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Conserved domains on  [gi|1169100883|ref|NP_001336757|]
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ATP-binding cassette sub-family B member 6 isoform 2 [Homo sapiens]

Protein Classification

ABC transporter ATP-binding protein/permease( domain architecture ID 12177173)

ABC transporter ATP-binding protein/permease similar to mitochondrial ATP-binding cassette sub-family B member 6, which binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
186-788 0e+00

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: 791.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 186 SAAQQSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLA--WTVTSY 263
Cdd:COG5265     5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVpvGLLLAY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 264 VFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVF 343
Cdd:COG5265    85 GLLRLL------SVLF-GELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 344 NVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAE 423
Cdd:COG5265   158 NILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 424 SYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGT 503
Cdd:COG5265   238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 504 YYRMIQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGK 583
Cdd:COG5265   318 VYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 584 STILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAI 663
Cdd:COG5265   398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 664 MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVV 743
Cdd:COG5265   478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1169100883 744 NADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSED 788
Cdd:COG5265   558 DADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEA 602
MTABC_N pfam16185
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ...
6-209 8.99e-61

Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five transmembrane helices of eukaryotic mitochondrial ABC-transporters.


:

Pssm-ID: 465049  Cd Length: 244  Bit Score: 205.59  E-value: 8.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883   6 NYCEAEGPVGPAWMQDGLSPCFFFTLVPSTRMALGTLALVLALPCRRRErpagADSLSWGAGPRISPYVLQLLLATLQAA 85
Cdd:pfam16185   1 SYCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRKY----GTPMEPKFIPRSRLYVLQLFLALLLPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  86 LPLAGLAGRVGTARGAPLPSYLLLASVLESLAGACGLWLLVVERSQARQRLAMgiwikFRHSPGLLLLWTVAFAAENLAL 165
Cdd:pfam16185  77 LALARFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPT-----RGHGLVLLLFWTLAFVAENLAF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 166 VSWNSPQWWWARADLGQQV-------------------------------------------------RSAAQQSTWRDF 196
Cdd:pfam16185 152 VSWNSPDWWWGLETLSDQVefglfvvryvctlllfvlglkapglprkpymllinederdvessqpllgDSEENGSTWRNF 231
                         250
                  ....*....|...
gi 1169100883 197 GRKLRLLSGYLWP 209
Cdd:pfam16185 232 GKKLRLLWPYLWP 244
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
186-788 0e+00

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: 791.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 186 SAAQQSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLA--WTVTSY 263
Cdd:COG5265     5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVpvGLLLAY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 264 VFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVF 343
Cdd:COG5265    85 GLLRLL------SVLF-GELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 344 NVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAE 423
Cdd:COG5265   158 NILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 424 SYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGT 503
Cdd:COG5265   238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 504 YYRMIQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGK 583
Cdd:COG5265   318 VYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 584 STILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAI 663
Cdd:COG5265   398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 664 MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVV 743
Cdd:COG5265   478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1169100883 744 NADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSED 788
Cdd:COG5265   558 DADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEA 602
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
222-518 0e+00

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 527.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEK---APWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18581     1 CLLLLAAGRVVNVLVPILYKKIVDSLTPDsadSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd18581    81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLV 458
Cdd:cd18581   161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 459 IGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18581   241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
207-782 2.30e-114

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: 358.65  E-value: 2.30e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 207 LWPRGSPALQLVVLICLGlMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQG-GGTGSTGFVSnlrt 285
Cdd:TIGR02203   5 LWSYVRPYKAGLVLAGVA-MILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGiCSFVSTYLLS---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 286 flWIRVQQFTSRRVELliFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYL--VFNVIPTLADIIIGIIYFSMFF 363
Cdd:TIGR02203  80 --WVSNKVVRDIRVRM--FEKLLGLPVSFFDRQPTGTLL---SRITFDSEQVASAAtdAFIVLVRETLTVIGLFIVLLYY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 364 NAWFGLIVFLCMSLyltLTIVVTEWRTKFRR-AMNTQE-NATRARAVDSLL-NFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:TIGR02203 153 SWQLTLIVVVMLPV---LSILMRRVSKRLRRiSKEIQNsMGQVTTVAEETLqGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 441 EWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFD 520
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 521 LLKEETEVKDlpGAGPLRFQKGRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG 599
Cdd:TIGR02203 310 LLDSPPEKDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 600 CIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRV-TAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERG 678
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVE 758
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
                         570       580
                  ....*....|....*....|....
gi 1169100883 759 RGRHEALLSRGGVYADMWQLQQGQ 782
Cdd:TIGR02203 548 RGTHNELLARNGLYAQLHNMQFRE 571
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
297-775 2.33e-111

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 351.19  E-value: 2.33e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELLI--FSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLlsYLVF--NVIPTLADIIIgIIYFSMFFNAWFGLIVF 372
Cdd:PRK13657   87 RRLAVLTeyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGL--WLEFmrEHLATLVALVV-LLPLALFMNWRLSLVLV 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEwRTK-FRRAMNTQENATRARAVDSLLNFETVKYYN---AESYEVERYREAIIKYQG--LEWKSSA 446
Cdd:PRK13657  164 VLGIVYTLITTLVMR-KTKdGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNLLAAQMpvLSWWALA 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 447 SLvlLNQTQN----LVIGLGLlagsllcAYFVTEQKLQVGD---YVLFGTYIIQlymplnwfgtyyRMIQT-NFID---- 514
Cdd:PRK13657  243 SV--LNRAAStitmLAILVLG-------AALVQKGQLRVGEvvaFVGFATLLIG------------RLDQVvAFINqvfm 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 515 ----MENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL 590
Cdd:PRK13657  302 aapkLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 591 FRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGY 670
Cdd:PRK13657  382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 671 RTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILV 750
Cdd:PRK13657  462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
                         490       500
                  ....*....|....*....|....*
gi 1169100883 751 IKDGCIVERGRHEALLSRGGVYADM 775
Cdd:PRK13657  542 FDNGRVVESGSFDELVARGGRFAAL 566
MTABC_N pfam16185
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ...
6-209 8.99e-61

Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five transmembrane helices of eukaryotic mitochondrial ABC-transporters.


Pssm-ID: 465049  Cd Length: 244  Bit Score: 205.59  E-value: 8.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883   6 NYCEAEGPVGPAWMQDGLSPCFFFTLVPSTRMALGTLALVLALPCRRRErpagADSLSWGAGPRISPYVLQLLLATLQAA 85
Cdd:pfam16185   1 SYCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRKY----GTPMEPKFIPRSRLYVLQLFLALLLPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  86 LPLAGLAGRVGTARGAPLPSYLLLASVLESLAGACGLWLLVVERSQARQRLAMgiwikFRHSPGLLLLWTVAFAAENLAL 165
Cdd:pfam16185  77 LALARFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPT-----RGHGLVLLLFWTLAFVAENLAF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 166 VSWNSPQWWWARADLGQQV-------------------------------------------------RSAAQQSTWRDF 196
Cdd:pfam16185 152 VSWNSPDWWWGLETLSDQVefglfvvryvctlllfvlglkapglprkpymllinederdvessqpllgDSEENGSTWRNF 231
                         250
                  ....*....|...
gi 1169100883 197 GRKLRLLSGYLWP 209
Cdd:pfam16185 232 GKKLRLLWPYLWP 244
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
560-709 3.30e-44

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: 156.27  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFND-TIADNI 638
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 639 RYGRVTAGNDEVEAAAQAAGIHDAiMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
555-751 4.12e-18

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 83.05  E-value: 4.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGCIRidgQDISQVTQASLRShIGVVPQDTVL---FN 631
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------AGVLR---PTSGTVRRAGGAR-VAYVPQRSEVpdsLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 DTIADNIRYG---------RVTAGN-DEVEAAAQAAGIHDAImafpegyRTQVGErglkLSGGEKQRVAIARTILKAPGI 701
Cdd:NF040873   72 LTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADL 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVNADQILVI 751
Cdd:NF040873  141 LLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
569-741 4.72e-11

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: 4.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  569 PGQTLALVGPSGAGKSTILRLLFRFYDISS-GCIRIDGQDISQVTQASLRSHIgvvpqdtvlfndtiadnirygrvtagn 647
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  648 deveaaaqaagihdaimafpegyrtqVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL---- 723
Cdd:smart00382  54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
                          170       180
                   ....*....|....*....|.
gi 1169100883  724 ---AKVCANRTTIVVAHRLST 741
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKD 128
GguA NF040905
sugar ABC transporter ATP-binding protein;
560-758 5.93e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 65.58  E-value: 5.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQ-----DISQvtqaSLRSHIGVVPQDTVLFND 632
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD----SEALGIVIIHQELALIPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 -TIADNIRYGRVTAGN---DEVEAAAQAA------GIHDAimafPEgyrTQVGERGLklsgGEKQRVAIARTILKAPGII 702
Cdd:NF040905   93 lSIAENIFLGNERAKRgviDWNETNRRARellakvGLDES----PD---TLVTDIGV----GKQQLVEIAKALSKDVKLL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 703 LLDEATSALdtsNERAIQASLAKVCANR----TTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:NF040905  162 ILDEPTAAL---NEEDSAALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
GguA NF040905
sugar ABC transporter ATP-binding protein;
548-712 9.42e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 55.57  E-value: 9.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF-RFY--DISsGCIRIDGQ--DISQVTQA-------- 614
Cdd:NF040905  264 TVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgrNIS-GTVFKDGKevDVSTVSDAidaglayv 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 -SLRSHIGVVPQDTVLFNDTIA--DNIRYGRVTAGNDEVEAAaqaagihdaimafpEGYRTQ-------VGERGLKLSGG 684
Cdd:NF040905  343 tEDRKGYGLNLIDDIKRNITLAnlGKVSRRGVIDENEEIKVA--------------EEYRKKmniktpsVFQKVGNLSGG 408
                         170       180
                  ....*....|....*....|....*...
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:NF040905  409 NQQKVVLSKWLFTDPDVLILDEPTRGID 436
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
544-610 5.67e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 40.11  E-value: 5.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 610
Cdd:NF033858    2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
186-788 0e+00

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: 791.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 186 SAAQQSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLA--WTVTSY 263
Cdd:COG5265     5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVpvGLLLAY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 264 VFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVF 343
Cdd:COG5265    85 GLLRLL------SVLF-GELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 344 NVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAE 423
Cdd:COG5265   158 NILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 424 SYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGT 503
Cdd:COG5265   238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 504 YYRMIQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGK 583
Cdd:COG5265   318 VYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 584 STILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAI 663
Cdd:COG5265   398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 664 MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVV 743
Cdd:COG5265   478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1169100883 744 NADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSED 788
Cdd:COG5265   558 DADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEA 602
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
194-783 0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 565.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 194 RDFGRKLRLLSGYLWPRgspalQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGgg 273
Cdd:COG1132     3 KSPRKLLRRLLRYLRPY-----RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRA-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 274 tgstgFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLAdII 353
Cdd:COG1132    76 -----LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV-TL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 354 IGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREA 433
Cdd:COG1132   150 IGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 434 IIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFI 513
Cdd:COG1132   230 NEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 514 DMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:COG1132   310 SAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQ 673
Cdd:COG1132   390 YDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTV 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 674 VGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKD 753
Cdd:COG1132   470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDD 549
                         570       580       590
                  ....*....|....*....|....*....|
gi 1169100883 754 GCIVERGRHEALLSRGGVYADMWQLQQGQE 783
Cdd:COG1132   550 GRIVEQGTHEELLARGGLYARLYRLQFGEE 579
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
222-518 0e+00

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 527.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEK---APWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18581     1 CLLLLAAGRVVNVLVPILYKKIVDSLTPDsadSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd18581    81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLV 458
Cdd:cd18581   161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 459 IGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18581   241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
544-779 1.93e-162

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: 470.17  E-value: 1.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:cd03253     1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIIL 703
Cdd:cd03253    81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:cd03253   161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
198-780 1.35e-141

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: 433.88  E-value: 1.35e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 198 RKLRLLSGYLWPRGSPALQLVVL-ICLGLMGLeralnvLVPIFYRNIVNL-LTEKAPwnSLAWTVTsyvflkFLQGGGTG 275
Cdd:COG2274   142 FGLRWFLRLLRRYRRLLLQVLLAsLLINLLAL------ATPLFTQVVIDRvLPNQDL--STLWVLA------IGLLLALL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 276 STGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIadRGTSSVTGLLSYLVFNvipTLADIII 354
Cdd:COG2274   208 FEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsRF--RDVESIREFLTGSLLT---ALLDLLF 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 355 GIIYFSM--FFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYRE 432
Cdd:COG2274   283 VLIFLIVlfFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEN 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 433 AIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNF 512
Cdd:COG2274   363 LLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAK 442
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 513 IDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYA-DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF 591
Cdd:COG2274   443 IALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 592 RFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYR 671
Cdd:COG2274   523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYD 602
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 672 TQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVI 751
Cdd:COG2274   603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
                         570       580
                  ....*....|....*....|....*....
gi 1169100883 752 KDGCIVERGRHEALLSRGGVYADMWQLQQ 780
Cdd:COG2274   683 DKGRIVEDGTHEELLARKGLYAELVQQQL 711
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
222-518 1.95e-128

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.


Pssm-ID: 350004 [Multi-domain]  Cd Length: 292  Bit Score: 385.04  E-value: 1.95e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTeKAPWNSLAWTVTSYVFLKFLQGggtgSTGFVSNLRTFLWIRVQQFTSRRVEL 301
Cdd:cd18560     1 SLLLLILGKACNVLAPLFLGRAVNALT-LAKVKDLESAVTLILLYALLRF----SSKLLKELRSLLYRRVQQNAYRELSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 302 LIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTL 381
Cdd:cd18560    76 KTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 382 TIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGL 461
Cdd:cd18560   156 TIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 462 GLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18560   236 GLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
544-776 6.20e-121

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: 363.47  E-value: 6.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03251     1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMW 776
Cdd:cd03251   161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
207-782 2.30e-114

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: 358.65  E-value: 2.30e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 207 LWPRGSPALQLVVLICLGlMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQG-GGTGSTGFVSnlrt 285
Cdd:TIGR02203   5 LWSYVRPYKAGLVLAGVA-MILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGiCSFVSTYLLS---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 286 flWIRVQQFTSRRVELliFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYL--VFNVIPTLADIIIGIIYFSMFF 363
Cdd:TIGR02203  80 --WVSNKVVRDIRVRM--FEKLLGLPVSFFDRQPTGTLL---SRITFDSEQVASAAtdAFIVLVRETLTVIGLFIVLLYY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 364 NAWFGLIVFLCMSLyltLTIVVTEWRTKFRR-AMNTQE-NATRARAVDSLL-NFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:TIGR02203 153 SWQLTLIVVVMLPV---LSILMRRVSKRLRRiSKEIQNsMGQVTTVAEETLqGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 441 EWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFD 520
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 521 LLKEETEVKDlpGAGPLRFQKGRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG 599
Cdd:TIGR02203 310 LLDSPPEKDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 600 CIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRV-TAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERG 678
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVE 758
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
                         570       580
                  ....*....|....*....|....
gi 1169100883 759 RGRHEALLSRGGVYADMWQLQQGQ 782
Cdd:TIGR02203 548 RGTHNELLARNGLYAQLHNMQFRE 571
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
544-779 1.77e-112

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: 341.44  E-value: 1.77e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAD--GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:cd03249     1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
297-775 2.33e-111

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 351.19  E-value: 2.33e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELLI--FSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLlsYLVF--NVIPTLADIIIgIIYFSMFFNAWFGLIVF 372
Cdd:PRK13657   87 RRLAVLTeyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGL--WLEFmrEHLATLVALVV-LLPLALFMNWRLSLVLV 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEwRTK-FRRAMNTQENATRARAVDSLLNFETVKYYN---AESYEVERYREAIIKYQG--LEWKSSA 446
Cdd:PRK13657  164 VLGIVYTLITTLVMR-KTKdGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNLLAAQMpvLSWWALA 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 447 SLvlLNQTQN----LVIGLGLlagsllcAYFVTEQKLQVGD---YVLFGTYIIQlymplnwfgtyyRMIQT-NFID---- 514
Cdd:PRK13657  243 SV--LNRAAStitmLAILVLG-------AALVQKGQLRVGEvvaFVGFATLLIG------------RLDQVvAFINqvfm 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 515 ----MENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL 590
Cdd:PRK13657  302 aapkLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 591 FRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGY 670
Cdd:PRK13657  382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 671 RTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILV 750
Cdd:PRK13657  462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
                         490       500
                  ....*....|....*....|....*
gi 1169100883 751 IKDGCIVERGRHEALLSRGGVYADM 775
Cdd:PRK13657  542 FDNGRVVESGSFDELVARGGRFAAL 566
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
542-770 2.32e-110

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: 335.73  E-value: 2.32e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:cd03254     1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03254    81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:cd03254   161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
222-518 5.15e-101

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.


Pssm-ID: 350027 [Multi-domain]  Cd Length: 290  Bit Score: 313.70  E-value: 5.15e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTE---KAPWNSlawtVTSYVFLKFLQGGGtgstgFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18583     1 CFLCLLAERVLNVLVPRQLGIIVDSLSGgsgKSPWKE----IGLYVLLRFLQSGG-----GLGLLRSWLWIPVEQYSYRA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGtSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd18583    72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQG-SSINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLV 458
Cdd:cd18583   151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 459 IGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18583   231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
278-779 3.80e-100

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: 321.65  E-value: 3.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 278 GFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYLVFNVIPTLADIIIGII 357
Cdd:TIGR02204  72 ALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVV---SRLTTDTTLLQSVIGSSLSMALRNALMCIG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 358 YFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQEN--ATRARAVDSLLNFETVKYYNAESYEVERYREAII 435
Cdd:TIGR02204 149 GLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRiaDAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 436 KYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDM 515
Cdd:TIGR02204 229 KAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAA 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 516 ENMFDLLKEETEV------KDLPGagPLRfqkGRIEFENVHFSYADGRET--LQDVSFTVMPGQTLALVGPSGAGKSTIL 587
Cdd:TIGR02204 309 ERLIELLQAEPDIkapahpKTLPV--PLR---GEIEFEQVNFAYPARPDQpaLDGLNLTVRPGETVALVGPSGAGKSTLF 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 588 RLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFP 667
Cdd:TIGR02204 384 QLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALP 463
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 668 EGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQ 747
Cdd:TIGR02204 464 EGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADR 543
                         490       500       510
                  ....*....|....*....|....*....|..
gi 1169100883 748 ILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:TIGR02204 544 IVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
222-518 5.96e-98

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350026 [Multi-domain]  Cd Length: 292  Bit Score: 305.96  E-value: 5.96e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLA--WTVTSYVFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRRV 299
Cdd:cd18582     1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVplLLLLAYGLARIL------SSLF-NELRDALFARVSQRAVRRL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 300 ELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYL 379
Cdd:cd18582    74 ALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 380 TLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVI 459
Cdd:cd18582   154 AFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALII 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 460 GLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18582   234 SLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
495-770 6.63e-98

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: 315.16  E-value: 6.63e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 495 YMPLNWFGTYY--RMIQTNFidMENMFDLLkEETEVKDLPGAGPLRFQKG-RIEFENVHFSYADGRETLQDVSFTVMPGQ 571
Cdd:COG4988   288 FLPLRDLGSFYhaRANGIAA--AEKIFALL-DAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRPALDGLSLTIPPGE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 572 TLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVE 651
Cdd:COG4988   365 RVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELE 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 652 AAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRT 731
Cdd:COG4988   445 AALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT 524
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1169100883 732 TIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:COG4988   525 VILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
518-782 1.77e-93

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 304.25  E-value: 1.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 518 MFDLLKEETEvKDLpGAGPLRFQKGRIEFENVHFSYaDGRET--LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYD 595
Cdd:PRK11176  318 LFAILDLEQE-KDE-GKRVIERAKGDIEFRNVTFTY-PGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 596 ISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRV-TAGNDEVEAAAQAAGIHDAIMAFPEGYRTQV 674
Cdd:PRK11176  395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVI 474
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 675 GERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:PRK11176  475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
                         250       260
                  ....*....|....*....|....*...
gi 1169100883 755 CIVERGRHEALLSRGGVYADMWQLQQGQ 782
Cdd:PRK11176  555 EIVERGTHAELLAQNGVYAQLHKMQFGQ 582
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
298-778 1.69e-92

