|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-233 |
8.97e-126 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 368.34 E-value: 8.97e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:COG1132 347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:COG1132 427 SGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQM 233
Cdd:COG1132 507 LDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFG 577
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
2.28e-110 |
|
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: 316.87 E-value: 2.28e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDA-PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:cd03251 7 TFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:cd03251 87 LFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELY 228
Cdd:cd03251 167 SALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-232 |
2.60e-104 |
|
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: 317.16 E-value: 2.60e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:COG2274 480 SFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:COG2274 560 LFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQ 232
Cdd:COG2274 640 SALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-231 |
7.76e-102 |
|
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: 295.22 E-value: 7.76e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVA 87
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:cd03249 95 ENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 168 EELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.10e-101 |
|
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: 305.91 E-value: 1.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:COG4988 343 SFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:COG4988 423 FAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSP 222
Cdd:COG4988 503 HLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-238 |
9.85e-100 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 302.12 E-value: 9.85e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:COG5265 365 FGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQMVAEEE 238
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAE 600
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-231 |
2.58e-99 |
|
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: 289.13 E-value: 2.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:cd03253 87 FNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-220 |
8.23e-98 |
|
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: 284.89 E-value: 8.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:cd03254 90 SGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMAS 220
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
3-227 |
2.53e-93 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 285.06 E-value: 2.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGY--QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:TIGR02204 345 FAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPV 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:TIGR02204 425 LFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYREL 227
Cdd:TIGR02204 505 SALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-242 |
1.62e-86 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 267.60 E-value: 1.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK13657 422 NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQMVAEEEGGAS 242
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQ 581
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
4.63e-86 |
|
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: 265.86 E-value: 4.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:COG4987 340 SFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:COG4987 420 LFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYN 229
Cdd:COG4987 500 EGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-231 |
3.12e-85 |
|
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: 263.89 E-value: 3.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVA 87
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGRP-DASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:TIGR02203 424 NNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 167 SEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:TIGR02203 504 SERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-231 |
1.71e-81 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 254.56 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQ-QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:PRK11176 349 FTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDA-SDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK11176 429 FNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-206 |
8.92e-80 |
|
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: 236.90 E-value: 8.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQ-QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:cd03228 7 SFSYPgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIrigrpdasdaeveeagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:cd03228 87 LFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKG 206
Cdd:cd03228 125 SALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-231 |
5.94e-78 |
|
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: 234.69 E-value: 5.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP-VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:cd03252 8 FRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-203 |
3.55e-74 |
|
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: 234.10 E-value: 3.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:TIGR02857 329 VAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:TIGR02857 409 AGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVL 203
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-212 |
1.12e-73 |
|
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: 223.24 E-value: 1.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSV 86
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03245 95 RDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524688421 167 SEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADG 212
Cdd:cd03245 175 SEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-231 |
3.00e-72 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 233.10 E-value: 3.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP-VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:TIGR01846 463 FRYAPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:TIGR01846 543 FSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:TIGR01846 623 ALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
3-239 |
8.09e-69 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 221.69 E-value: 8.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:TIGR01192 342 FEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:TIGR01192 422 NRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSA 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQMVAEEEG 239
Cdd:TIGR01192 502 LDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPA 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-227 |
8.23e-68 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 221.52 E-value: 8.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGY--QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:TIGR00958 486 FSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:TIGR00958 566 LFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 161 ASLDMKSEELIQKeiEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYREL 227
Cdd:TIGR00958 646 SALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-232 |
4.01e-67 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 217.41 E-value: 4.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRF--YdvlSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRG 84
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 165 MKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQ 232
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-208 |
4.09e-65 |
|
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: 201.93 E-value: 4.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGY--QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:cd03248 19 FAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:cd03248 99 LFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSV 208
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-213 |
3.17e-62 |
|
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: 194.25 E-value: 3.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADN 89
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IrigrpD----ASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDM 165
Cdd:cd03244 98 L-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524688421 166 KSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGT 213
Cdd:cd03244 173 ETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-236 |
4.14e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 203.79 E-value: 4.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:PRK10789 321 FTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQMVAE 236
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAA 555
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-227 |
1.68e-61 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 204.79 E-value: 1.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQ-QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:TIGR03796 485 FGYSpLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFL 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:TIGR03796 565 FEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATS 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 162 SLDMKSEELIQKEIEKlaSGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYREL 227
Cdd:TIGR03796 645 ALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
1.63e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 194.27 E-value: 1.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:PRK11160 345 SFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFInETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK11160 425 LFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-220 |
5.38e-58 |
|
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: 192.66 E-value: 5.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSV 86
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNirIGR-PDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDM 165
Cdd:COG4618 423 AEN--IARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 166 KSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4618 501 EGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-229 |
2.58e-53 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 182.63 E-value: 2.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:TIGR01193 481 YSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIG-RPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:TIGR01193 561 SGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 162 SLDMKSEELIQKEIEKLASgRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYN 229
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-237 |
5.18e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 180.30 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:PRK10790 348 FAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRpDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK10790 428 ADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQQmVAEE 237
Cdd:PRK10790 507 IDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQL-AGEE 580
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-208 |
4.15e-50 |
|
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: 161.62 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVA 87
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIrigrpdasdaeveeagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:cd03246 94 ENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 524688421 168 EELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKGSV 208
Cdd:cd03246 132 ERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-229 |
8.70e-49 |
|
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: 160.98 E-value: 8.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:COG1120 8 SVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 -FRGSVADNIRIGR---------PDASDAE-VEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKN 150
Cdd:COG1120 87 pFGLTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEHLAD-------RPVDE----LSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 151 APILVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAH------RFstirmADRILVLEKGSVIADGTHEELMaSSP 222
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL-TPE 229
|
....*..
gi 524688421 223 LYRELYN 229
Cdd:COG1120 230 LLEEVYG 236
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-231 |
9.42e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 170.14 E-value: 9.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAP-VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:TIGR03797 458 TFRYRPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGR 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDaEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:TIGR03797 538 LMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAfiIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYNKQ 231
Cdd:TIGR03797 617 SALDNRTQAIVSESLERLKVTRIV--IAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-190 |
1.64e-48 |
|
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: 167.15 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:TIGR02868 342 AGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:TIGR02868 422 DTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180
....*....|....*....|....*...
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHR 190
Cdd:TIGR02868 502 LDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-209 |
3.25e-48 |
|
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: 157.96 E-value: 3.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADN 89
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIgRPDASDAEVEEAGRMSavdsfinetgegysrmigEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEE 169
Cdd:cd03369 102 LDP-FDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 524688421 170 LIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVI 209
Cdd:cd03369 163 LIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-219 |
4.39e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 165.98 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGS 85
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNI-RIGRpDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:TIGR01842 408 VAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 165 MKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:TIGR01842 487 EEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-219 |
1.35e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 165.59 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVL-------------------------------------- 49
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefs 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 50 ----------------SGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADNIRIGRPDASDAEVEEAGRMSAVDS 113
Cdd:PTZ00265 1260 ltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 114 FINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIE--KLASGRTAFIIAHRF 191
Cdd:PTZ00265 1340 FIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRI 1419
|
250 260 270
....*....|....*....|....*....|...
gi 524688421 192 STIRMADRILVLEK----GSVI-ADGTHEELMA 219
Cdd:PTZ00265 1420 ASIKRSDKIVVFNNpdrtGSFVqAHGTHEELLS 1452
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-220 |
2.32e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPVLFRG-SVADNIR 91
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 -IGR-----PDASDAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDM 165
Cdd:COG1131 96 fFARlyglpRKEARERIDELLELFGLTDAAD-------RKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 166 KSEELIQKEIEKLAS-GRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG1131 165 EARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
1.92e-45 |
|
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: 151.33 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV- 80
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 -LFRGSVADNI-----RIGRPdasDAEVEEagrmsAVDSFINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAP 152
Cdd:COG1122 87 qLFAPTVEEDVafgpeNLGLP---REEIRE-----RVEEALELVGlEHLaDRPPHE----LSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIA-HRFSTI-RMADRILVLEKGSVIADGTHEELMA 219
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-217 |
5.67e-44 |
|
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: 147.71 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVL-----SGSVKVDGIDVREMaKKDLLSH---IALVSQYPVLF 82
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDL-DVDVLELrrrVGMVFQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIG-------RPDASDAEVEEAGRMSAVDsfinetGEGYSRMigeMGEGLSGGQRQRVSLARAfLKNAP-IL 154
Cdd:cd03260 94 PGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALW------DEVKDRL---HALGLSGGQQQRLCLARA-LANEPeVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-219 |
1.72e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 153.74 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADN 89
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRigrP--DASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:PLN03130 1333 LD---PfnEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 168 EELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
4.29e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.31 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdllshIALVSQYPVL 81
Cdd:COG1121 13 TVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IGYVPQRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRG---SVADNIRIG---------RPDASD-AEVEEAgrMSAVD--SFINetgegysRMIGEmgegLSGGQRQRVSLARA 146
Cdd:COG1121 87 DWDfpiTVRDVVLMGrygrrglfrRPSRADrEAVDEA--LERVGleDLAD-------RPIGE----LSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 147 FLKNAPILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIR-MADRILVLEKGsVIADGTHEELMASSPLY 224
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLLNRG-LVAHGPPEEVLTPENLS 232
|
.
gi 524688421 225 R 225
Cdd:COG1121 233 R 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
13-161 |
4.42e-42 |
|
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: 140.48 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRG-SVADNIR 91
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 IGRPDASDAEVEEAGRMSAVDSFINETGEGYSRmIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-206 |
1.22e-41 |
|
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: 139.30 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQypvlfrgsv 86
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 adnirigrpdasdaeveeagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 524688421 167 SEELIQKEIEKLA-SGRTAFIIAHRFSTIRMA-DRILVLEKG 206
Cdd:cd00267 115 SRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-207 |
3.17e-41 |
|
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: 139.91 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakkdllsHIALVSQYPVLFRGS 85
Cdd:cd03250 15 QETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPdaSDAE-VEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:cd03250 82 IRENILFGKP--FDEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 524688421 165 MKSEELIQKE--IEKLASGRTAFIIAHRFSTIRMADRILVLEKGS 207
Cdd:cd03250 160 AHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-219 |
7.39e-41 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 140.81 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 1 MCFGYQQD-APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP 79
Cdd:cd03288 25 LCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGSVADNIRIGRpDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:cd03288 105 ILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 160 TASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:cd03288 184 TASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-206 |
1.46e-40 |
|
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: 138.37 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP- 79
Cdd:cd03225 6 SFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 -VLFRGSVADNIRIG------RPDASDAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAP 152
Cdd:cd03225 86 dQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRD-------RSPFT----LSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIR-MADRILVLEKG 206
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLeLADRVIVLEDG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-208 |
1.61e-40 |
|
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: 137.14 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmAKKDLLSHIALVSQYPVLFRG-SVAD 88
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRigrpdasdaeveeagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSE 168
Cdd:cd03230 93 NLK-----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 524688421 169 ELIQKEIEKLAS-GRTAFIIAHRFSTI-RMADRILVLEKGSV 208
Cdd:cd03230 132 REFWELLRELKKeGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-219 |
1.91e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 147.82 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADN 89
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRigrP--DASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:PLN03232 1330 ID---PfsEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 168 EELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-212 |
4.96e-40 |
|
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: 135.90 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmAKKDLLSHIALVSQYPVL 81
Cdd:cd03247 8 FSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD-LEKALSSLISVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIrigrpdasdaeveeagrmsavdsfinetgegysrmigemGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:cd03247 87 FDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADG 212
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-212 |
7.26e-40 |
|
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: 135.64 E-value: 7.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDaPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQypVLf 82
Cdd:cd03214 7 VGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--AL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 rgsvadnirigrpdasdaevEEAGrmsaVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:cd03214 83 --------------------ELLG----LAHLAD-------RPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524688421 163 LDMKSEELIQKEIEKLA--SGRTAFIIAHRFS-TIRMADRILVLEKGSVIADG 212
Cdd:cd03214 128 LDIAHQIELLELLRRLAreRGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-224 |
8.86e-40 |
|
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: 145.86 E-value: 8.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAP-VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV 80
Cdd:TIGR00957 1291 CLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRigrP--DASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:TIGR00957 1371 LFSGSLRMNLD---PfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 159 ATASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLY 224
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-219 |
3.02e-39 |
|
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: 136.14 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPVLF-RGS 85
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYdRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRI-----GRPDASDAE-VEEAGRMSAVDSFINETGEGYSRmigemgeglsgGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:COG4555 91 VRENIRYfaelyGLFDEELKKrIEELIELLGLEEFLDRRVGELST-----------GMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 160 TASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMA 219
Cdd:COG4555 160 TNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-206 |
9.38e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.79 E-value: 9.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSV 86
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADN------IRIGRPDASDAE--VEEAGR-MSAVDSFINEtgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:COG4619 91 RDNlpfpfqLRERKFDRERALelLERLGLpPDILDKPVER---------------LSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 158 EATASLDMKSEELIQKEIEKLA--SGRTAFIIAH-----RfstiRMADRILVLEKG 206
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqiE----RVADRVLTLEAG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-212 |
3.05e-38 |
|
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: 132.27 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQdAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdllshIALVSQYPVL 81
Cdd:cd03235 6 TVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 ---FRGSVADNIRIGR---------PDASD-AEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFL 148
Cdd:cd03235 80 drdFPISVRDVVLMGLyghkglfrrLSKADkAKVDEALERVGLSELAD-------RQIGE----LSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAH-RFSTIRMADRILVLEKGsVIADG 212
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHdLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-229 |
5.31e-38 |
|
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: 133.00 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPvlfRGSV 86
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP---YASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ----------ADNIRIGRPDASDAEVEEAgrMSAV---DSFinetgegYSRMIGEmgegLSGGQRQRVSLARAFLKNAPI 153
Cdd:COG1124 93 hprhtvdrilAEPLRIHGLPDREERIAEL--LEQVglpPSF-------LDRYPHQ----LSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 154 LVLDEATASLDMkseeLIQKEI------EKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELM--ASSPLY 224
Cdd:COG1124 160 LLLDEPTSALDV----SVQAEIlnllkdLREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLagPKHPYT 235
|
....*
gi 524688421 225 RELYN 229
Cdd:COG1124 236 RELLA 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-212 |
9.10e-38 |
|
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: 131.10 E-value: 9.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQYPVLF-RGSV 86
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYsRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03259 90 AENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLN-RYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 524688421 167 SEELIQKEIEKL--ASGRTAFIIAH-RFSTIRMADRILVLEKGSVIADG 212
Cdd:cd03259 165 LREELREELKELqrELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-211 |
3.87e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.16 E-value: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDL----LSHIALVSQY----PVL 81
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFfnllPEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 frgSVADNIRI-----GRPDASDAE-VEE-------AGRMsavDSFINEtgegysrmigemgegLSGGQRQRVSLARAFL 148
Cdd:COG1136 102 ---TALENVALplllaGVSRKERRErAREllervglGDRL---DHRPSQ---------------LSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTIRMADRILVLEKGSVIAD 211
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-211 |
4.94e-37 |
|
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: 129.51 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKkdllsHIALVSQYPVLF--RgSVA 87
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DRGYVFQQDALLpwL-TVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIG--RPDASDAEVEEagrmsAVDSFINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:cd03293 92 DNVALGleLQGVPKAEARE-----RAEELLELVGlSGFeNAYPHQ----LSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524688421 164 DMKSEELIQKEIEKLAS--GRTAFIIAHRFS-TIRMADRILVLEK--GSVIAD 211
Cdd:cd03293 163 DALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-212 |
5.41e-37 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 129.55 E-value: 5.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLL---SHIALVSQYPVL----- 81
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQDPMSslnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 --FRGSVADNIRIGRPDASDAEVEEAGRMSAVDsfINETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:cd03257 99 mtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNRYPHE----LSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 160 TASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIR-MADRILVLEKGSVIADG 212
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-220 |
7.87e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.42 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAK---KDLLSHIALVSQYPV--LF-R 83
Cdd:COG1123 279 RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNpR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNI-------RIGRPDASDAEVEEAgrMSAVD---SFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPI 153
Cdd:COG1123 359 MTVGDIIaeplrlhGLLSRAERRERVAEL--LERVGlppDLAD-------RYPHE----LSGGQRQRVAIARALALEPKL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG1123 426 LILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRyIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-220 |
3.28e-36 |
|
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: 128.00 E-value: 3.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS---HIALVSQYPVLFRG 84
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -SVADNIriGRP-----DASDAEVEEAGRMsavdsFINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:cd03261 92 lTVFENV--AFPlrehtRLSEEEIREIVLE-----KLEAVGlRGAeDLYPAE----LSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 157 DEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-206 |
3.52e-36 |
|
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: 126.15 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAK--KDLLSHIALVSQYPVLFRG- 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIGMVFQDFALFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIrigrpdasdaeveeagrmsavdsfinetgegysrmigemGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:cd03229 92 TVLENI---------------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 524688421 165 MKSEELIQKEIEKLA--SGRTAFIIAHR-FSTIRMADRILVLEKG 206
Cdd:cd03229 133 PITRREVRALLKSLQaqLGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-206 |
5.50e-36 |
|
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: 126.84 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS----HIALVSQ-YPVLFRG 84
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrrrHIGFVFQsFNLLPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRI-----GRPDASDAEV--EEAGRMsavdsfinETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:cd03255 98 TALENVELplllaGVPKKERRERaeELLERV--------GLGDRLNHYPSE----LSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 158 EATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTIRMADRILVLEKG 206
Cdd:cd03255 166 EPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-211 |
1.61e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.74 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmakkdLLSHIALVSQYPVLF--RgSVA 87
Cdd:COG1116 25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDRGVVFQEPALLpwL-TVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGRP--DASDAEVEEagrmsAVDSFINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:COG1116 99 DNVALGLElrGVPKAERRE-----RARELLELVGlAGFeDAYPHQ----LSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 164 DMKSEELIQKEIEKL--ASGRTAFIIAHrfST---IRMADRILVLEK--GSVIAD 211
Cdd:COG1116 170 DALTRERLQDELLRLwqETGKTVLFVTH--DVdeaVFLADRVVVLSArpGRIVEE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
1.90e-35 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 125.86 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGyqqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLlshIALVSQYPVLF 82
Cdd:COG1127 15 FG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL---YELRRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RG-------SVADNIRIG---RPDASDAEVEEAGRM--SAV--DSFINetgegysRMIGEmgegLSGGQRQRVSLARAFL 148
Cdd:COG1127 89 QGgalfdslTVFENVAFPlreHTDLSEAEIRELVLEklELVglPGAAD-------KMPSE----LSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 149 KNAPILVLDEATASLDMKS----EELIQKEIEKLasGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITsaviDELIRELRDEL--GLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-232 |
2.84e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 132.85 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKV-DGIDVREMAKKDLLSHIALVSQYPVLFRG 84
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIR--------------------------------------------IGRPDAS-------------DAEVEEAGR 107
Cdd:PTZ00265 475 SIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNeliemrknyqtikDSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 108 MSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLA--SGRTAF 185
Cdd:PTZ00265 555 KVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITI 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 186 IIAHRFSTIRMADRILVL---EKGS-VIADGTHEELMASSPLYRELYNKQQ 232
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLsnrERGStVDVDIIGEDPTKDNKENNNKNNKDD 685
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-228 |
1.04e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.40 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLL---SHIALVSQYPVL 81
Cdd:COG3638 12 YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRIGMIFQQFNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 F-RGSVADNIRIGR-----------PDASDAEVEEAgrMSAVDSFinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLK 149
Cdd:COG3638 92 VpRLSVLTNVLAGRlgrtstwrsllGLFPPEDRERA--LEALERV------GLADKAYQRADQLSGGQQQRVAIARALVQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 150 NAPILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIRM-ADRILVLEKGSVIADGTHEELmaSSPLYRE 226
Cdd:COG3638 164 EPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPAEL--TDAVLRE 241
|
..
