevvdlvdcanRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVEThkLSEIIRFLRDhHD 234
Cdd:COG0488 424 -------DDAF-------------KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-IET--LEALEEALDD-FP 479
|
250 260
....*....|....*....|....*....
gi 1393793683 235 ITVLLIEHDMGMVMGISDDIIVLDHGDVI 263
Cdd:COG0488 480 GTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-260 |
3.81e-13 |
|
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: 66.30 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 2 NATILHVEHLmmhfGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqvlgqkf 81
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qPGDWLNPAQLgqrlfykmfggthlvNRAGLA-----RtfQNIRLFREMSVVENLLVAQhmrvnrnLLAGvlntpayrrs 156
Cdd:cd03215 63 -PVTRRSPRDA---------------IRAGIAyvpedR--KREGLVLDLSVAENIALSS-------LLSG---------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 157 endaldrafywlevvdlvdcanrlagemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNpVEThKlSEIIRFLRDHHD-- 234
Cdd:cd03215 108 ------------------------------GNQQKVVLARWLARDPRVLILDEPTRGVD-VGA-K-AEIYRLIRELADag 154
|
250 260
....*....|....*....|....*.
gi 1393793683 235 ITVLLIEHDMGMVMGISDDIIVLDHG 260
Cdd:cd03215 155 KAVLLISSELDELLGLCDRILVMYEG 180
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-263 |
5.18e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGG---------IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvi 74
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 75 qvLGQkfqpgdwLNPAQlgQRLFykmfggthlvnRAGLARTFQN-IRLFREMSVVENLLvAQHMRVNRNLlagvlntpay 153
Cdd:PRK10419 76 --LAK-------LNRAQ--RKAF-----------RRDIQMVFQDsISAVNPRKTVREII-REPLRHLLSL---------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 154 rrSENDALDRAFYWLEVVDLVD-CANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDH 232
Cdd:PRK10419 123 --DKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQ 200
|
250 260 270
....*....|....*....|....*....|.
gi 1393793683 233 HDITVLLIEHDMGMVMGISDDIIVLDHGDVI 263
Cdd:PRK10419 201 FGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-266 |
5.34e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHLMMHFGGIK-----------ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRaSGGNILFNArnktt 71
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDG----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 72 nviqvlgqkfQPGDWLNPAQLgqrlfykmfggthLVNRAGLARTFQ--NIRLFREMSVVEnlLVAQHMRVNRNLLagvln 149
Cdd:PRK15134 347 ----------QPLHNLNRRQL-------------LPVRHRIQVVFQdpNSSLNPRLNVLQ--IIEEGLRVHQPTL----- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 150 TPAYRRsendalDRAFYWLEVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRF 228
Cdd:PRK15134 397 SAAQRE------QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
250 260 270
....*....|....*....|....*....|....*...
gi 1393793683 229 LRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARG 266
Cdd:PRK15134 471 LQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-276 |
9.05e-13 |
|
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: 65.63 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGF--YRASGGNILFNARNKTTnviqvlgqkfqp 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwLNPaqlgqrlfykmfggtHLVNRAGLARTFQNIRLFREMSVVENLlvaqhmrvnrnllagvlntpayrRSENDALdr 163
Cdd:cd03217 69 ---LPP---------------EERARLGIFLAFQYPPEIPGVKNADFL-----------------------RYVNEGF-- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 afywlevvdlvdcanrlagemSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHD 243
Cdd:cd03217 106 ---------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHY 163
|
250 260 270
....*....|....*....|....*....|....
gi 1393793683 244 MGMVMGISDDII-VLDHGDVIARGKPAEIQHNEK 276
Cdd:cd03217 164 QRLLDYIKPDRVhVLYDGRIVKSGDKELALEIEK 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-271 |
1.52e-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: 65.59 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQRLFYK 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL---------------ADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 MFGGThLVNRAglarTFQNIRLFREMSVVENLLVAQHMrvnrnllAGVlntpayrrsendaldRAFywleVVDLVDCANR 179
Cdd:cd03252 82 LQENV-LFNRS----IRDNIALADPGMSMERVIEAAKL-------AGA---------------HDF----ISELPEGYDT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLseiirfLRDHHDI----TVLLIEHDMGMVMGiS 251
Cdd:cd03252 131 IVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAI------MRNMHDIcagrTVIIIAHRLSTVKN-A 203
|
250 260
....*....|....*....|
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI 271
Cdd:cd03252 204 DRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-281 |
3.04e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNArnkttnviQVLGQkfqpgdWLNPAqlgqrlfykm 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA--------QPLES------WSSKA---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnragLARtfQNIRLFREMSVVENLLVAQHMRVNRNLLAGVLNTpaYRRSENDALDRAfywLEVVDLVDCANRL 180
Cdd:PRK10575 83 -----------FAR--KVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGR--FGAADREKVEEA---ISLVGLKPLAHRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDHG 260
Cdd:PRK10575 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
250 260
....*....|....*....|.
gi 1393793683 261 DVIARGKPAEIQHNEKVIAAY 281
Cdd:PRK10575 225 EMIAQGTPAELMRGETLEQIY 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-243 |
3.16e-12 |
|
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: 66.62 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHF-GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpg 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 dwlnpaqlgqrlfykmFGGTHLVNRAGLarTFQNIRLFrEMSVVENLLVAQhmrvnrnllagvlntpayrrseNDALDRA 164
Cdd:TIGR02868 402 ----------------LDQDEVRRRVSV--CAQDAHLF-DTTVRENLRLAR----------------------PDATDEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 165 FYW-LEVVDLVDCANRLA-------GEM----SYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvETHklSEIIRFLRDH 232
Cdd:TIGR02868 441 LWAaLERVGLADWLRALPdgldtvlGEGgarlSGGERQRLALARALLADAPILLLDEPTEHLDA-ETA--DELLEDLLAA 517
|
250
....*....|..
gi 1393793683 233 HD-ITVLLIEHD 243
Cdd:TIGR02868 518 LSgRTVVLITHH 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-273 |
3.17e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI-----LFNARNKttNVIQ 75
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSR--QVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 76 VLGQkfqpgdwlNPAQLgQRlfykmfggthlVNRAGLARTFQN--IRLFREMSVVENllVAQHMRVNRNLlagvlntpay 153
Cdd:PRK10261 90 LSEQ--------SAAQM-RH-----------VRGADMAMIFQEpmTSLNPVFTVGEQ--IAESIRLHQGA---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 154 rrSENDALDRAFYWLEVVDLVDCA---NRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLR 230
Cdd:PRK10261 138 --SREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQ 215
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 231 DHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQH 273
Cdd:PRK10261 216 KEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-243 |
3.53e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnarnkttnviqvlgqkFQPGDWl 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------------------SIPKGL- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 npaqlgqRLfykmfggthlvnrAGLArtfQNIRLFREMSVVENLL-VAQHMRVNRNLLAGVLNTPAYRRSENDALDRAFY 166
Cdd:COG0488 62 -------RI-------------GYLP---QEPPLDDDLTVLDTVLdGDAELRALEAELEELEAKLAEPDEDLERLAELQE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 167 WLEVVD-----------------LVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVEThklseiIRFL 229
Cdd:COG0488 119 EFEALGgweaearaeeilsglgfPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES------IEWL 191
|
250
....*....|....*..