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: 300.91  E-value: 1.69e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 298 RVELliFSHLHELSLRWHLGRRTGEVL-RI-ADrgtssVTGLLSYLVFNVIPTLADI--IIGIIYFSMFFNAWFGLIVFL 373
Cdd:COG4987    91 RVRL--YRRLEPLAPAGLARLRSGDLLnRLvAD-----VDALDNLYLRVLLPLLVALlvILAAVAFLAFFSPALALVLAL 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 374 CMSLYLTLTIVVTEWRTKFR-RAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLN 452
Cdd:COG4987   164 GLLLAGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 453 QTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFgtyiiqLYMPLNWF-------GTYYRMIQTnfID-MENMFDLLKE 524
Cdd:COG4987   244 ALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL------VLAALALFealaplpAAAQHLGRV--RAaARRLNELLDA 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 525 ETEVKDlPGAGPLRFQKGRIEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI 603
Cdd:COG4987   316 PPAVTE-PAEPAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 604 DGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSG 683
Cdd:COG4987   395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSG 474
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:COG4987   475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554
                         490
                  ....*....|....*
gi 1169100883 764 ALLSRGGVYADMWQL 778
Cdd:COG4987   555 ELLAQNGRYRQLYQR 569
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
107-775 8.67e-91

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 300.49  E-value: 8.67e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 107 LLLASVLESLAGACGLWLLVVERSQARQRLAMGIWIKFRhspgLLLLWTVAFAAENLALVSWNS---------PQW--WW 175
Cdd:TIGR00958  51 VLWLGALGILLNKAGGLLAAVKPLVAALCLATPSLSSLR----ALAFWEALDPAVRVALGLWSWfvwsygaalPAAalWA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 176 ARADLGQQVRSAAQ-QSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMgleralnvLVPIFYRNIVNLLTEKAPWN 254
Cdd:TIGR00958 127 VLSSAGASEKEAEQgQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEM--------FIPFYTGRVIDTLGGDKGPP 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 255 SLAWTVTsyvFLKFLQGGGTGSTGFVSNLRTFLWIRVQqftsRRVELLIFSHLHELSLRWHLGRRTGEvlrIADRGTSSV 334
Cdd:TIGR00958 199 ALASAIF---FMCLLSIASSVSAGLRGGSFNYTMARIN----LRIREDLFRSLLRQDLGFFDENKTGE---LTSRLSSDT 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 335 TGLLSYLVFNVIPTLADIIIGI-IYFSMFFNAWFGLIVFLcmsLYLTLTIVVTEWRTKFRRAMNTQENATRARAVD---- 409
Cdd:TIGR00958 269 QTMSRSLSLNVNVLLRNLVMLLgLLGFMLWLSPRLTMVTL---INLPLVFLAEKVFGKRYQLLSEELQEAVAKANQvaee 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 410 SLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGT 489
Cdd:TIGR00958 346 ALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLL 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 490 YIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKdLPGAGPLRFQKGRIEFENVHFSYAD--GRETLQDVSFTV 567
Cdd:TIGR00958 426 YQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP-LTGTLAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTL 504
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 568 MPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGN 647
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPD 584
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 648 DEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKvc 727
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR-- 662
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 1169100883 728 ANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
544-779 1.30e-89

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: 282.07  E-value: 1.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03252     1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03252    81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:cd03252   161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
544-754 1.20e-81

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: 258.47  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03228     1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIrygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03228    81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
297-793 1.77e-81

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: 272.15  E-value: 1.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELLI--FSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGL-LSYLVFNVIPTLADIIIGIIYFSMffNAWFGLIVFL 373
Cdd:TIGR01192  87 RRATLLTeaFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwLEFMRQHLATFVALFLLIPTAFAM--DWRLSIVLMV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 374 CMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYN---AESYEVERYREAII--KYQGLEWKSSASL 448
Cdd:TIGR01192 165 LGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNrieAETSALKQFTNNLLsaQYPVLDWWALASG 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 449 vlLNQTQNLViglGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEV 528
Cdd:TIGR01192 245 --LNRMASTI---SMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQR 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 529 KDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI 608
Cdd:TIGR01192 320 EEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDI 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 609 SQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQR 688
Cdd:TIGR01192 400 NTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQR 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:TIGR01192 480 LAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
                         490       500
                  ....*....|....*....|....*.
gi 1169100883 769 GGVYADMwqLQQGQEETSED-TKPQT 793
Cdd:TIGR01192 560 DGRFYKL--LRRSGLLTNQPaTKPLR 583
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
541-756 4.33e-72

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: 235.06  E-value: 4.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 541 KGRIEFENVHFSYAD--GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS 618
Cdd:cd03248     9 KGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:cd03248    89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCI 756
Cdd:cd03248   169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
521-795 3.19e-71

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 244.24  E-value: 3.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 521 LLKEETEVKDlpGAGPLRFQKGRIEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG 599
Cdd:PRK10789  293 MLAEAPVVKD--GSEPVPEGRGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 600 CIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGL 679
Cdd:PRK10789  371 DIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 680 KLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVER 759
Cdd:PRK10789  451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQR 530
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1169100883 760 GRHEALLSRGGVYADMWQLQqgQEETSEDTKPQTME 795
Cdd:PRK10789  531 GNHDQLAQQSGWYRDMYRYQ--QLEAALDDAPEIRE 564
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
542-760 8.33e-71

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: 231.71  E-value: 8.33e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03245     1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPG 700
Cdd:cd03245    81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03245   161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
283-768 9.52e-70

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: 240.04  E-value: 9.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 283 LRTFLWIRVQQFTSRRVELLIFSHLHELSLRwHLGRRTGEVLRiaDrgtssVTGLLSYLVFNVIPTLAD-----IIIGII 357
Cdd:COG4618    79 VRSRILVRVGARLDRRLGPRVFDAAFRAALR-GGGGAAAQALR--D-----LDTLRQFLTGPGLFALFDlpwapIFLAVL 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 358 YFsmfFNAWFGLIVFLCMSLYLTLTIVvTEWRTKFRRAMNTQENATRARAVDSLLNfetvkyyNAESYE--------VER 429
Cdd:COG4618   151 FL---FHPLLGLLALVGALVLVALALL-NERLTRKPLKEANEAAIRANAFAEAALR-------NAEVIEamgmlpalRRR 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 430 YREAIIKYQGLE--------WKSSASLVLLNQTQNLVIGLGllagsllcAYFVTEQKLQVGdyVLFGTYII--QLYMPL- 498
Cdd:COG4618   220 WQRANARALALQarasdragGFSALSKFLRLLLQSAVLGLG--------AYLVIQGEITPG--AMIAASILmgRALAPIe 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 499 ----NWfgtyyRMIQ---TNFIDMENMFDLLKEETEVKDLPGAgplrfqKGRIEFENVHFSYADGRE-TLQDVSFTVMPG 570
Cdd:COG4618   290 qaigGW-----KQFVsarQAYRRLNELLAAVPAEPERMPLPRP------KGRLSVENLTVVPPGSKRpILRGVSFSLEPG 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 571 QTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNI-RYGRVTAgnDE 649
Cdd:COG4618   359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDADP--EK 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 650 VEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA- 728
Cdd:COG4618   437 VVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAr 516
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1169100883 729 NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG4618   517 GATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
219-751 2.83e-69

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: 237.57  E-value: 2.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFY--RNIVNLLTEKAPWNSLAW---TVTSYVFLKFLQGGGTGSTGFVSNLRtflwIRVQq 293
Cdd:TIGR02857   4 ALALLALLGVLGALLIIAQAWLlaRVVDGLISAGEPLAELLPalgALALVLLLRALLGWLQERAAARAAAA----VKSQ- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 ftsRRVELLifSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLS-YLVFNViptLADIIIGIIYFSMFFNAWFGLIVF 372
Cdd:TIGR02857  79 ---LRERLL--EAVAALGPRWLQGRPSGELATLALEGVEALDGYFArYLPQLV---LAVIVPLAILAAVFPQDWISGLIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEWRTKfrRAMNTQENAT---------RARAVDSLLNFETVKYYNAESYEV-ERYREAIIKYQGLEW 442
Cdd:TIGR02857 151 LLTAPLIPIFMILIGWAAQ--AAARKQWAALsrlsghfldRLRGLPTLKLFGRAKAQAAAIRRSsEEYRERTMRVLRIAF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 443 KSSASLVLLNQTQNLVIglgllagsllcAYFVTeQKLQVGDYVLFGTYIIQL-----YMPLNWFGTYYRMIQTNFIDMEN 517
Cdd:TIGR02857 229 LSSAVLELFATLSVALV-----------AVYIG-FRLLAGDLDLATGLFVLLlapefYLPLRQLGAQYHARADGVAAAEA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 518 MFDLLKEET----EVKDLPGAGPLRfqkgrIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:TIGR02857 297 LFAVLDAAPrplaGKAPVTAAPASS-----LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQ 673
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTP 451
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 674 VGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVI 751
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
196-775 3.09e-69

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: 242.16  E-value: 3.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 196 FGRKLRLLSGyLWPR--GSP-ALQLVVLICLGLMglerALNVLVPIFYRNIVN--LLTEKAPW-----NSLAWTVTSYVF 265
Cdd:TIGR03796 135 GGRKPSLLRA-LWRRlrGSRgALLYLLLAGLLLV----LPGLVIPAFSQIFVDeiLVQGRQDWlrpllLGMGLTALLQGV 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 266 LKFLQGGGTgstgfvsnlrtflwIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEV---LRIADRGTSSVTGLLsylv 342
Cdd:TIGR03796 210 LTWLQLYYL--------------RRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIasrVQLNDQVAEFLSGQL---- 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 343 fnvIPTLADIIIGIIYFS-MF-FNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYY 420
Cdd:TIGR03796 272 ---ATTALDAVMLVFYALlMLlYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKAS 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 421 NAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLN- 499
Cdd:TIGR03796 349 GLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNn 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 500 --WFGTYYRMIQTNFID----MENMFDLLKEETEVKDLPGAGPLRFQkGRIEFENVHFSY-ADGRETLQDVSFTVMPGQT 572
Cdd:TIGR03796 429 lvGFGGTLQELEGDLNRlddvLRNPVDPLLEEPEGSAATSEPPRRLS-GYVELRNITFGYsPLEPPLIENFSLTLQPGQR 507
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 573 LALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEA 652
Cdd:TIGR03796 508 VALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVR 587
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 653 AAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKV-CanrT 731
Cdd:TIGR03796 588 ACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRgC---T 664
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 1169100883 732 TIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR03796 665 CIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
542-760 5.87e-68

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: 223.91  E-value: 5.87e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03244     1 GDIEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIR-YGRVTagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:cd03244    81 SIIPQDPVLFSGTIRSNLDpFGEYS--DEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03244   159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
473-784 1.62e-66

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 231.92  E-value: 1.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 473 FVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLkeetevkDLPGAG------PLrfQKGRIEF 546
Cdd:PRK10790  273 FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM-------DGPRQQygnddrPL--QSGRIDI 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQD 626
Cdd:PRK10790  344 DNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFNDTIADNIRYGRvTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDE 706
Cdd:PRK10790  424 PVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 707 ATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEE 784
Cdd:PRK10790  503 ATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
280-775 7.47e-64

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: 226.93  E-value: 7.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 280 VSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIADrgTSSVTGLLSYLVFNVIPTLAdIIIGIIY 358
Cdd:TIGR01193 212 LSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVsRFTD--ASSIIDALASTILSLFLDMW-ILVIVGL 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 359 FSMFFNAWFGLIVFLCMSLYltlTIVVTEWRTKFRRaMNT---QENATRARAV-DSLLNFETVKYYNAES-------YEV 427
Cdd:TIGR01193 289 FLVRQNMLLFLLSLLSIPVY---AVIIILFKRTFNK-LNHdamQANAVLNSSIiEDLNGIETIKSLTSEAeryskidSEF 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 428 ERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLlagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRM 507
Cdd:TIGR01193 365 GDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTG-------AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPK 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 508 IQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTIL 587
Cdd:TIGR01193 438 LQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 588 RLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYG-RVTAGNDEVEAAAQAAGIHDAIMAF 666
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENM 597
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 667 PEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcANRTTIVVAHRLSTVVNAD 746
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSD 676
                         490       500
                  ....*....|....*....|....*....
gi 1169100883 747 QILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDRNGFYASL 705
MTABC_N pfam16185
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ...
6-209 8.99e-61

Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five transmembrane helices of eukaryotic mitochondrial ABC-transporters.


Pssm-ID: 465049  Cd Length: 244  Bit Score: 205.59  E-value: 8.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883   6 NYCEAEGPVGPAWMQDGLSPCFFFTLVPSTRMALGTLALVLALPCRRRErpagADSLSWGAGPRISPYVLQLLLATLQAA 85
Cdd:pfam16185   1 SYCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRKY----GTPMEPKFIPRSRLYVLQLFLALLLPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  86 LPLAGLAGRVGTARGAPLPSYLLLASVLESLAGACGLWLLVVERSQARQRLAMgiwikFRHSPGLLLLWTVAFAAENLAL 165
Cdd:pfam16185  77 LALARFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPT-----RGHGLVLLLFWTLAFVAENLAF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 166 VSWNSPQWWWARADLGQQV-------------------------------------------------RSAAQQSTWRDF 196
Cdd:pfam16185 152 VSWNSPDWWWGLETLSDQVefglfvvryvctlllfvlglkapglprkpymllinederdvessqpllgDSEENGSTWRNF 231
                         250
                  ....*....|...
gi 1169100883 197 GRKLRLLSGYLWP 209
Cdd:pfam16185 232 GKKLRLLWPYLWP 244
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
520-777 4.14e-56

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 202.36  E-value: 4.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 520 DLLKEETEVKdLPGAGPLRFQKGRIEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS 598
Cdd:PRK11160  316 EITEQKPEVT-FPTTSTAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 599 GCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIhDAIMAFPEGYRTQVGERG 678
Cdd:PRK11160  395 GEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGG 473
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILK-APgIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:PRK11160  474 RQLSGGEQRRLGIARALLHdAP-LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
                         250       260
                  ....*....|....*....|
gi 1169100883 758 ERGRHEALLSRGGVYADMWQ 777
Cdd:PRK11160  553 EQGTHQELLAQQGRYYQLKQ 572
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
540-761 2.08e-53

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: 183.77  E-value: 2.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYA-DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS 618
Cdd:cd03369     3 EHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFNDTIADNI-RYGRVTagNDEVEAAaqaagihdaimafpegyrTQVGERGLKLSGGEKQRVAIARTILK 697
Cdd:cd03369    83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGR 761
Cdd:cd03369   143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
544-756 1.16e-52

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: 180.49  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03246     1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIrygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03246    81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVNADQILVIKDGCI 756
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
495-784 1.58e-52

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 192.75  E-value: 1.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 495 YMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEV-----KDLPGAGPLRfqkgrIEFENVHFSYADGRETLQDVSFTVMP 569
Cdd:PRK11174  301 YQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHpqqgeKELASNDPVT-----IEAEDLEILSPDGKTLAGPLNFTLPA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 570 GQTLALVGPSGAGKSTILRLLFRF--YdisSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGN 647
Cdd:PRK11174  376 GQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASD 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 648 DEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC 727
Cdd:PRK11174  453 EQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 728 ANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMwqLQQGQEE 784
Cdd:PRK11174  533 RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL--LAHRQEE 587
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
516-739 1.20e-50

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: 186.03  E-value: 1.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 516 ENMFDLLKEETEVKD--LPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEgsAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQ 673
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 674 VGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRL 739
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
544-768 8.86e-49

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 171.75  E-value: 8.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG1122     1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagihDAIMAfpegyrtQVGERGLK------LSGGEKQRVAIARTI 695
Cdd:COG1122    81 FQnpDDQLFAPTVEEDVAFGPENLGLPREEIRERV----EEALE-------LVGLEHLAdrppheLSGGQKQRVAIAGVL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVV-NADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG1122   150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFSD 224
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
544-756 1.63e-48

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 170.38  E-value: 1.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG4619     1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADNI----RYGRVTAGNDEVEAAAQAAGIHDAIMAfpegyrTQVGErglkLSGGEKQRVAIARTILKAP 699
Cdd:COG4619    80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILD------KPVER----LSGGERQRLALIRALLLQP 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH------RLstvvnADQILVIKDGCI 756
Cdd:COG4619   150 DVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
544-758 1.02e-47

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 168.69  E-value: 1.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLRSHI 620
Cdd:COG2884     2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYG-RVT-AGNDEVEAAAQAA----GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:COG2884    82 GVVFQDFRLLPDrTVYENVALPlRVTgKSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVAIAR 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVNADQ-ILVIKDGCIVE 758
Cdd:COG2884   151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
545-754 1.33e-46

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: 165.33  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:cd03225     1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagihdaimafpEGYRTQVGERGLK------LSGGEKQRVAIARTI 695
Cdd:cd03225    81 FQnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERV-----------EEALELVGLEGLRdrspftLSGGQKQRVAIAGVL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDG 754
Cdd:cd03225   150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
544-761 5.84e-46

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 164.06  E-value: 5.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---- 616
Cdd:COG1136     5 LELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRV 689
Cdd:COG1136    85 RRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARellervGLGDRLDHRPS-----------QLSGGQQQRV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGR 761
Cdd:COG1136   154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
544-768 2.23e-45

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 170.47  E-value: 2.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET----LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---L 616
Cdd:COG1123   261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQD---------TVLfnDTIADNIR-YGRVTAG--NDEVEAAAQAAGIHDAIM-AFPegyrtqvGErglkLSG 683
Cdd:COG1123   341 RRRVQMVFQDpysslnprmTVG--DIIAEPLRlHGLLSRAerRERVAELLERVGLPPDLAdRYP-------HE----LSG 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:COG1123   408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487

                  ....*...
gi 1169100883 761 RHEALLSR 768
Cdd:COG1123   488 PTEEVFAN 495
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
544-760 4.15e-45

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: 159.79  E-value: 4.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRSHIGV 622
Cdd:cd03247     1 LSINNVSFSYPEQEQQvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIrygrvtagndeveaaaqaagihdaimafpegyrtqvgerGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03247    80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03247   121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
543-767 4.93e-45

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: 162.14  E-value: 4.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:COG1120     1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVL-FNDTIADNIRYGR---------VTAGNDE-VEAAAQAAGIHDaiMAfpegyrtqvgERGL-KLSGGEKQRVA 690
Cdd:COG1120    80 VPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEH--LA----------DRPVdELSGGERQRVL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:COG1120   148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLT 227
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
544-760 5.89e-45

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: 161.19  E-value: 5.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDI-----SSGCIRIDGQDI--SQVTQASL 616
Cdd:cd03260     1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFNDTIADNIRYG-------RVTAGNDEVEAAAQAAGIHDaimafpegyrtQVGER--GLKLSGGEKQ 687
Cdd:cd03260    80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD-----------EVKDRlhALGLSGGQQQ 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAH------RLstvvnADQILVIKDGCIVERG 760
Cdd:cd03260   149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
544-768 3.10e-44

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: 159.97  E-value: 3.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY---ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:COG1124     2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQD---------TVlfNDTIADNIRYGRVTAGNDEVEAAAQAAGIhdaimafPEGYRTQvgeRGLKLSGGEKQRVAI 691
Cdd:COG1124    82 QMVFQDpyaslhprhTV--DRILAEPLRIHGLPDREERIAELLEQVGL-------PPSFLDR---YPHQLSGGQRQRVAI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLStVVN--ADQILVIKDGCIVERGRHEALLS 767
Cdd:COG1124   150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLA 228

                  .
gi 1169100883 768 R 768
Cdd:COG1124   229 G 229
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
560-709 3.30e-44

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: 156.27  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFND-TIADNI 638
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 639 RYGRVTAGNDEVEAAAQAAGIHDAiMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
544-770 1.10e-43

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 158.10  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAsLRSHIGVV 623
Cdd:COG4555     2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAiMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGII 702
Cdd:COG4555    80 PDERGLYdRLTVRENIRYFAELYGLFDEELKKRIEELIEL-LGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:COG4555   155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
541-772 3.36e-43

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 169.82  E-value: 3.36e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  541 KGRIEFENVHFSYADGRET--LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDI---------------------- 596
Cdd:PTZ00265  1163 KGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdy 1242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  597 --------------------------------SSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVT 644
Cdd:PTZ00265  1243 qgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  645 AGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLA 724
Cdd:PTZ00265  1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883  725 --KVCANRTTIVVAHRLSTVVNADQILVI----KDGCIVE-RGRHEALLS-RGGVY 772
Cdd:PTZ00265  1403 diKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSvQDGVY 1458
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
544-760 5.95e-43

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: 154.98  E-value: 5.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03259     1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRtqvgeRGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03259    78 FQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNR-----YPHELSGGQQQRVALARALAREPSLL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03259   153 LLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
544-754 6.19e-43