gi 524688421 227 LY 228
Cdd:COG3638 242 IY 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-209 |
1.47e-34 |
|
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: 122.75 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVremAKKDLLSHIALVSQYP-- 79
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQDVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGSVADNIRIGRPDASDAEVEEAGRMSAVDsfINETGEGYSRmigemgeGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:cd03226 83 QLFTDSVREELLLGLKELDAGNEQAETVLKDLD--LYALKERHPL-------SLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 160 TASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFSTI-RMADRILVLEKGSVI 209
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-220 |
2.09e-34 |
|
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: 128.87 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTF---INLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP--VL 81
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEALRGRRIGMVFQDPmtQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIG------RPDASDAEVEEAGRMSAVDSFinetgegYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILV 155
Cdd:COG1123 97 NPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERR-------LDRYPHQ----LSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 156 LDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-216 |
2.66e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.47 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS---HIALVSQ-YPV 80
Cdd:COG2884 11 YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQdFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIR-----IGRPDASDAE-VEEA-------GRMsavDSFINEtgegysrmigemgegLSGGQRQRVSLARAF 147
Cdd:COG2884 91 LPDRTVYENVAlplrvTGKSRKEIRRrVREVldlvglsDKA---KALPHE---------------LSGGEQQRVAIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 148 LKNAPILVLDEATASLDMK-SEELIQ--KEIEKLasGrTAFIIA-HRFSTI-RMADRILVLEKGSVIADGTHEE 216
Cdd:COG2884 153 VNRPELLLADEPTGNLDPEtSWEIMEllEEINRR--G-TTVLIAtHDLELVdRMPKRVLELEDGRLVRDEARGV 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-222 |
2.74e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.94 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAkkdllshialVSQYPV--LFRG------- 84
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----------PAERPVsmLFQEnnlfphl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIG-----RPDASD-AEVEEAgrmsavdsfINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:COG3840 87 TVAQNIGLGlrpglKLTAEQrAQVEQA---------LERVGlAGLlDRLPGQ----LSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 157 DEATASLD--MKSEELiqKEIEKLAS--GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMASSP 222
Cdd:COG3840 154 DEPFSALDpaLRQEML--DLVDELCRerGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-237 |
2.51e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 4 GYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFR 83
Cdd:PRK11231 11 GYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 G-SVADNIRIGR-PDASdaeveEAGRMSA-----VDSFINETGegysrmIGEMGE----GLSGGQRQRVSLARAFLKNAP 152
Cdd:PRK11231 90 GiTVRELVAYGRsPWLS-----LWGRLSAednarVNQAMEQTR------INHLADrrltDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 153 ILVLDEATASLDMKSE-ELIQKEIEKLASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMASSpLYRELYNK 230
Cdd:PRK11231 159 VVLLDEPTTYLDINHQvELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG-LLRTVFDV 237
|
....*..
gi 524688421 231 QQMVAEE 237
Cdd:PRK11231 238 EAEIHPE 244
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-217 |
1.12e-32 |
|
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: 118.94 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS---HIALVSQ-YPV 80
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRIGMIFQhYNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDA-----------SDAEVEEAgrMSAVDSFiNETGEGYSRmigemGEGLSGGQRQRVSLARAFLK 149
Cdd:TIGR02315 91 IERLTVLENVLHGRLGYkptwrsllgrfSEEDKERA--LSALERV-GLADKAYQR-----ADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 150 NAPILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDLAKkYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-228 |
3.38e-32 |
|
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: 117.67 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLL---SHIALVSQ-YPV 80
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQIGMIFQqFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRpdasdaeveeAGRMSAVDSFINETGE-------------GYSRMIGEMGEGLSGGQRQRVSLARAF 147
Cdd:cd03256 90 IERLSVLENVLSGR----------LGRRSTWRSLFGLFPKeekqralaalervGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 148 LKNAPILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELmaSSPLY 224
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL--TDEVL 237
|
....
gi 524688421 225 RELY 228
Cdd:cd03256 238 DEIY 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-219 |
9.68e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 116.14 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTF---INLLCRfYDvlSGSVKVDGIDVREMAKKDLL---SHIALVSQ-YP 79
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER-PT--SGSVLVDGTDLTLLSGKELRkarRRIGMIFQhFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGSVADNI----RIGRpdASDAEVEEAgrmsavdsfINETGE--GYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPI 153
Cdd:cd03258 93 LLSSRTVFENValplEIAG--VPKAEIEER---------VLELLElvGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 154 LVLDEATASLDMKSE----ELIQKEIEKLasGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMA 219
Cdd:cd03258 162 LLCDEATSALDPETTqsilALLRDINREL--GLTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-217 |
1.04e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.05 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVremakKDLLSH---IALVSQYPVLFRG 84
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPPEkrnVGMVFQDYALFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -SVADNI----RIGRPDASDAE--VEEAGRMsavdsfineTG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPILV 155
Cdd:COG3842 92 lTVAENVafglRMRGVPKAEIRarVAELLEL---------VGlEGLaDRYPHQ----LSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 156 LDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEeALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-217 |
2.41e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.87 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQYPVLF-RGSV 86
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQSYALYpHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNI----RIGRPDAS--DAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:COG3839 93 YENIafplKLRKVPKAeiDRRVREAAELLGLEDLLD-------RKPKQ----LSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 161 ASLDMKSEELIQKEIEKLasgrtafiiaHR---FSTI----------RMADRILVLEKGSVIADGTHEEL 217
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRL----------HRrlgTTTIyvthdqveamTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-220 |
3.10e-31 |
|
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: 115.09 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF-R 83
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRI-----GRPDAS-DAEVEEAgrMSAVDSFINETGEGYSRMigemgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:cd03295 90 MTVEENIALvpkllKWPKEKiRERADEL--LALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 158 EATASLDMKSEELIQKEIEKL--ASGRTAFIIAHR-FSTIRMADRILVLEKGSVIADGTHEELMAS 220
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-229 |
3.96e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.18 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLfrgsv 86
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 adNIRI---------------GRPDASDAE-VEEA-GRMSAV---DSFINEtgegysrmigemgegLSGGQRQRVSLARA 146
Cdd:COG4604 87 --NSRLtvrelvafgrfpyskGRLTAEDREiIDEAiAYLDLEdlaDRYLDE---------------LSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 147 FLKNAPILVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHrfsTIRMA----DRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLH---DINFAscyaDHIVAMKDGRVVAQGTPEEIITP 226
|
....*....
gi 524688421 221 SPLyRELYN 229
Cdd:COG4604 227 EVL-SDIYD 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-220 |
5.78e-31 |
|
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: 114.07 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMaKKDLLSH--IALVSQYPVLFRG-SVADN 89
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGRPDASDAEVEEAGRMSAVDSFINETGE-----GYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREARERAEEllervGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 165 MK-SEELIQKeIEKLA-SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:cd03219 176 PEeTEELAEL-IRELReRGITVLLVEHDMDVVmSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-218 |
8.24e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 9 APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL-FRGSVA 87
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGR------PDASDAEVEEAgrMSAVDSfinetgEGYS-RMIGEmgegLSGGQRQRVSLARAFL------KNAPIL 154
Cdd:PRK13548 95 EVVAMGRaphglsRAEDDALVAAA--LAQVDL------AHLAgRDYPQ----LSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLASGRTAFIIA--HRFS-TIRMADRILVLEKGSVIADGTHEELM 218
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-188 |
9.20e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.96 E-value: 9.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmAKKDLLSHIALVSQYPVLFRG-SV 86
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNI----RIGRPDASDAEVEEAgrMSAVdsfinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:COG4133 93 RENLrfwaALYGLRADREAIDEA--LEAV---------GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180
....*....|....*....|....*.
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIA 188
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-219 |
2.21e-30 |
|
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: 112.14 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPVLFRG-S 85
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPDASDAEVEEagRMSAVdsfinetgegYSR------MIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:cd03224 92 VEENLLLGAYARRRAKRKA--RLERV----------YELfprlkeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 160 TASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMA 219
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
16-212 |
2.25e-30 |
|
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: 112.20 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 16 DIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQYPVLFRG-SVADNIRIGR 94
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 95 -PDASDAEVEEagrmSAVDSFINETG--EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELI 171
Cdd:cd03298 96 sPGLKLTAEDR----QAIEVALARVGlaGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 524688421 172 QKEIEKL--ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:cd03298 168 LDLVLDLhaETKMTVLMVTHQPEDAkRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-217 |
4.55e-30 |
|
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: 111.44 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmAKKDLLSHIALVSQYPVLFRG-SVAD 88
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRI-----GRPDAS-DAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:cd03263 95 HLRFyarlkGLPKSEiKEEVELLLRVLGLTDKAN-------KRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEEL 217
Cdd:cd03263 164 LDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-208 |
1.24e-29 |
|
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: 110.19 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKD---LLSHIALVSQ-YPV 80
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQdFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFInetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:cd03292 90 LPDRNVYENVAFALEVTGVPPREIRKRVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTI--RMADRILVLEKGSV 208
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-217 |
3.58e-29 |
|
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: 109.63 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVremakKDLLSH---IALVSQYPVLF-R 83
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHkrpVNTVFQNYALFpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNI----RIGRPDASD--AEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:cd03300 87 LTVFENIafglRLKKLPKAEikERVAEALDLVQLEGYAN-------RKPSQ----LSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 158 EATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
14-219 |
3.68e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 110.13 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV-----REMAKKdllsHIALVSQYPVLFRG-SVA 87
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglppHRIARL----GIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIG-----------------RPDASDAEV-EEAgrMSAVDSFinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLK 149
Cdd:COG0411 98 ENVLVAaharlgrgllaallrlpRARREEREArERA--EELLERV------GLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 150 NAPILVLDEATASLDMK-SEELIQKeIEKLA--SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMA 219
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAEL-IRRLRdeRGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-228 |
3.86e-29 |
|
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: 109.55 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVR--EMAKKDLLShIALVSQYPVLFRG-SV 86
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklPMHKRARLG-IGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGrpdASDAEVEEAGRMSAVDSFINETgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03218 93 EENILAV---LEIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 167 SEELIQKEIEKL-ASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMAsSPLYRELY 228
Cdd:cd03218 168 AVQDIQKIIKILkDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA-NELVRKVY 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-223 |
1.98e-28 |
|
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: 107.86 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSG-SVKV-----DGIDVREMAKkdllsHIALVS---- 76
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWELRK-----RIGLVSpalq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 -QYPVlfRGSVADNIR------IGRPDA-SDAEVEEAGRMSA---VDSFINetgegysRMIGEmgegLSGGQRQRVSLAR 145
Cdd:COG1119 89 lRFPR--DETVLDVVLsgffdsIGLYREpTDEQRERARELLEllgLAHLAD-------RPFGT----LSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 146 AFLKNAPILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFI-IAHR----FSTIrmaDRILVLEKGSVIADGTHEELMA 219
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVlVTHHveeiPPGI---THVLLLKDGRVVAAGPKEEVLT 232
|
....
gi 524688421 220 SSPL 223
Cdd:COG1119 233 SENL 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-225 |
2.42e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL-FRGSVAD 88
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGR------PDASDAEVEEAgrMSAVDSfinetgEGY-SRMIGEmgegLSGGQRQRVSLARAF--LKNAP-----IL 154
Cdd:COG4559 95 VVALGRaphgssAAQDRQIVREA--LALVGL------AHLaGRSYQT----LSGGEQQRVQLARVLaqLWEPVdggprWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMASSPLYR 225
Cdd:COG4559 163 FLDEPTSALDLAHQHAVLRLARQLARrGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-223 |
4.31e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.32 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL-FRGSV 86
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGRP----------DASDAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK09536 95 RQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 157 DEATASLDM----KSEELIQKEIEklaSGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMASSPL 223
Cdd:PRK09536 164 DEPTASLDInhqvRTLELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTL 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-208 |
4.46e-28 |
|
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: 106.18 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQ----YPvlfRGSV 86
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQnyalYP---HMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNI------RIGRPDASDAEVEEAGRMSAVDSFINEtgegYSRMigemgegLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:cd03301 90 YDNIafglklRKVPKDEIDERVREVAELLQIEHLLDR----KPKQ-------LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 161 ASLDMKSEELIQKEIEKL--ASGRTAFIIAH-RFSTIRMADRILVLEKGSV 208
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLqqRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-212 |
5.16e-28 |
|
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: 105.33 E-value: 5.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLC--RFYDVLSGSVKVDGIDVREMAKKdllSHIALVSQYPVLFrgsva 87
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDILH----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 dnirigrpdaSDAEVEEAGRMSAvdsfinetgegysrmigEMgEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:cd03213 95 ----------PTLTVRETLMFAA-----------------KL-RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524688421 168 EELIQKEIEKLAS-GRTAFIIAH--RFSTIRMADRILVLEKGSVIADG 212
Cdd:cd03213 147 ALQVMSLLRRLADtGRTIICSIHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-229 |
2.88e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.87 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAP-VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFR 83
Cdd:PTZ00243 1318 YREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIrigRP--DASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVL-DEAT 160
Cdd:PTZ00243 1398 GTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEAT 1474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEEL-MASSPLYRELYN 229
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVE 1544
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-217 |
3.13e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.12 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDV-----LSGSVKVDGIDVREmAKKDLL---SHIALVSQYP 79
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYD-PDVDVVelrRRVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGSVADNI----RI-GRPDASDAE--VEEAGRMSAV-DsfinetgEGYSRMiGEMGEGLSGGQRQRVSLARAfLKNA 151
Cdd:COG1117 102 NPFPKSIYDNVayglRLhGIKSKSELDeiVEESLRKAALwD-------EVKDRL-KKSALGLSGGQQQRLCIARA-LAVE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 152 P-ILVLDEATASLD----MKSEELIQkeieKLASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:COG1117 173 PeVLLMDEPTSALDpistAKIEELIL----ELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-216 |
4.42e-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: 103.95 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMA--KKDllshIALVSQYPVLF-RGSVA 87
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpeKRD----ISYVPQNYALFpHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIG-------RPDAsDAEVEEAGRMSAVDSFINETGEGysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:cd03299 90 KNIAYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 161 ASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEE 216
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWaLADKVAIMLNGKLIQVGKPEE 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
27-219 |
4.95e-27 |
|
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: 106.04 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 27 LVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdlLSHIALVSQYPVLF-RGSVADNIRIG-RPDASDAEvEE 104
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRA-EI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 105 AGRMSAVDSFINETGEGYSRMIGemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLAS--GR 182
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQ-----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlGI 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 524688421 183 TAFIIAH-RFSTIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:TIGR01187 153 TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-208 |
5.17e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.40 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 16 DIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQYPVLFRG-SVADNIRIGR 94
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHlTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 95 PDASDAEVEEAGRMSAVDSFInetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKE 174
Cdd:TIGR01277 96 HPGLKLNAEQQEKVVDAAQQV-----GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 524688421 175 IEKLASGR--TAFIIAHRFS-TIRMADRILVLEKGSV 208
Cdd:TIGR01277 171 VKQLCSERqrTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-223 |
5.49e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 106.35 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 15 IDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS----HIALVSQYPVLF-RGSVADN 89
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGRPDASDAEveeagRMSAVDSFINETGEGYsrMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEE 169
Cdd:TIGR02142 96 LRYGMKRARPSE-----RRISFERVIELLGIGH--LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 170 LIQKEIEKLAS--GRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMASSPL 223
Cdd:TIGR02142 169 EILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-238 |
6.19e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.91 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFInllcrfydvlsgSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADN 89
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLI------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGrpdaSDAEVEEAGRMSAVDSFINETG--EGYSRM-IGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:PLN03232 699 ILFG----SDFESERYWRAIDVTALQHDLDllPGRDLTeIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 167 -SEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELY-NKQQMVAEEE 238
Cdd:PLN03232 775 vAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMeNAGKMDATQE 848
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-227 |
1.03e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.16 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTF---INLLCRfYDvlSGSVKVDGIDVREMAKKDLL---SHIALVSQYPVLFRG-S 85
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER-PT--SGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNI----RI-GRPDAS-DAEVEE-------AGRMsavDSFINEtgegysrmigemgegLSGGQRQRVSLARAfLKNAP 152
Cdd:COG1135 99 VAENValplEIaGVPKAEiRKRVAEllelvglSDKA---DAYPSQ---------------LSGGQKQRVGIARA-LANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 153 -ILVLDEATASLDMKSE----ELIqKEI-EKLasGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS--SPL 223
Cdd:COG1135 160 kVLLCDEATSALDPETTrsilDLL-KDInREL--GLTIVLITHEMDVVRrICDRVAVLENGRIVEQGPVLDVFANpqSEL 236
|
....
gi 524688421 224 YREL 227
Cdd:COG1135 237 TRRF 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-220 |
1.17e-26 |
|
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: 103.88 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS----HIALVSQYPVLF-RGSVA 87
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGrpdASDAEVEEAGRMSAVDSFINETG-EGYS-RMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLD- 164
Cdd:cd03294 121 ENVAFG---LEVQGVPRAEREERAAEALELVGlEGWEhKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 165 -----MKSEEL-IQKEIeklasGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMAS 220
Cdd:cd03294 194 lirreMQDELLrLQAEL-----QKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
14-223 |
1.58e-26 |
|
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: 105.18 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINL---LCRfydVLSGSVKVDGIDVREMAKK-DLLSH---IALVSQYPVLF-RGS 85
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDSARGiFLPPHrrrIGYVFQEARLFpHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPDASDAEveeagRMSAVDSFINETGEGY--SRMIGemgeGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:COG4148 94 VRGNLLYGRKRAPRAE-----RRISFDEVVELLGIGHllDRRPA----TLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 164 DMKSEELIQKEIEKLasgrtafiiAHRFST------------IRMADRILVLEKGSVIADGTHEELMASSPL 223
Cdd:COG4148 165 DLARKAEILPYLERL---------RDELDIpilyvshsldevARLADHVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-227 |
1.76e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 103.28 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQ-QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLcrfyDVL----SGSVKVDGIDVREMAK-KDLLSHIALV 75
Cdd:TIGR04520 7 SFSYPeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL----NGLllptSGKVTVDGLDTLDEENlWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 76 SQYP--VLFRGSVAD-------NIRIGRPDAsDAEVEEAGRMSAVDSFINEtgEGYSrmigemgegLSGGQRQRVSLARA 146
Cdd:TIGR04520 83 FQNPdnQFVGATVEDdvafgleNLGVPREEM-RKRVDEALKLVGMEDFRDR--EPHL---------LSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 147 FLKNAPILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLY 224
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
...