gi 1393793683 230 RDH---HDITVLLIEHD 243
Cdd:COG0488 192 EEFlknYPGTVLVVSHD 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-276 |
4.86e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.11 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFG-------------GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTt 71
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 72 nviqvlgqKFQPGDWLNPAQLGQRLFYKMFggthlvnrAGLartfqNIRlfreMSVVEnlLVAQHMRVNRnllagvlntP 151
Cdd:PRK15079 87 --------GMKDDEWRAVRSDIQMIFQDPL--------ASL-----NPR----MTIGE--IIAEPLRTYH---------P 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 152 AYRRSENDALDRAFYwLEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRD 231
Cdd:PRK15079 131 KLSRQEVKDRVKAMM-LKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQR 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 232 HHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEIQHNEK 276
Cdd:PRK15079 210 EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-227 |
7.99e-12 |
|
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: 63.15 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgQKFQPGD 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-------QRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlNPAQLGqrlfykmfggthlvNRAGLARtfqnirlfrEMSVVENLlvaqhmRVNRNLLAGvlntpaYRRSENDALDRaf 165
Cdd:TIGR01189 74 --NILYLG--------------HLPGLKP---------ELSALENL------HFWAAIHGG------AQRTIEDALAA-- 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393793683 166 ywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIR 227
Cdd:TIGR01189 115 -----VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-266 |
1.38e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 9 EHLMMHFGGIK-ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwl 87
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT---------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 88 npaqlgqrlfykmfggthlVNRAGLART----FQNIRLFREmSVVENLLVAQHMRVNRNLLagvlntpayrrsenDALDR 163
Cdd:PRK13657 402 -------------------VTRASLRRNiavvFQDAGLFNR-SIEDNIRVGRPDATDEEMR--------------AAAER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 AfywlEVVDLV----DCANRLAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdhHDI 235
Cdd:PRK13657 448 A----QAHDFIerkpDGYDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGR 521
|
250 260 270
....*....|....*....|....*....|.
gi 1393793683 236 TVLLIEHDMGMVMGiSDDIIVLDHGDVIARG 266
Cdd:PRK13657 522 TTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-282 |
1.42e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 14 HFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnVIQVLGqkfqpgdwlnpaqLG 93
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----VSALLE-------------LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrlfykmfggthlvnrAGlartFQNirlfrEMSVVENLLvaqhmrvnrnLLAGVLNtpaYRRSE-NDALDrafywlEVVD 172
Cdd:COG1134 97 ----------------AG----FHP-----ELTGRENIY----------LNGRLLG---LSRKEiDEKFD------EIVE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 LVDCANRLAGEM---SYGQQRRLEIARAMCTSPEMICLDEP-AAGlNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMVM 248
Cdd:COG1134 133 FAELGDFIDQPVktySSGMRARLAFAVATAVDPDILLVDEVlAVG-DAAFQKKCLARIRELRESGR-TVIFVSHSMGAVR 210
|
250 260 270
....*....|....*....|....*....|....
gi 1393793683 249 GISDDIIVLDHGDVIARGKPAEiqhnekVIAAYL 282
Cdd:COG1134 211 RLCDRAIWLEKGRLVMDGDPEE------VIAAYE 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-262 |
1.64e-11 |
|
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: 61.46 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQRLFYKM 100
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ---------------WDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnraglartfQNIRLFrEMSVVENLLvaqhmrvnrnllagvlntpayrrsendaldrafywlevvdlvdcanrl 180
Cdd:cd03246 83 ----------------QDDELF-SGSIAENIL------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 agemSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGmVMGISDDIIVLDHG 260
Cdd:cd03246 98 ----SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPE-TLASADRILVLEDG 171
|
..
gi 1393793683 261 DV 262
Cdd:cd03246 172 RV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-270 |
1.83e-11 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 62.56 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQvlgqkfqpgdWLNpAQLGqrl 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR----------WLR-SQIG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 97 fykmfggthLVNraglartfQNIRLFrEMSVVENLLVAQHmrvnrnllagvlntPAYRRSENDALDRAFYWLEVVDLVDC 176
Cdd:cd03249 81 ---------LVS--------QEPVLF-DGTIAENIRYGKP--------------DATDEEVEEAAKKANIHDFIMSLPDG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLAGE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHK-----LSEIIRflrdhhDITVLLIEHDMGMV 247
Cdd:cd03249 129 YDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD-AESEKlvqeaLDRAMK------GRTTIVIAHRLSTI 201
|
250 260
....*....|....*....|...
gi 1393793683 248 MGiSDDIIVLDHGDVIARGKPAE 270
Cdd:cd03249 202 RN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-259 |
2.14e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLgqkfqp 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 gdwlnpaqlgqrlfykmfggtHLvnraglartfqnirlfremSVVENLLVAQHMRVNrnllagvlntPAYRRSEndaldr 163
Cdd:PRK09544 77 ---------------------YL-------------------DTTLPLTVNRFLRLR----------PGTKKED------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 afyWLEVVDLVDCANRLAGEM---SYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLI 240
Cdd:PRK09544 101 ---ILPALKRVQAGHLIDAPMqklSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMV 177
|
250
....*....|....*....
gi 1393793683 241 EHDMGMVMGISDDIIVLDH 259
Cdd:PRK09544 178 SHDLHLVMAKTDEVLCLNH 196
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
178-282 |
2.61e-11 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 64.08 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEMSYGQQRRLEIARAMCT--SPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMVmGISDDII 255
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRII 548
|
90 100 110
....*....|....*....|....*....|....
gi 1393793683 256 VLD------HGDVIARGKPAEIQHN-EKVIAAYL 282
Cdd:PRK00635 549 DIGpgagifGGEVLFNGSPREFLAKsDSLTAKYL 582
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-214 |
2.75e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKT-TNVIQVLgqkfqpgdwlnpAQLGQ 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEAC------------HYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 RLFYKmfggthlvnraglartfqnirlfREMSVVENLLvaqhmrvnrnLLAGVLNTpayrrsENDALDRAfywLEVVDLV 174
Cdd:PRK13539 81 RNAMK-----------------------PALTVAENLE----------FWAAFLGG------EELDIAAA---LEAVGLA 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1393793683 175 DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGL 214
Cdd:PRK13539 119 PLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-274 |
3.77e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTtvFNCLTGFYRASGGnilfnarnkttnVIQVLGQKFQPGDWLNPAQLGQRLfykmfg 102
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAG------------VRQTAGRVLLDGKPVAPCALRGRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 103 gthlvnragLARTFQNIRL----FREMS--VVENLLVAQHMRVNRNLLAGvlntpayrrsendaldrafywLEVVDLVDC 176
Cdd:PRK10418 81 ---------IATIMQNPRSafnpLHTMHthARETCLALGKPADDATLTAA---------------------LEAVGLENA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRL---AGEMSYGQQRRLEIARA-MCTSPEMIClDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISD 252
Cdd:PRK10418 131 ARVLklyPFEMSGGMLQRMMIALAlLCEAPFIIA-DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLAD 209
|
250 260
....*....|....*....|..
gi 1393793683 253 DIIVLDHGDVIARGKPAEIQHN 274
Cdd:PRK10418 210 DVAVMSHGRIVEQGDVETLFNA 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-266 |
8.64e-11 |
|
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: 59.63 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqvlgqkfqpgdwlnPAQLGQRLFY 98
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV---------------------PVSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 KMFGgthLVNraglartfQNIRLFrEMSVVENLlvaqhmrvnrnllagvlntpayrrsendaldrafywlevvdlvdcAN 178
Cdd:cd03247 75 SLIS---VLN--------QRPYLF-DTTLRNNL---------------------------------------------GR 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 179 RLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPV-ETHKLSEIIRFLRDHhdiTVLLIEHDMgmvMGIS--DDII 255
Cdd:cd03247 98 RFSG----GERQRLALARILLQDAPIVLLDEPTVGLDPItERQLLSLIFEVLKDK---TLIWITHHL---TGIEhmDKIL 167
|
250
....*....|.
gi 1393793683 256 VLDHGDVIARG 266
Cdd:cd03247 168 FLENGKIIMQG 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-267 |
1.22e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQkfqpgdwlnpaqlgqrlfykm 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ--------------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fgGTHLVNR--AGLARTF-QNIRLFREMS---VVENLLVAQHMRVNRNLLAGvLNTPayrrsendaldrafywlevvdLV 174
Cdd:PRK10790 416 --GVAMVQQdpVVLADTFlANVTLGRDISeeqVWQALETVQLAELARSLPDG-LYTP---------------------LG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 175 DCANRLagemSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHhdITVLLIEHDMGMVMGiSDDI 254
Cdd:PRK10790 472 EQGNNL----SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTI 544
|
250
....*....|...