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: 154.96  E-value: 6.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---- 616
Cdd:cd03255     1 IELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRV 689
Cdd:cd03255    81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEellervGLGDRLNHYPS-----------ELSGGQQQRV 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03255   150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDG 216
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
544-760 7.80e-43

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: 155.36  E-value: 7.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---R 617
Cdd:cd03257     2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQD--TVLfND--TIADNIRYGRVTAGNDEVEAAAQAAGIHDAIM-----AFPEGYRTQvgerglkLSGGEKQR 688
Cdd:cd03257    82 KEIQMVFQDpmSSL-NPrmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPHE-------LSGGQRQR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03257   154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
544-768 1.81e-42

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 154.45  E-value: 1.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAsLRSHIGVV 623
Cdd:COG1131     1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAImafpegyRTQVGerglKLSGGEKQRVAIARTIL 696
Cdd:COG1131    79 PQEPALYPDlTVRENLRFFARLYGLPRKEARERIDellelfGLTDAA-------DRKVG----TLSGGMKQRLGLALALL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG1131   148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
544-766 2.42e-42

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: 154.37  E-value: 2.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHI 620
Cdd:COG1127     6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNI-----RYGRVTAgnDEVEAAA----QAAGIHDAIMAFPegyrtqvGErglkLSGGEKQRVA 690
Cdd:COG1127    85 GMLFQGGALFDSlTVFENVafplrEHTDLSE--AEIRELVleklELVGLPGAADKMP-------SE----LSGGMRKRVA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILKAPGIILLDEATSALD--TSNE-----RAIQASLakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRH 762
Cdd:COG1127   152 LARALALDPEILLYDEPTAGLDpiTSAVideliRELRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226

                  ....
gi 1169100883 763 EALL 766
Cdd:COG1127   227 EELL 230
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
543-753 7.70e-42

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 165.59  E-value: 7.70e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  543 RIEFENVHFSYaDGR---ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQASLRS 618
Cdd:PTZ00265   382 KIQFKNVRFHY-DTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  619 HIGVVPQDTVLFNDTIADNIRYG-------------------------------RVTAGND------------------- 648
Cdd:PTZ00265   461 KIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscRAKCAGDlndmsnttdsneliemrkn 540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  649 -------EVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQA 721
Cdd:PTZ00265   541 yqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1169100883  722 SL--AKVCANRTTIVVAHRLSTVVNADQILVIKD 753
Cdd:PTZ00265   621 TInnLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
545-754 8.65e-42

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: 149.70  E-value: 8.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVP 624
Cdd:cd00267     1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QdtvlfndtiadnirygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGIILL 704
Cdd:cd00267    80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 705 DEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVNA-DQILVIKDG 754
Cdd:cd00267   105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDG 156
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
544-768 6.18e-41

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 150.14  E-value: 6.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQASLRSHIG 621
Cdd:COG1126     2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFND-TIADNIRYGRVTAGN---DEVEAAAQAA----GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:COG1126    81 MVFQQFNLFPHlTVLENVTLAPIKVKKmskAEAEERAMELlervGLADKADAYPA-----------QLSGGQQQRVAIAR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALD--TSNE--RAIQaSLAKvcANRTTIVVAHRLS---TVvnADQILVIKDGCIVERGRHEALL 766
Cdd:COG1126   150 ALAMEPKVMLFDEPTSALDpeLVGEvlDVMR-DLAK--EGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFF 224

                  ..
gi 1169100883 767 SR 768
Cdd:COG1126   225 EN 226
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
544-768 1.90e-40

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 148.50  E-value: 1.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---R 617
Cdd:cd03258     2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVA 690
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLellelvGLEDKADAYPA-----------QLSGGQKQRVG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNR----TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:cd03258   151 IARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228

                  ...
gi 1169100883 766 LSR 768
Cdd:cd03258   229 FAN 231
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
544-757 2.89e-40

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 148.67  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHI 620
Cdd:COG3638     3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQD-------TVLfndtiaDNI---RYGRVTA--------GNDEVEAAAQAAgihdaimafpegyrTQVG------E 676
Cdd:COG3638    83 GMIFQQfnlvprlSVL------TNVlagRLGRTSTwrsllglfPPEDRERALEAL--------------ERVGladkayQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 677 RGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKD 753
Cdd:COG3638   143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRD 222

                  ....
gi 1169100883 754 GCIV 757
Cdd:COG3638   223 GRVV 226
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
489-775 5.15e-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: 159.73  E-value: 5.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  489 TYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVK-DLPGAGPLRF--QKGRIEFENVHFSYADGRE-TLQDVS 564
Cdd:TIGR00957 1227 SYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGwpPRGRVEFRNYCLRYREDLDlVLRHIN 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  565 FTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIR-YGRV 643
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY 1386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  644 TagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL 723
Cdd:TIGR00957 1387 S--DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883  724 AKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR00957 1465 RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
544-751 1.42e-39

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 145.69  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHI 620
Cdd:cd03293     1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFN-DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEellelvGLSGFENAYPH-----------QLSGGMRQRVALAR 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIV-VAHRLSTVVN-ADQILVI 751
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDEAVFlADRVVVL 205
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
544-768 1.99e-39

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 153.14  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGR-ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS---SGCIRIDGQDISQVTQASLRSH 619
Cdd:COG1123     5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQD--TVLFNDTIADNI----RYGRVTAGN--DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAI 691
Cdd:COG1123    85 IGMVFQDpmTQLNPVTVGDQIaealENLGLSRAEarARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG1123   154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
544-760 4.40e-39

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: 144.95  E-value: 4.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHI 620
Cdd:cd03261     1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNI-----RYGRVTAG--NDEVEAAAQAAGIHDAIMAFPegyrtqvGErglkLSGGEKQRVAIA 692
Cdd:cd03261    80 GMLFQSGALFDSlTVFENVafplrEHTRLSEEeiREIVLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 693 RTILKAPGIILLDEATSALD--TSNE-----RAIQASLakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03261   149 RALALDPELLLYDEPTAGLDpiASGViddliRSLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
544-765 9.38e-39

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 144.08  E-value: 9.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHIGVV 623
Cdd:COG1121     7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ-------------DTVLFNdtiadniRYGRV-------TAGNDEVEAAAQAAGIhdaimafpEGYR-TQVGErglkLS 682
Cdd:COG1121    81 PQraevdwdfpitvrDVVLMG-------RYGRRglfrrpsRADREAVDEALERVGL--------EDLAdRPIGE----LS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 683 GGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVV-NADQILVIKDGCIVERG 760
Cdd:COG1121   142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVReYFDRVLLLNRGLVAHGP 221

                  ....*
gi 1169100883 761 RHEAL 765
Cdd:COG1121   222 PEEVL 226
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
545-760 1.01e-38

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: 141.80  E-value: 1.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVP 624
Cdd:cd03214     1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QdtvlfndtiadnirygrvtagndeveaAAQAAGIHDaiMAfpegyrtqvgERGLK-LSGGEKQRVAIARTILKAPGIIL 703
Cdd:cd03214    80 Q---------------------------ALELLGLAH--LA----------DRPFNeLSGGERQRVLLARALAQEPPILL 120
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03214   121 LDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
544-761 1.27e-38

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: 142.93  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLRSHI 620
Cdd:cd03292     1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraiPYLRRKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRVTAG------NDEVEAAAQAAGIHDAIMAFPEGyrtqvgerglkLSGGEKQRVAIAR 693
Cdd:cd03292    81 GVVFQDFRLLPDrNVYENVAFALEVTGvppreiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVikdgCIVERGR 761
Cdd:cd03292   150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRV----IALERGK 213
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
544-768 1.41e-38

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 147.17  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRsHIGVV 623
Cdd:COG3842     6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKR-NVGMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYG-RVtagnDEVEAAAQAAGIHDAImafpegyrTQVGERGL------KLSGGEKQRVAIARTI 695
Cdd:COG3842    83 FQDYALFpHLTVAENVAFGlRM----RGVPKAEIRARVAELL--------ELVGLEGLadryphQLSGGQQQRVALARAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 696 LKAPGIILLDEATSALD------TSNE-RAIQASLakvcaNRTTIVVAHRLS---TVvnADQILVIKDGCIVERGRHEAL 765
Cdd:COG3842   151 APEPRVLLLDEPLSALDaklreeMREElRRLQREL-----GITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223

                  ...
gi 1169100883 766 LSR 768
Cdd:COG3842   224 YER 226
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
544-754 1.68e-38

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: 141.17  E-value: 1.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS--LRSHIG 621
Cdd:cd03229     1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLF-NDTIADNIRYGrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPG 700
Cdd:cd03229    80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:cd03229   121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
544-754 2.37e-38

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: 141.45  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE----TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGciridgqdisqvtQASLRSH 619
Cdd:cd03250     1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------------SVSVPGS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDTVLFNDTIADNI---------RYGRVtagndeVEAAAqaagIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVA 690
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENIlfgkpfdeeRYEKV------IKACA----LEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 691 IARTILKAPGIILLDEATSALD--TSN---ERAIQASLAKvcaNRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03250   138 LARAVYSDADIYLLDDPLSAVDahVGRhifENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNG 203
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
543-750 4.68e-38

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 142.54  E-value: 4.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvtqasLRSH 619
Cdd:COG1116     7 ALELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDTVLFN-DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPegyrtqvGErglkLSGGEKQRVAIA 692
Cdd:COG1116    82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARellelvGLAGFEDAYP-------HQ----LSGGMRQRVAIA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH------RLstvvnADQILV 750
Cdd:COG1116   151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVV 211
PLN03232 PLN03232
ABC transporter C family member; Provisional
517-770 2.49e-37

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 151.28  E-value: 2.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  517 NMFDLLKEETEV--KDLPGAG-PLRfqkGRIEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFR 592
Cdd:PLN03232  1208 NYIDLPSEATAIieNNRPVSGwPSR---GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  593 FYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIryGRVTAGND-EVEAAAQAAGIHDAIMAFPEGYR 671
Cdd:PLN03232  1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI--DPFSEHNDaDLWEALERAHIKDVIDRNPFGLD 1362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  672 TQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVI 751
Cdd:PLN03232  1363 AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVL 1442
                          250
                   ....*....|....*....
gi 1169100883  752 KDGCIVERGRHEALLSRGG 770
Cdd:PLN03232  1443 SSGQVLEYDSPQELLSRDT 1461
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
544-761 2.96e-37

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 142.91  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILR---LLFRFydiSSGCIRIDGQDISQVTQASL- 616
Cdd:COG1135     2 IELENLSKTFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLERP---TSGSVLVDGVDLTALSERELr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 --RSHIGVVPQDtvlFN----DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGG 684
Cdd:COG1135    79 aaRRKIGMIFQH---FNllssRTVAENVALPLEIAGVPKAEIRKRVAellelvGLSDKADAYPS-----------QLSGG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNRT---TIVVA-HRLStVVN--ADQILVIKDGCIVE 758
Cdd:COG1135   145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRElglTIVLItHEMD-VVRriCDRVAVLENGRIVE 221

                  ...
gi 1169100883 759 RGR 761
Cdd:COG1135   222 QGP 224
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
544-765 3.23e-37

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: 139.63  E-value: 3.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHI 620
Cdd:cd03256     1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRVTAGN-----------DEVEAAAQA---AGIHDaiMAFpegyrtqvgERGLKLSGGE 685
Cdd:cd03256    81 GMIFQQFNLIERlSVLENVLSGRLGRRStwrslfglfpkEEKQRALAAlerVGLLD--KAY---------QRADQLSGGQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 686 KQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVV-NADQILVIKDGCIVERGRH 762
Cdd:cd03256   150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPP 229

                  ...
gi 1169100883 763 EAL 765
Cdd:cd03256   230 AEL 232
PTZ00243 PTZ00243
ABC transporter; Provisional
532-775 5.80e-37

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 150.31  E-value: 5.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  532 PGAGPLRFQKGRIEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 610
Cdd:PTZ00243  1297 TSAAPHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA 1376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  611 VTQASLRSHIGVVPQDTVLFNDTIADNIRyGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVA 690
Cdd:PTZ00243  1377 YGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMC 1455
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  691 IARTILK-APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGR-HEALLSR 768
Cdd:PTZ00243  1456 MARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSpRELVMNR 1535

                   ....*..
gi 1169100883  769 GGVYADM 775
Cdd:PTZ00243  1536 QSIFHSM 1542
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
542-773 1.53e-36

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: 138.50  E-value: 1.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03288    18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIRYGRvTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPG 700
Cdd:cd03288    98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR-GGVYA 773
Cdd:cd03288   177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFA 250
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
544-756 4.42e-36

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: 134.06  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRSHIGVV 623
Cdd:cd03230     1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNirygrvtagndeveaaaqaagihdaimafpegyrtqvgergLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03230    79 PEEPSLYENlTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCI 756
Cdd:cd03230   118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
544-767 6.80e-36

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 136.44  E-value: 6.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK13548    3 LEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVL-FNDTIADNIRYGRV--TAGNDEVEAAAQAAgihdaiMAfpegyrtQVGERGLK------LSGGEKQRVAIART 694
Cdd:PRK13548   82 PQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAA------LA-------QVDLAHLAgrdypqLSGGEQQRVQLARV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 695 IL------KAPGIILLDEATSALDTSNERAIqASLAKVCANR---TTIVVAHRLstvvN-----ADQILVIKDGCIVERG 760
Cdd:PRK13548  149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHV-LRLARQLAHErglAVIVVLHDL----NlaaryADRIVLLHQGRLVADG 223

                  ....*..
gi 1169100883 761 RHEALLS 767
Cdd:PRK13548  224 TPAEVLT 230
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
545-752 7.99e-36

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 134.58  E-value: 7.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHIGVVP 624
Cdd:cd03235     1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QDTVL---FNDTIADNIRYGRVTAGN----------DEVEAAAQAAGIhdaimafpEGYRT-QVGErglkLSGGEKQRVA 690
Cdd:cd03235    75 QRRSIdrdFPISVRDVVLMGLYGHKGlfrrlskadkAKVDEALERVGL--------SELADrQIGE----LSGGQQQRVL 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVN-ADQILVIK 752
Cdd:cd03235   143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEyFDRVLLLN 206
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
544-756 1.10e-35

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: 134.19  E-value: 1.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA--SLRSHIG 621
Cdd:cd03262     1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLF-NDTIADNIRYGRVTAGN---DEVEAAAQAA----GIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIAR 693
Cdd:cd03262    80 MVFQQFNLFpHLTVLENITLAPIKVKGmskAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAIAR 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 694 TILKAPGIILLDEATSALD--TSNE-RAIQASLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCI 756
Cdd:cd03262   149 ALAMNPKVMLFDEPTSALDpeLVGEvLDVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
544-768 3.00e-35

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: 133.97  E-value: 3.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:cd03295     1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIryGRVTAGNDEVEAAAQAAGihDAIMAF----PEGYRTQVGErglKLSGGEKQRVAIARTILKA 698
Cdd:cd03295    81 IQQIGLFpHMTVEENI--ALVPKLLKWPKEKIRERA--DELLALvgldPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKV--CANRTTIVVAHRL-STVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:cd03295   154 PPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
534-760 3.20e-35

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 134.39  E-value: 3.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 534 AGPLRFQKGRIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDI 608
Cdd:COG1117     2 TAPASTLEPKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 609 --SQVTQASLRSHIGVVPQDTVLFNDTIADNIRYG-RVtAGN------DE-VEAAAQAAGIHDaimafpegyrtQVGER- 677
Cdd:COG1117    81 ydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlRL-HGIkskselDEiVEESLRKAALWD-----------EVKDRl 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 678 ---GLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAH------RLStvvnaDQI 748
Cdd:COG1117   149 kksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYT 223
                         250
                  ....*....|..
gi 1169100883 749 LVIKDGCIVERG 760
Cdd:COG1117   224 AFFYLGELVEFG 235
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
544-761 1.14e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 133.19  E-value: 1.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK13632    8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYG----RVTAG--NDEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIART 694
Cdd:PRK13632   88 IFQnpDNQFIGATVEDDIAFGlenkKVPPKkmKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQA---SLAKVcANRTTIVVAHRLSTVVNADQILVIKDGCIVERGR 761
Cdd:PRK13632  157 LALNPEIIIFDESTSMLDPKGKREIKKimvDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
PLN03130 PLN03130
ABC transporter C family member; Provisional
516-777 2.01e-34

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 142.18  E-value: 2.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  516 ENMFDLLKEETEVKDLPGAGPLRFQ----------KGRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKS 584
Cdd:PLN03130  1200 ENSLNAVERVGTYIDLPSEAPLVIEnnrpppgwpsSGSIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKS 1279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  585 TILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIryGRVTAGND-EVEAAAQAAGIHDAI 663
Cdd:PLN03130  1280 SMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL--DPFNEHNDaDLWESLERAHLKDVI 1357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  664 MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLA---KVCanrTTIVVAHRLS 740
Cdd:PLN03130  1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIReefKSC---TMLIIAHRLN 1434
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1169100883  741 TVVNADQILVIKDGCIVERGRHEALLSR-GGVYADMWQ 777
Cdd:PLN03130  1435 TIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFSKMVQ 1472
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
544-768 5.18e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 131.40  E-value: 5.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK13647    5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAG------NDEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTI 695
Cdd:PRK13647   85 FQdpDDQVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13647  154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
547-757 9.84e-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: 128.53  E-value: 9.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtQASLRSHIGVVPQD 626
Cdd:cd03226     3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 T--VLFNDTIADNIRYG--RVTAGNDEVEAAAQAAGIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03226    80 VdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 703 LLDEATSALDTSNERAIqASLAKVCANRTT--IVVAHR---LSTVvnADQILVIKDGCIV 757
Cdd:cd03226   149 IFDEPTSGLDYKNMERV-GELIRELAAQGKavIVITHDyefLAKV--CDRVLLLANGAIV 205
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
542-757 1.82e-33

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 132.12  E-value: 1.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRsHIG 621
Cdd:COG3839     2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL-PPKDR-NIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLF-NDTIADNIRYG----RVTAG--NDEVEAAAQAAGIhdaimafpegyrTQVGERglK---LSGGEKQRVAI 691
Cdd:COG3839    79 MVFQSYALYpHMTVYENIAFPlklrKVPKAeiDRRVREAAELLGL------------EDLLDR--KpkqLSGGQRQRVAL 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 692 ARTILKAPGIILLDEATSALD------TSNE-RAIQASLakvcaNRTTIVVAH------RLstvvnADQILVIKDGCIV 757
Cdd:COG3839   145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQ 213
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
560-766 4.73e-33

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 128.53  E-value: 4.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL----RSHIGVVPQDTVLF-NDTI 634
Cdd:cd03294    40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:cd03294   120 LENVAFGLEVQGVPRAEREERAAealelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 709 SALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALL 766
Cdd:cd03294   189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
544-768 5.31e-33

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: 129.79  E-value: 5.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQ---DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYD---ISSGCIRIDGQDISQVTQASLR 617
Cdd:COG0444     2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 S----HIGVVPQD---------TVLfnDTIADNIRYGRVtAGNDEVEAAAQAA----GIHDAimafpegyrtqvgERGLK 680
Cdd:COG0444    82 KirgrEIQMIFQDpmtslnpvmTVG--DQIAEPLRIHGG-LSKAEARERAIELlervGLPDP-------------ERRLD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 -----LSGGEKQRVAIARTILKAPGIILLDEATSALDTSneraIQAS----LAKVCANR-TTIV-VAHRLSTVVN-ADQI 748
Cdd:COG0444   146 rypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVT----IQAQilnlLKDLQRELgLAILfITHDLGVVAEiADRV 221
                         250       260
                  ....*....|....*....|
gi 1169100883 749 LVIKDGCIVERGRHEALLSR 768
Cdd:COG0444   222 AVMYAGRIVEEGPVEELFEN 241
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
544-767 6.04e-33

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 127.92  E-value: 6.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG4559     2 LEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVL-FNDTIADNIRYGRVTAGNDeveaAAQAAGIHDAIMAfpegyrtQVGERGLK------LSGGEKQRVAIAR--- 693
Cdd:COG4559    81 PQHSSLaFPFTVEEVVALGRAPHGSS----AAQDRQIVREALA-------LVGLAHLAgrsyqtLSGGEQQRVQLARvla 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 ----TILKAPGIILLDEATSALDTSNERAIqASLAKVCANRTTIVVA--HRLstvvN-----ADQILVIKDGCIVERGRH 762
Cdd:COG4559   150 qlwePVDGGPRWLFLDEPTSALDLAHQHAV-LRLARQLARRGGGVVAvlHDL----NlaaqyADRILLLHQGRLVAQGTP 224