gi 524688421 225 REL 227
Cdd:TIGR04520 231 KEI 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-242 |
2.37e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.13 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFIN-LLCRFYDVLSGSVKVDGidvremakkdllsHIALVSQYPVLFRGSV 86
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGRP-DAsdAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDM 165
Cdd:PLN03130 696 RDNILFGSPfDP--ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 166 K-SEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELYN---KQQMVAEEEGGA 241
Cdd:PLN03130 774 HvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMEnagKMEEYVEENGEE 853
|
.
gi 524688421 242 S 242
Cdd:PLN03130 854 E 854
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-217 |
2.61e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPVLFRG-SVA 87
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGRpdasdaeveEAGRMSAVDSfiNETGEGYSRMIGEMG---------EGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:COG1129 98 ENIFLGR---------EPRRGGLIDW--RAMRRRARELLARLGldidpdtpvGDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 159 ATASLDmkseeliQKEIEKL--------ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEEL 217
Cdd:COG1129 167 PTASLT-------EREVERLfriirrlkAQGVAIIYISHRLDEVfEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-212 |
6.14e-26 |
|
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: 100.45 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPaGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS----HIALVSQYPVLF-RGSVAD 88
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGRPDASDAE----VEEAgrmsaVDSF-INETGEGYSrmigemgEGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:cd03297 95 NLAFGLKRKRNREdrisVDEL-----LDLLgLDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 164 DMKSEELIQKEIEKLAS--GRTAFIIAHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:cd03297 163 DRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-228 |
7.54e-26 |
|
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: 100.83 E-value: 7.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPVLFRG-S 85
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPDASDAEvEEAGRMSAVdsfinetgegYSR------MIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:COG0410 95 VEENLLLGAYARRDRA-EVRADLERV----------YELfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 160 TASLdmksEELIQKEIEKL-----ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMASSPLyRELY 228
Cdd:COG0410 164 SLGL----APLIVEEIFEIirrlnREGVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADPEV-REAY 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-217 |
1.09e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.45 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGyqqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTF---INLLCRFyDvlSGSVKVDGIDVrEMAKKDLL---SHIALVS 76
Cdd:COG1126 11 FG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEEP-D--SGTITVDGEDL-TDSKKDINklrRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 Q----YPVLfrgSVADNIRI------GRPDAsDAEveeagrmsavdsfinETGEGYSRMIGeMGE-------GLSGGQRQ 139
Cdd:COG1126 84 QqfnlFPHL---TVLENVTLapikvkKMSKA-EAE---------------ERAMELLERVG-LADkadaypaQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 140 RVSLARAFLKNAPILVLDEATASLD--MKSEELiqKEIEKLA-SGRTAFIIAH--RFSTiRMADRILVLEKGSVIADGTH 214
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDpeLVGEVL--DVMRDLAkEGMTMVVVTHemGFAR-EVADRVVFMDGGRIVEEGPP 220
|
...
gi 524688421 215 EEL 217
Cdd:COG1126 221 EEF 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-212 |
1.17e-25 |
|
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: 99.60 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQdapVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdlLSHIALVSQYPVLF 82
Cdd:cd03268 10 YGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RG-SVADNIRIGR--PDASDAEVEEAGRMsavdsfINETGEGySRMIGemgeGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:cd03268 85 PNlTARENLRLLArlLGIRKKRIDEVLDV------VGLKDSA-KKKVK----GFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 160 TASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
3-207 |
1.28e-25 |
|
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: 99.71 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH----IALVSQY 78
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 79 PVLFRGSVADNIRIGRPdASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:cd03290 88 PWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 159 ATASLDMK-SEELIQKEIEKLASG--RTAFIIAHRFSTIRMADRILVLEKGS 207
Cdd:cd03290 167 PFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-216 |
2.61e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.51 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV--REMAKKDLLSHIALVSQYP--VLFRGSVA 87
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIG--RPDASDAEVEEAgrmsaVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDM 165
Cdd:PRK13637 103 KDIAFGpiNLGLSEEEIENR-----VKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524688421 166 KSEELIQKEIEKLAS--GRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEE 216
Cdd:PRK13637 178 KGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
3.16e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.07 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP- 79
Cdd:PRK13632 14 SFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGS-VADNIRIG------RPDASDAEVEEAGRMSAVDSFINETgegysrmigemGEGLSGGQRQRVSLARAFLKNAP 152
Cdd:PRK13632 94 NQFIGAtVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKE-----------PQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIA--HRFSTIRMADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-217 |
3.26e-25 |
|
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: 99.34 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQYPVLFRG-SV 86
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIG--------RPDAS--DAEVEEAGRMSAVDSFinetgegYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:cd03296 92 FDNVAFGlrvkprseRPPEAeiRAKVHELLKLVQLDWL-------ADRYPAQ----LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 157 DEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-212 |
3.43e-25 |
|
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: 98.42 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGqVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPvlfrgSVADNI 90
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEF-----GVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 RI-----------GRPDA-SDAEVEEAgrMSAVDsfineTGEGYSRMIGemgeGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:cd03264 88 TVrefldyiawlkGIPSKeVKARVDEV--LELVN-----LGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 159 ATASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADG 212
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-211 |
4.35e-25 |
|
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: 96.73 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQypvlfrgsvad 88
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 nirigrpdasdaeveeagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK-S 167
Cdd:cd03216 83 --------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524688421 168 EELIqKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIAD 211
Cdd:cd03216 119 ERLF-KVIRRLrAQGVAVIFISHRLDEVfEIADRVTVLRDGRVVGT 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-212 |
1.02e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 97.44 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmAKKDLLSHIALVSQYPVLF-RGSVADN 89
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYdRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IR-IGR-----PDASDAEVEE-AGRMSavdsfINETGEgysrmigEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:cd03266 99 LEyFAGlyglkGDELTARLEElADRLG-----MEELLD-------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 163 LDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:cd03266 167 LDVMATRALREFIRQLrALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-217 |
1.52e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.45 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTfinLLcR------FYDvlSGSVKVDGID------VREmakkdllSHIALVSQ 77
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTT---LL-RiiagleTPD--SGRIVLNGRDlftnlpPRE-------RRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 YPVLFRG-SVADNIRIG---RPdASDAEVEEAgrmsaVDSFINETG-EGYS-RMIGEmgegLSGGQRQRVSLARAFLKNA 151
Cdd:COG1118 83 HYALFPHmTVAENIAFGlrvRP-PSKAEIRAR-----VEELLELVQlEGLAdRYPSQ----LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 152 PILVLDEATASLDMKseelIQKEIEKL------ASGRTAFiiahrFST------IRMADRILVLEKGSVIADGTHEEL 217
Cdd:COG1118 153 EVLLLDEPFGALDAK----VRKELRRWlrrlhdELGGTTV-----FVThdqeeaLELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-208 |
1.75e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.83 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFY-----DVLSGSVKVDGI--DVREMAKKDLLshialvsqypvLFR 83
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLEtpsagELLAGTAPLAEAreDTRLMFQDARL-----------LPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRIG-----RPDASDAeveeagrMSAVdsfinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:PRK11247 96 KKVIDNVGLGlkgqwRDAALQA-------LAAV---------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524688421 159 ATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFS-TIRMADRILVLEKGSV 208
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-217 |
2.23e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQdapVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQYPVLF 82
Cdd:PRK10851 12 FGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RG-SVADNIRIG--------RPDAS--DAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNA 151
Cdd:PRK10851 87 RHmTVFDNIAFGltvlprreRPNAAaiKAKVTQLLEMVQLAHLAD-------RYPAQ----LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAH-RFSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-225 |
2.28e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGyqqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLL--SHIALVSQYPV 80
Cdd:PRK09493 11 FG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVA-DNIRIGrP----DASDAEVEEAGR--MSAVdsfinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK09493 88 LFPHLTAlENVMFG-PlrvrGASKEEAEKQARelLAKV---------GLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMASSPLYR 225
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEeGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVLIKNPPSQR 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-217 |
2.74e-24 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 96.28 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPVLFRGSVA-DNIR 91
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDELTGwENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 I-----GRPDASDAEveeagRMSAVDSFInETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03265 96 IharlyGVPGAERRE-----RIDELLDFV-GLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524688421 167 SEELIQKEIEKL--ASGRTAFIIAHRFSTIRM-ADRILVLEKGSVIADGTHEEL 217
Cdd:cd03265 166 TRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
8-203 |
5.04e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGiDVRemakkdllshIALVSQY---PVLFRG 84
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-GAR----------VAYVPQRsevPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIG---------RPDASD-AEVEEAgrMSAVDsfINETGEgysRMIGEmgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:NF040873 73 TVRDLVAMGrwarrglwrRLTRDDrAAVDDA--LERVG--LADLAG---RQLGE----LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 524688421 155 VLDEATASLDMKSEELIQKEI-EKLASGRTAFIIAHRFSTIRMADRILVL 203
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-217 |
5.16e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPVLFRG-SVADNI 90
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVPNlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 RIGRPDASDAEVeeagRMSAVDSFINETGEGY------SRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL- 163
Cdd:COG3845 102 VLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLt 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 164 DMKSEELIqKEIEKLAS-GRTAFIIAHRFSTIR-MADRILVLEKGSVIADG-----THEEL 217
Cdd:COG3845 174 PQEADELF-EILRRLAAeGKSIIFITHKLREVMaIADRVTVLRRGKVVGTVdtaetSEEEL 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-207 |
5.88e-24 |
|
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: 95.58 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVD----GIDVREMAKKDLL----SHIALVSQY-PV 80
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREILalrrRTIGYVSQFlRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGS----VADNIRIGRPDASDAEvEEAGRMsavdsfinetgegYSRMigEMGEGL--------SGGQRQRVSLARAFL 148
Cdd:COG4778 105 IPRVSaldvVAEPLLERGVDREEAR-ARAREL-------------LARL--NLPERLwdlppatfSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 149 KNAPILVLDEATASLDMKSE----ELIQkeiEKLASGrTAFI-IAHRFSTI-RMADRILVLEKGS 207
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRavvvELIE---EAKARG-TAIIgIFHDEEVReAVADRVVDVTPFS 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-216 |
7.01e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREM-AKKdllSHIALVSQYPVLF-RGS 85
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAEN---RHVNTVFQSYALFpHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIG-----RPDASDAE-VEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:PRK09452 103 VFENVAFGlrmqkTPAAEITPrVMEALRMVQLEEFAQ-------RKPHQ----LSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 160 TASLDMKSEELIQKEIEKLAS--GRTaFIiahrFST------IRMADRILVLEKGSVIADGTHEE 216
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRklGIT-FV----FVThdqeeaLTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-206 |
8.36e-24 |
|
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: 94.90 E-value: 8.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVrEMAKKDLL---SHIALVSQYPVLF-R 83
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINelrQKVGMVFQQFNLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRIG---RPDASDAEVEEAGR--------MSAVDSFINEtgegysrmigemgegLSGGQRQRVSLARAFLKNAP 152
Cdd:cd03262 91 LTVLENITLApikVKGMSKAEAEERALellekvglADKADAYPAQ---------------LSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 153 ILVLDEATASLDmksEELIQ---KEIEKLA-SGRTAFIIAHRFSTIR-MADRILVLEKG 206
Cdd:cd03262 156 VMLFDEPTSALD---PELVGevlDVMKDLAeEGMTMVVVTHEMGFAReVADRVIFMDDG 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-242 |
8.82e-24 |
|
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: 99.63 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakkdllsHIALVSQYPVLFRGS 85
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRP--DASDAEVEEAGRMSAvDSFINETGEgySRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:TIGR00957 715 LRENILFGKAlnEKYYQQVLEACALLP-DLEILPSGD--RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 164 DMKSEELIQKEI---EKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRELY-----NKQQMVA 235
Cdd:TIGR00957 792 DAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrtyapDEQQGHL 871
|
....*..
gi 524688421 236 EEEGGAS 242
Cdd:TIGR00957 872 EDSWTAL 878
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-220 |
1.87e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVD------GIDVREMAKKDLLSHIALVSQY 78
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 79 PVLF-RGSVADNirIGRPDASDAEVEEAGRMSAVDSFINETG---EGYSRMIGEMGEgLSGGQRQRVSLARAFLKNAPIL 154
Cdd:PRK14246 99 PNPFpHLSIYDN--IAYPLKSHGIKEKREIKKIVEECLRKVGlwkEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
9-222 |
7.00e-23 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.15 E-value: 7.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 9 APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakkdllsHIALVSQYPVLFRGSVAD 88
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGrpdASDAEVEEAGRMSA--VDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03291 117 NIIFG---VSYDEYRYKSVVKAcqLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 167 SE-ELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSP 222
Cdd:cd03291 194 TEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-222 |
8.80e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.90 E-value: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakkdllsHIALVSQYPVLFRGSVADN 89
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGrpdASDAEVEEAGRMSA--VDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:TIGR01271 507 IIFG---LSYDEYRYTSVIKAcqLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 168 E-ELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSP 222
Cdd:TIGR01271 584 EkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-209 |
1.07e-22 |
|
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: 92.33 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLL-CRF--YDVLSGSVKVDGidvREMAKKDLLSHIALVSQYPVLFRG-SV 86
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVegGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 AD------NIRIGR--PDASDAEVEEAGRMSAVdsfinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:cd03234 99 REtltytaILRLPRksSDAIRKKRVEDVLLRDL---------ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524688421 159 ATASLDMKSEELIQKEIEKLA-SGRTAFIIAH--RFSTIRMADRILVLEKGSVI 209
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-189 |
1.53e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.62 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 4 GYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVR----EMA---KKDLLshialvs 76
Cdd:COG4525 15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaDRGvvfQKDAL------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 qYPVLfrgSVADNIRIGrpdASDAEVEEAGRMSAVDSFINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:COG4525 88 -LPWL---NVLDNVAFG---LRLRGVPKAERRARAEELLALVGlADFaRRRIWQ----LSGGMRQRVGIARALAADPRFL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAH 189
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
16-219 |
1.56e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.95 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 16 DIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKkdllshialvSQYPV--LFRG-------SV 86
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP----------SRRPVsmLFQEnnlfshlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIG-----RPDASD-AEVEE-AGRMSAVDSFinetgegySRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:PRK10771 89 AQNIGLGlnpglKLNAAQrEKLHAiARQMGIEDLL--------ARLPGQ----LSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 160 TASLD--MKSEELiqKEIEKLASGR--TAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:PRK10771 157 FSALDpaLRQEML--TLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-221 |
1.93e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGY-QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP-V 80
Cdd:PRK13635 13 FRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGS-VAD-------NIRIGRPDASDaEVEEAGRMSAVDSFINEtgEGYSrmigemgegLSGGQRQRVSLARAFLKNAP 152
Cdd:PRK13635 93 QFVGAtVQDdvafgleNIGVPREEMVE-RVDQALRQVGMEDFLNR--EPHR---------LSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASS 221
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-229 |
2.47e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.18 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdllSHIALVSQYPVLF 82
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK---QRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSV-ADNIR------IGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMiGEMGEGLSGGQRQRVSLARAFLKNAPILV 155
Cdd:TIGR02769 95 QDSPsAVNPRmtvrqiIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA-DKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 156 LDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIAD-GTHEELMASSPLYRELYN 229
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEEcDVAQLLSFKHPAGRNLQS 251
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-223 |
3.06e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAK-KDLLSHIALVSQYP-V 80
Cdd:PRK13644 9 YSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPeT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRG-SVADNIRIGRPDASDAEVEEAGRmsaVDSFINETGEGYSRMigEMGEGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:PRK13644 89 QFVGrTVEEDLAFGPENLCLPPIEIRKR---VDRALAEIGLEKYRH--RSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 160 TASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPL 223
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-220 |
4.42e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 92.42 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYD---VLSGSVKVDGIDVREMAKKDL----LSHIALVSQYPV-----L 81
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELrkirGREIQMIFQDPMtslnpV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FR-G-SVADNIRIGRpDASDAEVEEAGR--MSAVDsfINETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:COG0444 103 MTvGdQIAEPLRIHG-GLSKAEARERAIelLERVG--LPDPERRLDRYPHE----LSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 158 EATASLDMkseeLIQKEIEKL-----ASGRTAFI-IAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG0444 176 EPTTALDV----TIQAQILNLlkdlqRELGLAILfITHDLGVVAeIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-216 |
8.19e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVdGIDVRemakkdllshIALVSQYPVL 81
Cdd:COG0488 322 SKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRG--SVADNIRIGRPDASDAEVEE-AGRM----SAVDSFInetgegysrmigemgEGLSGGQRQRVSLARAFLKNAPIL 154
Cdd:COG0488 390 LDPdkTVLDELRDGAPGGTEQEVRGyLGRFlfsgDDAFKPV---------------GVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 155 VLDEATASLDMKSEELIqkeIEKLAS--GrTAFIIAH-RFSTIRMADRILVLEKGSVIA-DGTHEE 216
Cdd:COG0488 455 LLDEPTNHLDIETLEAL---EEALDDfpG-TVLLVSHdRYFLDRVATRILEFEDGGVREyPGGYDD 516
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-227 |
9.00e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 93.69 E-value: 9.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVkvdgidvreMAKKDllshIALVSQYPVLFRGSVADNI 90
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS----IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 RIGRPDASdAEVEEAGRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEEL 170
Cdd:PTZ00243 742 LFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 171 IQKE--IEKLAsGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMAsSPLYREL 227
Cdd:PTZ00243 821 VVEEcfLGALA-GKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-TSLYATL 877
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-230 |
1.08e-21 |
|
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: 89.12 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRF--YDVLSGSVKVDGIDVREM-----AKKDllshIALVSQYPV 80
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLppeerARLG----IFLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRG-SVADNIRigrpdasdaeveeagrmsavdsfinetgegysrmigEMGEGLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:cd03217 88 EIPGvKNADFLR------------------------------------YVNEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 160 TASLDMKSEELIQKEIEKLASGRTAF-IIAHR---FSTIRmADRILVLEKGSVIADGTHEelmasspLYRELYNK 230
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVlIITHYqrlLDYIK-PDRVHVLYDGRIVKSGDKE-------LALEIEKK 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-228 |
1.38e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREM-----AKKDllshIALVSQYPVLFRG 84
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrARLG----IGYLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -SVADNIRIGrpdASDAEVEEAGRMSAVDSFINETGEGYSRmiGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:COG1137 93 lTVEDNILAV---LELRKLSKKEREERLEELLEEFGITHLR--KSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 164 DMKSEELIQKEIEKLASGRTAFIIA-HRF-STIRMADRILVLEKGSVIADGTHEELmASSPLYRELY 228
Cdd:COG1137 168 DPIAVADIQKIIRHLKERGIGVLITdHNVrETLGICDRAYIISEGKVLAEGTPEEI-LNNPLVRKVY 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
2.23e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP--V 80
Cdd:PRK13647 12 FRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIG------RPDASDAEVEEAgrMSAVDSFINETGEGYSrmigemgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:PRK13647 92 VFSSTVWDDVAFGpvnmglDKDEVERRVEEA--LKAVRMWDFRDKPPYH---------LSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-218 |
2.55e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.63 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS----HIALVSQ-YPVLFRGSV 86
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQsFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGRPDASDAEVEEagRMSAVDSFINETGEGYSRmigEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:PRK10070 124 LDNTAFGMELAGINAEER--REKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 167 SEELIQKEIEKLASG--RTAFIIAHRF-STIRMADRILVLEKGSVIADGTHEELM 218
Cdd:PRK10070 199 IRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-220 |
2.99e-21 |
|
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: 91.67 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRfydvL---SGSVKVDGIDVREMAKKDLL---SHIALVSQYPvlF---- 82
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR----LipsEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDP--Fgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 -RGSVADNI----RIGRPDASDAEVEEagrmsAVDSFINETG---EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:COG4172 377 pRMTVGQIIaeglRVHGPGLSAAERRA-----RVAEALEEVGldpAARHRYPHE----FSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 155 VLDEATASLDMkseeLIQKEIEKL-----ASGRTAFI-IAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4172 448 VLDEPTSALDV----SVQAQILDLlrdlqREHGLAYLfISHDLAVVRaLAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-217 |
3.23e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGyqqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV--REMAKKDllshIALVSQYPV 80
Cdd:PRK11432 16 FG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD----ICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LF-RGSVADNI-----RIGRPDASDAE-VEEAGRMSAVDSFinetGEGYSRMIgemgeglSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK11432 89 LFpHMSLGENVgyglkMLGVPKEERKQrVKEALELVDLAGF----EDRYVDQI-------SGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-216 |
3.77e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL---FRGSVA 87
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DN------------IRIGRPDASDAEVEEAgrmsavdsfINETGEGY-SRMIGEMGEgLSGGQRQRVSLARAFLKNAPIL 154
Cdd:COG1101 101 ENlalayrrgkrrgLRRGLTKKRRELFREL---------LATLGLGLeNRLDTKVGL-LSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLASGR--TAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEE 216
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRIILDVSGEE 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-227 |
1.07e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.61 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCrfyDVL---SGSVKVDGID-VREmaKKDLLSHIALV----SQypvLFrg 84
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GILvptSGEVRVLGYVpFKR--RKEFARRIGVVfgqrSQ---LW-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 svadnirigrPDasdaeveeagrMSAVDSF--------INEtgEGYSRMIGEMGEG-------------LSGGQRQRVSL 143
Cdd:COG4586 109 ----------WD-----------LPAIDSFrllkaiyrIPD--AEYKKRLDELVELldlgelldtpvrqLSLGQRMRCEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 144 ARAFLKNAPILVLDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEELKER 245
|
....*..