gi 1393793683 255 IVLDHGDVIARGK 267
Cdd:PRK10790 545 LVLHRGQAVEQGT 557
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-270 |
2.17e-10 |
|
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: 59.73 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSIT-----ALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnvIQVLGQKFQPgdwlnpaqlg 93
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIE----------IELDTVSYKP---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrlfykmfggthlvnraglartfQNIRLFREMSVvenllvaqhmrvnRNLLAGVLNtpayrrsenDALDRAFYWLEVVD- 172
Cdd:cd03237 68 -----------------------QYIKADYEGTV-------------RDLLSSITK---------DFYTHPYFKTEIAKp 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 --LVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGI 250
Cdd:cd03237 103 lqIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYL 182
|
250 260
....*....|....*....|
gi 1393793683 251 SDDIIVLDhgdviarGKPAE 270
Cdd:cd03237 183 ADRLIVFE-------GEPSV 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-280 |
2.27e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.89 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIL--------FNARNKTTNVIQVlGQKFQpgdwlnpaql 92
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqYDHHYLHRQVALV-GQEPV---------- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 gqrlfykMFGGTHLVNRA-GLARTfqnirlfrEMSVVENLLVAQHMRvnrNLLAGVLNTpayrrsendaldrafYWLEVv 171
Cdd:TIGR00958 566 -------LFSGSVRENIAyGLTDT--------PDEEIMAAAKAANAH---DFIMEFPNG---------------YDTEV- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 dlvdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEiirfLRDHHDITVLLIEHDMGMVMGiS 251
Cdd:TIGR00958 612 ------GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTVER-A 680
|
250 260
....*....|....*....|....*....
gi 1393793683 252 DDIIVLDHGDVIARGKPAEIQHNEKVIAA 280
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-247 |
2.72e-10 |
|
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: 58.66 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqvlGQKFQPGD 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG----------PLDFQRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 WlnpaqlGQRLFYkmfggthLVNRAGLARTfqnirlfreMSVVENL--LVAQHMRvnrnllAGVLntpayrrsenDALDR 163
Cdd:cd03231 71 I------ARGLLY-------LGHAPGIKTT---------LSVLENLrfWHADHSD------EQVE----------EALAR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 164 afywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHD 243
Cdd:cd03231 113 -------VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
....
gi 1393793683 244 MGMV 247
Cdd:cd03231 186 LGLS 189
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-267 |
4.59e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASG--GNILFNARNKTTNVIQvlgqkfqpgdwlnpaqlgqrlfy 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK----------------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 kmfggthlvnRAGLARtfQNIRLFREMSVVENLLVAQHMRVNRNLlagvlntpayrrSENDALDRAFYWLEVVDLVDCAN 178
Cdd:PLN03211 141 ----------RTGFVT--QDDILYPHLTVRETLVFCSLLRLPKSL------------TKQEKILVAESVISELGLTKCEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 179 RLAGE-----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDD 253
Cdd:PLN03211 197 TIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDS 276
|
250
....*....|....
gi 1393793683 254 IIVLDHGDVIARGK 267
Cdd:PLN03211 277 VLVLSEGRCLFFGK 290
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-260 |
6.47e-10 |
|
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: 56.30 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKttnvIQVLGQkfqpgd 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK----IGYFEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 86 wlnpaqlgqrlfykmfggthlvnraglartfqnirlfremsvvenllvaqhmrvnrnllagvlntpayrrsendaldraf 165
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 166 ywlevvdlvdcanrlageMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVEThkLSEIIRFLRDHHDiTVLLIEHDMG 245
Cdd:cd03221 71 ------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD-LES--IEALEEALKEYPG-TVILVSHDRY 128
|
250
....*....|....*
gi 1393793683 246 MVMGISDDIIVLDHG 260
Cdd:cd03221 129 FLDQVATKIIELEDG 143
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-244 |
1.08e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIK--ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVlgqkfq 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV------ 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 83 pgdwlnpaqlgqrlfykmfggthlvnraglartFQNIRLFREMSVVENLLVAqhmRVNRNLLAGVLNTPAyrrsenDALD 162
Cdd:TIGR01257 2011 ---------------------------------HQNMGYCPQFDAIDDLLTG---REHLYLYARLRGVPA------EEIE 2048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 163 RAFYW-LEVVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKL-SEIIRFLRDHHdiTVLLI 240
Cdd:TIGR01257 2049 KVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGR--AVVLT 2126
|
....
gi 1393793683 241 EHDM 244
Cdd:TIGR01257 2127 SHSM 2130
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-244 |
1.25e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkfqpGDWLNPAQLGQRlfykm 100
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN------------------GQPMSKLSSAAK----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggTHLVNRAgLARTFQNIRLFREMSVVENllvaqhmrVNRNLLAGVLNtPAyrrsenDALDRAFYWLEVVDLVDCANRL 180
Cdd:PRK11629 82 ---AELRNQK-LGFIYQFHHLLPDFTALEN--------VAMPLLIGKKK-PA------EINSRALEMLAAVGLEHRANHR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393793683 181 AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDM 244
Cdd:PRK11629 143 PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-263 |
1.30e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGfyrasggnilfnarnkttnviQVLGQKFQPGDWLNPAQLGqrlfykm 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------------------ALKGTPVAGCVDVPDNQFG------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnraglartfqnirlfREMSVVENLLvaqhmrvnrnllagvlntpayrrSENDALDrAFYWLEVVDLVDCANRL 180
Cdd:COG2401 98 ----------------------REASLIDAIG-----------------------RKGDFKD-AVELLNAVGLSDAVLWL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 A--GEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDD-IIVL 257
Cdd:COG2401 132 RrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDlLIFV 211
|
....*.
gi 1393793683 258 DHGDVI 263
Cdd:COG2401 212 GYGGVP 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-282 |
1.34e-09 |
|
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: 58.68 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF---GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYR-ASGGNILFNARnkttnviqvlgqk 80
Cdd:TIGR02633 257 ILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGK------------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 81 fqPGDWLNPAQlgqrlfykmfggthlVNRAGLA-----RTFQNIrlFREMSVVENLLVAQhmrVNRNLLAGVLNTPAyrr 155
Cdd:TIGR02633 324 --PVDIRNPAQ---------------AIRAGIAmvpedRKRHGI--VPILGVGKNITLSV---LKSFCFKMRIDAAA--- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 156 sENDALDRAFYWLEVV----DLVdcanrlAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRd 231
Cdd:TIGR02633 379 -ELQIIGSAIQRLKVKtaspFLP------IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA- 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1393793683 232 HHDITVLLIEHDMGMVMGISDDIIVLDHGDViargKPAEIQHN---EKVIAAYL 282
Cdd:TIGR02633 451 QEGVAIIVVSSELAEVLGLSDRVLVIGEGKL----KGDFVNHAltqEQVLAAAL 500
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-271 |
2.43e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKT-TVFnCLTGFYRASG---GNILFNARNkttnviqv 76
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGRE-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 77 lgqkfqpgdWLNpaqLGQRLFYKMfggthlvnRA-GLARTFQNirlfrEMSVVEnllvaQHMRVNRNLLAGVLNTPAYRR 155
Cdd:PRK09473 83 ---------ILN---LPEKELNKL--------RAeQISMIFQD-----PMTSLN-----PYMRVGEQLMEVLMLHKGMSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 156 SEndALDRAFYWLEVVDLVDCANRLA---GEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDH 232
Cdd:PRK09473 133 AE--AFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRE 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1393793683 233 HDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK09473 211 FNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-68 |
3.04e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 3.04e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 1 MNATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGF--YRASGGNILFNARN 68
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGES 72
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-276 |
3.79e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFN---CL----TGFYRASGGNIlfnarnkttnviqvlgqkfqpgDWLNPA 90
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNilgCLdkptSGTYRVAGQDV----------------------ATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 91 QLGQrlfykmfggthlVNRAGLARTFQNIRLFREMSVVENLLVAQhmrvnrnLLAGVlntpayrrSENDALDRAFYWLEV 170
Cdd:PRK10535 79 ALAQ------------LRREHFGFIFQRYHLLSHLTAAQNVEVPA-------VYAGL--------ERKQRLLRAQELLQR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 171 VDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDH-HdiTVLLIEHDmGMVMG 249
Cdd:PRK10535 132 LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgH--TVIIVTHD-PQVAA 208
|
250 260
....*....|....*....|....*..