                  ....*
gi 1169100883 763 EALLS 767
Cdd:COG4559   225 EEVLT 229
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
544-769 8.30e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 128.21  E-value: 8.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK13635    6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYGRVTAG--NDE----VEAAAQAAGIHDaiMAFPEGYRtqvgerglkLSGGEKQRVAIART 694
Cdd:PRK13635   86 VFQnpDNQFVGATVQDDVAFGLENIGvpREEmverVDQALRQVGMED--FLNREPHR---------LSGGQKQRVAIAGV 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13635  155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
544-768 2.24e-32

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 125.64  E-value: 2.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYadGRETLQdVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRShIGVV 623
Cdd:COG3840     2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSML 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYG-----RVTAGN-DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTIL 696
Cdd:COG3840    77 FQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG3840   146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
544-761 2.37e-32

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 128.77  E-value: 2.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGR---ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS-- 618
Cdd:PRK11153    2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 -HIGVVPQDtvlFN----DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQ 687
Cdd:PRK11153   82 rQIGMIFQH---FNllssRTVFDNVALPLELAGTPKAEIKARVTellelvGLSDKADRYPA-----------QLSGGQKQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNRT---TIV-VAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK11153  148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRElglTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
560-768 5.39e-32

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: 124.37  E-value: 5.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVVPQDTVLF-NDTIADNI 638
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 639 RYGRVTAGNDEVEaaaqaagIHDAIMAFPE--GYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNE 716
Cdd:cd03299    93 AYGLKKRKVDKKE-------IERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 717 RAIQASLAKV--CANRTTIVVAHRLSTV-VNADQILVIKDGCIVERGRHEALLSR 768
Cdd:cd03299   166 EKLREELKKIrkEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
544-769 2.21e-31

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: 123.69  E-value: 2.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQasLRSH 619
Cdd:TIGR04520   1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWE--IRKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQ--DTVLFNDTIADNIRYGRVTAG--NDE----VEAAAQAAGIhdaimafpEGYRTQVGERglkLSGGEKQRVAI 691
Cdd:TIGR04520  79 VGMVFQnpDNQFVGATVEDDVAFGLENLGvpREEmrkrVDEALKLVGM--------EDFRDREPHL---LSGGQKQRVAI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRG 769
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
544-768 2.77e-31

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 125.64  E-value: 2.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqVTQASLRSHIGVV 623
Cdd:COG1118     3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYG-RVtAGNDEVEAAA---------QAAGIHDAimafpegYRTQvgerglkLSGGEKQRVAIA 692
Cdd:COG1118    81 FQHYALFpHMTVAENIAFGlRV-RPPSKAEIRArveellelvQLEGLADR-------YPSQ-------LSGGQRQRVALA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH------RLstvvnADQILVIKDGCIVERGRHEA 764
Cdd:COG1118   146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220

                  ....
gi 1169100883 765 LLSR 768
Cdd:COG1118   221 VYDR 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
543-760 3.75e-31

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: 120.73  E-value: 3.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENV-----HFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISQvtqAS 615
Cdd:cd03213     3 TLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQDTVLF-NDTIADNIRYgrvtagndeveaaaqAAGIhdaimafpegyrtqvgeRGLklSGGEKQRVAIART 694
Cdd:cd03213    80 FRKIIGYVPQDDILHpTLTVRETLMF---------------AAKL-----------------RGL--SGGERKRVSIALE 125
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAHRLSTVV--NADQILVIKDGCIVERG 760
Cdd:cd03213   126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
231-498 4.34e-31

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 123.14  E-value: 4.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLkflqgGGTGSTGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHEL 310
Cdd:pfam00664  13 AISPAFPLVLGRILDVLLPDGDPETQALNVYSLALL-----LLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 311 SLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIyFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRT 390
Cdd:pfam00664  88 PMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGII-VMFYYGWKLTLVLLAVLPLYILVSAVFAKILR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 391 KFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLC 470
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFG 246
                         250       260
                  ....*....|....*....|....*...
gi 1169100883 471 AYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:pfam00664 247 AYLVISGELSVGDLVAFLSLFAQLFGPL 274
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
544-760 9.75e-31

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: 119.99  E-value: 9.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTlALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAsLRSHIGVV 623
Cdd:cd03264     1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQD-------TVL-FNDTIA--DNIRYGRVTAgndEVEAAAQAAGIHDAimafpegYRTQVGerglKLSGGEKQRVAIAR 693
Cdd:cd03264    78 PQEfgvypnfTVReFLDYIAwlKGIPSKEVKA---RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQ 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTV-VNADQILVIKDGCIVERG 760
Cdd:cd03264   144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
cbiO PRK13650
energy-coupling factor transporter ATPase;
544-770 1.77e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 121.38  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE--TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:PRK13650    5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAG------NDEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:PRK13650   85 MVFQnpDNQFVGATVEDDVAFGLENKGipheemKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
544-767 1.85e-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: 119.46  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqaSLRSH---- 619
Cdd:cd03224     1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPPHerar 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 --IGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAqaagihDAIMA-FP---EGYRTQVGErglkLSGGEKQRVAIA 692
Cdd:cd03224    75 agIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARL------ERVYElFPrlkERRKQLAGT----LSGGEQQMLAIA 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV----AHRLSTVvnADQILVIKDGCIVERGRHEALLS 767
Cdd:cd03224   145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
560-768 2.21e-30

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: 126.34  E-value: 2.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQA---SLRSHIGVVPQD------ 626
Cdd:COG4172   302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfgsls 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 ---TVLfnDTIADNIRYGRVTAGNDEVEAAAQAA----GIHDAIMA-FP-EgyrtqvgerglkLSGGEKQRVAIART-IL 696
Cdd:COG4172   377 prmTVG--QIIAEGLRVHGPGLSAAERRARVAEAleevGLDPAARHrYPhE------------FSGGQRQRIAIARAlIL 442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 697 KaPGIILLDEATSALDtsneRAIQAS----LAKVCANR--TTIVVAHRLStVVNA--DQILVIKDGCIVERGRHEALLSR 768
Cdd:COG4172   443 E-PKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVFDA 516
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
560-767 8.37e-30

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 120.99  E-value: 8.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHIGVVPQD---------T 627
Cdd:COG4608    34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDpyaslnprmT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VlfNDTIADNIRYGRVTAGnDEVEAAAQaagihdAIMAfpegyrtQVgerGLK----------LSGGEKQRVAIARTILK 697
Cdd:COG4608   114 V--GDIIAEPLRIHGLASK-AERRERVA------ELLE-------LV---GLRpehadrypheFSGGQRQRIGIARALAL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 698 APGIILLDEATSALDTSneraIQA-------------SLakvcanrTTIVVAHRLStVVN--ADQILVIKDGCIVERG-- 760
Cdd:COG4608   175 NPKLIVCDEPVSALDVS----IQAqvlnlledlqdelGL-------TYLFISHDLS-VVRhiSDRVAVMYLGKIVEIApr 242
                         250
                  ....*....|....*..
gi 1169100883 761 -------RH---EALLS 767
Cdd:COG4608   243 delyarpLHpytQALLS 259
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
544-761 1.66e-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: 117.34  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03300     1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVTAGNDEveaAAQAAGIHDAI-MAFPEGYRtqvGERGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03300    78 FQNYALFPHlTVFENIAFGLRLKKLPK---AEIKERVAEALdLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKV 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLS-TVVNADQILVIKDGCIVERGR 761
Cdd:cd03300   152 LLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
543-753 2.01e-29

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: 116.04  E-value: 2.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRSHIGV 622
Cdd:COG4133     2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFND-TIADNIRY----GRVTAGNDEVEAAAQAAGIhdaimafpEGYR-TQVGerglKLSGGEKQRVAIARTIL 696
Cdd:COG4133    80 LGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGL--------AGLAdLPVR----QLSAGQKRRVALARLLL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKD 753
Cdd:COG4133   148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
544-760 4.40e-29

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: 115.54  E-value: 4.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQ---DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRSHI 620
Cdd:cd03266     2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRY-GRV-----TAGNDEVEAAAQAAGIHDAImafpegyrtqvGERGLKLSGGEKQRVAIAR 693
Cdd:cd03266    81 GFVSDSTGLYDRlTARENLEYfAGLyglkgDELTARLEELADRLGMEELL-----------DRRVGGFSTGMRQKVAIAR 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03266   150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
542-759 4.68e-29

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: 125.02  E-value: 4.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  542 GRIEFENVHFSYA-DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQASLRSHI 620
Cdd:TIGR01271 1216 GQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAF 1294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  621 GVVPQDTVLFNDTIADNIR-YGRVTagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDpYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  700 GIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIkDGCIVER 759
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVI-EGSSVKQ 1431
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
544-760 8.26e-29

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 114.66  E-value: 8.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRShIGVV 623
Cdd:cd03301     1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDE------VEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTIL 696
Cdd:cd03301    78 FQNYALYpHMTVYDNIAFGLKLRKVPKdeiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAH-RLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03301   147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
544-764 8.76e-29

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: 115.22  E-value: 8.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLR 617
Cdd:COG4181     9 IELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarARLR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 S-HIGVVPQD-------TVLFNdtiadnirygrVT-----AGNDEVEAAAQAA----GIHDAIMAFPEGyrtqvgerglk 680
Cdd:COG4181    89 ArHVGFVFQSfqllptlTALEN-----------VMlplelAGRRDARARARALlervGLGHRLDHYPAQ----------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR-TTIV-VAHRLSTVVNADQILVIKDGCIVE 758
Cdd:COG4181   147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVlVTHDPALAARCDRVLRLRAGRLVE 226

                  ....*.
gi 1169100883 759 RGRHEA 764
Cdd:COG4181   227 DTAATA 232
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
553-739 9.39e-29

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 115.64  E-value: 9.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 553 YADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQASLRSHIGVVPQ 625
Cdd:PRK14239   14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFNDTIADNIRYGRVTAG-------NDEVEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:PRK14239   94 QPNPFPMSIYENVVYGLRLKGikdkqvlDEAVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATS 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRL 739
Cdd:PRK14239  167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
542-793 1.01e-28

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: 116.49  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYAD-GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISsGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03289     1 GQMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIR-YGRVTagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:cd03289    80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVY------A 773
Cdd:cd03289   158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFkqaispS 237
                         250       260
                  ....*....|....*....|
gi 1169100883 774 DMWQLQQGQEETSEDTKPQT 793
Cdd:cd03289   238 DRLKLFPRRNSSKSKRKPRP 257
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
544-766 1.10e-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: 115.57  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGC-IRIDGQDISQVTQASLRSHIGV 622
Cdd:COG1119     4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 V---------PQDTVL------FNDTIAdniRYGRVTagnDEVEAAAqaagihDAIMAFpegyrtqVGERGLK------L 681
Cdd:COG1119    83 VspalqlrfpRDETVLdvvlsgFFDSIG---LYREPT---DEQRERA------RELLEL-------LGLAHLAdrpfgtL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 682 SGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR-TTIV-VAHRLSTVVNA-DQILVIKDGCIVE 758
Cdd:COG1119   144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIPPGiTHVLLLKDGRVVA 223

                  ....*...
gi 1169100883 759 RGRHEALL 766
Cdd:COG1119   224 AGPKEEVL 231
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
560-758 2.16e-28

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 119.74  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGVVPQDTVLFND-TIADN 637
Cdd:COG1129    20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAEN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 638 IRYGR--VTAG---NDEVEAAAQAA----GIH-DAimafpegyRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:COG1129   100 IFLGRepRRGGlidWRAMRRRARELlarlGLDiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 708 TSALdTSNERAI-QASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:COG1129   168 TASL-TEREVERlFRIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVG 220
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
544-769 4.26e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 114.46  E-value: 4.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK13648    8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYG---RVTAGNDEVEAAAQAagIHDAIMAFPEGYRTQvgerglKLSGGEKQRVAIARTILK 697
Cdd:PRK13648   88 VFQnpDNQFVGSIVKYDVAFGlenHAVPYDEMHRRVSEA--LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLAL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13648  160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
544-757 6.51e-28

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: 110.21  E-value: 6.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGV 622
Cdd:cd03216     1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQdtvlfndtiadnirygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03216    80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIV 757
Cdd:cd03216   105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
544-774 9.55e-28

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: 120.82  E-value: 9.55e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  544 IEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqaslrshIGV 622
Cdd:TIGR00957  637 ITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAY 703
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  623 VPQDTVLFNDTIADNIRYGRVTAGNdEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:TIGR00957  704 VPQQAWIQNDSLRENILFGKALNEK-YYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883  703 LLDEATSALDTSNERAIQASL---AKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYAD 774
Cdd:TIGR00957  783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE 857
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
545-767 1.17e-27

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: 112.00  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqaSLRSH----- 619
Cdd:COG0410     5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-----GLPPHriarl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 -IGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQaagihDAIMA-FP--EGYRTQvgeRGLKLSGGEKQRVAIART 694
Cdd:COG0410    79 gIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYElFPrlKERRRQ---RAGTLSGGEQQMLAIGRA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV----AHRLSTVvnADQILVIKDGCIVERGRHEALLS 767
Cdd:COG0410   151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
544-756 1.59e-27

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 115.04  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRsHIGVV 623
Cdd:PRK09452   15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNTV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYG----RVtaGNDEVEAAaqaagIHDAI-MAFPEGYRTQvgeRGLKLSGGEKQRVAIARTILK 697
Cdd:PRK09452   92 FQSYALFpHMTVFENVAFGlrmqKT--PAAEITPR-----VMEALrMVQLEEFAQR---KPHQLSGGQQQRVAIARAVVN 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 698 APGIILLDEATSALD------TSNE-RAIQASLakvcaNRTTIVVAH----RLSTvvnADQILVIKDGCI 756
Cdd:PRK09452  162 KPKVLLLDESLSALDyklrkqMQNElKALQRKL-----GITFVFVTHdqeeALTM---SDRIVVMRDGRI 223
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
544-765 1.80e-27

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 111.64  E-value: 1.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQA----SLR 617
Cdd:COG4161     3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVV-------PQDTVLFNDTIADNirygRVtAGNDEVEAAAQAAGI------HDAIMAFPegyrtqvgergLKLSGG 684
Cdd:COG4161    82 QKVGMVfqqynlwPHLTVMENLIEAPC----KV-LGLSKEQAREKAMKLlarlrlTDKADRFP-----------LHLSGG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTsnerAIQASLAKVCANR-----TTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:COG4161   146 QQQRVAIARALMMEPQVLLFDEPTAALDP----EITAQVVEIIRELsqtgiTQVIVTHEVEFARKvASQVVYMEKGRIIE 221

                  ....*..
gi 1169100883 759 RGRHEAL 765
Cdd:COG4161   222 QGDASHF 228
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
544-717 2.07e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 110.96  E-value: 2.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK10247    8 LQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADN------IRygrvtagNDEVEAAAQAAGIhdAIMAFPEgyrTQVGERGLKLSGGEKQRVAIARTILK 697
Cdd:PRK10247   87 AQTPTLFGDTVYDNlifpwqIR-------NQQPDPAIFLDDL--ERFALPD---TILTKNIAELSGGEKQRISLIRNLQF 154
                         170       180
                  ....*....|....*....|
gi 1169100883 698 APGIILLDEATSALDTSNER 717
Cdd:PRK10247  155 MPKVLLLDEITSALDESNKH 174
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
564-767 2.52e-27

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 110.83  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 564 SFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVVPQDTVLFND-TIADNIRYG- 641
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 642 ----RVTAGN-DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNE 716
Cdd:PRK10771   97 npglKLNAAQrEKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 717 RAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK10771  166 QEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
548-760 2.68e-27

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: 110.46  E-value: 2.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETLqDVSFTVmPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdISQVTQASL-----RSHIGV 622
Cdd:cd03297     3 CVDIEKRLPDFTL-KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLF-NDTIADNIRYGRVTAGNDE----VEAAAQAAGIhdaimafpegyrTQVGERG-LKLSGGEKQRVAIARTIL 696
Cdd:cd03297    80 VFQQYALFpHLNVRENLAFGLKRKRNREdrisVDELLDLLGL------------DHLLNRYpAQLSGGEKQRVALARALA 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03297   148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
544-760 4.17e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 111.71  E-value: 4.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL--RSHIG 621
Cdd:PRK13639    2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAG--NDEVEA----AAQAAGIhdaimafpEGYRTQVGERglkLSGGEKQRVAIAR 693
Cdd:PRK13639   82 IVFQnpDDQLFAPTVEEDVAFGPLNLGlsKEEVEKrvkeALKAVGM--------EGFENKPPHH---LSGGQKKRVAIAG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTV-VNADQILVIKDGCIVERG 760
Cdd:PRK13639  151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
560-754 6.74e-27

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: 109.45  E-value: 6.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI--DGQDISqVTQAS------LRSH-IGVVPQdtvlF 630
Cdd:COG4778    27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVD-LAQASpreilaLRRRtIGYVSQ----F 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 NDTIAdnirygRVTA-----------GNDEVEAAAQAAgihdAIMAfpegyRTQVGERGLKL-----SGGEKQRVAIART 694
Cdd:COG4778   102 LRVIP------RVSAldvvaepllerGVDREEARARAR----ELLA-----RLNLPERLWDLppatfSGGEQQRVNIARG 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDG 754
Cdd:COG4778   167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
544-712 8.69e-27

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 109.19  E-value: 8.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---LRSHI 620
Cdd:PRK10908    2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRVTAGNDE------VEAAAQAAGIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIAR 693
Cdd:PRK10908   82 GMIFQDHHLLMDrTVYDNVAIPLIIAGASGddirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
                         170
                  ....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALD 712
Cdd:PRK10908  151 AVVNKPAVLLADEPTGNLD 169
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
544-739 1.07e-26

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 110.26  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCiRIDGQDI--------SQVTQAS 615
Cdd:PRK14243   11 LRTENLNVYYGSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQDTVLFNDTIADNIRYG-RVTA--GN-DE-VEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRVA 690
Cdd:PRK14243   89 VRRRIGMVFQKPNPFPKSIYDNIAYGaRINGykGDmDElVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLC 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRL 739
Cdd:PRK14243  162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
cbiO PRK13640
energy-coupling factor transporter ATPase;
544-768 1.11e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 110.66  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRL---LFRFYDISSGCIRIDGQDISQVTQASLRSH 619
Cdd:PRK13640    6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQ--DTVLFNDTIADNIRYG---RVTAGNDEVEAAAQA---AGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAI 691
Cdd:PRK13640   86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVladVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13640  155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
544-760 1.16e-26

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: 108.35  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdgrETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03298     1 VRLDKIRFSYG---EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRV-----TAGNDE-VEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTIL 696
Cdd:cd03298    76 FQENNLFAHlTVEQNVGLGLSpglklTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03298   145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
544-754 3.33e-26

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: 107.42  E-value: 3.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCI----RIDGQDISQVTQASLRSH 619
Cdd:cd03290     1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDTVLFNDTIADNIRYGRvTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:cd03290    81 VAYAAQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 700 GIILLDEATSALDTS-NERAIQASLAKVCAN--RTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03290   160 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
562-783 3.94e-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: 110.58  E-value: 3.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 562 DVSFTVMPGQTLALVGPSGAGKSTILRL---LFRFydiSSGCIRIDG---QDISQVTqaSLRSH---IGVVPQDTVLFND 632
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGevlQDSARGI--FLPPHrrrIGYVFQEARLFPH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 -TIADNIRYG--RVTAGNDEV--EAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:COG4148    92 lSVRGNLLYGrkRAPRAERRIsfDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEP 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 708 TSALDTSNERAIQASLAKVCAN-RTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRggvyADMWQLQQGQE 783
Cdd:COG4148   161 LAALDLARKAEILPYLERLRDElDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR----PDLLPLAGGEE 235
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
556-767 1.53e-25

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 106.37  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIR-----ID-----GQDISQVTQasLRSHIGVVPQ 625
Cdd:PRK11264   15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDtarslSQQKGLIRQ--LRQHVGFVFQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLF-NDTIADNIRYGRVTAGNDEVEAAAQAA-------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILK 697
Cdd:PRK11264   93 NFNLFpHRTVLENIIEGPVIVKGEPKEEATARArellakvGLAGKETSYPR-----------RLSGGQQQRVAIARALAM 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQA---SLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK11264  162 RPEVILFDEPTSALDPELVGEVLNtirQLAQ--EKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
544-754 1.84e-25

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: 105.28  E-value: 1.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRSHIGV 622
Cdd:cd03263     1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFND-TIADNIR-YGRV-----TAGNDEVEAAAQAAGIHDaimafpegYR-TQVGErglkLSGGEKQRVAIART 694
Cdd:cd03263    80 CPQFDALFDElTVREHLRfYARLkglpkSEIKEEVELLLRVLGLTD--------KAnKRART----LSGGMKRKLSLAIA 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:cd03263   148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
544-760 2.11e-25