gi 524688421 221 SPLYREL 227
Cdd:COG4586 246 FGPYKTI 252
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-218 |
1.46e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.91 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 21 AGQVVALVGPSGAGKTTfinLLCRFYDVL--SGSVKVDGIDVREMAKKDLLSHIALVSQ------------YPVLFRGSV 86
Cdd:PRK03695 21 AGEILHLVGPNGAGKST---LLARMAGLLpgSGSIQFAGQPLEAWSAAELARHRAYLSQqqtppfampvfqYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 AdnirigRPDASDAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLK-------NAPILVLDEA 159
Cdd:PRK03695 98 T------RTEAVASALNEVAEALGLDDKLG-------RSVNQ----LSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 160 TASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELM 218
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-227 |
1.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTT---FINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP-VLFRG- 84
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPdNQFVGa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIGrpdASDAEVEEAGRMSAVDSFINETGegYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:PRK13640 101 TVGDDVAFG---LENRAVPRPEMIKIVRDVLADVG--MLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 165 MKSEELIQKEIEKLA--SGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYREL 227
Cdd:PRK13640 176 PAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEI 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-207 |
1.83e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTF---INLLCRFYdvlSGSVKVDGidvremakkdlLSHIALVSQYPVLFR 83
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLlraIAGLWPYG---SGRIARPA-----------GARVLFLPQRPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRigRPDA----SDAEVEEAGRMSAVDSFIN--ETGEGYSRMigemgegLSGGQRQRVSLARAFLkNAP-ILVL 156
Cdd:COG4178 440 GTLREALL--YPATaeafSDAELREALEAVGLGHLAErlDEEADWDQV-------LSLGEQQRLAFARLLL-HKPdWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 157 DEATASLDMKSEE----LIQKEIEKlasgrTAFI-IAHRFSTIRMADRILVLEKGS 207
Cdd:COG4178 510 DEATSALDEENEAalyqLLREELPG-----TTVIsVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-226 |
2.12e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSG-----SVKVDGIDVreMAKKDLLS---HIALVSQYPVLF 82
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEfrrRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIG--------RPD---ASDAEVEEAGRMSAVDSFINETGEGysrmigemgegLSGGQRQRVSLARAFLKNA 151
Cdd:PRK14271 114 PMSIMDNVLAGvrahklvpRKEfrgVAQARLTEVGLWDAVKDRLSDSPFR-----------LSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMaSSPLYRE 226
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF-SSPKHAE 257
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-217 |
2.55e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDV-----LSGSVKVDGIDVREMAKKDLLSHIALVSQYP--- 79
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 ---VLFRgSVADNIRIGRPDASDAEVEEAGRMSAVDSFINEtgEGYSRMIGEMGEgLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK14247 95 pnlSIFE-NVALGLKLNRLVKSKKELQERVRWALEKAQLWD--EVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 157 DEATASLDMKSEELIQKEIEKLASGRTAFIIAH-RFSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-208 |
2.68e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.79 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVS----QYPVLFRGSVA 87
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrkREGLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGRpdasdaeveeagrmsavdsfinetgegysrmigemgeGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:cd03215 97 ENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524688421 168 EELIQKEIEKLASGRTAFIIahrFST-----IRMADRILVLEKGSV 208
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-211 |
2.74e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.40 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS----HIALVSQ-YPV 80
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQrYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIgrpDASDAEVEEAGRMSAVDSFINETGEGysRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK10535 98 LSHLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLGLE--DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 161 ASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKGSVIAD 211
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-239 |
2.83e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCrFYD----VLSGSVKVDG--IDVREMAKKDllshiALVSQYPvLFRGS 85
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSpkgvKGSGSVLLNGmpIDAKEMRAIS-----AYVQQDD-LFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 --------VADNIRIGRPDASDaeveeaGRMSAVDSFINETGEGYSR--MIGEMG--EGLSGGQRQRVSLARAFLKNAPI 153
Cdd:TIGR00955 114 ltvrehlmFQAHLRMPRRVTKK------EKRERVDEVLQALGLRKCAntRIGVPGrvKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFST--IRMADRILVLEKGSVIADGTHEELmasSPLYREL--- 227
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA---VPFFSDLghp 264
|
250 260
....*....|....*....|
gi 524688421 228 ----YNK----QQMVAEEEG 239
Cdd:TIGR00955 265 cpenYNPadfyVQVLAVIPG 284
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-220 |
4.21e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV---REMAK-----KDLLSHIALVSQYPVLF 82
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 -RGSVADNIrIGRP----DASDAEVEEAGRMSAVDSFINETGEGYSRMigemgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:PRK11264 98 pHRTVLENI-IEGPvivkGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 158 EATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-212 |
5.24e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 85.46 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREmAKKDLLSHIALV--SQYPVLFRG 84
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIGRpDASDAEVEEAGRmsavdsfineTGEGYSRMIgEMGE-------GLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:cd03267 111 PVIDSFYLLA-AIYDLPPARFKK----------RLDELSELL-DLEElldtpvrQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 158 EATASLDMKSEELIQKEIEKLASGRTAFII--AHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-225 |
8.54e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQ----YPV 80
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEvdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LfrgsVADNIRIGR---------PDASDAEVEEAGrMSAVDSFinetgEGYSRMIGEmgegLSGGQRQRVSLARAFLKNA 151
Cdd:PRK15056 96 L----VEDVVMMGRyghmgwlrrAKKRDRQIVTAA-LARVDMV-----EFRHRQIGE----LSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYR 225
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLEL 236
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-215 |
1.03e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.73 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRF--YDVLSGSVKVDGIDVREM-----AKKDllshIALVSQYPV 80
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELspderARAG----IFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRG-SVAD-------NIRIGRPDASDAEVEEAGRMSAVD---SFINetgegysRmigEMGEGLSGGQRQRVSLARAFLK 149
Cdd:COG0396 88 EIPGvSVSNflrtalnARRGEELSAREFLKLLKEKMKELGldeDFLD-------R---YVNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 150 NAPILVLDEATASLDMKSEELIQKEIEKLASGRTAF-IIAH--RFSTIRMADRILVLEKGSVIADGTHE 215
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGIlIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-237 |
1.11e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQ----------YPV 80
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnattpgditvQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGSVADNIRIGRPDASDAEveeagrmsAVDSFINETgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEE--------AVTKAMQAT--GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 161 ASLDMKSE----ELIQkEIEKlASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMaSSPLYRELYNKQQMVA 235
Cdd:PRK10253 172 TWLDISHQidllELLS-ELNR-EKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV-TAELIERIYGLRCMII 248
|
..
gi 524688421 236 EE 237
Cdd:PRK10253 249 DD 250
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-237 |
1.34e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFIN-----LLCRFYDVLSGSVKV-DGIDVREMAK----------KDLLSHIAL 74
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIgDKKNNHELITnpyskkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 75 VSQYP--VLFRGSVADNIRIGrPDASDAEVEEAGRMSAVdsFINETGEGYSrMIGEMGEGLSGGQRQRVSLARAFLKNAP 152
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKF--YLNKMGLDDS-YLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 153 ILVLDEATASLDMKSE-ELIQKEIEKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGT------HEELMASS--- 221
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTpyeiftDQHIINSTsiq 276
|
250 260 270
....*....|....*....|....*....|.
gi 524688421 222 ---------------PLYRELYNKQQMVAEE 237
Cdd:PRK13631 277 vprviqvindlikkdPKYKKLYQKQPRTIEQ 307
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-218 |
1.42e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 21 AGQVVALVGPSGAGKTTfinLLCRFYDVLS--GSVKVDGIDVREMAKKDLLSHIALVSQ------------YPVLFRGSV 86
Cdd:COG4138 21 AGELIHLIGPNGAGKST---LLARMAGLLPgqGEILLNGRPLSDWSAAELARHRAYLSQqqsppfampvfqYLALHQPAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADnirigrPDASDAEVEE-AGRMSAVDSfinetgegYSRMIGEmgegLSGGQRQRVSLARAFLK-------NAPILVLDE 158
Cdd:COG4138 98 AS------SEAVEQLLAQlAEALGLEDK--------LSRPLTQ----LSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 159 ATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELM 218
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-164 |
1.71e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.30 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYD---VLSGSVKVDGIDVREMAKkdLLSHIALVSQYPVLF 82
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPA--EQRRIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 -RGSVADNIRIGRPdasdAEVEEAGRMSAVDSFINETGEG--YSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:COG4136 89 pHLSVGENLAFALP----PTIGRAQRRARVEQALEEAGLAgfADRDPAT----LSGGQRARVALLRALLAEPRALLLDEP 160
|
....*
gi 524688421 160 TASLD 164
Cdd:COG4136 161 FSKLD 165
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-213 |
2.33e-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: 83.64 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREM---AKKDLLS-HIALVSQ----YPVLf 82
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRArHVGFVFQsfqlLPTL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 rgSVADNIRI-----GRPDASDAEVEEAGRMsavdsfinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:COG4181 106 --TALENVMLplelaGRRDARARARALLERV------------GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 158 EATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGT 213
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELnrERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-220 |
2.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAP----VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHI----ALVS 76
Cdd:PRK13646 12 YQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVrkriGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 QYP--VLFRGSVADNIRIGrPDASDAEVEEAgRMSAVDSFINEtgeGYSRMIGEMGE-GLSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK13646 92 QFPesQLFEDTVEREIIFG-PKNFKMNLDEV-KNYAHRLLMDL---GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-217 |
3.18e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 85.27 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKkdLLSHIALVSQYPVLF-RGSVAD 88
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGRPDASDAEVEEAGRMSAVDSFINetgegYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSE 168
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEMLGLVH-----MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 169 ELIQKEIEKLAS--GRTAFIIAH-RFSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK11607 186 DRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-213 |
3.99e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP----VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAK----KDLLSHIAL 74
Cdd:PRK13643 9 YTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 75 VSQYP--VLFRGSVADNIRIGrPDASDAEVEEAGRMSAVD-SFINETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNA 151
Cdd:PRK13643 89 VFQFPesQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEKlEMVGLADEFWEKSPFE----LSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGT 213
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGT 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
14-220 |
4.24e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.40 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS---HIALVSQYPvlF-----RGS 85
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDP--YaslnpRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNI-------RIGRPDASDAEVEEAgrMSAVdsfinetG---EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILV 155
Cdd:COG4608 114 VGDIIaeplrihGLASKAERRERVAEL--LELV-------GlrpEHADRYPHE----FSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 156 LDEATASLDmKS---------EELiQKEIeklasGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4608 181 CDEPVSALD-VSiqaqvlnllEDL-QDEL-----GLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
4.36e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.74 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 1 MCFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDG--IDVREMAKKDLLSHIALVSQY 78
Cdd:PRK13636 11 LNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 79 P--VLFRGSVADNIRIGRPDASDAEVEEAGRmsaVDSFINETgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK13636 91 PdnQLFSASVYQDVSFGAVNLKLPEDEVRKR---VDNALKRT--GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 157 DEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIRM-ADRILVLEKGSVIADGTHEELMASSPLYR 225
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
5.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.26 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP-VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPV- 80
Cdd:PRK13648 15 FQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LFRGS-VADNIRIGRPDAS------DAEVEEAgrMSAVDSFINETGEGYSrmigemgegLSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK13648 95 QFVGSiVKYDVAFGLENHAvpydemHRRVSEA--LKQVDMLERADYEPNA---------LSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLASGRTAFIIA--HRFSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
8.73e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.82 E-value: 8.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTfinLLCRFYDVL---SGSVKVDGIDVReMAKKDLLS---HIALVS 76
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKST---LFLHFNGILkptSGEVLIKGEPIK-YDKKSLLEvrkTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 QYP--VLFRGSVADNIRIGRPDA--SDAEVEEagrmsAVDSFINETG-EGYSRmigEMGEGLSGGQRQRVSLARAFLKNA 151
Cdd:PRK13639 85 QNPddQLFAPTVEEDVAFGPLNLglSKEEVEK-----RVKEALKAVGmEGFEN---KPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRM-ADRILVLEKGSVIADGTHEELMASSPLYRE 226
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETIRK 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-220 |
8.87e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPVL---Frg 84
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGVVPQFDNLdpdF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRI-GRP-DASDAEVEEAgrmsaVDSFInETGEGYSRMIGEMGEgLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK13537 96 TVRENLLVfGRYfGLSAAAARAL-----VPPLL-EFAKLENKADAKVGE-LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 163 LDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK13537 169 LDPQARHLMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-208 |
1.01e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.93 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQ----YPVLfr 83
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQsyalYPHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 gSVADNIRIGRPDASDAEVEEAGRMSAVDSFINetgegYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:PRK11000 91 -SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524688421 164 DMKSEELIQKEIEKLAS--GRTAFIIAH-RFSTIRMADRILVLEKGSV 208
Cdd:PRK11000 165 DAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-198 |
1.03e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDvLSGSVKVDG--------IDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIG------RPDASDAEVEEAGRMSAvdsfinETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK14258 101 PMSVYDNVAYGvkivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 524688421 157 DEATASLD----MKSEELIQKeiEKLASGRTAFIIAHRFSTI-RMAD 198
Cdd:PRK14258 175 DEPCFGLDpiasMKVESLIQS--LRLRSELTMVIVSHNLHQVsRLSD 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-219 |
1.15e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.47 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLL----------------------CRFYDVLS-------------GS 52
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvalcekCGYVERPSkvgepcpvcggtlEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 53 VKVDGIDVREMAKKDLLSHIALVSQYPVLFRG--SVADNIRIGRPDASDAEVEEAGRmsAVDsFINETGEGYsRMIgEMG 130
Cdd:TIGR03269 92 EEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYEGKEAVGR--AVD-LIEMVQLSH-RIT-HIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 131 EGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTI-RMADRILVLEKGS 207
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIeDLSDKAIWLENGE 246
|
250
....*....|..
gi 524688421 208 VIADGTHEELMA 219
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-225 |
1.41e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.48 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV-----REMAKKDllshIALVSQYPVLFRG- 84
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplHARARRG----IGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIGRPDASDAEVEEagRMSAVDSFINETGEGYSRmiGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQ--REDRANELMEEFHIEHLR--DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 165 MKSEELIQKEIEKLA-SGRTAFIIAHRF-STIRMADRILVLEKGSVIADGTHEELMASSPLYR 225
Cdd:PRK10895 170 PISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-226 |
1.49e-18 |
|
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: 82.21 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVlSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADNI 90
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 RigrPDA--SDAEV----EEAGRMSAVDSFINEtgegYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:cd03289 98 D---PYGkwSDEEIwkvaEEVGLKSVIEQFPGQ----LDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 165 MKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRE 226
Cdd:cd03289 171 PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-217 |
2.17e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 80.65 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ----YPVLfrgS 85
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQgreiFPRL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIG---RPDASDAEVEEAGRMSAVdsfinetgegYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATas 162
Cdd:TIGR03410 92 VEENLLTGlaaLPRRSRKIPDEIYELFPV----------LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 163 ldmkseELIQ----KEIEK----LAS--GRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:TIGR03410 160 ------EGIQpsiiKDIGRvirrLRAegGMAILLVEQYLDFAReLADRYYVMERGRVVASGAGDEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-209 |
2.19e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGiDVRemakkdllshIALVSQYPVLFRG-SVAD 88
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQEPPLDDDlTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGRPDASDAEVEEAgRMSAVDSFINETGEGYSRMIGEMGEG-----------------------------LSGGQRQ 139
Cdd:COG0488 81 TVLDGDAELRALEAELE-ELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpeedldrpvseLSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 140 RVSLARAFLKNAPILVLDEATASLDMKSeeliqkeIEKLASgrtaFIIAHRFSTI----------RMADRILVLEKGSVI 209
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLES-------IEWLEE----FLKNYPGTVLvvshdryfldRVATRILELDRGKLT 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-189 |
2.65e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVremakKDLLSHIALVSQYPVLFR-GS 85
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQNEGLLPwRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGrpdASDAEVEEAGRMSAVDSFINETG-EGY-SRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:PRK11248 87 VQDNVAFG---LQLAGVEKMQRLEIAHQMLKKVGlEGAeKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 524688421 164 DMKSEELIQKEIEKL--ASGRTAFIIAH 189
Cdd:PRK11248 160 DAFTREQMQTLLLKLwqETGKQVLLITH 187
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-227 |
3.33e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFI---NLLCRfydVLSGSVKVDGIDVREMAKKDLLS---HIALVSQ-YPVLFRGS 85
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQhFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRI-----GRPDAS-DAEVEE----AGRMSAVDSFINEtgegysrmigemgegLSGGQRQRVSLARAfLKNAP-IL 154
Cdd:PRK11153 99 VFDNVALplelaGTPKAEiKARVTEllelVGLSDKADRYPAQ---------------LSGGQKQRVAIARA-LASNPkVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 155 VLDEATASLDMKSE----ELIqKEI-EKLasGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS--SPLYRE 226
Cdd:PRK11153 163 LCDEATSALDPATTrsilELL-KDInREL--GLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSEVFSHpkHPLTRE 239
|
.