gi 1393793683 250 ISDDIIVLDHGDVIaRGKPAEIQHNEK 276
Cdd:PRK10535 209 QAERVIEIRDGEIV-RNPPAQEKVNVA 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-268 |
5.05e-09 |
|
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: 55.19 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFQ--PGDwlnpAQLgqrlf 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISiiPQD----PVL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 98 ykmFGGThlvnraglartfqnIRlfremsvvENLlvaqhmrvnrnllagvlntPAYRRSENDALDRAfywLEVVDLVDCA 177
Cdd:cd03244 90 ---FSGT--------------IR--------SNL-------------------DPFGEYSDEELWQA---LERVGLKEFV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEM-----------SYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIR--FlrdhHDITVLLIEHDM 244
Cdd:cd03244 123 ESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIReaF----KDCTVLTIAHRL 198
|
250 260
....*....|....*....|....
gi 1393793683 245 GMVMGiSDDIIVLDHGDVIARGKP 268
Cdd:cd03244 199 DTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-262 |
6.08e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlGQKFQPGDWLNPAQLGQRLFY 98
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN------------GKDISPRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 99 KmfggthlvNRaglartfqnirlfREMSVVENLLVAQHMRVNRNL-------LAGVLNTPAYRRSENDAldRAFYWLEvv 171
Cdd:PRK09700 345 E--------SR-------------RDNGFFPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQRTAENQ--RELLALK-- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 dlvdCA--NRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGlnpVETHKLSEIIRFLRDHHD--ITVLLIEHDMGMV 247
Cdd:PRK09700 400 ----CHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG---IDVGAKAEIYKVMRQLADdgKVILMVSSELPEI 472
|
250
....*....|....*
gi 1393793683 248 MGISDDIIVLDHGDV 262
Cdd:PRK09700 473 ITVCDRIAVFCEGRL 487
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-62 |
6.88e-09 |
|
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: 54.85 E-value: 6.88e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1393793683 16 GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI 62
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-217 |
7.19e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILfnarnkttnviqvlgqkfqpgdwlnpaqlgqrlfyKM 100
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDL-----------------------------------TL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 FGgthlvNRAGLARTFQNIRlfREMSVVENLLvaqHM--RVN---RN-LLAGVLNTPAYRRSENDALDR-AFYWLevvDL 173
Cdd:PRK10938 321 FG-----RRRGSGETIWDIK--KHIGYVSSSL---HLdyRVStsvRNvILSGFFDSIGIYQAVSDRQQKlAQQWL---DI 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1393793683 174 VDCANRLAG----EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPV 217
Cdd:PRK10938 388 LGIDKRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-232 |
8.39e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLtgfyrasggnilfnARNKTTNVIQvlgqkfqpgdwlnpaqlgqrlfykm 100
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVL--------------AERVTTGVIT------------------------- 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fGGTHLVNRAGLARTF---------QNIRLfREMSVVENLLVAQHMRVNRNLlagvlntpaYRRSENDALDRAFYWLEVV 171
Cdd:TIGR00956 820 -GGDRLVNGRPLDSSFqrsigyvqqQDLHL-PTSTVRESLRFSAYLRQPKSV---------SKSEKMEYVEEVIKLLEME 888
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393793683 172 DLVDCANRLAGE-MSYGQQRRLEIARAMCTSPEMIC-LDEPAAGLNPVETHKLSEIIRFLRDH 232
Cdd:TIGR00956 889 SYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH 951
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
178-283 |
1.11e-08 |
|
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: 55.79 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEMSYGQQRRLEIARAMCT--SPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDmgmvmgiSDDII 255
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHD-------EDTIR 554
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1393793683 256 VLDH------------GDVIARGKPAEI-QHNEKVIAAYLG 283
Cdd:TIGR00630 555 AADYvidigpgagehgGEVVASGTPEEIlANPDSLTGQYLS 595
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
184-268 |
1.16e-08 |
|
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: 53.96 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 184 MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRflRDHHDITVLLIEHDMGMVMGIsDDIIVLDHGDVI 263
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
....*
gi 1393793683 264 ARGKP 268
Cdd:cd03369 203 EYDHP 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-257 |
1.49e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 2 NATILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkf 81
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 82 qpgdwLNPAQLGQRLFYkmfggthlvnraglarTFQNIRLFREmSVVENLLVAQHMRvnrnllagvlntpaYRRSENDAL 161
Cdd:PRK10247 74 -----LKPEIYRQQVSY----------------CAQTPTLFGD-TVYDNLIFPWQIR--------------NQQPDPAIF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 162 --DRAFYWLEVVDLVDCANRLAGemsyGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEII-RFLRDhHDITVL 238
Cdd:PRK10247 118 ldDLERFALPDTILTKNIAELSG----GEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIhRYVRE-QNIAVL 192
|
250
....*....|....*....
gi 1393793683 239 LIEHDMGMVMGiSDDIIVL 257
Cdd:PRK10247 193 WVTHDKDEINH-ADKVITL 210
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
262-285 |
1.73e-08 |
|
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: 49.17 E-value: 1.73e-08
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-269 |
2.03e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQ-----RGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnviqvlgqkfqpgdwlnpaql 92
Cdd:PRK13409 347 TKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 gQRLFYKMfggthlvnraglartfQNIRLFREMSVVENLlvaqhmrvnrnllagvlntpayrRSENDALDRAFYWLEVVD 172
Cdd:PRK13409 400 -LKISYKP----------------QYIKPDYDGTVEDLL-----------------------RSITDDLGSSYYKSEIIK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 ---LVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMG 249
Cdd:PRK13409 440 plqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDY 519
|
250 260
....*....|....*....|
gi 1393793683 250 ISDDIIVLDhgdviarGKPA 269
Cdd:PRK13409 520 ISDRLMVFE-------GEPG 532
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-271 |
2.23e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGG----IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFY----RASGGNILFNARNKTT----N 72
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRisekE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 73 VIQVLGQK----FQ-PGDWLNPAqlgqrlfYKMfggthlvnraglarTFQnirlfremsVVENLLVaqHMRVNRnllagv 147
Cdd:PRK11022 83 RRNLVGAEvamiFQdPMTSLNPC-------YTV--------------GFQ---------IMEAIKV--HQGGNK------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 148 lntpAYRRsendalDRAFYWLEVVDLVDCANRL---AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSE 224
Cdd:PRK11022 125 ----KTRR------QRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIE 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1393793683 225 IIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK11022 195 LLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-271 |
3.19e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.31 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASgGNILFNARNkttnviqvLGQkfqpgdwLNPAQLGQRlfykm 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRP--------LSD-------WSAAELARH----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnRAGLArtfQNIRLFREMSVVENLLVAQHMRVNRNLLAGVLNTPAYRRSENDALDRAFywlevvdlvdcaNRL 180
Cdd:COG4138 71 --------RAYLS---QQQSPPFAMPVFQYLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPL------------TQL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 AGemsyGQQRRLEIArAMC------TSPE--MICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGMVMGISD 252
Cdd:COG4138 128 SG----GEWQRVRLA-AVLlqvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHAD 201
|
250
....*....|....*....
gi 1393793683 253 DIIVLDHGDVIARGKPAEI 271
Cdd:COG4138 202 RVWLLKQGKLVASGETAEV 220
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
178-266 |
5.95e-08 |
|
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: 52.26 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEMSYGQQRRLEIARAMCTSPEMIC--LDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMVMgISDDII 255
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIR-AADHVI 209
|
90
....*....|....*..