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: 104.67  E-value: 2.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqvtQASLRSHIGVV 623
Cdd:cd03269     1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQaagIHDAIMAFP-EGYRTQVGErglKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03269    76 PEERGLYPKmKVIDQLVYLAQLKGLKKEEARRR---IDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPEL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03269   150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
542-754 2.46e-25

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 111.44  E-value: 2.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISqvtqaslrshi 620
Cdd:COG4178   361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------- 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 gVVPQDTVLFNDTIADNIRYGRVTA--GNDEVEAAAQAAGIHDAIMAFPEGYR-TQVgerglkLSGGEKQRVAIARTILK 697
Cdd:COG4178   430 -FLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLH 502
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:COG4178   503 KPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
544-764 5.18e-25

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 104.71  E-value: 5.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQA----SLR 617
Cdd:PRK11124    3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkairELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVV-------PQDTVLFNDTIADNirygRVtAGNDEVEAAAQAAGI------HDAIMAFPegyrtqvgergLKLSGG 684
Cdd:PRK11124   82 RNVGMVfqqynlwPHLTVQQNLIEAPC----RV-LGLSKDQALARAEKLlerlrlKPYADRFP-----------LHLSGG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALD---TSNERAIQASLAKVcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK11124  146 QQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAET--GITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223

                  ....
gi 1169100883 761 RHEA 764
Cdd:PRK11124  224 DASC 227
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
560-761 6.52e-25

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: 104.06  E-value: 6.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRSHIGVVP--QDTVLFND-TIAD 636
Cdd:cd03219    16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGRtfQIPRLFPElTVLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRygrvtagndeveAAAQAAGIHDAIMAFPEGYRTQVGER--------GL---------KLSGGEKQRVAIARTILKAP 699
Cdd:cd03219    95 NVM------------VAAQARTGSGLLLARARREEREARERaeellervGLadladrpagELSYGQQRRLEIARALATDP 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:cd03219   163 KLLLLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
544-767 7.28e-25

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 108.01  E-value: 7.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK09536    4 IDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVL-FNDTIADNIRYGRV----------TAGNDEVEAAAQAAGIhdaimafpegyrTQVGERGL-KLSGGEKQRVAI 691
Cdd:PRK09536   83 PQDTSLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGV------------AQFADRPVtSLSGGERQRVLL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNE-RAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK09536  151 ARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
555-714 7.95e-25

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 102.95  E-value: 7.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL-------FRFydisSGCIRIDGQDISQVtQASLRsHIGVVPQDT 627
Cdd:COG4136    12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFSA----SGEVLLNGRRLTAL-PAEQR-RIGILFQDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VLF-NDTIADNIRYG---RVTAGN--DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGI 701
Cdd:COG4136    86 LLFpHLSVGENLAFAlppTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRA 154
                         170
                  ....*....|...
gi 1169100883 702 ILLDEATSALDTS 714
Cdd:COG4136   155 LLLDEPFSKLDAA 167
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
560-768 1.16e-24

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 105.82  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQASLRSHIGVVPQDTvlfndtiad 636
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 nirYG----RVTAG---------NDEVEAAAQAAGIHdAIMAfpegyrtQVgerGLK----------LSGGEKQRVAIAR 693
Cdd:PRK11308  102 ---YGslnpRKKVGqileeplliNTSLSAAERREKAL-AMMA-------KV---GLRpehydryphmFSGGQRQRIAIAR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALDTSneraIQASLAKVCAN-----RTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGRHEALL 766
Cdd:PRK11308  168 ALMLDPDVVVADEPVSALDVS----VQAQVLNLMMDlqqelGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 243

                  ..
gi 1169100883 767 SR 768
Cdd:PRK11308  244 NN 245
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
560-754 1.21e-24

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: 104.55  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqaslrshIGVVPQDTVLFNDTIADNIR 639
Cdd:cd03291    53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENII 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 YGrVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAI 719
Cdd:cd03291   120 FG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1169100883 720 -QASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03291   199 fESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
544-768 1.23e-24

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 103.25  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQASLRSHIG 621
Cdd:PRK09493    2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIA-DNIRYG-RVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:PRK09493   81 MVFQQFYLFPHLTAlENVMFGpLRVRGASKEEAEKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKP 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 700 GIILLDEATSALDTS--NE--RAIQaSLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK09493  156 KLMLFDEPTSALDPElrHEvlKVMQ-DLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
219-516 1.34e-24

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 104.55  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd07346     1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRA-------LLSYLRRYLAARLGQRVVFD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd07346    74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVL-TLIGALVILFYLNWKLTLVALLLLPLY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEW-RTKFRRAMNTQENATrARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNL 457
Cdd:cd07346   153 VLILRYFRRRiRKASREVRESLAELS-AFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 458 VIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDME 516
Cdd:cd07346   232 LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
544-761 2.38e-24

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 102.85  E-value: 2.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG4604     2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDtvlfND-----TIADNI---RY----GRVTAgNDEveaaaqaAGIHDAIMAFP-EGYRtqvgERGLK-LSGGEKQRV 689
Cdd:COG4604    81 RQE----NHinsrlTVRELVafgRFpyskGRLTA-EDR-------EIIDEAIAYLDlEDLA----DRYLDeLSGGQRQRA 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:COG4604   145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
cbiO PRK13649
energy-coupling factor transporter ATPase;
544-761 4.25e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 102.90  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----AS 615
Cdd:PRK13649    3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQA------AGIHDAIMafpegyrtqvGERGLKLSGGEKQ 687
Cdd:PRK13649   83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAreklalVGISESLF----------EKNPFELSGGQMR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK13649  153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
544-760 4.87e-24

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: 101.65  E-value: 4.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03296     3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYG-RVTAGNDEVEAAAQAAGIHD-----AIMAFPEGYRTQvgerglkLSGGEKQRVAIARTIL 696
Cdd:cd03296    80 FQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHEllklvQLDWLADRYPAQ-------LSGGQRQRVALARALA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03296   153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVG 219
cbiO PRK13642
energy-coupling factor transporter ATPase;
544-767 5.71e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 102.48  E-value: 5.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET--LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:PRK13642    5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQaagIHDAIMAFPE-GYRTQVGERglkLSGGEKQRVAIARTILKA 698
Cdd:PRK13642   85 MVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKR---VDEALLAVNMlDFKTREPAR---LSGGQKQRVAVAGIIALR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKV--CANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK13642  159 PEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
544-760 7.23e-24

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 104.01  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRsHIGVV 623
Cdd:PRK10851    3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HARDR-KVGFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYG-RVTAGNDEVEAAAqaagIHDAIMAFPEGYR-TQVGER-GLKLSGGEKQRVAIARTILKAP 699
Cdd:PRK10851   80 FQHYALFRHmTVFDNIAFGlTVLPRRERPNAAA----IKAKVTQLLEMVQlAHLADRyPAQLSGGQKQRVALARALAVEP 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK10851  156 QILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAG 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
544-760 7.70e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 102.43  E-value: 7.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS--QVTQASLR 617
Cdd:PRK13637    3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQ--DTVLFNDTIADNIRYGRVTAG------NDEVEAAAQAAGIHdaimafPEGYRTQvgeRGLKLSGGEKQRV 689
Cdd:PRK13637   83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGlseeeiENRVKRAMNIVGLD------YEDYKDK---SPFELSGGQKRRV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIqasLAKVCA-----NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13637  154 AIAGVVAMEPKILILDEPTAGLDPKGRDEI---LNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
544-760 8.94e-24

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 101.24  E-value: 8.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK11231    3 LRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVT--------AGNDE--VEAAAQAAGIhdaimafpegyrTQVGERGL-KLSGGEKQRVAI 691
Cdd:PRK11231   82 PQHHLTPEGiTVRELVAYGRSPwlslwgrlSAEDNarVNQAMEQTRI------------NHLADRRLtDLSGGQRQRAFL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNeraiQASLAKVC-----ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK11231  150 AMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQG 220
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
524-758 1.13e-23

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.53  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 524 EETEVKDLPGAGPLRFQKGR------IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS 597
Cdd:COG0488   290 EREEPPRRDKTVEIRFPPPErlgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 598 SGCIRIdGQDIsqvtqaslrsHIGVVPQDTVLF--NDTIADNIRYGRvtAGNDEVEAAAQAAGihdaiMAFPegyrtqvG 675
Cdd:COG0488   369 SGTVKL-GETV----------KIGYFDQHQEELdpDKTVLDELRDGA--PGGTEQEVRGYLGR-----FLFS-------G 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 676 ERGLK----LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAK----VcanrttIVVAH-R--LSTVvn 744
Cdd:COG0488   424 DDAFKpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV-- 495
                         250
                  ....*....|....
gi 1169100883 745 ADQILVIKDGCIVE 758
Cdd:COG0488   496 ATRILEFEDGGVRE 509
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
544-757 1.42e-23

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 106.35  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---- 616
Cdd:PRK10535    5 LELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTI 695
Cdd:PRK10535   85 REHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARAL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:PRK10535  160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
544-768 2.04e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 101.03  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK13652    4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAGNDE------VEAAAQAAGIHDaimafpegYRTQVGERglkLSGGEKQRVAIARTI 695
Cdd:PRK13652   84 FQnpDDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEE--------LRDRVPHH---LSGGEKKRVAIAGVI 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13652  153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
544-785 2.77e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 100.86  E-value: 2.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA----S 615
Cdd:PRK13634    3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHdAIMAFPEGYRTQvgeRGLKLSGGEKQRVAIAR 693
Cdd:PRK13634   83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMI-ELVGLPEELLAR---SPFELSGGQMRRVAIAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGg 770
Cdd:PRK13634  159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP- 237
                         250
                  ....*....|....*
gi 1169100883 771 vyADMWQLQQGQEET 785
Cdd:PRK13634  238 --DELEAIGLDLPET 250
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
556-760 5.51e-23

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: 97.67  E-value: 5.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqVTQASLRSHIGVVPQDTVLF-NDTI 634
Cdd:cd03268    12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYpNLTA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAG--NDEVEAAAQAAGIHDAimafpegYRTQVGerglKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:cd03268    90 RENLRLLARLLGirKKRIDEVLDVVGLKDS-------AKKKVK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169100883 713 TSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03268   159 PDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
553-754 1.02e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 97.58  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 553 YADGR---ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT---QASLRSH-IGVVPQ 625
Cdd:PRK11629   15 YQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFND-TIADNIRYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILL 704
Cdd:PRK11629   95 FHHLLPDfTALENVAMPLLIGKKKPAEINSRALEMLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 705 DEATSALDTSNERAIQASLAKVCANRTT--IVVAHRLSTVVNADQILVIKDG 754
Cdd:PRK11629  170 DEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDG 221
cbiO PRK13646
energy-coupling factor transporter ATPase;
544-778 1.38e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 98.70  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----AS 615
Cdd:PRK13646    3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagiHDAIMAFpeGYRTQVGERG-LKLSGGEKQRVAIA 692
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA---HRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAK--VCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13646  158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237

                  ....*....
gi 1169100883 770 GVYADmWQL 778
Cdd:PRK13646  238 KKLAD-WHI 245
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
544-766 2.10e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 99.52  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRSHIGVV 623
Cdd:PRK13536   42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ-DTVLFNDTIADNI----RYGRVTAgnDEVEAAAQaagihdAIMAFPEgYRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:PRK13536  120 PQfDNLDLEFTVRENLlvfgRYFGMST--REIEAVIP------SLLEFAR-LESKADARVSDLSGGMKRRLTLARALIND 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV-------AHRLstvvnADQILVIKDGCIVERGRHEALL 766
Cdd:PRK13536  191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
545-765 2.20e-22

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: 96.44  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVV 623
Cdd:TIGR03410   2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITkLPPHERARAGIAYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGrvtagndeveAAAQAAG---IHDAIMA-FPEgYRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:TIGR03410  81 PQGREIFPRlTVEENLLTG----------LAALPRRsrkIPDEIYElFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
544-763 2.95e-22

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 99.52  E-value: 2.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqASLRSHIGVV 623
Cdd:PRK11607   20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGrvtAGNDEVEAAAQAAGIHDaiMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:PRK11607   97 FQSYALFpHMTVEQNIAFG---LKQDKLPKAEIASRVNE--MLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 703 LLDEATSALDTSNERAIQAS----LAKVCAnrTTIVVAH-RLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:PRK11607  172 LLDEPMGALDKKLRDRMQLEvvdiLERVGV--TCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE 235
cbiO PRK13641
energy-coupling factor transporter ATPase;
544-767 3.77e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 97.59  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA----S 615
Cdd:PRK13641    3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQA------AGIHDAIMAfpegyrtqvgERGLKLSGGEKQ 687
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKAlkwlkkVGLSEDLIS----------KSPFELSGGQMR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALD-TSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:PRK13641  153 RVAIAGVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232

                  ..
gi 1169100883 766 LS 767
Cdd:PRK13641  233 FS 234
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
560-767 4.20e-22

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 99.34  E-value: 4.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS----HIGVVPQDTVLF-NDTI 634
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGNDEVEAAAQA------AGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:PRK10070  124 LDNTAFGMELAGINAEERREKAldalrqVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 709 SALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK10070  193 SALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
544-768 4.29e-22

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 100.91  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQ---DVSFTVMPGQTLALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQASL 616
Cdd:COG4172     7 LSVEDLSVAFGQGGGTVEavkGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 R----SHIGVVPQD--TVLfND--TIADNIRYG-RVTAGNDEVEAAAQAA------GIHDA---IMAFPEgyrtqvgerg 678
Cdd:COG4172    87 RrirgNRIAMIFQEpmTSL-NPlhTIGKQIAEVlRLHRGLSGAAARARALellervGIPDPerrLDAYPH---------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 lKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTT--IVVAHRLSTVVN-ADQILVIKDGC 755
Cdd:COG4172   156 -QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMalLLITHDLGVVRRfADRVAVMRQGE 234
                         250
                  ....*....|...
gi 1169100883 756 IVERGRHEALLSR 768
Cdd:COG4172   235 IVEQGPTAELFAA 247
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
560-754 7.56e-22

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: 101.91  E-value: 7.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqaslrshIGVVPQDTVLFNDTIADNIR 639
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  640 YGrVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAI 719
Cdd:TIGR01271  509 FG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1169100883  720 -QASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:TIGR01271  588 fESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
544-742 9.02e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 95.87  E-value: 9.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS-----GCIRIDGQDI--SQVTQASL 616
Cdd:PRK14258    8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFNDTIADNIRYGRVTAG-------NDEVEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRV 689
Cdd:PRK14258   87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASL--AKVCANRTTIVVAHRLSTV 742
Cdd:PRK14258  160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQV 214
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
551-767 1.15e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 95.11  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ------DISQVTQASLRSHIGVVP 624
Cdd:PRK14246   17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QDTVLF-NDTIADNIRYGRVTAGNDE-------VEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRVAIARTIL 696
Cdd:PRK14246   97 QQPNPFpHLSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLWKEV-------YDRLNSPASQLSGGQQQRLTIARALA 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK14246  170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
548-761 1.21e-21

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 97.41  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETlQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRShIGVVPQDT 627
Cdd:PRK11000    8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RG-VGMVFQSY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VLF-NDTIADNIRYGRVTAGNDEVEAAA---QAAGIhdaimafpegyrTQVG---ERGLK-LSGGEKQRVAIARTILKAP 699
Cdd:PRK11000   85 ALYpHLSVAENMSFGLKLAGAKKEEINQrvnQVAEV------------LQLAhllDRKPKaLSGGQRQRVAIGRTLVAEP 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH-RLSTVVNADQILVIKDGCIVERGR 761
Cdd:PRK11000  153 SVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
544-753 1.36e-21

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: 92.22  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGqdisqvtqaslRSHIGVV 623
Cdd:cd03223     1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADNIRY--GRVtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03223    70 PQRPYLPLGTLREQLIYpwDDV-------------------------------------LSGGEQQRLAFARLLLHKPKF 112
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCAnrTTIVVAHRLSTVVNADQILVIKD 753
Cdd:cd03223   113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDG 162
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
544-770 1.38e-21

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 95.95  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqaslRSHIGVV 623
Cdd:COG4152     2 LELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRY-GRVTaGNDEVEAAAQAagihDAIMAfpegyRTQVGERGLK----LSGGEKQRVAIARTILK 697
Cdd:COG4152    77 PEERGLYpKMKVGEQLVYlARLK-GLSKAEAKRRA----DEWLE-----RLGLGDRANKkveeLSKGNQQKVQLIAALLH 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:COG4152   147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFG 221
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
562-769 1.43e-21

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: 97.10  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 562 DVSFTVmPGQTL-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDG---QDISQVTQASL-RSHIGVVPQDTVLFND-TIA 635
Cdd:TIGR02142  15 DADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPPeKRRIGYVFQEARLFPHlSVR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRYGRVTAGNDEVEAAaqaagiHDAIMAFpEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSN 715
Cdd:TIGR02142  94 GNLRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 716 ERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRG 769
Cdd:TIGR02142 167 KYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
544-760 2.35e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 94.91  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQASLRSHIG 621
Cdd:PRK13636    6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagihDAIMAfpegyRTQVGERGLK----LSGGEKQRVAIARTI 695
Cdd:PRK13636   86 MVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV----DNALK-----RTGIEHLKDKpthcLSFGQKKRVAIAGVL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 696 LKAPGIILLDEATSALD---TSNERAIQASLAKVcANRTTIVVAHRLSTV-VNADQILVIKDGCIVERG 760
Cdd:PRK13636  157 VMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKE-LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQG 224
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
560-751 3.11e-21

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: 93.95  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRSHIGVVP--QDTVLFND-TIAD 636
Cdd:COG0411    20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-PPHRIARLGIARtfQNPRLFPElTVLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRYGRVTAGN---------------DEVEAAAQAagihDAIMAFP--EGYR-TQVGErglkLSGGEKQRVAIARTILKA 698
Cdd:COG0411    99 NVLVAAHARLGrgllaallrlprarrEEREARERA----EELLERVglADRAdEPAGN----LSYGQQRRLEIARALATE 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVI 751
Cdd:COG0411   171 PKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVL 226
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
545-760 3.23e-21

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 93.59  E-value: 3.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISQ--VTQaslRSHI 620
Cdd:COG0396     2 EIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILElsPDE---RARA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GV---------VPQDTVL-FNDTIADNIRYGRVTAG--NDEVEAAAQAAGIHDAIMafpegyrtqvgERGL--KLSGGEK 686
Cdd:COG0396    78 GIflafqypveIPGVSVSnFLRTALNARRGEELSARefLKLLKEKMKELGLDEDFL-----------DRYVneGFSGGEK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALDTSnerAIQAsLAKVC-----ANRTTIVVAH--RLSTVVNADQILVIKDGCIVER 759
Cdd:COG0396   147 KRNEILQMLLLEPKLAILDETDSGLDID---ALRI-VAEGVnklrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKS 222

                  .
gi 1169100883 760 G 760
Cdd:COG0396   223 G 223
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
543-726 3.81e-21

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 93.77  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVTQASLRSh 619
Cdd:COG4525     3 MLTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 iGVVPQDTVLFN-DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIA 692
Cdd:COG4525    79 -GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEellalvGLADFARRRI-----------WQLSGGMRQRVGIA 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKV 726
Cdd:COG4525   147 RALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
PLN03232 PLN03232
ABC transporter C family member; Provisional
494-787 5.60e-21

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 98.89  E-value: 5.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  494 LYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVkdLPGAGPLRFQKGRIEFENVHFSYADGRE--TLQDVSFTVMPGQ 571
Cdd:PLN03232   567 LRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI--LAQNPPLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEIPVGS 644
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  572 TLALVGPSGAGKSTILR-LLFRFYDISSGCIRIdgqdisqvtqaslRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEV 650
Cdd:PLN03232   645 LVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFESERYW 711
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  651 EAAAQAAGIHDAIMaFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAK-VCAN 729
Cdd:PLN03232   712 RAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdELKG 790
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883  730 RTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSE 787
Cdd:PLN03232   791 KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQE 848
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
544-768 6.94e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 94.10  E-value: 6.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRSHIGVV 623
Cdd:PRK13537    8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIR-YGRVTAgndevEAAAQAAGIHDAIMAFP---EGYRTQVGErglkLSGGEKQRVAIARTILKA 698
Cdd:PRK13537   86 PQFDNLDPDfTVRENLLvFGRYFG-----LSAAAARALVPPLLEFAkleNKADAKVGE----LSGGMKRRLTLARALVND 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV-------AHRLstvvnADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13537  157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALIES 228
PLN03130 PLN03130
ABC transporter C family member; Provisional
521-788 8.57e-21