gi 524688421 227 L 227
Cdd:PRK11153 240 F 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-243 |
8.52e-18 |
|
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: 82.37 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVrEMAKKDLLSHIALVSQYPVLFRG-SVAD 88
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NI----RIGRPDASDAEVEeagrmsaVDSFINETGEGYSRmiGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:TIGR01257 1023 HIlfyaQLKGRSWEEAQLE-------MEAMLEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 165 MKSEELIQKEIEKLASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMASS------PLYRELYNKQQMVAEE 237
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCFgtgfylTLVRKMKNIQSQRGGC 1173
|
....*.
gi 524688421 238 EGGASC 243
Cdd:TIGR01257 1174 EGTCSC 1179
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-213 |
9.35e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP----VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAK-KDLLS---HIAL 74
Cdd:PRK13649 10 YTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQirkKVGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 75 VSQYP--VLFRGSVADNIRIGRPD--ASDAEVEEAGRMSAVDSFINEtgEGYSRMIGEmgegLSGGQRQRVSLARAFLKN 150
Cdd:PRK13649 90 VFQFPesQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGISE--SLFEKNPFE----LSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 151 APILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGT 213
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-217 |
1.22e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.12 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDV-----LSGSVKVDGIDV--REMAKKDLLSHIALVSQ 77
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 YPVLF-RGSVADNIRIG--------RPDASDAEVEEAGRMSAVDSFINETGEGYSrmigemgEGLSGGQRQRVSLARAFL 148
Cdd:PRK14267 93 YPNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDYP-------SNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHR-FSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-232 |
1.47e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakkdllsHIAlvsqyPVL-----FRG- 84
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVS-----ALLelgagFHPe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -SVADNIRI-----GrpdASDAEVEEagRMSAVDSFinetgegysrmiGEMGEGL-------SGGQRQRVSLARAFLKNA 151
Cdd:COG1134 103 lTGRENIYLngrllG---LSRKEIDE--KFDEIVEF------------AELGDFIdqpvktySSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 152 PILVLDEATASLDM----KSEELIQkeiEKLASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAsspLYRE 226
Cdd:COG1134 166 DILLVDEVLAVGDAafqkKCLARIR---ELRESGRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGDPEEVIA---AYEA 239
|
....*.
gi 524688421 227 LYNKQQ 232
Cdd:COG1134 240 LLAGRE 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-217 |
1.54e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 15 IDIRIPAGQVVALVGPSGAGKTTFINLLCRF----------YDVLSGSVKVDGIDVREMAKKDllSHIALV-SQYPVLFR 83
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKSR--ANTGYIfQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRIGRPDASD------AEVEEAGRMSAVDSFineTGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:PRK09984 101 LSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQAL---TRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 158 EATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-219 |
1.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP-VLFRG- 84
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIGRPDASDAEVEEAGRMSAVDSFInetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHEEMKERVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 165 MKSE-ELIQ--KEIEKlASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMA 219
Cdd:PRK13650 173 PEGRlELIKtiKGIRD-DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-221 |
1.72e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLC------RFYDVLSGSVKVDgidvreMAKKDLLS----HIALVSQYPVLF- 82
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISgltrpqKGRIVLNGRVLFD------AEKGICLPpekrRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINEtgegYSRmigemgeGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK11144 90 HYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDR----YPG-------SLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 163 LDM-KSEELIQKeIEKLAsgRTAFI----IAHRFSTI-RMADRILVLEKGSVIADGTHEELMASS 221
Cdd:PRK11144 159 LDLpRKRELLPY-LERLA--REINIpilyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-212 |
1.82e-17 |
|
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: 78.09 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKkdllSHIALVSQYPVLFRG-SVADN 89
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR----NRIGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IR-IGRpdASDAEVEEAGRmsAVDSFIN--ETGEGYSRMIgemgEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03269 91 LVyLAQ--LKGLKKEEARR--RIDEWLErlELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524688421 167 SEELIQKEIEKLA-SGRTAFIIAHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:cd03269 163 NVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-226 |
2.02e-17 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.11 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVlSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADNI 90
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 RigrPDA--SDAEV----EEAGRMSAVDSFINEtgegYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:TIGR01271 1313 D---PYEqwSDEEIwkvaEEVGLKSVIEQFPDK----LDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 165 MKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASSPLYRE 226
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-218 |
2.23e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDV-----LSGSVKVDGIDV--REMAKKDLLSHIALVSQ 77
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 YPVLFRGSVADNI----RI-GRPDAS--DAEVEEAGRMSAVdsfINETGEgysrMIGEMGEGLSGGQRQRVSLARAFLKN 150
Cdd:PRK14239 94 QPNPFPMSIYENVvyglRLkGIKDKQvlDEAVEKSLKGASI---WDEVKD----RLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 151 APILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVIA-DGTHEELM 218
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEyNDTKQMFM 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
2.46e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP----VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVdGIDVREMAK-----KDLLSHIA 73
Cdd:PRK13634 10 HRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKknkklKPLRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 74 LVSQYP--VLFRGSVADNIRIGrPDASDAEVEEAGRMSavdsfinetgegySRMIGEMGEG----------LSGGQRQRV 141
Cdd:PRK13634 89 IVFQFPehQLFEETVEKDICFG-PMNFGVSEEDAKQKA-------------REMIELVGLPeellarspfeLSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 142 SLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELM 218
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREIF 234
|
.
gi 524688421 219 A 219
Cdd:PRK13634 235 A 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-223 |
3.10e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 20 PAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIA-LVSQYPVLFRGSVADNIRIGR-P-- 95
Cdd:PRK10575 35 PAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAyLPQQLPAAEGMTVRELVAIGRyPwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 96 ------DASDAE-VEEAGRMSAVDSFINetgegysRMIgemgEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSE 168
Cdd:PRK10575 115 galgrfGAADREkVEEAISLVGLKPLAH-------RLV----DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 169 ELIQKEIEKLASGRTAFIIAhRFSTIRMA----DRILVLEKGSVIADGTHEELMASSPL 223
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMRGETL 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-212 |
3.57e-17 |
|
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: 77.57 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakkdllsHIALVSQYPVLFRG--SVAD 88
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSLLGLGGGFNPelTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRI-----GRpdaSDAEVEEagRMSAVDSFiNETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:cd03220 104 NIYLngrllGL---SRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524688421 164 D----MKSEELIQkeiEKLASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADG 212
Cdd:cd03220 174 DaafqEKCQRRLR---ELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-218 |
4.10e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.10 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPVLFRG-S 85
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL-ARARIGVVPQFDNLDLEfT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRI-GRP-DASDAEVEEAgrMSAVDSFINETGEGYSRMigemgEGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:PRK13536 131 VRENLLVfGRYfGMSTREIEAV--IPSLLEFARLESKADARV-----SDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 164 DMKSEELIQKEIEK-LASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELM 218
Cdd:PRK13536 204 DPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
12-206 |
4.53e-17 |
|
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: 77.12 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLshiaLVSQYPVLFRGSVADNIR 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV----VFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 IG----RPDASDAEveeagRMSAVDSFINETG--EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDM 165
Cdd:TIGR01184 77 LAvdrvLPDLSKSE-----RRAIVEEHIALVGltEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 524688421 166 KSEELIQKEIEKLA--SGRTAFIIAHRF-STIRMADRILVLEKG 206
Cdd:TIGR01184 148 LTRGNLQEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
5.34e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.92 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 1 MCFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYP- 79
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 -VLFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFInetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:PRK13652 89 dQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 159 ATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMASSPLYRE 226
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-189 |
5.63e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVL-----SGSV----------KVDGIDVRemakkdllSHIALVS 76
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVtfhgknlyapDVDPVEVR--------RRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 QYPVLFRGSVADNI----RI-GRPDASDAEVEEAGRMSAVDSFINETgegysrmIGEMGEGLSGGQRQRVSLARAFLKNA 151
Cdd:PRK14243 98 QKPNPFPKSIYDNIaygaRInGYKGDMDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAH 189
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-217 |
5.74e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidVREMAKKDLLSH---IALVSQYPVLFRG-S 85
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG--NPCARLTPAKAHqlgIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPDASDAEVEEAGRMSAVDSFINEtgegysrmigEMGEG-LSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDL----------DSSAGsLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 165 -MKSEELIQKEIEKLASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:PRK15439 173 pAETERLFSRIRELLAQGVGIVFISHKLPEIRqLADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-223 |
5.99e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAP----VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKK-----DLLSHIA 73
Cdd:PRK13645 14 YTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkRLRKEIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 74 LVSQYP--VLFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNA 151
Cdd:PRK13645 94 LVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMASSPL 223
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-221 |
1.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTfinlLCRFYDVL----SGSVKVDG--IDVREMAK--KDLLSHIALVSQYP--VLFR 83
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKST----LMQHFNALlkpsSGTITIAGyhITPETGNKnlKKLRKKVSLVFQFPeaQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRIGRPD--ASDAEVEEAGRmsavdSFINETGEGYSrMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:PRK13641 101 NTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKVGLSED-LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 162 SLDMKS-EELIQKEIEKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMASS 221
Cdd:PRK13641 175 GLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-189 |
1.38e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremaKKDLLSHIALVSQY--------PVL 81
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-------GDIDDPDVAEACHYlghrnamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 frgSVADNIRIGRP--DASDAEVEEAgrMSAVD-SFINETGEGYsrmigemgegLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:PRK13539 89 ---TVAENLEFWAAflGGEELDIAAA--LEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 524688421 159 ATASLDMKSEELIQKEI-EKLASGRTAFIIAH 189
Cdd:PRK13539 154 PTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-217 |
2.31e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV-----REMAKKDLL---SHIALVSQYPVLFRGS 85
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpgHQIARMGVVrtfQHVRLFREMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGR---------PDASDAEVEEAGRMSAVDSFINETgEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK11300 103 VAQHQQLKTglfsgllktPAFRRAESEALDRAATWLERVGLL-EHANRQAGN----LAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 157 DEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEI 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-229 |
3.34e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREM---AKKDLLSHIALVSQYP 79
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VlfrGSVADNIRIGR----PDASDAEVEEAGRMSAVDSFINETG---EGYSRMIGEMgeglSGGQRQRVSLARAFLKNAP 152
Cdd:PRK10419 99 I---SAVNPRKTVREiirePLRHLLSLDKAERLARASEMLRAVDlddSVLDKRPPQL----SGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFI-IAHRFSTI-RMADRILVLEKGSVIADGTHEELMA-SSPLYRELY 228
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLfITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTfSSPAGRVLQ 251
|
.
gi 524688421 229 N 229
Cdd:PRK10419 252 N 252
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-220 |
3.38e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvREMAKKDLlSHIA-------LvsqYPvlfRGS 85
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDR-RRIGylpeergL---YP---KMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIR-IGR---PDASDAEvEEAGRMsaVDSFinETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:COG4152 88 VGEQLVyLARlkgLSKAEAK-RRADEW--LERL--GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 162 SLDMKSEELIQKEIEKLA-SGRTafII--AHRFSTI-RMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTT--VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-219 |
3.78e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ----YPVLfrgSVAD 88
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVAIIYQelhlVPEM---TVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGR-PdasdaeveeaGRMSAVDS--FINETGEgysrMIGEMGEG---------LSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK11288 99 NLYLGQlP----------HKGGIVNRrlLNYEARE----QLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 157 DEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVI------ADGTHEELMA 219
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVatfddmAQVDRDQLVQ 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-205 |
5.05e-16 |
|
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: 72.96 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKvdgidvremakKDLLSHIALVSQYPVLFRGSV 86
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRigRPdasdaeveeagrmsavdsfinetgegysrmigeMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:cd03223 81 REQLI--YP---------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 524688421 167 SEELIQKEIEKLasgRTAFI-IAHRFSTIRMADRILVLEK 205
Cdd:cd03223 126 SEDRLYQLLKEL---GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-215 |
5.33e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFI---NLLcrfyDV-LSGSVKVDG------IDVREMAKKDLLSHIALVSQ-- 77
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLL----ETpDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 --YPVLfrgSVADNIrigrpdaSDAEVEEAGrMSAVDSfINETGEGYSRM-IGEMGEG----LSGGQRQRVSLARAFLKN 150
Cdd:COG4161 92 nlWPHL---TVMENL-------IEAPCKVLG-LSKEQA-REKAMKLLARLrLTDKADRfplhLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 151 APILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHE 215
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSqTGITQVIVTHEVEFARkVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-204 |
9.93e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.98 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFINLLcrfydvlSGSVKVDGIDV-----------------REMAKKDLLSHIALVSQYPVLFRG 84
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIeieldtvsykpqyikadYEGTVRDLLSSITKDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIgrPDASDAEVEEagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLD 164
Cdd:cd03237 98 EIAKPLQI--EQILDREVPE----------------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 524688421 165 MKSEELIQKEIEKLA--SGRTAFIIAHRFSTIRM-ADRILVLE 204
Cdd:cd03237 148 VEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-227 |
1.08e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLFRGSVADNI 90
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 RIGRPDASDAEVEEAgrmsavdsfINETG-EGYSRMIGEMgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEE 169
Cdd:cd03231 95 RFWHADHSDEQVEEA---------LARVGlNGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 170 LIqkeieklasgrtafiiahrfsTIRMADRilvLEKGSVIADGTHEELMASSPLYREL 227
Cdd:cd03231 163 RF---------------------AEAMAGH---CARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-221 |
1.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 1 MCFGYQQDAPV--MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQY 78
Cdd:PRK13642 10 LVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 79 P--VLFRGSVADNIRIGRPDASDAEVEEAGRMS----AVDSFINETGEGYSrmigemgegLSGGQRQRVSLARAFLKNAP 152
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDeallAVNMLDFKTREPAR---------LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEKLASGR--TAFIIAHRFSTIRMADRILVLEKGSVIADGTHEELMASS 221
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-217 |
1.52e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKK-DLLSHIALVSQYP----- 79
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNPdnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 -VLFRGSVA---DNIRIgRPDASDAEVEEAgrMSAVDSFinetgeGYSRMIGEMgegLSGGQRQRVSLARAFLKNAPILV 155
Cdd:PRK13633 100 aTIVEEDVAfgpENLGI-PPEEIRERVDES--LKKVGMY------EYRRHAPHL---LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 156 LDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAHRFSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-220 |
1.80e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPVLF-RGSVAD 88
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGRPDASDAEVEEagRMSAVDSFINETGEGYSRMIGEMgeglSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSE 168
Cdd:PRK11614 100 NLAMGGFFAERDQFQE--RIKWVYELFPRLHERRIQRAGTM----SGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524688421 169 ELIQKEIEKL-ASGRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK11614 174 QQIFDTIEQLrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-214 |
1.95e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFY--DVLSGSVKVDGIDVREMAKKDL-LSHIALVSQYPVLFRG-SVADN 89
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGRpdasdaEVEEAGRMSavdsfINETGEGYSRMIGEMG---------EGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK13549 103 IFLGN------EITPGGIMD-----YDAMYLRAQKLLAQLKldinpatpvGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 161 ASLDMKSEELIQKEIEKLASGRTAFI-IAHRFSTI-RMADRIlvlekgSVIADGTH 214
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIyISHKLNEVkAISDTI------CVIRDGRH 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-203 |
3.65e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 4 GYQQDA-PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVLF 82
Cdd:PRK10247 14 GYLAGDaKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADN------IRIGRPDaSDAEVEEAGRMSAVDSFINETgegysrmIGEmgegLSGGQRQRVSLAR--AFLKNapIL 154
Cdd:PRK10247 94 GDTVYDNlifpwqIRNQQPD-PAIFLDDLERFALPDTILTKN-------IAE----LSGGEKQRISLIRnlQFMPK--VL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLASGRTAFII--AHRFSTIRMADRILVL 203
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITL 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-217 |
4.22e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 15 IDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLL---SHIALVSQYPVLF---RGSVAD 88
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrSDIQMIFQDPLASlnpRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NI----RIGRPDASDAEVEEAGR--MSAVDSFINetgegysrMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK15079 120 IIaeplRTYHPKLSRQEVKDRVKamMLKVGLLPN--------LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 163 LDMKseelIQ-------KEIEKlASGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:PRK15079 192 LDVS----IQaqvvnllQQLQR-EMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-206 |
4.51e-15 |
|
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: 69.78 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVdGIDVRemakkdllshIALVSQypvlfrgsva 87
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 dnirigrpdasdaeveeagrmsavdsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:cd03221 71 ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 524688421 168 EELIQKEIEKLAsgRTAFIIAHRFSTI-RMADRILVLEKG 206
Cdd:cd03221 106 IEALEEALKEYP--GTVILVSHDRYFLdQVATKIIELEDG 143
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-231 |
6.75e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVlSGSVKVDGIDVREMAKKDLL---SHIALVSQYP-------- 79
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 -VLfrGSVADNIRIGRPDASDAEVEEAgrmsaVDSFINETG---EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILV 155
Cdd:PRK15134 380 nVL--QIIEEGLRVHQPTLSAAQREQQ-----VIAVMEEVGldpETRHRYPAE----FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 156 LDEATASLDmkseELIQKEIEKLASG-----RTAFI-IAHRFSTIR-MADRILVLEKGSVIADGTHEELMASSplyRELY 228
Cdd:PRK15134 449 LDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLfISHDLHVVRaLCHQVIVLRQGEVVEQGDCERVFAAP---QQEY 521
|
...