gi 1393793683 256 VL-----DH-GDVIARG 266
Cdd:cd03270 210 DIgpgagVHgGEIVAQG 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-266 |
6.24e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF---GGI--------KALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNarnkttnv 73
Cdd:PRK10261 313 ILQVRNLVTRFplrSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN-------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 74 iqvlGQKFqpgDWLNPAQLgQRLfykmfggthlvnRAGLARTFQNI------RLFREMSVVENLLVaqhmrvnRNLLAGv 147
Cdd:PRK10261 385 ----GQRI---DTLSPGKL-QAL------------RRDIQFIFQDPyasldpRQTVGDSIMEPLRV-------HGLLPG- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 148 lntpayrrseNDALDRAFYWLEVVDLV-DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLnpvETHKLSEII 226
Cdd:PRK10261 437 ----------KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL---DVSIRGQII 503
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1393793683 227 RFLRDHH---DITVLLIEHDMGMVMGISDDIIVLDHGDVIARG 266
Cdd:PRK10261 504 NLLLDLQrdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-283 |
9.56e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 4 TILHVEHLMMHF---GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYR-ASGGNILFNARNKTTNviqvlgq 79
Cdd:PRK13549 258 VILEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIR------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 80 kfqpgdwlNPAQlgqrlfykmfggthlVNRAGLA-----RTFQNIRLfrEMSVVENLLVAQHMRVNRnllAGVLNTPAYR 154
Cdd:PRK13549 331 --------NPQQ---------------AIAQGIAmvpedRKRDGIVP--VMGVGKNITLAALDRFTG---GSRIDDAAEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 155 RSENDALDRafywLEvvdlVDCAN-RLA-GEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDH 232
Cdd:PRK13549 383 KTILESIQR----LK----VKTASpELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1393793683 233 HdITVLLIEHDMGMVMGISDDIIVLDHGdviaRGKPAEIQHN---EKVIAAYLG 283
Cdd:PRK13549 455 G-VAIIVISSELPEVLGLSDRVLVMHEG----KLKGDLINHNltqEQVMEAALR 503
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-67 |
1.86e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 50.55 E-value: 1.86e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNAR 67
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-271 |
1.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.14 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARN-----KTTNVIQVLGQKFQpgdwlNPAq 91
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdfsKLQGIRKLVGIVFQ-----NPE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 92 lgqrlfykmfggTHLVNRaglartfqnirlfremSVVENLLVAQhmrvnRNLlagVLNTPAYRRSendaLDRAfywLEVV 171
Cdd:PRK13644 88 ------------TQFVGR----------------TVEEDLAFGP-----ENL---CLPPIEIRKR----VDRA---LAEI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 DLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMvMGIS 251
Cdd:PRK13644 125 GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDA 202
|
250 260
....*....|....*....|
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI 271
Cdd:PRK13644 203 DRIIVMDRGKIVLEGEPENV 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-65 |
2.56e-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: 51.72 E-value: 2.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1393793683 24 VNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFN 65
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-53 |
3.35e-07 |
|
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: 51.09 E-value: 3.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTG 53
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-271 |
3.46e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGfyrasggnilfnARNKTTNVIQVLGqkfqpG 84
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG------------ARKIQQGRVEVLG-----G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 85 DWLNPA---QLGQRLFYkMfggthlvnRAGLARtfqNirLFREMSVVENL-----LVAQhmrvnrnllagvlnTPAYRRS 156
Cdd:NF033858 64 DMADARhrrAVCPRIAY-M--------PQGLGK---N--LYPTLSVFENLdffgrLFGQ--------------DAAERRR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 157 ENDALDRAfywlevVDLVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPvethkLS-----EIIRFLR- 230
Cdd:NF033858 116 RIDELLRA------TGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP-----LSrrqfwELIDRIRa 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1393793683 231 DHHDITVLliehdmgmvmgIS----------DDIIVLDHGDVIARGKPAEI 271
Cdd:NF033858 185 ERPGMSVL-----------VAtaymeeaerfDWLVAMDAGRVLATGTPAEL 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-275 |
3.91e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVI----------QVLGQKfQPGDWLNPAQL 92
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTneqdyqgdeeQNVGMK-NVNEFSLTKEG 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 GQRLFYKMFGGTHLVNRAGLARTFQNIRLFREM-SVVENLLVAQHMRVNRNLLAGVLNTP---AYRRSENDALDRAFYWL 168
Cdd:PTZ00265 1265 GSGEDSTVFKNSGKILLDGVDICDYNLKDLRNLfSIVSQEPMLFNMSIYENIKFGKEDATredVKRACKFAAIDEFIESL 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 169 EvvDLVDCANRLAGE-MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMV 247
Cdd:PTZ00265 1345 P--NKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
250 260
....*....|....*....|....*...
gi 1393793683 248 MGiSDDIIVLDHGDVIARGKPAEIQHNE 275
Cdd:PTZ00265 1423 KR-SDKIVVFNNPDRTGSFVQAHGTHEE 1449
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-271 |
4.34e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 18 IKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTN---VIQVLGQKFQ-----PGDWLNP 89
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQivfqnPYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 90 AQ-LGQRLfykmfggthlvnraglartfqnirlfremsvVENLLVaqhmrvNRNLlagvlnTPAYRRsendalDRAFYWL 168
Cdd:PRK11308 108 RKkVGQIL-------------------------------EEPLLI------NTSL------SAAERR------EKALAMM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 169 EVVDL-VDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLN-PVETHKLSeIIRFLRDHHDITVLLIEHDMGM 246
Cdd:PRK11308 139 AKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVLN-LMMDLQQELGLSYVFISHDLSV 217
|
250 260
....*....|....*....|....*
gi 1393793683 247 VMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK11308 218 VEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
178-260 |
4.36e-07 |
|
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: 48.86 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 NRLAGEMSYGQQRRLEIARAMCTSPE--MICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGMvMGISDDII 255
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDV-LSSADWII 159
|
....*
gi 1393793683 256 VLDHG 260
Cdd:cd03238 160 DFGPG 164
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-283 |
4.63e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNviqvlgqkfQPGDWLNpaqlgqrlfykm 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR---------SPQDGLA------------ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnrAGLARTFQNIR---LFREMSVVENLlvaqhmrvnrnllagVLNTPAYRRSENDALDRAFYWLEVVDLVDCA 177
Cdd:PRK10762 327 ---------NGIVYISEDRKrdgLVLGMSVKENM---------------SLTALRYFSRAGGSLKHADEQQAVSDFIRLF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 178 N-------RLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLN---PVETHKLseIIRFLRDhhDITVLLIEHDMGMV 247
Cdd:PRK10762 383 NiktpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgaKKEIYQL--INQFKAE--GLSIILVSSEMPEV 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 1393793683 248 MGISDDIIVLdHGDVIARGKPAEIQHNEKVIAAYLG 283
Cdd:PRK10762 459 LGMSDRILVM-HEGRISGEFTREQATQEKLMAAAVG 493
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-246 |
7.49e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNkttnvIQVLGQKFQpgdwlnpaqlgQRLFYkmFG 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-----IRRQRDEYH-----------QDLLY--LG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 103 gtHLvnrAGLArtfqnirlfREMSVVENLLVAQHmrvnrnlLAGVLNTpayrrsendalDRAFYWLEVVDLVDCANRLAG 182
Cdd:PRK13538 81 --HQ---PGIK---------TELTALENLRFYQR-------LHGPGDD-----------EALWEALAQVGLAGFEDVPVR 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393793683 183 EMSYGQQRRLEIARAMCTSPEMICLDEPaagLNPVETHKLSEIIRFLRDHHD---ITVLLIEHDMGM 246
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEP---FTAIDKQGVARLEALLAQHAEqggMVILTTHQDLPV 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-62 |
1.23e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI 62
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-270 |
1.86e-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: 49.01 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 19 KALNDVNLEVQRGSI-----TALIGPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqvlgqkfqpgdwlnpaqlg 93
Cdd:COG1245 349 KSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 qrLFYKMfggthlvnraglartfQNIRLFREMSVVENLlvaqhmrvnrnllagvlntpayRRSENDALDRAFYWLEVVD- 172
Cdd:COG1245 403 --ISYKP----------------QYISPDYDGTVEEFL----------------------RSANTDDFGSSYYKTEIIKp 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 --LVDCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGI 250
Cdd:COG1245 443 lgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYI 522
|
250 260
....*....|....*....|
gi 1393793683 251 SDDIIVLDhgdviarGKPAE 270
Cdd:COG1245 523 SDRLMVFE-------GEPGV 535
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-63 |
2.74e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 2.74e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIL 63
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
17-76 |
2.75e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 47.11 E-value: 2.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393793683 17 GIKALNDVNLEVQRGsITALIGPNGAGKTTVFNC----LTGFYRASGGN---------ILFNARNKTTNVIQV 76
Cdd:pfam13476 5 NFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAiklaLYGKTSRLKRKsgggfvkgdIRIGLEGKGKAYVEI 76
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-289 |
2.76e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.07 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGsITALIGPNGAGKTTVFNCLTGFYRASGGNIL----FNARNKTTNVIQVLGQKFQpgdwlnpaQL 92
Cdd:COG3593 10 NFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedFYLGDDPDLPEIEIELTFG--------SL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 93 GQRLFYKMFGGTHlvnRAGLARTFQNIRlfremSVVENLLVAQHMRVNRNLLAGVLNTPAYRRSENDALDRAFYWLEVVd 172
Cdd:COG3593 81 LSRLLRLLLKEED---KEELEEALEELN-----EELKEALKALNELLSEYLKELLDGLDLELELSLDELEDLLKSLSLR- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 173 LVDCANRLAGEMSYGQQRRL------EIARAMCTSPE-MICLDEPAAGLNPvetHKLSEIIRFLRD--HHDITVLLIEHD 243
Cdd:COG3593 152 IEDGKELPLDRLGSGFQRLIllallsALAELKRAPANpILLIEEPEAHLHP---QAQRRLLKLLKElsEKPNQVIITTHS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1393793683 244 MGMVMGIS-DDIIVL--DHGDVIARGKPAEIQHNEKVIAAYLGTDESEV 289
Cdd:COG3593 229 PHLLSEVPlENIRRLrrDSGGTTSTKLIDLDDEDLRKLLRYLGVTRSEL 277
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
168-263 |
2.82e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 168 LEVVDLVDCANRLAG---EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDM 244
Cdd:PRK15134 138 LDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL 217
|
90
....*....|....*....