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 98.66  E-value: 8.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  521 LLKEETEVKDLPgagPLRFQKGRIEFENVHFSY-ADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS 598
Cdd:PLN03130   595 LLAEERVLLPNP---PLEPGLPAISIKNGYFSWdSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  599 GciridgqdisqvTQASLRSHIGVVPQDTVLFNDTIADNIRYGrVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERG 678
Cdd:PLN03130   672 D------------ASVVIRGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERG 738
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAI-QASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:PLN03130   739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIK 818
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1169100883  758 ERGRHEALLSRGGVYADMWQLQQGQEETSED 788
Cdd:PLN03130   819 EEGTYEELSNNGPLFQKLMENAGKMEEYVEE 849
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
556-725 2.41e-20

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 89.93  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGvvPQDTVLFNDTIA 635
Cdd:PRK13539   14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRYGRVTAGNDE--VEAAAQAAGIHDaIMAFPEGYrtqvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDT 713
Cdd:PRK13539   92 ENLEFWAAFLGGEEldIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
                         170
                  ....*....|....*.
gi 1169100883 714 SNERA----IQASLAK 725
Cdd:PRK13539  161 AAVALfaelIRAHLAQ 176
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
546-712 3.81e-20

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 94.75  E-value: 3.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 546 FENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqasLRshIGVVPQ 625
Cdd:COG0488     1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFND-TIADNI-----------------------------RYGRVTAGNDEV---EAAAQAAGIHDAiMAFPEGYRT 672
Cdd:COG0488    69 EPPLDDDlTVLDTVldgdaelraleaeleeleaklaepdedleRLAELQEEFEALggwEAEARAEEILSG-LGFPEEDLD 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1169100883 673 Q-VGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:COG0488   148 RpVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
544-760 4.31e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 91.30  E-value: 4.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET-----LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA-SLR 617
Cdd:PRK13633    5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQDTVlfNDTIAdnirygrvTAGNDEVEAAAQAAGIHdaimafPEGYRTQVGErGLK--------------LSG 683
Cdd:PRK13633   85 NKAGMVFQNPD--NQIVA--------TIVEEDVAFGPENLGIP------PEEIRERVDE-SLKkvgmyeyrrhaphlLSG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:PRK13633  148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
551-758 6.47e-20

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: 90.25  E-value: 6.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---LRSHIGVVPQD 626
Cdd:TIGR02769  17 LFGAKQRAPvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TV-LFN------DTIADNIR-YGRVtagnDEVEAAAQAAGIHDAImafpeGYRTQVGER-GLKLSGGEKQRVAIARTILK 697
Cdd:TIGR02769  97 SPsAVNprmtvrQIIGEPLRhLTSL----DESEQKARIAELLDMV-----GLRSEDADKlPRQLSGGQLQRINIARALAV 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTT--IVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
560-767 7.09e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.00  E-value: 7.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQASL---RSHIGVVPQD------ 626
Cdd:PRK15134  302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnssln 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 ---TVLfnDTIADNIR--YGRVTAGNDE--VEAAAQAAGIHdaimafPEGYRTQVGErglkLSGGEKQRVAIARTILKAP 699
Cdd:PRK15134  377 prlNVL--QIIEEGLRvhQPTLSAAQREqqVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALILKP 444
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLStVVNA--DQILVIKDGCIVERGRHEALLS 767
Cdd:PRK15134  445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFA 515
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
544-712 8.92e-20

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 91.83  E-value: 8.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRShIGVV 623
Cdd:PRK11650    4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAMV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDEVEAA---AQAAGIHDaIMAFPEgyrtqvgERGLKLSGGEKQRVAIARTILKAP 699
Cdd:PRK11650   82 FQNYALYpHMSVRENMAYGLKIRGMPKAEIEervAEAARILE-LEPLLD-------RKPRELSGGQRQRVAMGRAIVREP 153
                         170
                  ....*....|...
gi 1169100883 700 GIILLDEATSALD 712
Cdd:PRK11650  154 AVFLFDEPLSNLD 166
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
544-763 1.17e-19

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: 87.97  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTqASLRSHIG 621
Cdd:cd03217     1 LEIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VvpqdTVLFND-------TIADNIRYgrvtagndeveaaaqaagihdaimafpegyrtqVGErglKLSGGEKQRVAIART 694
Cdd:cd03217    79 I----FLAFQYppeipgvKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQL 118
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAK-VCANRTTIVVAH--RLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:cd03217   119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
PTZ00243 PTZ00243
ABC transporter; Provisional
557-775 1.27e-19

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 94.85  E-value: 1.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDgqdisqvtqaslRShIGVVPQDTVLFNDTIAD 636
Cdd:PTZ00243   673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRG 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  637 NIRYgrvtagNDEveaaAQAAGIHDAI---------MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:PTZ00243   740 NILF------FDE----EDAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883  708 TSALDTS-NERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLsRGGVYADM 775
Cdd:PTZ00243   810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL 877
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
560-737 1.50e-19

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: 88.10  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQdisQVTQASLRSHIGVVPQ-DTVLFNDTIA 635
Cdd:cd03234    23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPGLTVR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRY------GRVTAGNDEVEAAAQAAGIHDAImafpegyrTQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:cd03234   100 ETLTYtailrlPRKSSDAIRKKRVEDVLLRDLAL--------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPT 171
                         170       180       190
                  ....*....|....*....|....*....|
gi 1169100883 709 SALDTSNERAIQASLAKVCA-NRTTIVVAH 737
Cdd:cd03234   172 SGLDSFTALNLVSTLSQLARrNRIVILTIH 201
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
540-765 1.50e-19

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 90.93  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDisqVTQASLRSH 619
Cdd:PRK11432    3 QKNFVVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 -IGVVPQDTVLF-NDTIADNIRYGRVTAG--NDEV-EAAAQAAGIHDaIMAFPEGYRTQVgerglklSGGEKQRVAIART 694
Cdd:PRK11432   79 dICMVFQSYALFpHMSLGENVGYGLKMLGvpKEERkQRVKEALELVD-LAGFEDRYVDQI-------SGGQQQRVALARA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERA-------IQASLakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:PRK11432  151 LILKPKVLLFDEPLSNLDANLRRSmrekireLQQQF-----NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL 224
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
557-738 1.85e-19

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 87.71  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFY--DISSGCIRIDGQDISQvtqaslrshigvvpqdtvlfNDTI 634
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIryGRVTAGNDEVEAAAqAAGIHDAIMafpegYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTS 714
Cdd:COG2401   103 IDAI--GRKGDFKDAVELLN-AVGLSDAVL-----WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
                         170       180
                  ....*....|....*....|....*.
gi 1169100883 715 NERAIQASLAKVC--ANRTTIVVAHR 738
Cdd:COG2401   171 TAKRVARNLQKLArrAGITLVVATHH 196
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
542-706 2.32e-19

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 88.16  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTIlrllfrFYDI------SSGCIRIDGQDIsqvTQAS 615
Cdd:COG1137     2 MTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDI---THLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 L--RSH--IGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIhdaimafpEGYRTQvgeRGLKLSGG 684
Cdd:COG1137    72 MhkRARlgIGYLPQEASIFRKlTVEDNILAVLELRKLSKKEREERLEelleefGI--------THLRKS---KAYSLSGG 140
                         170       180
                  ....*....|....*....|..
gi 1169100883 685 EKQRVAIARTILKAPGIILLDE 706
Cdd:COG1137   141 ERRRVEIARALATNPKFILLDE 162
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
543-763 2.61e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 88.05  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGrETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDISQVTQASLR 617
Cdd:PRK14247    3 KIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQ-DTVLFNDTIADNIRYG----RVTAGNDEVEA----AAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQR 688
Cdd:PRK14247   82 RRVQMVFQiPNPIPNLSIFENVALGlklnRLVKSKKELQErvrwALEKAQLWDEV-------KDRLDAPAGKLSGGQQQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAH------RLStvvnaDQILVIKDGCIVERG-- 760
Cdd:PRK14247  155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGpt 229
                         250
                  ....*....|
gi 1169100883 761 -------RHE 763
Cdd:PRK14247  230 revftnpRHE 239
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
560-760 2.73e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 89.52  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILR-----LLFRFYDISSGCIRIdGQDISQVTQAS------------LRSHIGV 622
Cdd:PRK13631   42 LNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYI-GDKKNNHELITnpyskkiknfkeLRRRVSM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAaQAAGIHDAIMAFPEGYRtqvgERG-LKLSGGEKQRVAIARTILKAP 699
Cdd:PRK13631  121 VFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAK-KLAKFYLNKMGLDDSYL----ERSpFGLSGGQKRRVAIAGILAIQP 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 700 GIILLDEATSALDTSNERA-IQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13631  196 EILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
560-757 3.64e-19

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 91.63  E-value: 3.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVTQAS----LRSHIGVVPQDTVLFND-TI 634
Cdd:COG3845    21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIALGIGMVHQHFMLVPNlTV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAG---------NDEVEAAAQAAGIH---DAImafpegyrtqVGErglkLSGGEKQRVAIARTILKAPGII 702
Cdd:COG3845    98 AENIVLGLEPTKggrldrkaaRARIRELSERYGLDvdpDAK----------VED----LSVGEQQRVEILKALYRGARIL 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 703 LLDEATSALdTSNE-RAIQASLAKVCANRTTIV-VAHRLSTVV-NADQILVIKDGCIV 757
Cdd:COG3845   164 ILDEPTAVL-TPQEaDELFEILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
556-760 5.20e-19

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 87.29  E-value: 5.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---------RSHIGVVPQD 626
Cdd:PRK11701   18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQH 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TvlfndtiADNIR--------------------YGRV--TAGN--DEVEAAAqaAGIHDAIMAFpegyrtqvgerglklS 682
Cdd:PRK11701   98 P-------RDGLRmqvsaggnigerlmavgarhYGDIraTAGDwlERVEIDA--ARIDDLPTTF---------------S 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 683 GGEKQRVAIARTILKAPGIILLDEATSALDTSneraIQASLAKVCANRTT------IVVAHRLSTV-VNADQILVIKDGC 755
Cdd:PRK11701  154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVArLLAHRLLVMKQGR 229

                  ....*
gi 1169100883 756 IVERG 760
Cdd:PRK11701  230 VVESG 234
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
555-767 5.81e-19

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 87.20  E-value: 5.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRetLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQASLRSHIGVVPQDTV------ 628
Cdd:COG4138     9 AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSppfamp 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 629 ------LFNDTIADnirygrVTAGNDEVEAAAQAAGIHDAIMafpegyrtqvgeRGL-KLSGGEKQRVAIARTILKA-PG 700
Cdd:COG4138    86 vfqylaLHQPAGAS------SEAVEQLLAQLAEALGLEDKLS------------RPLtQLSGGEWQRVRLAAVLLQVwPT 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 701 I------ILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAHRLS-TVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:COG4138   148 InpegqlLLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
560-758 7.70e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 86.37  E-value: 7.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLRS-HIGVVPQDTVLFNDTIA 635
Cdd:PRK10584   26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAkHVGFVFQSFMLIPTLNA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 -DNIRYGRVTAGNDEVEAAAQAAGIHDAImafpegyrtQVGER----GLKLSGGEKQRVAIARTILKAPGIILLDEATSA 710
Cdd:PRK10584  106 lENVELPALLRGESSRQSRNGAKALLEQL---------GLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 711 LDTSNERAIQASLAKVcaNR----TTIVVAHRLSTVVNADQILVIKDGCIVE 758
Cdd:PRK10584  177 LDRQTGDKIADLLFSL--NRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
548-767 8.98e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 87.07  E-value: 8.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDISQVTQA-SLRSHIG 621
Cdd:PRK14271   26 NLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRVG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIADNIRYG---RVTAGNDEVEAAAQA----AGIHDAImafpegyRTQVGERGLKLSGGEKQRVAIART 694
Cdd:PRK14271  105 MLFQRPNPFPMSIMDNVLAGvraHKLVPRKEFRGVAQArlteVGLWDAV-------KDRLSDSPFRLSGGQQQLLCLART 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK14271  178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
540-763 1.63e-18

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 86.48  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLrsh 619
Cdd:PRK15056    3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDT-------VLFNDTIADNiRYG-----RVTAGNDE--VEAAAQAAGIHDaimafpegYR-TQVGErglkLSGG 684
Cdd:PRK15056   80 VAYVPQSEevdwsfpVLVEDVVMMG-RYGhmgwlRRAKKRDRqiVTAALARVDMVE--------FRhRQIGE----LSGG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:PRK15056  147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
544-760 1.64e-18

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 85.78  E-value: 1.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDISQVtQASLRSHIG 621
Cdd:TIGR01978   1 LKIKDLHVSVED-KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLEL-EPDERARAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 V---------VPQDTVLFNDTIADNIRygRVTAGNDEVEAAAQAAGIHD--AIMAFPEGYRtqvgERGLK--LSGGEKQR 688
Cdd:TIGR01978  79 LflafqypeeIPGVSNLEFLRSALNAR--RSARGEEPLDLLDFEKLLKEklALLDMDEEFL----NRSVNegFSGGEKKR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAH--RLSTVVNADQILVIKDGCIVERG 760
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
544-765 1.99e-18

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: 84.73  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRSHIGVV 623
Cdd:cd03265     1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQdtvlfnDTIADNIRYGRvtagnDEVEaaaqaagIHDAIMAFPEGYRTQVGERGLKL--------------SGGEKQRV 689
Cdd:cd03265    79 FQ------DLSVDDELTGW-----ENLY-------IHARLYGVPGAERRERIDELLDFvglleaadrlvktySGGMRRRL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVV-------AHRLstvvnADQILVIKDGCIVERGR 761
Cdd:cd03265   141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGT 215

                  ....
gi 1169100883 762 HEAL 765
Cdd:cd03265   216 PEEL 219
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
560-754 2.23e-18

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: 84.82  E-value: 2.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLrshigVVPQDTVLFN-DTIADNI 638
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 639 rYGRVTAGNDEVEAAAQAAGIHDAIMAFpeGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERA 718
Cdd:TIGR01184  76 -ALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1169100883 719 IQASLAKVC--ANRTTIVVAHRL-STVVNADQILVIKDG 754
Cdd:TIGR01184 153 LQEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
545-754 3.40e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 88.43  E-value: 3.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVV 623
Cdd:PRK11288    6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNI-------RYGRVTAGNDEVEAAAQAAGIHDAIMafPEgyrTQVGErglkLSGGEKQRVAIARTI 695
Cdd:PRK11288   85 YQELHLVPEmTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDID--PD---TPLKY----LSIGQRQMVEIAKAL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 696 LKAPGIILLDEATSALdTSNE-----RAIQASLAKvcaNRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK11288  156 ARNARVIAFDEPTSSL-SAREieqlfRVIRELRAE---GRVILYVSHRMEEIFAlCDAITVFKDG 216
cbiO PRK13644
energy-coupling factor transporter ATPase;
544-767 3.66e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 85.42  E-value: 3.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ-ASLRSHIGV 622
Cdd:PRK13644    2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYGR------VTAGNDEVEAAAQAAGIhdaimafpEGYRTQVGErglKLSGGEKQRVAIART 694
Cdd:PRK13644   82 VFQnpETQFVGRTVEEDLAFGPenlclpPIEIRKRVDRALAEIGL--------EKYRHRSPK---TLSGGQGQCVALAGI 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK13644  151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
555-751 4.12e-18

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 83.05  E-value: 4.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGCIRidgQDISQVTQASLRShIGVVPQDTVL---FN 631
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------AGVLR---PTSGTVRRAGGAR-VAYVPQRSEVpdsLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 DTIADNIRYG---------RVTAGN-DEVEAAAQAAGIHDAImafpegyRTQVGErglkLSGGEKQRVAIARTILKAPGI 701
Cdd:NF040873   72 LTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADL 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVNADQILVI 751
Cdd:NF040873  141 LLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
544-726 4.46e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 84.75  E-value: 4.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqaslrSHIGVV 623
Cdd:PRK11248    2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFN-DTIADNIRYGRVTAG--NDEVEAAAQAAGIHDAIMAFPEGYRTQvgerglkLSGGEKQRVAIARTILKAPG 700
Cdd:PRK11248   76 FQNEGLLPwRNVQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQ-------LSGGQRQRVGIARALAANPQ 148
                         170       180
                  ....*....|....*....|....*.
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKV 726
Cdd:PRK11248  149 LLLLDEPFGALDAFTREQMQTLLLKL 174
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
549-765 5.20e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 85.91  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 549 VHFSYADGR-------ETLQ---DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL-- 616
Cdd:PRK15079   16 VHFDIKDGKqwfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWra 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 -RSHIGVVPQD---------TVlfNDTIADNIRYGRVTAGNDEVEAAAQAagihdaiMAFPEGYRTQVGER-GLKLSGGE 685
Cdd:PRK15079   96 vRSDIQMIFQDplaslnprmTI--GEIIAEPLRTYHPKLSRQEVKDRVKA-------MMLKVGLLPNLINRyPHEFSGGQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 686 KQRVAIARTILKAPGIILLDEATSALDTSneraIQASLAKVCAN------RTTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:PRK15079  167 CQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQlqremgLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242

                  ....*..
gi 1169100883 759 RGRHEAL 765
Cdd:PRK15079  243 LGTYDEV 249
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
560-758 5.23e-18

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 84.74  E-value: 5.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHIGVVPQDTV-LFN--DT 633
Cdd:PRK10419   28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSIsAVNprKT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYG-RVTAGNDEVEAAAQAAGIHDAIMAFPEgyrtQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PRK10419  108 VREIIREPlRHLLSLDKAERLARASEMLRAVDLDDS----VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169100883 713 TSNERAIQASLAKVCANRTT--IVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:PRK10419  184 LVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
556-764 6.19e-18

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 87.77  E-value: 6.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQAsLRSHIGVVPQD----TVL 629
Cdd:COG1129   264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDA-IRAGIAYVPEDrkgeGLV 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 FNDTIADNI---RYGRVTAG-----NDEVEAAAQ--------AAGIHDAIMAfpegyrtqvgerglkLSGGEKQRVAIAR 693
Cdd:COG1129   343 LDLSIRENItlaSLDRLSRGglldrRRERALAEEyikrlrikTPSPEQPVGN---------------LSGGNQQKVVLAK 407
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAhrlST----VV-NADQILVIKDGCIV-ERGRHEA 764
Cdd:COG1129   408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpeLLgLSDRILVMREGRIVgELDREEA 481
cbiO PRK13645
energy-coupling factor transporter ATPase;
542-760 9.51e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 84.67  E-value: 9.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGR----ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG-------CIRIDGQDISQ 610
Cdd:PRK13645    5 KDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 611 VTQasLRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDaIMAFPEGYrtqVGERGLKLSGGEKQR 688
Cdd:PRK13645   85 VKR--LRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK-LVQLPEDY---VKRSPFELSGGQKRR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13645  159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIG 233
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
547-756 9.54e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 83.57  E-value: 9.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHIGVVPQD 626
Cdd:PRK11247   16 NAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFN-DTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGyrtqvgerglkLSGGEKQRVAIARTILKAPGIILLD 705
Cdd:PRK11247   90 ARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 706 EATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCI 756
Cdd:PRK11247  159 EPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAmADRVLLIEEGKI 212
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
544-719 1.17e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 83.24  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqasLRshIGVV 623
Cdd:PRK09544    5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLfNDTIADNI-RYGRVTAG---NDEVEAAA--QAAGIHDAIMAfpegyrtqvgerglKLSGGEKQRVAIARTILK 697
Cdd:PRK09544   73 PQKLYL-DTTLPLTVnRFLRLRPGtkkEDILPALKrvQAGHLIDAPMQ--------------KLSGGETQRVLLARALLN 137
                         170       180
                  ....*....|....*....|..
gi 1169100883 698 APGIILLDEATSALDTSNERAI 719
Cdd:PRK09544  138 RPQLLVLDEPTQGVDVNGQVAL 159
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
544-754 1.32e-17

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: 80.19  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQDISqvtqaslrshIGVV 623
Cdd:cd03221     1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQdtvlfndtiadnirygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGIIL 703
Cdd:cd03221    69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVcaNRTTIVVAH-R--LSTVvnADQILVIKDG 754
Cdd:cd03221    94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
544-712 1.34e-17

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: 82.59  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRSHIGV- 622
Cdd:cd03218     1 LRAENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-MHKRARLGIg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 -VPQDTVLFND-TIADNIRygrvtagndeveAAAQaagihdaIMAFPEGYRTQVGE--------------RGLKLSGGEK 686
Cdd:cd03218    79 yLPQEASIFRKlTVEENIL------------AVLE-------IRGLSKKEREEKLEelleefhithlrksKASSLSGGER 139
                         170       180
                  ....*....|....*....|....*.
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALD 712
Cdd:cd03218   140 RRVEIARALATNPKFLLLDEPFAGVD 165
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
544-760 2.17e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 82.58  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGrETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQASL 616
Cdd:PRK14267    5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLF-NDTIADNI----RYGRVTAGNDE----VEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQ 687
Cdd:PRK14267   84 RREVGMVFQYPNPFpHLTIYDNVaigvKLNGLVKSKKElderVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQ 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK14267  157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
543-760 3.02e-17