gi 524688421 229 NKQ 231
Cdd:PRK15134 522 TRQ 524
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-223 |
7.26e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.96 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGiDVREMAKKDLLS---HIALVSQYP 79
Cdd:PRK13638 9 FRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLAlrqQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 --VLFRGSVADNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMigemgEGLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:PRK13638 87 eqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 158 EATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMASSPL 223
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-220 |
8.24e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 71.79 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVmKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVlf 82
Cdd:COG4167 21 FRRQQFEAV-KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPN-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 rGSVADNIRIGR----P-----DASDAEVEEAgrmsavdsfINETgegySRMIGEMGEG-------LSGGQRQRVSLARA 146
Cdd:COG4167 98 -TSLNPRLNIGQileePlrlntDLTAEEREER---------IFAT----LRLVGLLPEHanfyphmLSSGQKQRVALARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 147 FLKNAPILVLDEATASLDM--KSE--ELIQKEIEKLAsgrTAFI-IAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4167 164 LILQPKIIIADEALAALDMsvRSQiiNLMLELQEKLG---ISYIyVSQHLGIVKhISDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-171 |
1.11e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.08 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKdLLSHIALVSQYPVL-FRGSVAD 88
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGLkPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGRPDASDAE--VEEAgrMSAVDSfinetgEGYSRMIGEMgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:TIGR01189 93 NLHFWAAIHGGAQrtIEDA--LAAVGL------TGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
....*
gi 524688421 167 SEELI 171
Cdd:TIGR01189 162 GVALL 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-204 |
1.50e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.51 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFINLLcrfydvlSGSVKVDGIDVREMAKkdllshIALVSQYPvlfrgsvadnirigRPDaSDAE 101
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDEDLK------ISYKPQYI--------------SPD-YDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 102 VEEAGRMSAVDSFinETGEGYSRMIGEMG---------EGLSGGQRQRVSLARAFLKNAPILVLDEATASLDmkSEELIQ 172
Cdd:COG1245 418 VEEFLRSANTDDF--GSSYYKTEIIKPLGleklldknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLA 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 524688421 173 --KEIEKLA--SGRTAFIIAHRFSTIRM-ADRILVLE 204
Cdd:COG1245 494 vaKAIRRFAenRGKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-220 |
1.50e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKD-------------LLSHIALVSQ 77
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 YPVLFRG-SVADNIRIGRPDASDAEVEEAgRMSAVdSFINETGEGySRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLGLSKQEA-RERAV-KYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 157 DEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEELMAS 220
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-206 |
1.57e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYD---VLSGSVKVDGIDVRE--------MAKKDLlsHIALVSqyp 79
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSsfqrsigyVQQQDL--HLPTST--- 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 vlFRGSVADNIRIGRPdasdAEVEEAGRMSAVDSFINETG-EGYSR-MIGEMGEGLSGGQRQRVSLARAFLKNAPILV-L 156
Cdd:TIGR00956 853 --VRESLRFSAYLRQP----KSVSKSEKMEYVEEVIKLLEmESYADaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524688421 157 DEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIRMA--DRILVLEKG 206
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-206 |
1.97e-14 |
|
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: 69.19 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYD--VLSGSVKVDGIDVremaKKDLLSHIALVSQYPVLFR 83
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPL----DKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVadnirigrpdasdaeVEEAGRMSAvdsfinetgegYSRmigemgeGLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:cd03232 93 NLT---------------VREALRFSA-----------LLR-------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524688421 164 DMKSEELIQKEIEKLA-SGRTAFIIAHRFS--TIRMADRILVLEKG 206
Cdd:cd03232 140 DSQAAYNIVRFLKKLAdSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-209 |
3.35e-14 |
|
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: 68.83 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 9 APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLC---RFYDVLSGSVKVDGIDVREMAKKdllshialvsqypvlFRGS 85
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnrtEGNVSVEGDIHYNGIPYKEFAEK---------------YPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNiriGRPDASDAE--VEEAGRMSAvdsfinetgegysRMIG-EMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:cd03233 85 IIYV---SEEDVHFPTltVRETLDFAL-------------RCKGnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 163 LD-MKSEELIQKeIEKLA--SGRTAFIIAHRFS--TIRMADRILVLEKGSVI 209
Cdd:cd03233 149 LDsSTALEILKC-IRTMAdvLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-220 |
3.82e-14 |
|
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: 70.98 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 15 IDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALV-SQYpVLFrgsvaDNIRIG 93
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVfSDF-HLF-----DRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 94 RPDASDAEVE--------------EAGRMSAVDsfinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDEA 159
Cdd:COG4615 425 DGEADPARARellerleldhkvsvEDGRFSTTD--------------------LSQGQRKRLALLVALLEDRPILVFDEW 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 160 TASLD-----MKSEELIQkeieKL-ASGRTAFIIAH--R-FStirMADRILVLEKGSVIADGTHEELMAS 220
Cdd:COG4615 485 AADQDpefrrVFYTELLP----ELkARGKTVIAISHddRyFD---LADRVLKMDYGKLVELTGPAALAAS 547
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-215 |
4.10e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFI---NLL-----------CRFYDVlsgSVKVDGIDVREMAKKdllshIALVSQ-- 77
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLrvlNLLemprsgtlniaGNHFDF---SKTPSDKAIRELRRN-----VGMVFQqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 --YPVLfrgSVADNIrigrpdasdaeVEEAGRMSAVD--SFINETGEGYSRM-IGEMGEG----LSGGQRQRVSLARAFL 148
Cdd:PRK11124 92 nlWPHL---TVQQNL-----------IEAPCRVLGLSkdQALARAEKLLERLrLKPYADRfplhLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHE 215
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAeTGITQVIVTHEVEVARkTASRVVYMENGHIVEQGDAS 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-212 |
5.68e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ-YPVLFRGSVADN 89
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQeLSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGRpdasdAEVEEAGRMSAVD-SFINETGE------GYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK09700 101 LYIGR-----HLTKKVCGVNIIDwREMRVRAAmmllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524688421 163 LDMKSEELIQKEIEKLASGRTAFI-IAHRFSTIR-MADRILVLEKGSVIADG 212
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRrICDRYTVMKDGSSVCSG 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-217 |
6.45e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 5 YQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDllSHIALVSQ----YPV 80
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQnyalYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LfrgSVADN------IRiGRPDAS-DAEVEEAGRMSAVDSFINetgegysRMIGEmgegLSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK11650 91 M---SVRENmayglkIR-GMPKAEiEERVAEAARILELEPLLD-------RKPRE----LSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKL--ASGRTAFIIAH-RFSTIRMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLhrRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-214 |
6.60e-14 |
|
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: 70.62 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFY--DVLSGSVKVDGIDVREMAKKDL-LSHIALVSQYPVLFRG 84
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -SVADNIRIGRpdasdaEVEEAGRMSAVDSFINETGE----------GYSRMIGEMGeglsGGQRQRVSLARAFLKNAPI 153
Cdd:TIGR02633 93 lSVAENIFLGN------EITLPGGRMAYNAMYLRAKNllrelqldadNVTRPVGDYG----GGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMadrilVLEKGSVIADGTH 214
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKA-----VCDTICVIRDGQH 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-219 |
9.06e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLC-RFY-DVLSGSVKVDGidvREMAKKdLLSHIALVSQ----YPV 80
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQ-ILKRTGFVTQddilYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 L-FRGSVADNIRIGRPDASDAEVeeagRMSAVDSFINETG--EGYSRMIGE-MGEGLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PLN03211 155 LtVRETLVFCSLLRLPKSLTKQE----KILVAESVISELGltKCENTIIGNsFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 157 DEATASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFST--IRMADRILVLEKGSVIADGTHEELMA 219
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-205 |
9.49e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVRemaKKDLLSHIALVSQYPVLFRG- 84
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRI-----GR-----PDASDAEVEEAGRmsaVDSFINEtgegysrmigemgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:PRK13543 98 STLENLHFlcglhGRrakqmPGSALAIVGLAGY---EDTLVRQ---------------LSAGQKKRLALARLWLSPAPLW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524688421 155 VLDEATASLDMKSEELIQKEIE-KLASGRTAFIIAH-RFSTIRMADRILVLEK 205
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTHgAYAAPPVRTRMLTLEA 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-217 |
1.02e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSV----------KVDGIDVREMAK--------------K 66
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKlviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 67 DLLSHIALVSQYP--VLFRGSVADNIRIGrPDASDAEVEEAGRMSAvdsfinetgeGYSRMIGEMGE-------GLSGGQ 137
Cdd:PRK13651 102 EIRRRVGVVFQFAeyQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAA----------KYIELVGLDESylqrspfELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 138 RQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRF-STIRMADRILVLEKGSVIADG-TH 214
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTY 250
|
...
gi 524688421 215 EEL 217
Cdd:PRK13651 251 DIL 253
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-215 |
1.39e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRF--YDVLSGSVKVDGIDVREMaKKDLLSH--IALVSQYPVLFR 83
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDL-EPEERAHlgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 G-SVADNIRI---------GRPDASDAEVEE--AGRMSAVD---SFINETgegysrmigeMGEGLSGGQRQRVSLARAFL 148
Cdd:CHL00131 98 GvSNADFLRLaynskrkfqGLPELDPLEFLEiiNEKLKLVGmdpSFLSRN----------VNEGFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIAH--RFSTIRMADRILVLEKGSVIADGTHE 215
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-219 |
1.43e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.84 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 21 AGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVRE---MAKKDLLSHIALVSQYPVlfrGSVADNIRIGR--- 94
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY---GSLNPRKKVGQile 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 95 -PDASDAEVEEAGRMSAVDSFINETG---EGYSR---MigemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKs 167
Cdd:PRK11308 117 ePLLINTSLSAAERREKALAMMAKVGlrpEHYDRyphM-------FSGGQRQRIAIARALMLDPDVVVADEPVSALDVS- 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 168 eelIQKEIEKL-----ASGRTAFI-IAHRFSTIR-MADRILVLEKGSVIADGTHEELMA 219
Cdd:PRK11308 189 ---VQAQVLNLmmdlqQELGLSYVfISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-204 |
1.99e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 19 IPAGQVVALVGPSGAGKTTFINLLcrfydvlSGSVKVDGidvremakkdllshialvsqypvlfrGSVADNIRIG----- 93
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDE--------------------------GEVDPELKISykpqy 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 94 -RPDaSDAEVEEAGRMSAVD---SFINE---TGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:PRK13409 409 iKPD-YDGTVEDLLRSITDDlgsSYYKSeiiKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 524688421 167 SEELIQKEIEKLA--SGRTAFIIAHRFSTIRM-ADRILVLE 204
Cdd:PRK13409 488 QRLAVAKAIRRIAeeREATALVVDHDIYMIDYiSDRLMVFE 528
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-219 |
2.59e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 9 APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVS----QYPVLFR 83
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 GSVADNIRIgrpdASDAEVEEAGRMS------AVDSFINETG---EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:COG1129 345 LSIRENITL----ASLDRLSRGGLLDrrreraLAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 155 VLDEATASLDM--KSEelIQKEIEKLASGRTAFIIAhrfST-----IRMADRILVLEKGSVIA-----DGTHEELMA 219
Cdd:COG1129 417 ILDEPTRGIDVgaKAE--IYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIVGeldreEATEEAIMA 488
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-209 |
2.89e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDgidvremakkdllshialVSQYPVLFRGSVADN 89
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 irIGRPDASDAEVEEAGRMSAVDSFInetgegYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEE 169
Cdd:COG2401 106 --IGRKGDFKDAVELLNAVGLSDAVL------WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 524688421 170 LIQKEIEKLA--SGRTAFIIAHRFSTIR--MADRILVLEKGSVI 209
Cdd:COG2401 174 RVARNLQKLArrAGITLVVATHHYDVIDdlQPDLLIFVGYGGVP 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-219 |
1.20e-12 |
|
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: 66.75 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKV-----------DGIDVREMAKKdllsHIALVSQYPVLF 82
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRAKR----YIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 -RGSVADN----IRIGRPDasdaeveEAGRMSAVDSF--INETGEGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILV 155
Cdd:TIGR03269 378 pHRTVLDNlteaIGLELPD-------ELARMKAVITLkmVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 156 LDEATASLD----MKSEELIQKEIEKLasGRTAFIIAHRFSTIRM-ADRILVLEKGSVIADGTHEELMA 219
Cdd:TIGR03269 451 LDEPTGTMDpitkVDVTHSILKAREEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-204 |
1.49e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVdGIDVremakkdllsHIALVSQypvlFRGSVA 87
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQ----SRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DN-------------IRIGRpdasdaeVEEAGRmSAVDSFiNETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPIL 154
Cdd:TIGR03719 399 PNktvweeisggldiIKLGK-------REIPSR-AYVGRF-NFKGSDQQKKVGQ----LSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 155 VLDEATASLDMKSEELIQKEIEKLASgrTAFIIAH-RFSTIRMADRILVLE 204
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdRWFLDRIATHILAFE 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-217 |
1.53e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDG----------IDVREMAKKDLL----SH 71
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 72 IALVSQYPVLFRGSV-------ADNIRIGRPDASDAEVEEAGRMsaVDSF-INETGEGYSRMIGEmgegLSGGQRQRVSL 143
Cdd:PRK10261 106 MAMIFQEPMTSLNPVftvgeqiAESIRLHQGASREEAMVEAKRM--LDQVrIPEAQTILSRYPHQ----LSGGMRQRVMI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 144 ARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLASGRT--AFIIAHRFSTI-RMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-220 |
1.55e-12 |
|
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: 66.25 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKT----TFINLLCRFYDVLSGSVKVDGIDVREMAKKDLL----SHIALVSQ 77
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 YPV-----LFRgsVADNI--------RIGRPDASDAEVE--------EAGRMsaVDSFINEtgegysrmigemgegLSGG 136
Cdd:COG4172 100 EPMtslnpLHT--IGKQIaevlrlhrGLSGAAARARALEllervgipDPERR--LDAYPHQ---------------LSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 137 QRQRVSLARAfLKNAP-ILVLDEATASLDMkseeLIQKEIEKL------ASGRTAFIIAHRFSTIR-MADRILVLEKGSV 208
Cdd:COG4172 161 QRQRVMIAMA-LANEPdLLIADEPTTALDV----TVQAQILDLlkdlqrELGMALLLITHDLGVVRrFADRVAVMRQGEI 235
|
250
....*....|..
gi 524688421 209 IADGTHEELMAS 220
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-204 |
3.43e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 1 MCFGYQQ---DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREM---AKKDLLSH-IA 73
Cdd:PRK11629 11 LCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNQkLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 74 LVSQYPVLFRG-----SVADNIRIGRPDASDAEVEEAGRMSAVdsfinetgeGYSRMIGEMGEGLSGGQRQRVSLARAfL 148
Cdd:PRK11629 91 FIYQFHHLLPDftaleNVAMPLLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVAIARA-L 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 149 KNAPILVL-DEATASLDMKSEELIQKEIEKL-ASGRTAFII-------AHRFS-TIRMADRILVLE 204
Cdd:PRK11629 161 VNNPRLVLaDEPTGNLDARNADSIFQLLGELnRLQGTAFLVvthdlqlAKRMSrQLEMRDGRLTAE 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
12-213 |
4.69e-12 |
|
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: 63.79 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLcrFYDVLSGSVKVDGIDVREMAKKDLLSHI---ALVSQYPVlfrG---- 84
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDT--LYPALARRLHLKKEQPGNHDRIEGLEHIdkvIVIDQSPI---Grtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -------SVADNIRI-------GR----------------PDASDAEVEEAgrmsaVDSFIN------------ETGEGY 122
Cdd:cd03271 86 snpatytGVFDEIRElfcevckGKrynretlevrykgksiADVLDMTVEEA-----LEFFENipkiarklqtlcDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 123 SRmIGEMGEGLSGGQRQRVSLARAFLKNAP---ILVLDEATASLDMkseELIQKEIEKLAS----GRTAFIIAHRFSTIR 195
Cdd:cd03271 161 IK-LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHF---HDVKKLLEVLQRlvdkGNTVVVIEHNLDVIK 236
|
250 260
....*....|....*....|....
gi 524688421 196 MADRILVL------EKGSVIADGT 213
Cdd:cd03271 237 CADWIIDLgpeggdGGGQVVASGT 260
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
22-206 |
5.56e-12 |
|
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: 61.62 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIalvsqypvlfrgsvadnirigrpdasdae 101
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLI----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 102 veeagrmsavdsfinetgegysrMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIE----- 176
Cdd:smart00382 53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 524688421 177 --KLASGRTAFIIAHRFS------TIRMADRILVLEKG 206
Cdd:smart00382 110 llKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLI 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-206 |
6.11e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 2 CFGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSHIALVSQYPVL 81
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRgsvadniRIGRPDASDAEVEeagrmsAVDSFINETgegysrmigEMGEG------------LSGGQRQRVSLARAFLK 149
Cdd:PRK10522 409 FD-------QLLGPEGKPANPA------LVEKWLERL---------KMAHKleledgrisnlkLSKGQKKRLALLLALAE 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 150 NAPILVLDEATASLD-MKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRILVLEKG 206
Cdd:PRK10522 467 ERDILLLDEWAADQDpHFRREFYQVLLPLLqEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-198 |
6.56e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVremaKKDLLSHialvsQYPVLF 82
Cdd:PRK13540 9 FDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTY-----QKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RG---------SVADNIRIGRPDASDA-EVEEAGRMSAVDSFINetgegYSRMIgemgegLSGGQRQRVSLARAFLKNAP 152
Cdd:PRK13540 79 VGhrsginpylTLRENCLYDIHFSPGAvGITELCRLFSLEHLID-----YPCGL------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 524688421 153 ILVLDEATASLDMKSEELIQKEIEK-LASGRTAFIIAHRFSTIRMAD 198
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-227 |
1.13e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKK---DLL--SHIALVsqYPVLfrgSVAD 88
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLylGHQPGI--KTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 89 NIRIGRPDASDAEVEE----------AGRMSAVDSFinetgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:PRK13538 94 NLRFYQRLHGPGDDEAlwealaqvglAGFEDVPVRQ------------------LSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 159 ATASLDMKSEELIqkeieklasgrTAFIIAHrfstirmadrilvLEKGSVIADGTHEELMASSPLYREL 227
Cdd:PRK13538 156 PFTAIDKQGVARL-----------EALLAQH-------------AEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
12-207 |
1.66e-11 |
|
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: 60.80 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINllcrfydvlsgsvkvDGIdvREMAKKDLLSHIALVSQYPVLFRGSVadnir 91
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGL--YASGKARLISFLPKFSRNKLIFIDQL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 igrpdasdaeveeagrmsavdSFINETGEGYSRMIGEMGEgLSGGQRQRVSLARAFLKNAP--ILVLDEATASLDMKSEE 169
Cdd:cd03238 69 ---------------------QFLIDVGLGYLTLGQKLST-LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 524688421 170 LIQKEIEKLAS-GRTAFIIAHRFSTIRMADRILVLEKGS 207
Cdd:cd03238 127 QLLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-225 |
1.69e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFY--DVLSGSVKVDG---IDVREMAKKDLLSHIALVSQYPVL---- 81
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARVTGdvtLNGEPLAAIDAPRLARLRAVLPQAaqpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 FRGSVADNIRIGR-PDAsdaevEEAGRMSAVDSFINETG---EGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAP----- 152
Cdd:PRK13547 96 FAFSAREIVLLGRyPHA-----RRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 153 ----ILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFS-TIRMADRILVLEKGSVIADGTHEELMASSPLYR 225
Cdd:PRK13547 171 qpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLTPAHIAR 250
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-210 |
2.40e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPVLFRG-SVADNIR 91
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQrSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 IGRPDASDAEVEEagrmsavDSFINETGEGYSRM-----IGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:PRK10982 96 LGRYPTKGMFVDQ-------DKMYRDTKAIFDELdididPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524688421 167 SEELIQKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIA 210
Cdd:PRK10982 169 EVNHLFTIIRKLkERGCGIVYISHKMEEIfQLCDEITILRDGQWIA 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-206 |
4.51e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKD---LLSHIALVSQ-YPVLFRGSVA 87
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQdHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 88 DNIRIGRPDASDAEVEEAGRMSAVDSFINETGEGYSRMIGemgegLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 524688421 168 EELIQKEIEKLAS-GRTAFIIAHRFSTI-RMADRILVLEKG 206
Cdd:PRK10908 173 SEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDG 213
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-214 |
5.43e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 7 QDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLC--RFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQYPV--- 80
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 -----LFRGSVADNIRIGRpdasdaEVEEAGRMSAVDsFINETGEGYSR----MIGEMGEGLSGGQRQRVSLARAFLKNA 151
Cdd:PRK09580 92 gvsnqFFLQTALNAVRSYR------GQEPLDRFDFQD-LMEEKIALLKMpedlLTRSVNVGFSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 152 PILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIR---MADRILVLEKGSVIADGTH 214
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILdyiKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-171 |
7.09e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREM---AKKDLLS-HIALVSQ----YPVLf 82
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAkHVGFVFQsfmlIPTL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 rgSVADNIRIgrPDASDAEVEEAGRMSAVDsFINETGEGysRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK10584 104 --NALENVEL--PALLRGESSRQSRNGAKA-LLEQLGLG--KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
....*....