gi 1393793683 245 GMVMGISDDIIVLDHGDVI 263
Cdd:PRK15134 218 SIVRKLADRVAVMQNGRCV 236
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
207-282 |
3.38e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.10 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 207 LDEPAAGLNPVETHKLSEIIRFLRdhhDI--TVLLIEHDmgmvmgisDDII-----VLD-------H-GDVIARGKPAEI 271
Cdd:COG0178 511 LDEPSIGLHQRDNDRLIETLKRLR---DLgnTVIVVEHD--------EDTIraadyIIDigpgageHgGEVVAQGTPEEI 579
|
90
....*....|..
gi 1393793683 272 QHNEKVI-AAYL 282
Cdd:COG0178 580 LKNPDSLtGQYL 591
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-271 |
3.83e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 24 VNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASgGNILFNARNKTTnviqvlgqkfqpgdwLNPAQLGQRlfykmfgg 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEA---------------WSAAELARH-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 104 thlvnRAGLArtfQNIRLFREMSVVENLLVAQHMRVNRNLLAGVLNtpayrrsendaldrafYWLEVVDLVDCANRLAGE 183
Cdd:PRK03695 71 -----RAYLS---QQQTPPFAMPVFQYLTLHQPDKTRTEAVASALN----------------EVAEALGLDDKLGRSVNQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 184 MSYGQQRR-------LEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGMVMGISDDIIV 256
Cdd:PRK03695 127 LSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWL 205
|
250
....*....|....*
gi 1393793683 257 LDHGDVIARGKPAEI 271
Cdd:PRK03695 206 LKQGKLLASGRRDEV 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-62 |
4.16e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 4.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393793683 6 LHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-72 |
4.36e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.47 E-value: 4.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRAS--GGNILFNARNKTTN 72
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN 76
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-271 |
5.51e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 5 ILHVEHLMMHF----GGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGF----YRASGGNILFN--------ARN 68
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDdidllrlsPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 69 KTTNVIQVLGQKFQ-PGDWLNPAQ-LGQRLFYKMFGGTHLvnraglARTFQNIRlFREMSVVENLlvaqHmRVnrnllaG 146
Cdd:PRK15093 83 RRKLVGHNVSMIFQePQSCLDPSErVGRQLMQNIPGWTYK------GRWWQRFG-WRKRRAIELL----H-RV------G 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 147 VlntpayrRSENDALdRAFYWlevvdlvdcanrlagEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEII 226
Cdd:PRK15093 145 I-------KDHKDAM-RSFPY---------------ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLL 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1393793683 227 RFLRDHHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:PRK15093 202 TRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-216 |
7.41e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 35 ALI--GPNGAGKTTVFNCLTGFYRASGGNILFNARnkttnviqvlgqkfqpgdwlnPAQLGQRLFYKMFGGtHLVNragl 112
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---------------------TATRGDRSRFMAYLG-HLPG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 113 artfqnirLFREMSVVENLlvaqhmrvnrNLLAGVLNTPAYRRSENDaldrafywLEVVDLVDCANRLAGEMSYGQQRRL 192
Cdd:PRK13543 93 --------LKADLSTLENL----------HFLCGLHGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRL 146
|
170 180
....*....|....*....|....
gi 1393793683 193 EIARAMCTSPEMICLDEPAAGLNP 216
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
183-258 |
8.19e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 8.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393793683 183 EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDITVLLIEHDMGMVMGISDDIIVLD 258
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-269 |
8.83e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 28 VQRGSITALIGPNGAGKTTVFNCLTgfyrasgGNILFNarnkttnviqvLGQKFQPGDWLNpaqlgqrlFYKMFGGTHLV 107
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------GELIPN-----------LGDYEEEPSWDE--------VLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 108 N-----RAGlartfqNIRLFREMSVVENLLVAQHMRVnRNLLAGVlntpayrrSENDALDrafywlEVVDLVDCAN---R 179
Cdd:PRK13409 150 NyfkklYNG------EIKVVHKPQYVDLIPKVFKGKV-RELLKKV--------DERGKLD------EVVERLGLENildR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 180 LAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhhDITVLLIEHDMGMVMGISDDIivldh 259
Cdd:PRK13409 209 DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV----- 281
|
250
....*....|
gi 1393793683 260 gdVIARGKPA 269
Cdd:PRK13409 282 --HIAYGEPG 289
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-271 |
1.39e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFnarnkttnviqvlgqkfqpgDWLNPAQLGqrlfykm 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII--------------------DGLNIAKIG------- 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 fggthlvnraglartFQNIRLFREMSVVENLLVAQHMRVNRNllagvlntPAYRRSEND---ALDRAFYWLEVVDLVD-- 175
Cdd:TIGR00957 1355 ---------------LHDLRFKITIIPQDPVLFSGSLRMNLD--------PFSQYSDEEvwwALELAHLKTFVSALPDkl 1411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 ---CANrlAGE-MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHKL-SEIIRFLRDhhDITVLLIEHDMGMVMGI 250
Cdd:TIGR00957 1412 dheCAE--GGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVD-LETDNLiQSTIRTQFE--DCTVLTIAHRLNTIMDY 1486
|
250 260
....*....|....*....|.
gi 1393793683 251 SdDIIVLDHGDVIARGKPAEI 271
Cdd:TIGR00957 1487 T-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-266 |
1.41e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFqpgdwlnpAQLGQRLFyk 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL--------AVVSQTPF-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 100 MFGGThLVNRAGLAR---TFQNI-RLFREMSVVENLLvaqhmrvnrNLLAGvlntpayrrsendaldrafYWLEVvdlvd 175
Cdd:PRK10789 400 LFSDT-VANNIALGRpdaTQQEIeHVARLASVHDDIL---------RLPQG-------------------YDTEV----- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 176 canrlaGE----MSYGQQRRLEIARAMCTSPEMICLDEpaaGLNPVETHKLSEIIRFLRD-HHDITVLLIEHDMGMVMGi 250
Cdd:PRK10789 446 ------GErgvmLSGGQKQRISIARALLLNAEILILDD---ALSAVDGRTEHQILHNLRQwGEGRTVIISAHRLSALTE- 515
|
250
....*....|....*.