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 82.34  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYadGRETL-QDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:PRK10253    7 RLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFND-TIADNIRYGRV----------TAGNDEVEAAAQAAGIHDAimafpegyrtqVGERGLKLSGGEKQRVA 690
Cdd:PRK10253   85 LLAQNATTPGDiTVQELVARGRYphqplftrwrKEDEEAVTKAMQATGITHL-----------ADQSVDTLSGGQRQRAW 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNR----TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK10253  154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
560-754 5.91e-17

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: 79.40  E-value: 5.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-VTQASLRSHIGVVPQD---TVLFND-TI 634
Cdd:cd03215    16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPEDrkrEGLVLDlSV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIrygrvtagndeveaaaqAAGIHdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTS 714
Cdd:cd03215    96 AENI-----------------ALSSL--------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1169100883 715 NERAIQASLAKVCANRTTIVVahrLST-----VVNADQILVIKDG 754
Cdd:cd03215   139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEG 180
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
544-768 6.19e-17

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 84.85  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL--FRFYDISSG-----------CIRIDGQ---- 606
Cdd:TIGR03269   1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekCGYVERPskvg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 607 ------------------DISQVTQASLRSHIGVVPQDT-VLF-NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDaimaf 666
Cdd:TIGR03269  80 epcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 667 pegyRTQVGER----GLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAK-VCANRTTIVVAHRLST 741
Cdd:TIGR03269 155 ----MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPE 230
                         250       260
                  ....*....|....*....|....*....
gi 1169100883 742 VVN--ADQILVIKDGCIVERGRHEALLSR 768
Cdd:TIGR03269 231 VIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
557-767 7.54e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 84.37  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKS----TILRLLFR---FYdiSSGCIRIDGQDISQVTQASLR----SHIGVVPQ 625
Cdd:PRK15134   22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 D-TVLFN--DTIADNI-------RYGRVTAGNDEVEAAAQAAGIHDA---IMAFPEgyrtqvgerglKLSGGEKQRVAIA 692
Cdd:PRK15134  100 EpMVSLNplHTLEKQLyevlslhRGMRREAARGEILNCLDRVGIRQAakrLTDYPH-----------QLSGGERQRVMIA 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLA--KVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK15134  169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
547-712 9.56e-17

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 80.32  E-value: 9.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGVVPQ 625
Cdd:PRK10895    7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFND-TIADNIRygRVTAGNDEVEAAAQAAGIHDAIMAFP-EGYRTQVGErglKLSGGEKQRVAIARTILKAPGIIL 703
Cdd:PRK10895   86 EASIFRRlSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHiEHLRDSMGQ---SLSGGERRRVEIARALAANPKFIL 160

                  ....*....
gi 1169100883 704 LDEATSALD 712
Cdd:PRK10895  161 LDEPFAGVD 169
cbiO PRK13643
energy-coupling factor transporter ATPase;
544-760 1.06e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 81.32  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAD----GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---- 615
Cdd:PRK13643    2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERG-LKLSGGEKQRVAIA 692
Cdd:PRK13643   82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSpFELSGGQMRRVAIA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13643  157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
544-760 1.50e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 83.30  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA-SLRSHIGV 622
Cdd:PRK09700    6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFND-TIADNIRYGRVTA----GNDEVEAAAQAagIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILK 697
Cdd:PRK09700   85 IYQELSVIDElTVLENLYIGRHLTkkvcGVNIIDWREMR--VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK09700  163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
558-760 4.63e-16

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: 78.14  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRSHIGVV-PQDTVLFND-TIA 635
Cdd:cd03267    35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfGQKTQLWWDlPVI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYrTQVgeRglKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSN 715
Cdd:cd03267   114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLD-TPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1169100883 716 ERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03267   189 QENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
540-767 4.97e-16

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 78.86  E-value: 4.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA----- 614
Cdd:PRK10619    2 SENKLNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 --------SLRSHIGVVPQDtvlFNdtiadniRYGRVTAGNDEVEAAAQAAGIHDAIM-AFPEGYRTQVG--ERG----- 678
Cdd:PRK10619   81 vadknqlrLLRTRLTMVFQH---FN-------LWSHMTVLENVMEAPIQVLGLSKQEArERAVKYLAKVGidERAqgkyp 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALD---TSNERAIQASLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK10619  151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQG 228
                         250
                  ....*....|...
gi 1169100883 755 CIVERGRHEALLS 767
Cdd:PRK10619  229 KIEEEGAPEQLFG 241
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
563-767 5.80e-16

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: 81.77  E-value: 5.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG--CIRIdGQDISQVTQ------ASLRSHIGVVPQDTVLF-NDT 633
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRV-GDEWVDMTKpgpdgrGRAKRYIGILHQEYDLYpHRT 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYGRVTAGNDEVeaaAQAAGIHDAIMA-FPEGYRTQVGER-GLKLSGGEKQRVAIARTILKAPGIILLDEATSAL 711
Cdd:TIGR03269 382 VLDNLTEAIGLELPDEL---ARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 712 DTSNERAIQASL--AKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:TIGR03269 459 DPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
555-752 8.65e-16

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: 76.76  E-value: 8.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTI 634
Cdd:cd03231    11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGNDEVEAA-AQA--AGIHDAIMAfpegyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEATSAL 711
Cdd:cd03231    91 LENLRFWHADHSDEQVEEAlARVglNGFEDRPVA--------------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1169100883 712 DTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIK 752
Cdd:cd03231   157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
556-754 9.53e-16

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 82.37  E-value: 9.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsQVTQASLRSHIGVVPQDTVLFND-TI 634
Cdd:TIGR01257  942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTV 1020
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  635 ADNIRYGRVTAGND------EVEAAAQAAGIHDaimafpegyrtQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:TIGR01257 1021 AEHILFYAQLKGRSweeaqlEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1169100883  709 SALDTSNERAIQASLAKVCANRTTIVVAHRLSTV-VNADQILVIKDG 754
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQG 1136
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
556-759 1.22e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 80.43  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVVPQDTVLF-NDT 633
Cdd:PRK10762   16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIpQLT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYGR--VTA--GNDEVEAAAQAagihDAIMA---FPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDE 706
Cdd:PRK10762   96 IAENIFLGRefVNRfgRIDWKKMYAEA----DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 707 ATSAL-DTSNEraiqaSLAKVC----ANRTTIV-VAHRLSTVVN-ADQILVIKDG-CIVER 759
Cdd:PRK10762  168 PTDALtDTETE-----SLFRVIrelkSQGRGIVyISHRLKEIFEiCDDVTVFRDGqFIAER 223
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
560-714 1.27e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 81.05  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHIGVVPQD---------T 627
Cdd:PRK10261  340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDpyasldprqT 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VlfNDTIADNIRYGRVTAGNdevEAAAQAAGIHDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:PRK10261  420 V--GDSIMEPLRVHGLLPGK---AAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEA 490

                  ....*..
gi 1169100883 708 TSALDTS 714
Cdd:PRK10261  491 VSALDVS 497
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
547-766 1.91e-15

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 77.14  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQD 626
Cdd:PRK10575   15 RNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFND-TIADNIRYGRVTAgndeveaaaqaagiHDAIMAFPEGYRTQVGER----GLK---------LSGGEKQRVAIA 692
Cdd:PRK10575   94 LPAAEGmTVRELVAIGRYPW--------------HGALGRFGAADREKVEEAislvGLKplahrlvdsLSGGERQRAWIA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALL 766
Cdd:PRK10575  160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
544-760 2.07e-15

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 76.66  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY------------------ADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIR 602
Cdd:COG1134     5 IEVENVSKSYrlyhepsrslkelllrrrRTRREEfwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 603 IDGqdisqvTQASLrshIGV----VPQDTVlfndtiADNIR-----YGRVTAGNDEVEAAAQA-AGIHDAIMAfPegYRT 672
Cdd:COG1134    85 VNG------RVSAL---LELgagfHPELTG------RENIYlngrlLGLSRKEIDEKFDEIVEfAELGDFIDQ-P--VKT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTS-NERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILV 750
Cdd:COG1134   147 --------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIW 218
                         250
                  ....*....|
gi 1169100883 751 IKDGCIVERG 760
Cdd:COG1134   219 LEKGRLVMDG 228
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
543-765 2.61e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 77.43  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRET----LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS--- 615
Cdd:PRK13651    2 QIKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKeke 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 ---------------------LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDaIMAFPEGYRt 672
Cdd:PRK13651   82 kvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE-LVGLDESYL- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgERG-LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVN-ADQIL 749
Cdd:PRK13651  160 ---QRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTI 236
                         250
                  ....*....|....*..
gi 1169100883 750 VIKDGCIVERGR-HEAL 765
Cdd:PRK13651  237 FFKDGKIIKDGDtYDIL 253
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
559-763 2.98e-15

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 77.99  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 559 TLQDVSFTV---MPGQTL-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----ASLRSHIGVVPQDTVLF 630
Cdd:PRK11144    9 QLGDLCLTVnltLPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclPPEKRRIGYVFQDARLF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 -NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:PRK11144   89 pHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 710 ALDTSNERAIQASLAKVCAN-RTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGRHE 763
Cdd:PRK11144  158 SLDLPRKRELLPYLERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLE 214
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
558-760 3.62e-15

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 76.37  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqVTQASLRSH-IGVVPQDTvlfNDTIAD 636
Cdd:PRK15112   27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQrIRMIFQDP---STSLNP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRYGRVTAG----NDEVEAAAQAAGIHDAImafpegyrTQVGERG-------LKLSGGEKQRVAIARTILKAPGIILLD 705
Cdd:PRK15112  103 RQRISQILDFplrlNTDLEPEQREKQIIETL--------RQVGLLPdhasyypHMLAPGQKQRLGLARALILRPKVIIAD 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 706 EATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK15112  175 EALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
531-740 3.97e-15

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: 79.41  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 531 LPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD--- 607
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklf 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 608 -ISQ---VTQASLRshigvvpqDTVLFNDTIADNIRYGrvtAGNDEVEAAAQAAGIHDAIMAfpEGYRTQVGERGLKLSG 683
Cdd:TIGR00954 519 yVPQrpyMTLGTLR--------DQIIYPDSSEDMKRRG---LSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSG 585
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKvcANRTTIVVAHRLS 740
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
540-761 4.25e-15

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 75.69  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS-LRS 618
Cdd:PRK11614    2 EKVMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAaqaagIHDAIMAFPEGYRTQVgERGLKLSGGEKQRVAIARTILK 697
Cdd:PRK11614   81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRlstvvNADQILVIKD-GCIVERGR 761
Cdd:PRK11614  155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQ-----NANQALKLADrGYVLENGH 214
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
543-764 4.55e-15

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 78.53  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSH-IG 621
Cdd:COG3845   257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQD-----TVLfNDTIADNI---RYGRVTAGN----DEVEAAAQAAGIhdaIMAF---PEGYRTQVGerglKLSGGEK 686
Cdd:COG3845   337 YIPEDrlgrgLVP-DMSVAENLilgRYRRPPFSRggflDRKAIRAFAEEL---IEEFdvrTPGPDTPAR----SLSGGNQ 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTI-VVAHRLSTVVN-ADQILVIKDGCIV-ERGRHE 763
Cdd:COG3845   409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLISEDLDEILAlSDRIAVMYEGRIVgEVPAAE 488

                  .
gi 1169100883 764 A 764
Cdd:COG3845   489 A 489
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
560-760 6.19e-15

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 74.88  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqaSLRSHIGVVPQDTVLfndtiaDNIR 639
Cdd:cd03220    38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-----LLGLGGGFNPELTGR------ENIY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 -----YGRVTAGNDEVEaaaqaagihDAIMAFPE-GyrtQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:cd03220   107 lngrlLGLSRKEIDEKI---------DEIIEFSElG---DFIDLPVKtYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169100883 713 TS-NERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03220   175 AAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
560-757 9.24e-15

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 75.12  E-value: 9.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVL---FNDTIAD 636
Cdd:COG1101    22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 N--IRYGRvtagndeveaaAQAAGIHDAIM-AFPEGYRTQVGERGL-----------KLSGGEKQRVAIARTILKAPGII 702
Cdd:COG1101   102 NlaLAYRR-----------GKRRGLRRGLTkKRRELFRELLATLGLglenrldtkvgLLSGGQRQALSLLMATLTKPKLL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 703 LLDEATSALD--TSN------ERAIQASlakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIV 757
Cdd:COG1101   171 LLDEHTAALDpkTAAlvleltEKIVEEN------NLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
555-736 1.33e-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: 73.16  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTI 634
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRvtagndEVEAAAQAAgIHDAImafpegyrTQVGERGLK------LSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:TIGR01189  91 LENLHFWA------AIHGGAQRT-IEDAL--------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPT 155
                         170       180
                  ....*....|....*....|....*...
gi 1169100883 709 SALDTSNERAIQASLAKVCAnRTTIVVA 736
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLA-RGGIVLL 182
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
544-757 1.63e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 77.01  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSH---I 620
Cdd:PRK15439   12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHqlgI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLF-NDTIADNIRYG--RVTAGNDEVEAAAQAAGIH---DAIMAfpegyrtqvgerglKLSGGEKQRVAIART 694
Cdd:PRK15439   89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQldlDSSAG--------------SLEVADRQIVEILRG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIV 757
Cdd:PRK15439  155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIA 219
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
544-765 1.97e-14

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 74.42  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHI 620
Cdd:PRK11831    8 VDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRvtagndEVEAAAQAAGIHDAIMAFPEGyrtqVGERGL------KLSGGEKQRVAIAR 693
Cdd:PRK11831   87 SMLFQSGALFTDmNVFDNVAYPL------REHTQLPAPLLHSTVMMKLEA----VGLRGAaklmpsELSGGMARRAALAR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTsnerAIQASLAKVCANR------TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:PRK11831  157 AIALEPDLIMFDEPFVGQDP----ITMGVLVKLISELnsalgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
552-712 4.43e-14

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: 75.74  E-value: 4.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 552 SYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQASLRSHIGVVPQD----- 626
Cdd:TIGR03719  13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KDFNGEARPQPGIKVGYLPQEpqldp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 --TVLFN--DTIAD-----------NIRYGRVTAGND-------EVEAAAQAAGIHD-------AIMAF--PEGyRTQVG 675
Cdd:TIGR03719  82 tkTVRENveEGVAEikdaldrfneiSAKYAEPDADFDklaaeqaELQEIIDAADAWDldsqleiAMDALrcPPW-DADVT 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1169100883 676 erglKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:TIGR03719 161 ----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
543-768 5.22e-14

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 72.81  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYAdgRETLQDVSFTVMPGQTLALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISqvtQASLRS 618
Cdd:PRK10418    4 QIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 -HIGVVPQDT-VLFN--DTIADNIR-----YGRvTAGNDEVEAAAQAAGIHDAimafpegyrtqvgERGLKL-----SGG 684
Cdd:PRK10418   79 rKIATIMQNPrSAFNplHTMHTHARetclaLGK-PADDATLTAALEAVGLENA-------------ARVLKLypfemSGG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRT--TIVVAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK10418  145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGD 224

                  ....*..
gi 1169100883 762 HEALLSR 768
Cdd:PRK10418  225 VETLFNA 231
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
542-712 6.78e-14

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 75.37  E-value: 6.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRI--EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ-DISQVTQ--ASL 616
Cdd:PRK11147  316 GKIvfEMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQhrAEL 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RshigvvPQDTVLfnDTIADnirygrvtaGNDEVEAAAQAAGIHDAIMAF---PEGYRTQVGerglKLSGGEKQRVAIAR 693
Cdd:PRK11147  395 D------PEKTVM--DNLAE---------GKQEVMVNGRPRHVLGYLQDFlfhPKRAMTPVK----ALSGGERNRLLLAR 453
                         170
                  ....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALD 712
Cdd:PRK11147  454 LFLKPSNLLILDEPTNDLD 472
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
548-763 1.10e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 74.89  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGR-ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ----------DISQVTQASL 616
Cdd:PRK10261   19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 R----SHIGVVPQD--TVL-----FNDTIADNIrygRVTAGNDEVEAAAQAAGIHDAIMaFPEGyRTQVGERGLKLSGGE 685
Cdd:PRK10261   99 RhvrgADMAMIFQEpmTSLnpvftVGEQIAESI---RLHQGASREEAMVEAKRMLDQVR-IPEA-QTILSRYPHQLSGGM 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 686 KQRVAIARTILKAPGIILLDEATSALDTSneraIQA---SLAKVCANRTT---IVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:PRK10261  174 RQRVMIAMALSCRPAVLIADEPTTALDVT----IQAqilQLIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQGEAVE 249

                  ....*
gi 1169100883 759 RGRHE 763
Cdd:PRK10261  250 TGSVE 254
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
555-754 1.16e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 74.20  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDI-SQVTQASLRSHIGVVPQDTVLFN 631
Cdd:PRK13549   16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqASNIRDTERAGIAIIHQELALVK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 D-TIADNIRYGRvtagndEVEaaaqaagiHDAIMAFPEGYR----------------TQVGErglkLSGGEKQRVAIART 694
Cdd:PRK13549   96 ElSVLENIFLGN------EIT--------PGGIMDYDAMYLraqkllaqlkldinpaTPVGN----LGLGQQQLVEIAKA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 695 ILKAPGIILLDEATSALdTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK13549  158 LNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDG 219
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
544-741 2.00e-13

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: 73.82  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQaslrSHIGV 622
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ----SRDAL 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLfnDTIADNIRYGRVtaGNDEVEAAAQaagihdaIMAFP-EGYRTQ--VGErglkLSGGEKQRVAIARTiLKAP 699
Cdd:TIGR03719 398 DPNKTVW--EEISGGLDIIKL--GKREIPSRAY-------VGRFNfKGSDQQkkVGQ----LSGGERNRVHLAKT-LKSG 461
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 700 G-IILLDEATSALDTSNERAIQASLAKV--CAnrttIVVAH------RLST 741
Cdd:TIGR03719 462 GnVLLLDEPTNDLDVETLRALEEALLNFagCA----VVISHdrwfldRIAT 508
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
543-706 2.03e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 73.47  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK10522  322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADnirygrvtaGNDEVEAAAQAAGIHDAIMAfpEGYRTQVGE-RGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:PRK10522  402 VFTDFHLFDQLLGP---------EGKPANPALVEKWLERLKMA--HKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470

                  ....*
gi 1169100883 702 ILLDE 706
Cdd:PRK10522  471 LLLDE 475
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
563-767 2.09e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 70.73  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKSTilrLLFRFYDI--SSGCIRIDGQDISQVTQASLRSHIG-VVPQDTVLFNdtiADNIR 639
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFA---MPVFQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 Y--------GRVTAGNDEVEAAAQAAGIHDAImafpegyrtqvgERGL-KLSGGEKQRVAIARTILK-APGI------IL 703
Cdd:PRK03695   89 YltlhqpdkTRTEAVASALNEVAEALGLDDKL------------GRSVnQLSGGEWQRVRLAAVVLQvWPDInpagqlLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLS-TVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK03695  157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
558-754 5.58e-13

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 69.66  E-value: 5.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFY--DISSGC-IRIDGQDISQVTQASL-----RSHIGVVPQDTVL 629
Cdd:PRK09984   18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREGRLARdirksRANTGYIFQQFNL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 FND-TIADNIRYGRVTA-----------GNDEVEAAAQAAgihdaimafpegyrTQVG------ERGLKLSGGEKQRVAI 691
Cdd:PRK09984   98 VNRlSVLENVLIGALGStpfwrtcfswfTREQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQQQRVAI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK09984  164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQG 229
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
563-754 1.06e-12

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 68.86  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqvtqASLRSH----IGVVP--QDTVLFND-TIA 635
Cdd:PRK11300   24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-----EGLPGHqiarMGVVRtfQHVRLFREmTVI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNI---RYGRVTAG------------NDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTILKAPG 700
Cdd:PRK11300   99 ENLlvaQHQQLKTGlfsgllktpafrRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK11300  174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
560-761 1.71e-12

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 70.85  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLfRFYDIS----SGCIRIDGQ--DISQVTQASlrshiGVVPQD------- 626
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMpiDAKEMRAIS-----AYVQQDdlfiptl 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFNDTIADNIRYGRVTAGNDE---VEAAAQAAGIHDAimafpEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIIL 703
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKrerVDEVLQALGLRKC-----ANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLF 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVV--NADQILVIKDGCIVERGR 761
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELfeLFDKIILMAEGRVAYLGS 250
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
515-761 2.48e-12