gi 524688421 163 LDMKSEELI 171
Cdd:PRK10584 177 LDRQTGDKI 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-221 |
1.19e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLS---HIALVSQYPVLFRG 84
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 -SVADNirIGRPDASDAEVEEAGRMSAVDSFINETG-EGYSRMigeMGEGLSGGQRQRVSLARAFLKNAPILVLDEATAS 162
Cdd:PRK11831 99 mNVFDN--VAYPLREHTQLPAPLLHSTVMMKLEAVGlRGAAKL---MPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524688421 163 LDMKSEELIQKEIEKL--ASGRTAFIIAHRF-STIRMADRILVLEKGSVIADGTHEELMASS 221
Cdd:PRK11831 174 QDPITMGVLVKLISELnsALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-241 |
1.29e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKT----TFINLLCRFYDVLSGSVKVDGIDVremAKKDLLS-HIALVSQYPv 80
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGrKIATIMQNP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 lfRG------SVADNIR-----IGRPdASDAEVEEAgrMSAVDsfINETGEGYSRMIGEMgeglSGGQRQRVSLARAFLK 149
Cdd:PRK10418 89 --RSafnplhTMHTHARetclaLGKP-ADDATLTAA--LEAVG--LENAARVLKLYPFEM----SGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 150 NAPILVLDEATASLDMKSEELIQKEIEKLASGRT--AFIIAHRFSTI-RMADRILVLEKGSVIADGTHEELMAS--SPLY 224
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNApkHAVT 237
|
250
....*....|....*..
gi 524688421 225 RELYNKQQMVAEEEGGA 241
Cdd:PRK10418 238 RSLVSAHLALYGMELAS 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-224 |
2.19e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvREMAKKDLL---SHIALVSQYPvlf 82
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGDYSyrsQRIRMIFQDP--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 RGSVADNIRIGR----PDASDAEVEEAGRMSAvdsfINETgegySRMIGEMGE-------GLSGGQRQRVSLARAFLKNA 151
Cdd:PRK15112 97 STSLNPRQRISQildfPLRLNTDLEPEQREKQ----IIET----LRQVGLLPDhasyyphMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 152 PILVLDEATASLDMK-SEELIQKEIEKLASGRTAFI--IAHRFSTIRMADRILVLEKGSVIADGTHEELMAsSPLY 224
Cdd:PRK15112 169 KVIIADEALASLDMSmRSQLINLMLELQEKQGISYIyvTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA-SPLH 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-219 |
2.72e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 9 APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDV-----REMAKKDLlSHI-------ALVS 76
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLGV-AYIpedrlgrGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 QYpvlfrgSVADNIRIGRPDasDAEVEEAGRMSAvdSFINETGEgysRMIGEMG----------EGLSGGQRQRVSLARA 146
Cdd:COG3845 350 DM------SVAENLILGRYR--RPPFSRGGFLDR--KAIRAFAE---ELIEEFDvrtpgpdtpaRSLSGGNQQKVILARE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 147 FLKNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIahrFST-----IRMADRILVLEKGSVI-----ADGTHEE 216
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL---ISEdldeiLALSDRIAVMYEGRIVgevpaAEATREE 493
|
....*.
gi 524688421 217 L---MA 219
Cdd:COG3845 494 IgllMA 499
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
12-217 |
2.76e-10 |
|
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: 60.03 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFIN--LLCRFYDVLSGSVKVDGiDVREMAKKDLLSHIALVSQYPV--------- 80
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPG-RYTSIEGLEHLDKVIHIDQSPIgrtprsnpa 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 -----------LF--------RGSVAD----NIRIGR-----------------PDAS---------------------- 98
Cdd:TIGR00630 703 tytgvfdeireLFaetpeakvRGYTPGrfsfNVKGGRceacqgdgvikiemhflPDVYvpcevckgkrynretlevkykg 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 99 -------DAEVEEAGRM-SAVDS------FINETGEGYSRmIGEMGEGLSGGQRQRVSLARAFLKNA---PILVLDEATA 161
Cdd:TIGR00630 783 kniadvlDMTVEEAYEFfEAVPSisrklqTLCDVGLGYIR-LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTT 861
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 162 SLDMkseELIQKEIEKLAS----GRTAFIIAHRFSTIRMADRILVL------EKGSVIADGTHEEL 217
Cdd:TIGR00630 862 GLHF---DDIKKLLEVLQRlvdkGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-209 |
4.23e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLC----RFYDVLSGSVKVDGIDVREMaKKDLLSHIALVSQ----YPVLf 82
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAEtdvhFPHL- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 83 rgSVADNIRIG--------RPDASDAEvEEAGRMSAVDSFINETGEGYSRMIG-EMGEGLSGGQRQRVSLARAFLKNAPI 153
Cdd:TIGR00956 154 --TVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFS--TIRMADRILVLEKGSVI 209
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSqdAYELFDKVIVLYEGYQI 290
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-209 |
4.38e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINllcrfydVLSGSVKVDgiDVREMAKKDLLshIALVSQYPVlfR---G 84
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK-------ILNGEVLLD--DGRIIYEQDLI--VARLQQDPP--RnveG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIG------------------RPDASDAEVEEAGRMSAV---------DSFINETGEgysrMIGEMGEG----L 133
Cdd:PRK11147 82 TVYDFVAEGieeqaeylkryhdishlvETDPSEKNLNELAKLQEQldhhnlwqlENRINEVLA----QLGLDPDAalssL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 134 SGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIeKLASGRTAFiIAHRFSTIR-MADRILVLEKGSVI 209
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQGSIIF-ISHDRSFIRnMATRIVDLDRGKLV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-206 |
9.90e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVM----------KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLsHIALV 75
Cdd:PRK15439 263 AAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRL-ARGLV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 76 ------SQYPVLFRGSVADNI------RIG---RPdasdaeveeaGRMSAVdsfinetGEGYSRMIG-------EMGEGL 133
Cdd:PRK15439 342 ylpedrQSSGLYLDAPLAWNVcalthnRRGfwiKP----------ARENAV-------LERYRRALNikfnhaeQAARTL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 134 SGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFI-IAHRFSTI-RMADRILVLEKG 206
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIeQMADRVLVMHQG 479
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-219 |
1.05e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ------YPVLfrgSV 86
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPrIAYMPQglgknlYPTL---SV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIR-IGRPDASDAEvEEAGRMsavDSFINETG--EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:NF033858 96 FENLDfFGRLFGQDAA-ERRRRI---DELLRATGlaPFADRPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 164 DMKSE----ELiqkeIEKLASGR--------TAFII-AHRFstirmaDRILVLEKGSVIADGTHEELMA 219
Cdd:NF033858 168 DPLSRrqfwEL----IDRIRAERpgmsvlvaTAYMEeAERF------DWLVAMDAGRVLATGTPAELLA 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-172 |
1.37e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDgidvremAKKDllshIALVSQYpvlfRG------SV 86
Cdd:PRK11147 336 KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------TKLE----VAYFDQH----RAeldpekTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 87 ADNIRIGRpdasdAEVEEAGRMSAVDSFINETGEGYSRMIGEMgEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:PRK11147 401 MDNLAEGK-----QEVMVNGRPRHVLGYLQDFLFHPKRAMTPV-KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
....*.
gi 524688421 167 SEELIQ 172
Cdd:PRK11147 475 TLELLE 480
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-209 |
2.36e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLS--GSVKVDGidvREMAKKDLLS---------H--IALVsqyPV 80
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRDsealgiviiHqeLALI---PY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 LfrgSVADNIRIGRpdasdaeveEAGRMSAVDSfiNETGEGYSRMIGEMG---------EGLSGGQRQRVSLARAFLKNA 151
Cdd:NF040905 93 L---SIAENIFLGN---------ERAKRGVIDW--NETNRRARELLAKVGldespdtlvTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 152 PILVLDEATASL-DMKSEELIQKEIEKLASGRTAFIIAHRFSTI-RMADRILVLEKGSVI 209
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTI 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-189 |
2.80e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFINLL--------CRFydvlSGSVKVDGIdVREMAKKDLLSHIALVS----------QY----P 79
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILsgelipnlGDY----EEEPSWDEV-LKRFRGTELQNYFKKLYngeikvvhkpQYvdliP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGSVADNIRigrpdasdaEVEEAGRMsavDSFINETG--EGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:PRK13409 174 KVFKGKVRELLK---------KVDERGKL---DEVVERLGleNILDRDISE----LSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|..
gi 524688421 158 EATASLDMKSEELIQKEIEKLASGRTAFIIAH 189
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-217 |
4.58e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRipAGQVVALVGPSGAGK--TTF--INLLCRfYDVLSGSVKVDGIDVREMAKKDL----LSHIALVSQYPVLfrgS 85
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKsqTAFalMGLLAA-NGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDPMT---S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIG-----------RPDASDAeVEEAGRM-SAVdsfinETGEGYSRMiGEMGEGLSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK09473 110 LNPYMRVGeqlmevlmlhkGMSKAEA-FEESVRMlDAV-----KMPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLASG-RTAFI-IAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAgICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-217 |
5.54e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 21 AGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKD-LLSHIALVSQ----YPVLfrgSVADNIRIGRp 95
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsQEAGIGIIHQelnlIPQL---TIAENIFLGR- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 96 dasdaevEEAGRMSAV---------DSFINETGEGYS--RMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATASL- 163
Cdd:PRK10762 105 -------EFVNRFGRIdwkkmyaeaDKLLARLNLRFSsdKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524688421 164 DMKSEELIqKEIEKL-ASGRTAFIIAHRFSTI-RMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK10762 174 DTETESLF-RVIRELkSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-221 |
5.88e-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: 55.60 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYD-VLSGSVKVDG--IDVREMAKKdLLSHIALVSQ-------YPVLfr 83
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNPAQA-IRAGIAMVPEdrkrhgiVPIL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 84 gSVADNIRIGRPD--ASDAEVEEAGRMSAVDSFINETGEGYSRMIGEMGeGLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:TIGR02633 355 -GVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 162 SLDMKSEELIQKEIEKLASGRTAFII--AHRFSTIRMADRILVLEKGSVIADG-----THEELMASS 221
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVvsSELAEVLGLSDRVLVIGEGKLKGDFvnhalTQEQVLAAA 499
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-189 |
7.19e-09 |
|
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: 55.56 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 18 RIPA---GQVVALVGPSGAGKTTFINllcrfydVLSGSVKVD-GIDVREMAKKDLLSHialvsqypvlFRGS-------- 85
Cdd:COG1245 92 GLPVpkkGKVTGILGPNGIGKSTALK-------ILSGELKPNlGDYDEEPSWDEVLKR----------FRGTelqdyfkk 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADN-IRIGR--------PDASDAEVEE----AGRMSAVDSFINETGEGYS--RMIGEmgegLSGGQRQRVSLARAFLKN 150
Cdd:COG1245 155 LANGeIKVAHkpqyvdliPKVFKGTVREllekVDERGKLDELAEKLGLENIldRDISE----LSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 524688421 151 APILVLDEATASLD----MKSEELIQKEIEKlasGRTAFIIAH 189
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEH 270
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
133-204 |
2.82e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 2.82e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 133 LSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTIR-MADRILVLE 204
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDyLSDRIHVFE 146
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-220 |
3.96e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 1 MCFGYQqDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKvdgidvremakkdllshialvsqypv 80
Cdd:PRK15064 325 LTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-------------------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 81 lfrgsVADNIRIGRPdASDAEVEEAGRMSAVDSFINETGEG---------YSRM------IGEMGEGLSGGQRQRVSLAR 145
Cdd:PRK15064 378 -----WSENANIGYY-AQDHAYDFENDLTLFDWMSQWRQEGddeqavrgtLGRLlfsqddIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688421 146 AFLKNAPILVLDEATASLDMKSEELIQKEIEKLASgrTAFIIAH-RFSTIRMADRIL-VLEKGSVIADGTHEELMAS 220
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdREFVSSLATRIIeITPDGVVDFSGTYEEYLRS 526
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-239 |
4.03e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTtfINLLCRFYDVLSGSVKVDGIDVReMAKKDLL------------SHIA 73
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSILRLLPSPPVVYPSGDIR-FHGESLLhaseqtlrgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 74 LVSQYPV------------------LFRGSvadnirigRPDASDAEV----EEAGRMSAvdsfinetgegySRMIGEMGE 131
Cdd:PRK15134 96 MIFQEPMvslnplhtlekqlyevlsLHRGM--------RREAARGEIlnclDRVGIRQA------------AKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 132 GLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLAS--GRTAFIIAHRFSTIR-MADRILVLEKGSV 208
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRkLADRVAVMQNGRC 235
|
250 260 270
....*....|....*....|....*....|.
gi 524688421 209 IADGTHEELMaSSPLYRelYNKQQMVAEEEG 239
Cdd:PRK15134 236 VEQNRAATLF-SAPTHP--YTQKLLNSEPSG 263
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-201 |
5.57e-08 |
|
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: 50.82 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCrfydvlsgsvkvdgidvremakkdllshIALVSQYPVLFRGSVAdNIR 91
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG----------------------------LALGGAQSATRRRSGV-KAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 IGRPDasdaevEEAGRMSAVDsfinetgegysrmigemgeGLSGGQRQRVSLARAF----LKNAPILVLDEATASLDMKS 167
Cdd:cd03227 62 CIVAA------VSAELIFTRL-------------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....*
gi 524688421 168 EELIQKEIEKLA-SGRTAFIIAHRFSTIRMADRIL 201
Cdd:cd03227 117 GQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-219 |
9.35e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ---YPVLFRG- 84
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISEdrkRDGLVLGm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIgrpDASDAEVEEAGRMS------AVDSFI---NETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILV 155
Cdd:PRK10762 346 SVKENMSL---TALRYFSRAGGSLKhadeqqAVSDFIrlfNIKTPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688421 156 LDEATASLDMKSeeliQKEIEKL-----ASGRTAFIIAHRF-STIRMADRILVLEKGSV-----IADGTHEELMA 219
Cdd:PRK10762 419 LDEPTRGVDVGA----KKEIYQLinqfkAEGLSIILVSSEMpEVLGMSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-204 |
1.82e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLcrfydvlSGSVKVDG--IDVREMAKkdllshIALVSQypvlFRGSVADN 89
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI-------TGQEQPDSgtIKIGETVK------LAYVDQ----SRDALDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 -------------IRIGRpdasdaeVEEAGRmSAVDSFiNETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:PRK11819 403 ktvweeisggldiIKVGN-------REIPSR-AYVGRF-NFKGGDQQKKVGV----LSGGERNRLHLAKTLKQGGNVLLL 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 524688421 157 DEATASLDMKSEELIQKEIEKLASgrTAFIIAH-RFSTIRMADRILVLE 204
Cdd:PRK11819 470 DEPTNDLDVETLRALEEALLEFPG--CAVVISHdRWFLDRIATHILAFE 516
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-165 |
2.17e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQdapVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVD-GIDVREMAKKdllshIALVSQYPVl 81
Cdd:PRK09544 14 FGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYVPQK-----LYLDTTLPL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 82 frgSVADNIRIgRPDASDAEVEEA-GRMSAvdsfinetgegySRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK09544 85 ---TVNRFLRL-RPGTKKEDILPAlKRVQA------------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
....*
gi 524688421 161 ASLDM 165
Cdd:PRK09544 149 QGVDV 153
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
11-195 |
2.64e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.90 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 11 VMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDgidvremAKKDLLshiaLVSQYPVLFRGSVADNI 90
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-------AKGKLF----YVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 91 -------RIGRPDASDAEVEEAGRMSAVDSFINETGeGYSRMIGEMGEgLSGGQRQRVSLARAFLKNAPILVLDEATASL 163
Cdd:TIGR00954 536 iypdsseDMKRRGLSDKDLEQILDNVQLTHILEREG-GWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180 190
....*....|....*....|....*....|..
gi 524688421 164 DMKSEELIQKEIEKLasGRTAFIIAHRFSTIR 195
Cdd:TIGR00954 614 SVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-203 |
4.03e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFINLL--------CRFY------DVLS---GS------VKVDGIDVREMAKKDLLSHIalvsqy 78
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILagklkpnlGKFDdppdwdEILDefrGSelqnyfTKLLEGDVKVIVKPQYVDLI------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 79 PVLFRGSVADNI-RIGRPDASDAEVEEAGRMSAVDSFINEtgegysrmigemgegLSGGQRQRVSLARAFLKNAPILVLD 157
Cdd:cd03236 100 PKAVKGKVGELLkKKDERGKLDELVDQLELRHVLDRNIDQ---------------LSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524688421 158 EATASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFSTIRM-ADRILVL 203
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-217 |
5.55e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.01 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 9 APVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvremakKDLLSHIALVSQ---YPVLFrgS 85
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------KSILTNISDVHQnmgYCPQF--D 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPD---------ASDAEVEEAGRMSaVDSFinetgeGYSRMIGEMGEGLSGGQRQRVSLARAFLKNAPILVL 156
Cdd:TIGR01257 2022 AIDDLLTGREHlylyarlrgVPAEEIEKVANWS-IQSL------GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 157 DEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIR-MADRILVLEKGSVIADGTHEEL 217
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEaLCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
127-217 |
7.36e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 127 GEMGEGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRF--STIRMADRILVLE 204
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
90
....*....|...
gi 524688421 205 KGSVIADGTHEEL 217
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
133-217 |
9.47e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFI-IAHRFSTIR-MADRILVLEKGSVIA 210
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIvISSELPEVLgLSDRVLVMHEGKLKG 485
|
....*..