gi 1393793683 251 SDDIIVLDHGDVIARG 266
Cdd:PRK10789 516 ASEILVMQHGHIAQRG 531
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-271 |
1.46e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 3 ATILHVEHL-MMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNAR---NKTTNVIQVLG 78
Cdd:COG3845 255 EVVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 79 QKFQPGDwlnpaqlgqRLfykmfggthlvnRAGLArtfqnirlfREMSVVENLLVAQHMR--VNRNllaGVLNTPAYRRS 156
Cdd:COG3845 335 VAYIPED---------RL------------GRGLV---------PDMSVAENLILGRYRRppFSRG---GFLDRKAIRAF 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 157 ENDALDRaFywlevvDlVDCAN--RLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNP--VET-HKLseiIRFLRD 231
Cdd:COG3845 382 AEELIEE-F------D-VRTPGpdTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaIEFiHQR---LLELRD 450
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1393793683 232 hHDITVLLIEHDMGMVMGISDDIIVLDHGDVIARGKPAEI 271
Cdd:COG3845 451 -AGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-62 |
1.97e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1393793683 8 VEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI 62
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-68 |
2.26e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 2.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393793683 5 ILHVEHLMMHFGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGF--YRASGGNILFNARN 68
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD 66
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
182-275 |
2.86e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 182 GEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRFLRdHHDITVLLIEHDMGMVMGISDDIIVLDHGD 261
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
90
....*....|....
gi 1393793683 262 VIARGKPAEIQHNE 275
Cdd:PRK10982 469 VAGIVDTKTTTQNE 482
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
184-271 |
6.09e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 184 MSYGQQRRLEIARAM---CTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGmVMGISDDIIVL--- 257
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKTADYIIDLgpe 907
|
90
....*....|....*..
gi 1393793683 258 --DH-GDVIARGKPAEI 271
Cdd:TIGR00630 908 ggDGgGTVVASGTPEEV 924
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
175-271 |
6.26e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.74 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 175 DCANRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVeTHklSEIIRFL---RDHHDITVLLIEHDMGMVMGIS 251
Cdd:COG4170 150 DIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST-TQ--AQIFRLLarlNQLQGTSILLISHDLESISQWA 226
|
90 100
....*....|....*....|
gi 1393793683 252 DDIIVLDHGDVIARGKPAEI 271
Cdd:COG4170 227 DTITVLYCGQTVESGPTEQI 246
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
181-268 |
6.98e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 AGEMSYGQQRRLEIARAM---CTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGmVMGISDDIIVL 257
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKCADWIIDL 244
|
90
....*....|....*..
gi 1393793683 258 -----DH-GDVIARGKP 268
Cdd:cd03271 245 gpeggDGgGQVVASGTP 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-260 |
7.09e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARN----KTTNVIQvLGQKFQPGDwlnpAQ-----LG 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEinalSTAQRLA-RGLVYLPED----RQssglyLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 94 QRLFYKMFGGTHlvNRAGLArtfqnIRLFREMSVVENllvaqhmrvnrnllagvlntpaYRRSENDALDRAfywlevvdl 173
Cdd:PRK15439 356 APLAWNVCALTH--NRRGFW-----IKPARENAVLER----------------------YRRALNIKFNHA--------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 174 vdcaNRLAGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGlnpVETHKLSEIIRFLRD--HHDITVLLIEHDMGMVMGIS 251
Cdd:PRK15439 398 ----EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG---VDVSARNDIYQLIRSiaAQNVAVLFISSDLEEIEQMA 470
|
....*....
gi 1393793683 252 DDIIVLDHG 260
Cdd:PRK15439 471 DRVLVMHQG 479
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-68 |
7.75e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 7.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARN 68
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS 64
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-272 |
9.96e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.38 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVqrGSITALIGPNGAGKTTVFNCLtGFYRAS-------------GGNILFNARNKTTNVIQVLGQKFQP 83
Cdd:COG4637 9 NFKSLRDLELPL--GPLTVLIGANGSGKSNLLDAL-RFLSDAargglqdalarrgGLEELLWRGPRTITEPIRLELEFAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 84 GD--------------------------WLNPAQLGQRLFYKMFGGTHLVNRAG-------LARTFQNIRLFREMSVVEN 130
Cdd:COG4637 86 EDerdlryelelglpepggrpevkeerlWLKRGSGGRPFLDFRPKGRAVGGEPErldspesLLSQLGDPERFPELRALRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 131 LL--------VAQHMR----VNRNL--------LAGVLNT-----PAYRRSENDALDRAFYWLEVVDLV-DCANRL---- 180
Cdd:COG4637 166 ALrswrfydfHPAPLRqpqpAGRTPvlapdgsnLAAVLATlrethPERFERILEALRDAFPGFEDIEVEpDEDGRVllef 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 ----------AGEMSYGQQRRLEIARAMCT--SPEMICLDEPAAGLNPVEthkLSEIIRFLRDH-HDITVLLIEHDMGMV 247
Cdd:COG4637 246 rekgldrpfpARELSDGTLRFLALLAALLSprPPPLLCIEEPENGLHPDL---LPALAELLREAsERTQVIVTTHSPALL 322
|
330 340 350
....*....|....*....|....*....|
gi 1393793683 248 MGIS-DDIIVLDHGD----VIARGKPAEIQ 272
Cdd:COG4637 323 DALEpEEVLVLEREDdgetRIRRLSDLELP 352
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-260 |
2.34e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 41.55 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTnviqvlgqkfqpgdwlnpaqlgqrl 96
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESE------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 97 fyKMFGGTHLVNRAGLARTFQNIRLFrEMSVVENLlvaqhmrvnrnllagVLNTPaYRRSENDALDRAFYWLEVVDLVDC 176
Cdd:cd03290 68 --PSFEATRSRNRYSVAYAAQKPWLL-NATVEENI---------------TFGSP-FNKQRYKAVTDACSLQPDIDLLPF 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 177 ANRLA-GE----MSYGQQRRLEIARAMCTSPEMICLDEPAAGLN-PVETHKLSE-IIRFLRDHHDiTVLLIEHDMGMVMG 249
Cdd:cd03290 129 GDQTEiGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEgILKFLQDDKR-TLVLVTHKLQYLPH 207
|
250
....*....|.
gi 1393793683 250 iSDDIIVLDHG 260
Cdd:cd03290 208 -ADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
181-275 |
2.46e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 181 AGE-MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHKL-SEIIRflRDHHDITVLLIEHDMGMVMGiSDDIIVLD 258
Cdd:PLN03130 1371 AGEnFSVGQRQLLSLARALLRRSKILVLDEATAAVD-VRTDALiQKTIR--EEFKSCTMLIIAHRLNTIID-CDRILVLD 1446
|
90
....*....|....*..
gi 1393793683 259 HGDVIARGKPAEIQHNE 275
Cdd:PLN03130 1447 AGRVVEFDTPENLLSNE 1463
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-251 |
2.53e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 156 SENDALDRAF-YWLEVVDLV-DCANRLAGEMSYGQQR------RLEIARAMCTSPEMICLDEPAAGLN--PVET--HKLS 223
Cdd:TIGR00606 1170 ENVSASDKRRnYNYRVVMLKgDTALDMRGRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDreNIESlaHALV 1249
|
90 100 110
....*....|....*....|....*....|
gi 1393793683 224 EIIRFLRDHHDITVLLIEHDMGMV--MGIS 251
Cdd:TIGR00606 1250 EIIKSRSQQRNFQLLVITHDEDFVelLGRS 1279
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
182-275 |
2.54e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 182 GE-MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHKLseIIRFLRDH-HDITVLLIEHDMGMVMGiSDDIIVLDH 259
Cdd:PLN03232 1369 GEnFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSL--IQRTIREEfKSCTMLVIAHRLNTIID-CDKILVLSS 1444
|
90
....*....|....*.