gi 524688421 211 DGTHEEL 217
Cdd:PRK13549 486 DLINHNL 492
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
13-201 |
1.18e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 47.46 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGqVVALVGPSGAGKTTFINLLcRFydVL-SGSVKvdgiDVREMAKKDllshialvsqypVLFRGSVadnir 91
Cdd:cd03278 14 DKTTIPFPPG-LTAIVGPNGSGKSNIIDAI-RW--VLgEQSAK----SLRGEKMSD------------VIFAGSE----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 iGRPDASDAEVE-----EAGRMS-----AVDSFINETGEGYSRMigemgEGLSGGQRQRVSLARAF----LKNAPILVLD 157
Cdd:cd03278 69 -TRKPANFAEVTltfdnSDGRYSiisqgDVSEIIEAPGKKVQRL-----SLLSGGEKALTALALLFaifrVRPSPFCVLD 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 524688421 158 EATASLDMKSEELIQKEIEKLaSGRTAFI-IAHRFSTIRMADRIL 201
Cdd:cd03278 143 EVDAALDDANVERFARLLKEF-SKETQFIvITHRKGTMEAADRLY 186
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-218 |
1.51e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 6 QQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTF-INLLCRFYDV-LSGSVKVDGIDVREMAKKDLLSH-IALVS----QY 78
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAgLAYVTedrkGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 79 PVLFRGSVADNIRIgrpdASDAEVEEAGrmsavdsFINET-----GEGY-SRM------IGEMGEGLSGGQRQRVSLARA 146
Cdd:NF040905 350 GLNLIDDIKRNITL----ANLGKVSRRG-------VIDENeeikvAEEYrKKMniktpsVFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 147 FLKNAPILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIahrfST-----IRMADRILVLEKGSV-----IADGTHE 215
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVI----SSelpelLGMCDRIYVMNEGRItgelpREEASQE 494
|
...
gi 524688421 216 ELM 218
Cdd:NF040905 495 RIM 497
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-212 |
1.97e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDG-----IDVREM--AKKDLL--SHIALVSQYPVL-FRGSVADNIR 91
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALseAERRRLlrTEWGFVHQHPRDgLRMQVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 92 IG--------------RPDASD--AEVE-EAGRmsavdsfinetgegysrmIGEMGEGLSGGQRQRVSLARAfLKNAPIL 154
Cdd:PRK11701 112 IGerlmavgarhygdiRATAGDwlERVEiDAAR------------------IDDLPTTFSGGMQQRLQIARN-LVTHPRL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688421 155 VL-DEATASLDMKSE----ELIQKEIEKLasGRTAFIIAHRFSTIRM-ADRILVLEKGSVIADG 212
Cdd:PRK11701 173 VFmDEPTGGLDVSVQarllDLLRGLVREL--GLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-212 |
4.01e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDG--IDVREMAK-KDLLSHIALVSQYPVLF---RGS 85
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKlQALRRDIQFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNI----RIGRPDASDAEveeAGRMSAVDSFINETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEATA 161
Cdd:PRK10261 420 VGDSImeplRVHGLLPGKAA---AARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 162 SLDMKSEELI-------QKEIeklasGRTAFIIAHRFSTI-RMADRILVLEKGSVIADG 212
Cdd:PRK10261 493 ALDVSIRGQIinllldlQRDF-----GIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
127-201 |
4.19e-06 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 45.76 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 127 GEMGEGLSGGQRQRVSLARAF----LKNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFI-IAHRFSTIRMADRIL 201
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIvITLKKEMFENADKLI 168
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-213 |
5.87e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTFInllcrfyDVLSGSvKVDGI---DVREMAKKDLLSHIALVSQY---------PVLFRGSVADN 89
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLM-------DVLAGR-KTGGYiegDIRISGFPKKQETFARISGYceqndihspQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 90 IRIGRPdasdAEVEEAGRMSAVDSFIN--ETGEGYSRMIGEMG-EGLSGGQRQRVSLARAFLKNAPILVLDEATASLDMK 166
Cdd:PLN03140 978 AFLRLP----KEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524688421 167 SEELIQKEIEK-LASGRTAFIIAHRFS--TIRMADRILVLEK-GSVIADGT 213
Cdd:PLN03140 1054 AAAIVMRTVRNtVDTGRTVVCTIHQPSidIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-219 |
6.24e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ-------YPVLfrg 84
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITEsrrdngfFPNF--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 85 SVADNIRIGRP--------------DASDAEVEEAGR--MSAVDSFINETgegysrmIGEmgegLSGGQRQRVSLARAFL 148
Cdd:PRK09700 357 SIAQNMAISRSlkdggykgamglfhEVDEQRTAENQRelLALKCHSVNQN-------ITE----LSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTI-RMADRILVLEKGSV------IADGTHEELMA 219
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIiTVCDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-224 |
2.51e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 10 PVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGidvREMAKKDLLSHI----ALV---------- 75
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAInhgfALVteerrstgiy 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 76 SQYPVLFRgSVADNIR--IGRPDASDAEVEEAGRMSAVDSFINETgEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPI 153
Cdd:PRK10982 339 AYLDIGFN-SLISNIRnyKNKVGLLDNSRMKSDTQWVIDSMRVKT-PGHRTQIGS----LSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLASGRTAFII--AHRFSTIRMADRILVLEKGSV-----IADGTHEELMASSPLY 224
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIisSEMPELLGITDRILVMSNGLVagivdTKTTTQNEILRLASLH 490
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
24-205 |
3.55e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 24 VVALVGPSGAGKTTFInlLCRFYdVLSGSV---KVDGIDVREMA-KKDLLSHIALVsqypvlFRGSVADNIRIGRpdasd 99
Cdd:cd03240 24 LTLIVGQNGAGKTTII--EALKY-ALTGELppnSKGGAHDPKLIrEGEVRAQVKLA------FENANGKKYTITR----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 100 aeveeagRMSAVDSFINETGEGYSRMIGEMGEGLSGGQRQ------RVSLARAFLKNAPILVLDEATASLDmksEELIQK 173
Cdd:cd03240 90 -------SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 524688421 174 EIEKL------ASGRTAFIIAHRFSTIRMADRILVLEK 205
Cdd:cd03240 160 SLAEIieerksQKNFQLIVITHDEELVDAADHIYRVEK 197
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
21-43 |
5.32e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.77 E-value: 5.32e-05
10 20
....*....|....*....|...
gi 524688421 21 AGQVVALVGPSGAGKTTFINLLC 43
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALL 106
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-172 |
6.91e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 3 FGYQQDAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLCRFYDVLSGSV--------------KVDGIDVremakkdl 68
Cdd:PLN03073 516 FGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDL-------- 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 69 lshialvSQYPVL-----FRGSVADNIRigrpdasdaeveeagrmSAVDSFinetGEGYSRMIGEMgEGLSGGQRQRVSL 143
Cdd:PLN03073 588 -------SSNPLLymmrcFPGVPEQKLR-----------------AHLGSF----GVTGNLALQPM-YTLSGGQKSRVAF 638
|
170 180 190
....*....|....*....|....*....|
gi 524688421 144 ARAFLKNAPILVLDEATASLDMKS-EELIQ 172
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
133-227 |
8.91e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLARAFLKNAPILVLDEATASLDMKSEELIQKEIEKLAS-GRTAFIIAHRFSTI-RMADRILVLEKGSVIA 210
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsGITLVLVLNRFDEIpDFVQFAGVLADCTLAE 215
|
90
....*....|....*..
gi 524688421 211 DGTHEELMASSpLYREL 227
Cdd:PRK10938 216 TGEREEILQQA-LVAQL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-221 |
1.00e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLAR---AFLKNApILVLDEATASLDMK-SEELIQ--KEIEKLasGRTAFIIAHRFSTIRMADRILVL--- 203
Cdd:TIGR00630 489 LSGGEAQRIRLATqigSGLTGV-LYVLDEPSIGLHQRdNRRLINtlKRLRDL--GNTLIVVEHDEDTIRAADYVIDIgpg 565
|
90 100
....*....|....*....|.
gi 524688421 204 ---EKGSVIADGTHEELMASS 221
Cdd:TIGR00630 566 ageHGGEVVASGTPEEILANP 586
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-194 |
1.06e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 8 DAPVMKNIDIRIPAGQVVALVGPSGAGKTTFINLLC----RFYD---VLSGSVKVDGIDVRemakkDLLSHIALVS---- 76
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYSndlTLFGRRRGSGETIW-----DIKKHIGYVSsslh 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 77 -QYPVlfRGSVADNIRIGRPDA-------SDAEVEEAGRMSAVDSFINETGEGYSRmigemgeGLSGGQRQRVSLARAFL 148
Cdd:PRK10938 347 lDYRV--STSVRNVILSGFFDSigiyqavSDRQQKLAQQWLDILGIDKRTADAPFH-------SLSWGQQRLALIVRALV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 149 KNAPILVLDEATASLDMKSEELIQKEIEKLAS-GRTAFI------------IAHRFSTI 194
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLLfvshhaedapacITHRLEFV 476
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-218 |
1.19e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLARAFL---KNAPILVLDEATASLDMKSeelIQKEIEKLAS----GRTAFIIAHRFSTIRMADRILVL-- 203
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHD---IKALIYVLQSlthqGHTVVIIEHNMHVVKVADYVLELgp 886
|
90
....*....|....*....
gi 524688421 204 ----EKGSVIADGTHEELM 218
Cdd:PRK00635 887 eggnLGGYLLASCSPEELI 905
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-216 |
1.45e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 21 AGQVVALVGPSGAGKTTFINLLCRFYDVLSGSVKVDGIDVREMAKKDLLSH-IALVSQ-------YPVLfrgSVADNIRI 92
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPEdrkaegiIPVH---SVADNINI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 93 G-RPDASDA--------EVEEAgrmsavDSFI---NETGEGYSRMIGEmgegLSGGQRQRVSLARAFLKNAPILVLDEAT 160
Cdd:PRK11288 355 SaRRHHLRAgclinnrwEAENA------DRFIrslNIKTPSREQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 161 ASLDM--KSEelIQKEIEKLASGRTAFIIAhrfST-----IRMADRILVLEKGSVIADGTHEE 216
Cdd:PRK11288 425 RGIDVgaKHE--IYNVIYELAAQGVAVLFV---SSdlpevLGVADRIVVMREGRIAGELAREQ 482
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
14-217 |
1.50e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 14 NIDIRIPAGQVVALVGPSGAGKT----TFINLLCRFYDVLSGSVKVDGIDVREMAKKD----LLSHIALVSQYPVLfrgS 85
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKErrnlVGAEVAMIFQDPMT---S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 86 VADNIRIGRPDASDAEVEEAG-----RMSAVDsFINETG--EGYSRmIGEMGEGLSGGQRQRVSLARAFLKNAPILVLDE 158
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGnkktrRQRAID-LLNQVGipDPASR-LDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688421 159 ATASLDMKSE--------ELIQKEIEKLasgrtaFIIAHRFSTI-RMADRILVLEKGSVIADGTHEEL 217
Cdd:PRK11022 180 PTTALDVTIQaqiielllELQQKENMAL------VLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
13-40 |
2.76e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.76e-04
10 20
....*....|....*....|....*...
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFIN 40
Cdd:PRK00349 626 KNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
133-167 |
2.87e-04 |
|
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: 41.46 E-value: 2.87e-04
10 20 30
....*....|....*....|....*....|....*
gi 524688421 133 LSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
21-43 |
3.26e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.22 E-value: 3.26e-04
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
13-40 |
3.57e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 3.57e-04
10 20
....*....|....*....|....*...
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTTFIN 40
Cdd:COG0178 622 KNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
12-200 |
4.61e-04 |
|
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: 40.32 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTT-------------FINLLCRFYDVLSGSVKVDGIDVREmakkDLLSHIAL---- 74
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrrYVESLSAYARQFLGQMDKPDVDSIE----GLSPAIAIdqkt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 75 VSQYPVLFRGSVAD----------NIRIGRpdasdaeveeagRMSavdsFINETGEGYSRMIGEMGEgLSGGQRQRVSLA 144
Cdd:cd03270 87 TSRNPRSTVGTVTEiydylrllfaRVGIRE------------RLG----FLVDVGLGYLTLSRSAPT-LSGGEAQRIRLA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688421 145 RAFLKN--APILVLDEATASLDMKSEELIQKEIEKL-ASGRTAFIIAHRFSTIRMADRI 200
Cdd:cd03270 150 TQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHV 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
131-220 |
5.54e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 131 EGLSGGQRQRVSLARAFLKNAPILVLDEAT-----ASLDMKSEELIQkeiekLA--SGRTAFIiahrfSTIRM-----AD 198
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTsgvdpVARDMFWRLLIE-----LSreDGVTIFI-----STHFMneaerCD 465
|
90 100
....*....|....*....|..
gi 524688421 199 RILVLEKGSVIADGTHEELMAS 220
Cdd:NF033858 466 RISLMHAGRVLASDTPAALVAA 487
|
|
| TsaE |
pfam02367 |
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ... |
18-44 |
7.92e-04 |
|
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).
Pssm-ID: 460540 Cd Length: 127 Bit Score: 38.18 E-value: 7.92e-04
10 20
....*....|....*....|....*..
gi 524688421 18 RIPAGQVVALVGPSGAGKTTFINLLCR 44
Cdd:pfam02367 17 LLKPGDVILLSGDLGAGKTTFTRGLAR 43
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
133-167 |
1.31e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*
gi 524688421 133 LSGGQRQRVSLARAFLKNAPILVLDEATASLDMKS 167
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
22-50 |
1.79e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.50 E-value: 1.79e-03
10 20
....*....|....*....|....*....
gi 524688421 22 GQVVALVGPSGAGKTTFINLLCRFYDVLS 50
Cdd:COG4639 2 LSLVVLIGLPGSGKSTFARRLFAPTEVVS 30
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-219 |
1.82e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLARAFLKNA---PILVLDEATASLDMkseELIQKEIEKLAS----GRTAFIIAHRFSTIRMADRILVL-- 203
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHF---EDIRKLLEVLHRlvdkGNTVVVIEHNLDVIKTADWIIDLgp 907
|
90 100
....*....|....*....|
gi 524688421 204 EKGS----VIADGTHEELMA 219
Cdd:PRK00349 908 EGGDgggeIVATGTPEEVAK 927
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
133-201 |
2.81e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688421 133 LSGGQRQRVSLARAF----LKNAPILVLDEATASLDMKSEELIQKEIEKLASGRTAFIIAHRFSTIRMADRIL 201
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| TsaE |
COG0802 |
tRNA A37 threonylcarbamoyladenosine biosynthesis protein TsaE [Translation, ribosomal ... |
18-44 |
2.81e-03 |
|
tRNA A37 threonylcarbamoyladenosine biosynthesis protein TsaE [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine biosynthesis protein TsaE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440565 Cd Length: 146 Bit Score: 36.99 E-value: 2.81e-03
10 20
....*....|....*....|....*..
gi 524688421 18 RIPAGQVVALVGPSGAGKTTFINLLCR 44
Cdd:COG0802 17 LLKPGDVILLEGDLGAGKTTFVRGLAR 43
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-221 |
3.31e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLAR---AFLKNApILVLDEATASLDMKSEELIQKEIEKLA-SGRTAFIIAHRFSTIRMADRILVLEKGS- 207
Cdd:PRK00635 477 LSGGEQERTALAKhlgAELIGI-TYILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMISLADRIIDIGPGAg 555
|
90
....*....|....*....
gi 524688421 208 -----VIADGTHEELMASS 221
Cdd:PRK00635 556 ifggeVLFNGSPREFLAKS 574
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-220 |
4.42e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 37.86 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 133 LSGGQRQRVSLARAfLKNAP-ILVLDEATASLDMKSEELIQKEIEKLA--SGRTAFIIAHRFSTI-RMADRILVLEKGSV 208
Cdd:PRK15093 159 LTEGECQKVMIAIA-LANQPrLLIADEPTNAMEPTTQAQIFRLLTRLNqnNNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|..
gi 524688421 209 IADGTHEELMAS 220
Cdd:PRK15093 238 VETAPSKELVTT 249
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
22-43 |
4.65e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 4.65e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
12-40 |
5.31e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.31e-03
10 20
....*....|....*....|....*....
gi 524688421 12 MKNIDIRIPAGQVVALVGPSGAGKTTFIN 40
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLIN 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-201 |
5.66e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 37.73 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 78 YPVLFRGSVADnIRIGRPDasdaEVEEAGrmsaVDSFINETGEGYSRMigemgEGLSGGQRQRVSLARAF----LKNAPI 153
Cdd:TIGR02168 1049 FPKLFGGGEAE-LRLTDPE----DLLEAG----IEIFAQPPGKKNQNL-----SLLSGGEKALTALALLFaifkVKPAPF 1114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 524688421 154 LVLDEATASLDMKSEELIQKEIEKLaSGRTAFI-IAHRFSTIRMADRIL 201
Cdd:TIGR02168 1115 CILDEVDAPLDDANVERFANLLKEF-SKNTQFIvITHNKGTMEVADQLY 1162
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
25-44 |
6.92e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.29 E-value: 6.92e-03
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
22-37 |
8.36e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 36.77 E-value: 8.36e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
13-37 |
9.02e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 36.93 E-value: 9.02e-03
10 20
....*....|....*....|....*
gi 524688421 13 KNIDIRIPAGQVVALVGPSGAGKTT 37
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| CDC3 |
COG5019 |
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ... |
13-73 |
9.23e-03 |
|
Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 227352 [Multi-domain] Cd Length: 373 Bit Score: 36.92 E-value: 9.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524688421 13 KNIDIRIpagqvvALVGPSGAGKTTFINLLCRfyDVLSGSVKVDGIDVrEMAKKDLLSHIA 73
Cdd:COG5019 20 KGIDFTI------MVVGESGLGKTTFINTLFG--TSLVDETEIDDIRA-EGTSPTLEIKIT 71
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
22-55 |
9.47e-03 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 36.23 E-value: 9.47e-03
10 20 30
....*....|....*....|....*....|....
gi 524688421 22 GQVVALVGPSGAGKTTFINLLCRFYdVLSGSVKV 55
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARL-KLKGGKKV 33
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-165 |
9.90e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 36.76 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 22 GQVVALVGPSGAGKTTF--------INLLCRFYDVLSGSVKVDGIDVR--------EMAKKDLLSH-IALVSQ-----YP 79
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFlrymamhaIDGIPKNCQILHVEQEVVGDDTTalqcvlntDIERTQLLEEeAQLVAQqreleFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688421 80 VLFRGSVADNIRIGRPDASDAEVEEA-GRMSAVDSFINETGEG--------YSRMIGEMGEGLSGGQRQRVSLARAFLKN 150
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAVSQRLEEIyKRLELIDAYTAEARAAsilaglsfTPEMQVKATKTFSGGWRMRIALARALFIE 362
|
170
....*....|....*
gi 524688421 151 APILVLDEATASLDM 165
Cdd:PLN03073 363 PDLLLLDEPTNHLDL 377
|
|
| |