gi 1393793683 260 GDVIARGKPAEIQHNE 275
Cdd:PLN03232 1445 GQVLEYDSPQELLSRD 1460
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-242 |
3.04e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.10 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKttnviqVLgqkFQPgdwlnpaqlgQRLFykM 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR------VL---FLP----------QRPY--L 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 101 FGGThlvnraglartfqnirlfremsvvenllvaqhmrvnrnlLAGVLNTPAYRRSENDALDRAfyWLEVVDLVDCANRL 180
Cdd:COG4178 438 PLGT---------------------------------------LREALLYPATAEAFSDAELRE--ALEAVGLGHLAERL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393793683 181 AGE------MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRflRDHHDITVLLIEH 242
Cdd:COG4178 477 DEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
184-246 |
3.60e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 3.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393793683 184 MSYGQQRRLEIARAM----CTSPEMICLDEPAAGLNPVETHKLSEIIRFLRDhHDITVLLIEHDMGM 246
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPEL 143
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-62 |
4.53e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 4.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI 62
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-76 |
5.04e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 5.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393793683 20 ALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIlfnARNKTTNVIQV 76
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAI 92
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
184-273 |
5.59e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 184 MSYGQQRRLEIARAMCTS---PEMICLDEPAAGLNPVETHKLSEIIRFLrDHHDITVLLIEHDMGMVMgISDDIIVLD-- 258
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVVK-VADYVLELGpe 887
|
90
....*....|....*....
gi 1393793683 259 ----HGDVIARGKPAEIQH 273
Cdd:PRK00635 888 ggnlGGYLLASCSPEELIH 906
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-247 |
6.33e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 23 DVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNV--------IQVLGQKfqpgDWLNPAQLGQ 94
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInlkwwrskIGVVSQD----PLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 95 RLFYKMFggthlvnraglarTFQNIRLFREMSVvENLLVAQHMRVNRNLL----AGVLNTPAYRRSENDALD--RAFYWL 168
Cdd:PTZ00265 479 NIKYSLY-------------SLKDLEALSNYYN-EDGNDSQENKNKRNSCrakcAGDLNDMSNTTDSNELIEmrKNYQTI 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 169 EVVDLVDCANRL--------------------AGEMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIIRF 228
Cdd:PTZ00265 545 KDSEVVDVSKKVlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
250
....*....|....*....
gi 1393793683 229 LRDHHDITVLLIEHDMGMV 247
Cdd:PTZ00265 625 LKGNENRITIIIAHRLSTI 643
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
14-51 |
7.80e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 7.80e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1393793683 14 HFGGIKALnDVNLEVQRGsITALIGPNGAGKTTVFNCL 51
Cdd:COG3950 10 NFRGFEDL-EIDFDNPPR-LTVLVGENGSGKTTLLEAI 45
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-243 |
9.50e-04 |
|
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: 39.51 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 33 ITALIGPNGAGKTTVFNCL------TGFYRASGGNILFNARNKTTNVIQVlgqkfqpgdwlnpaqlgqRLFYKMFGGThl 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyaltgELPPNSKGGAHDPKLIREGEVRAQV------------------KLAFENANGK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 107 vnraglartfqNIRLFREMSVVEN-LLVAQhmrvnrnllaGVLNTPAYRrsendaldrafywlevvdlvdcanrLAGEMS 185
Cdd:cd03240 84 -----------KYTITRSLAILENvIFCHQ----------GESNWPLLD-------------------------MRGRCS 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393793683 186 YGQQR------RLEIARAMCTSPEMICLDEPAAGLNP--VEtHKLSEIIRFLRDHHDITVLLIEHD 243
Cdd:cd03240 118 GGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenIE-ESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-263 |
1.10e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.17 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 15 FGGIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTG---FYRASGGNILFNARNkttnviqvlgqkfqpgdwlnpaq 91
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrteGNVSVEGDIHYNGIP----------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 92 lgqrlfYKMFGGTHlvnRAGLARTFQNIRLFREMSVVENLLVAQHMRVNRNLlAGVlntpayrrsendaldrafywlevv 171
Cdd:cd03233 74 ------YKEFAEKY---PGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFV-RGI------------------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 172 dlvdcanrlagemSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHklsEIIRFLRdhhditvlLIEHDMGMVMGIS 251
Cdd:cd03233 120 -------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL---EILKCIR--------TMADVLKTTTFVS 175
|
250 260
....*....|....*....|....
gi 1393793683 252 ------------DDIIVLDHGDVI 263
Cdd:cd03233 176 lyqasdeiydlfDKVLVLYEGRQI 199
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
207-276 |
1.20e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393793683 207 LDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGmVMGISDDIIVL-----DH-GDVIARGKPAEIQHNEK 276
Cdd:COG0178 853 LDEPTTGLHFHDIRKLLEVLHRLVDKGN-TVVVIEHNLD-VIKTADWIIDLgpeggDGgGEIVAEGTPEEVAKVKA 926
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
207-276 |
1.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393793683 207 LDEPAAGLNPVETHKLSEIIRFLRDHHDiTVLLIEHDMGmVMGISDDIIVL--DHGD----VIARGKPAEIQHNEK 276
Cdd:PRK00349 857 LDEPTTGLHFEDIRKLLEVLHRLVDKGN-TVVVIEHNLD-VIKTADWIIDLgpEGGDgggeIVATGTPEEVAKVEA 930
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
11-51 |
1.71e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 1.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1393793683 11 LMMHFGGIKALNDVNLEVQR----GSITALIGPNGAGKTTVFNCL 51
Cdd:TIGR00606 4 LKMSILGVRSFGIEDKDKQIidffSPLTILVGPNGAGKTTIIECL 48
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-53 |
1.73e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.77 E-value: 1.73e-03
10 20
....*....|....*....|....*
gi 1393793683 29 QRGSITALIGPNGAGKTTVFNCLTG 53
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSG 121
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
207-282 |
1.76e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 207 LDEPAAGLNPVETHKLSEIIRFLRdhhDI--TVLLIEHDmgmvmgiSDDIIVLDH------------GDVIARGKPAEIQ 272
Cdd:PRK00349 515 LDEPSIGLHQRDNDRLIETLKHLR---DLgnTLIVVEHD-------EDTIRAADYivdigpgagvhgGEVVASGTPEEIM 584
|
90
....*....|.
gi 1393793683 273 HNEKVI-AAYL 282
Cdd:PRK00349 585 KNPNSLtGQYL 595
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-52 |
1.99e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 1.99e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1393793683 14 HFGGIKALNDVNLEvqrGSITALIGPNGAGKTTVFNCLT 52
Cdd:COG0419 9 NFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIR 44
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-85 |
2.96e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1393793683 33 ITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNKTTNVIQVLGQKFQPGD 85
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGID 53
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-63 |
4.59e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.61 E-value: 4.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNIL 63
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW 718
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
183-263 |
5.45e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.01 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 183 EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNpVETHKLSEiiRFLRDHHDiTVLLIEHDMGMVMGISDDIIVLDHGDV 262
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IETIEWLE--GFLKTFQG-SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
.
gi 1393793683 263 I 263
Cdd:PRK11147 232 V 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-64 |
5.85e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.58 E-value: 5.85e-03
10 20 30
....*....|....*....|....*....|....*
gi 1393793683 30 RGSITALIGPNGAGKTTVFNCLTGFYRASGGNILF 64
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-62 |
5.98e-03 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 36.75 E-value: 5.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1393793683 21 LNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNI 62
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI 58
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
183-242 |
6.27e-03 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 36.75 E-value: 6.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393793683 183 EMSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVETHKLSEIirfLRDHHdITVLLIEH 242
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL---LKELG-ITVISVGH 146
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
184-242 |
6.58e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 37.53 E-value: 6.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393793683 184 MSYGQQRRLEIARAMCTSPEMICLDEPAAGLNPVEthklSEIIRFLRDH--HDITVLLIEH 242
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT----YQVIRKTLKQafADCTVILSEH 195
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| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-69 |
6.65e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 37.81 E-value: 6.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1393793683 17 GIKALNDVNLEVQRGSITALIGPNGAGKTTVFNCLTGFYRASGGNILFNARNK 69
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGK 516
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