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 68.98  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 515 MENMFDLLkeetEVKDLpgagplrfqkgriefeNVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKS----TILRL 589
Cdd:PRK09473    6 QQQADALL----DVKDL----------------RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 590 LFRFYDISsGCIRIDGQDISQVTQASL---RSHigvvpQDTVLFNDTIADNIRYGRVTA----------GNDEVEAAAQA 656
Cdd:PRK09473   66 LAANGRIG-GSATFNGREILNLPEKELnklRAE-----QISMIFQDPMTSLNPYMRVGEqlmevlmlhkGMSKAEAFEES 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 657 AGIHDAImAFPEGyRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL--AKVCANRTTIV 734
Cdd:PRK09473  140 VRMLDAV-KMPEA-RKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIM 217
                         250       260
                  ....*....|....*....|....*...
gi 1169100883 735 VAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK09473  218 ITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
544-737 4.42e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 69.38  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQ--DISQVTQaslrSHIG 621
Cdd:PRK11819  325 IEAENLSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDQ----SRDA 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLfnDTIADNIRYGRVtaGNDEVEAAAQAAgihdaimAFpeGYRTQ-----VGErglkLSGGEKQRVAIARTiL 696
Cdd:PRK11819  399 LDPNKTVW--EEISGGLDIIKV--GNREIPSRAYVG-------RF--NFKGGdqqkkVGV----LSGGERNRLHLAKT-L 460
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1169100883 697 KAPG-IILLDEATSALDTSNERAIQASLAKV--CAnrttIVVAH 737
Cdd:PRK11819  461 KQGGnVLLLDEPTNDLDVETLRALEEALLEFpgCA----VVISH 500
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
560-772 7.20e-12

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 67.42  E-value: 7.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfYDI---SSGCIRIDGQDISQvTQASLRSHIGVV------------P 624
Cdd:COG4586    38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKML---TGIlvpTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QDTVLFNDTIadnirYgRVtagnDEVEAAAQAA------GIHDAImafpegyRTQVgeRglKLSGGEKQRVAIARTILKA 698
Cdd:COG4586   114 IDSFRLLKAI-----Y-RI----PDAEYKKRLDelvellDLGELL-------DTPV--R--QLSLGQRMRCELAAALLHR 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANR-TTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGGVY 772
Cdd:COG4586   173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
541-754 7.71e-12

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: 64.96  E-value: 7.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 541 KGRIEFENVHFSYA---DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS--SGCIRIDGQDISQvtqaS 615
Cdd:cd03232     1 GSVLTWKNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----N 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQDTVLF-NDTIADNIRYgrvtagndeveaaaqAAGIhdaimafpegyrtqvgeRGLKLSggEKQRVAIART 694
Cdd:cd03232    77 FQRSTGYVEQQDVHSpNLTVREALRF---------------SALL-----------------RGLSVE--QRKRLTIGVE 122
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVV--NADQILVIKDG 754
Cdd:cd03232   123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASIfeKFDRLLLLKRG 185
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
553-712 8.11e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 68.61  E-value: 8.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 553 YADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQASLRSHIGVVPQD------ 626
Cdd:PRK11819   16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KEFEGEARPAPGIKVGYLPQEpqldpe 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 -TVLFN---------------DTIADNirYGRVTAGND-------EVEAAAQAAGIHD-------AIMAF--PEGyRTQV 674
Cdd:PRK11819   85 kTVRENveegvaevkaaldrfNEIYAA--YAEPDADFDalaaeqgELQEIIDAADAWDldsqleiAMDALrcPPW-DAKV 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1169100883 675 GerglKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PRK11819  162 T----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
219-502 1.42e-11

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 65.92  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18542     1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRG-------VFRYLQGYLAEKASQKVAYD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRiadRGTSSVTGL---LSYLVFNVIPTLAdIIIGIIYFSMFFNAWFGLIVFLCM 375
Cdd:cd18542    74 LRNDLYDHLQRLSFSFHDKARTGDLMS---RCTSDVDTIrrfLAFGLVELVRAVL-LFIGALIIMFSINWKLTLISLAII 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 376 SLYLTLTIVVtewRTKFRRA----------MNT--QENATRARavdsllnfeTVKYYNAESYEVER-------YREAIIK 436
Cdd:cd18542   150 PFIALFSYVF---FKKVRPAfeeireqegeLNTvlQENLTGVR---------VVKAFAREDYEIEKfdkeneeYRDLNIK 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 437 YQGLEWKSSASLVLLNQTQNLVIGLGllagsllCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFG 502
Cdd:cd18542   218 LAKLLAKYWPLMDFLSGLQIVLVLWV-------GGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
548-730 1.63e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 64.20  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDT 627
Cdd:PRK13540    6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VLFNDTIADNIRYgrvtagndEVEAAAQAAGIHDAIMAFPEGYRTQVgERGLkLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:PRK13540   85 INPYLTLRENCLY--------DIHFSPGAVGITELCRLFSLEHLIDY-PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEP 154
                         170       180
                  ....*....|....*....|...
gi 1169100883 708 TSALDtsnERAIQASLAKVCANR 730
Cdd:PRK13540  155 LVALD---ELSLLTIITKIQEHR 174
PLN03211 PLN03211
ABC transporter G-25; Provisional
557-765 2.21e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 67.21  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF-RFYDIS-SGCIRIDGQDIsqvTQASLRsHIGVVPQDTVLF-NDT 633
Cdd:PLN03211   81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKP---TKQILK-RTGFVTQDDILYpHLT 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNI------RYGRVTAGNDEVEAAAQAAgihdAIMAFPEGYRTQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDE 706
Cdd:PLN03211  157 VRETLvfcsllRLPKSLTKQEKILVAESVI----SELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 707 ATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVNA--DQILVIKDG-CIVERGRHEAL 765
Cdd:PLN03211  233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEGrCLFFGKGSDAM 295
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
231-487 4.24e-11

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 64.77  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIV-NLLTEKApWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRRVELLIFSHLHE 309
Cdd:cd18570    16 LLGIAGSFFFQILIdDIIPSGD-INLLNIISIGLILLYLFQS-------LLSYIRSYLLLKLSQKLDIRLILGYFKHLLK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 310 LSLRWHLGRRTGEVL-RIADrgTSSVTGLLSYLVFNV-IPTLADIIIGIIyfsMFFNAWF-GLIVFLCMSLYLTLTIVVT 386
Cdd:cd18570    88 LPLSFFETRKTGEIIsRFND--ANKIREAISSTTISLfLDLLMVIISGII---LFFYNWKlFLITLLIIPLYILIILLFN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 387 E-WRTKFRRAMntQENA-TRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLL 464
Cdd:cd18570   163 KpFKKKNREVM--ESNAeLNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
                         250       260
                  ....*....|....*....|...
gi 1169100883 465 AGSLLCAYFVTEQKLQVGDYVLF 487
Cdd:cd18570   241 LILWIGSYLVIKGQLSLGQLIAF 263
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
569-741 4.72e-11

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: 4.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  569 PGQTLALVGPSGAGKSTILRLLFRFYDISS-GCIRIDGQDISQVTQASLRSHIgvvpqdtvlfndtiadnirygrvtagn 647
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  648 deveaaaqaagihdaimafpegyrtqVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL---- 723
Cdd:smart00382  54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
                          170       180
                   ....*....|....*....|.
gi 1169100883  724 ---AKVCANRTTIVVAHRLST 741
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKD 128
GguA NF040905
sugar ABC transporter ATP-binding protein;
560-758 5.93e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 65.58  E-value: 5.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQ-----DISQvtqaSLRSHIGVVPQDTVLFND 632
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD----SEALGIVIIHQELALIPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 -TIADNIRYGRVTAGN---DEVEAAAQAA------GIHDAimafPEgyrTQVGERGLklsgGEKQRVAIARTILKAPGII 702
Cdd:NF040905   93 lSIAENIFLGNERAKRgviDWNETNRRARellakvGLDES----PD---TLVTDIGV----GKQQLVEIAKALSKDVKLL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 703 LLDEATSALdtsNERAIQASLAKVCANR----TTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:NF040905  162 ILDEPTAAL---NEEDSAALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
ycf16 CHL00131
sulfate ABC transporter protein; Validated
544-760 7.80e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 63.12  E-value: 7.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTqASLRSHIG 621
Cdd:CHL00131    8 LEIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 V------------VPQDTVLfndTIADNIRygRVTAGNDEVEAaaqaagihdaiMAFPEGYRTQVGERGLK--------- 680
Cdd:CHL00131   86 IflafqypieipgVSNADFL---RLAYNSK--RKFQGLPELDP-----------LEFLEIINEKLKLVGMDpsflsrnvn 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 --LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAH--RLSTVVNADQILVIKDGC 755
Cdd:CHL00131  150 egFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGK 229

                  ....*
gi 1169100883 756 IVERG 760
Cdd:CHL00131  230 IIKTG 234
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
559-754 9.38e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 65.14  E-value: 9.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 559 TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-------------VTQAslRSHIGVVPQ 625
Cdd:PRK10982  263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTEE--RRSTGIYAY 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFNDTIAdNIRYGRVTAG---NDEVEAAAQaaGIHDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGII 702
Cdd:PRK10982  341 LDIGFNSLIS-NIRNYKNKVGlldNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEIL 413
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 703 LLDEATSALDTSNERAIQ---ASLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK10982  414 MLDEPTRGIDVGAKFEIYqliAELAK--KDKGIIIISSEMPELLGiTDRILVMSNG 467
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
555-754 9.86e-11

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 64.85  E-value: 9.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDI-SQVTQASLRSHIGVVPQDTVLFN 631
Cdd:TIGR02633  12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTERAGIVIIHQELTLVP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 D-TIADNIRYGRvtagndevEAAAQAAGIHDAIMAfpegYRTQVGERGLKLS------------GGEKQRVAIARTILKA 698
Cdd:TIGR02633  92 ElSVAENIFLGN--------EITLPGGRMAYNAMY----LRAKNLLRELQLDadnvtrpvgdygGGQQQLVEIAKALNKQ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 699 PGIILLDEATSALdTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:TIGR02633 160 ARLLILDEPSSSL-TEKETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDG 217
hmuV PRK13547
heme ABC transporter ATP-binding protein;
555-760 1.06e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 63.31  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS--------SGCIRIDGQDISQVTQASLRSHIGVVPQD 626
Cdd:PRK13547   12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TV-LFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPeGYRTQVGERGLKLSGGEKQRVAIARTILK-------- 697
Cdd:PRK13547   92 AQpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 698 -APGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVV-NADQILVIKDGCIVERG 760
Cdd:PRK13547  171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHG 237
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
219-509 1.47e-10

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 62.91  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYR----NIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQF 294
Cdd:cd18563     1 LILGFLLMLLGTALGLVPPYLTKilidDVLIQLGPGGNTSLLLLLVLGLAGAYVLSA-------LLGILRGRLLARLGER 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 295 TSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIadrgTSSVTGLLSYLVFNVIPTLADII----IGIIYFSMffNAWFGL 369
Cdd:cd18563    74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMsRV----TSDTDRLQDFLSDGLPDFLTNILmiigIGVVLFSL--NWKLAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 370 IVFLCMSLYLTLTIVVteW---RTKFRR------AMNTQENatraravDSLLNFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:cd18563   148 LVLIPVPLVVWGSYFF--WkkiRRLFHRqwrrwsRLNSVLN-------DTLPGIRVVKAFGQEKREIKRFDEANQELLDA 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 441 EWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQ 509
Cdd:cd18563   219 NIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWIT 287
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
554-757 2.30e-10

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: 60.74  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 554 ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQDISQVTQaSLRSHIGVVPQDTVLF 630
Cdd:cd03233    17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAE-KYPGEIIYVSEEDVHF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 -NDTIADNIRYGRVTAGNDEVeaaaqaagihdaimafpegyrtqvgeRGLklSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:cd03233    96 pTLTVRETLDFALRCKGNEFV--------------------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTR 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 710 ALDTSNerAIQ-ASLAKVCANRTtivvahRLSTVVNA-----------DQILVIKDGCIV 757
Cdd:cd03233   148 GLDSST--ALEiLKCIRTMADVL------KTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
557-754 3.53e-10

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 63.31  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-SGCIRIDGQDISQVT-QASLRSHIGVVPQDT------- 627
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgivp 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 ---VLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIH-----DAIMAFPEGyrtqvgerglKLSGGEKQRVAIARTILKAP 699
Cdd:TIGR02633 353 ilgVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlkvkTASPFLPIG----------RLSGGNQQKAVLAKMLLTNP 422
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTT-IVVAHRLSTVVN-ADQILVIKDG 754
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEG 479
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
274-508 4.98e-10

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 61.37  E-value: 4.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 274 TGSTGFVSNLRTFLWIRV-QQFTSR-RVELliFSHLHELSLRWHLGRRTGEVLRiadRGTSSVTGLLSYLVFNVIPTLAD 351
Cdd:cd18564    64 ALLRGLASYAGTYLTALVgQRVVLDlRRDL--FAHLQRLSLSFHDRRRTGDLLS---RLTGDVGAIQDLLVSGVLPLLTN 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 352 IIIGIIYFS-MFFNAW-FGLIVFLCMSLYLTLTIVVTEwrtKFRRAMNTQ---ENATRARAVDSLLNFETVKYYNAESYE 426
Cdd:cd18564   139 LLTLVGMLGvMFWLDWqLALIALAVAPLLLLAARRFSR---RIKEASREQrrrEGALASVAQESLSAIRVVQAFGREEHE 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 427 VERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYR 506
Cdd:cd18564   216 ERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTG 295

                  ..
gi 1169100883 507 MI 508
Cdd:cd18564   296 RI 297
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
556-754 1.02e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVVPQD-TVLFNDT 633
Cdd:PRK10982   10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYGRVTAGNDEVEaaaQAAGIHDAIMAFPE-GYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALd 712
Cdd:PRK10982   90 VMDNMWLGRYPTKGMFVD---QDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1169100883 713 TSNE-----RAIQASLAKVCAnrtTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK10982  166 TEKEvnhlfTIIRKLKERGCG---IVYISHKMEEIFQlCDEITILRDG 210
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
551-769 1.11e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 60.02  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQASLRSHIGVVPQD-- 626
Cdd:PRK13638    9 FRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpe 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFNDTIADNIRYGRVTAGNDEVEAAAQaagIHDAI-MAFPEGYRTQVGErglKLSGGEKQRVAIARTILKAPGIILLD 705
Cdd:PRK13638   88 QQIFYTDIDSDIAFSLRNLGVPEAEITRR---VDEALtLVDAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLD 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 706 EATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13638  162 EPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT 227
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
543-764 1.39e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.08  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVhfsyaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIG 621
Cdd:PRK11288  257 RLRLDGL-----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIM 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDT----VLFNDTIADNI----RYGRVTAG---NDEVEAAAQAAGIHDAIMAFPEGyRTQVGerglKLSGGEKQRVA 690
Cdd:PRK11288  332 LCPEDRkaegIIPVHSVADNInisaRRHHLRAGcliNNRWEAENADRFIRSLNIKTPSR-EQLIM----NLSGGNQQKAI 406
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQA---SLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCIV-ERGRHEA 764
Cdd:PRK11288  407 LGRWLSEDMKVILLDEPTRGIDVGAKHEIYNviyELAA--QGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQA 483
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
537-771 1.41e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 61.45  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 537 LRFQKGR------IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIridgqdisq 610
Cdd:PRK15064  307 IRFEQDKklhrnaLEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 611 vtQASLRSHIGVVPQDTV--------LFN-----DTIADN---IR--YGRVTAGNDEVEAAAQAagihdaimafpegyrt 672
Cdd:PRK15064  377 --KWSENANIGYYAQDHAydfendltLFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVKV---------------- 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNRTTIVVAHRLSTVVN-ADQILVI 751
Cdd:PRK15064  439 --------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHDREFVSSlATRIIEI 508
                         250       260
                  ....*....|....*....|.
gi 1169100883 752 KDGCIVE-RGRHEALLSRGGV 771
Cdd:PRK15064  509 TPDGVVDfSGTYEEYLRSQGI 529
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
551-737 1.72e-09

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: 58.96  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADGRETLQDVSFTVMPG-----QTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslrshigVVPQ 625
Cdd:cd03237     1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKAD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFNDTIADNIR-YGRVTAGNDEVEAAAQAAGIHDaimafpegyrTQVGErglkLSGGEKQRVAIARTILKAPGIILL 704
Cdd:cd03237    74 YEGTVRDLLSSITKdFYTHPYFKTEIAKPLQIEQILD----------REVPE----LSGGELQRVAIAACLSKDADIYLL 139
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1169100883 705 DEATSALDtSNERAIQASLAKVCA---NRTTIVVAH 737
Cdd:cd03237   140 DEPSAYLD-VEQRLMASKVIRRFAennEKTAFVVEH 174
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
542-756 1.98e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 60.71  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYAD----GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYD-ISSGCIRIDGQ--DISQVTQA 614
Cdd:PRK13549  256 GEVILEVRNLTAWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQA 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 sLRSHIGVVPQD-----TVLFNDtIADNIR---YGRVTAGNdEVEAAAQAAGIHDAI------MAFPEgyrTQVGerglK 680
Cdd:PRK13549  336 -IAQGIAMVPEDrkrdgIVPVMG-VGKNITlaaLDRFTGGS-RIDDAAELKTILESIqrlkvkTASPE---LAIA----R 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQ---ASLAK--VCanrtTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK13549  406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYkliNQLVQqgVA----IIVISSELPEVLGlSDRVLVMHEG 481

                  ..
gi 1169100883 755 CI 756
Cdd:PRK13549  482 KL 483
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
562-756 2.16e-09

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 60.79  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 562 DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGVVPQD----------TVLF 630
Cdd:PRK10762  270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDrkrdglvlgmSVKE 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 NDTIAdNIRYGRVTAGNDEVEAAAQAAGihDAIMAFpeGYRTQVGER--GLkLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:PRK10762  350 NMSLT-ALRYFSRAGGSLKHADEQQAVS--DFIRLF--NIKTPSMEQaiGL-LSGGNQQKVAIARGLMTRPKVLILDEPT 423
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169100883 709 SALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCI 756
Cdd:PRK10762  424 RGVDVGAKKEIYQLINQFKAEGLSIIlVSSEMPEVLGmSDRILVMHEGRI 473
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
563-767 2.44e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 59.76  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVvpQDTVLFNDTIAD-N 637
Cdd:PRK11022   26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGA--EVAMIFQDPMTSlN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 638 IRYgrvTAGNDEVEA------AAQAAGIHDAIMAFpegyrTQVG----ERGL-----KLSGGEKQRVAIARTILKAPGII 702
Cdd:PRK11022  104 PCY---TVGFQIMEAikvhqgGNKKTRRQRAIDLL-----NQVGipdpASRLdvyphQLSGGMSQRVMIAMAIACRPKLL 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 703 LLDEATSALDTSneraIQASLAKVC------ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK11022  176 IADEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFR 243
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
555-729 2.99e-09

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 57.51  E-value: 2.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS------HIGVvpqDTV 628
Cdd:PRK13538   12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGI---KTE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 629 LfndTIADNIR-YGRVTAGNDEvEAAAQAAGihdaimafpegyrtQVGERGLK------LSGGEKQRVAIARTILKAPGI 701
Cdd:PRK13538   89 L---TALENLRfYQRLHGPGDD-EALWEALA--------------QVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAPL 150
                         170       180
                  ....*....|....*....|....*...
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCAN 729
Cdd:PRK13538  151 WILDEPFTAIDKQGVARLEALLAQHAEQ 178
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
550-752 6.69e-09

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: 55.83  E-value: 6.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 550 HFSYADGretlQDVSFTvmPGQTLALVGPSGAGKSTILRllfrfyDISSGCIRidgqdisqvTQASLRSHIGVVPQDTVl 629
Cdd:cd03227     7 FPSYFVP----NDVTFG--EGSLTIITGPNGSGKSTILD------AIGLALGG---------AQSATRRRSGVKAGCIV- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 fndtiadnirygrvtagndeveaAAQAAGIHDAIMafpegyrtqvgerglKLSGGEKQRVAIA-----RTILKAPgIILL 704
Cdd:cd03227    65 -----------------------AAVSAELIFTRL---------------QLSGGEKELSALAlilalASLKPRP-LYIL 105
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169100883 705 DEATSALDTSNERAIQASLAK-VCANRTTIVVAHRLSTVVNADQILVIK 752
Cdd:cd03227   106 DEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
PLN03073 PLN03073
ABC transporter F family; Provisional
544-712 7.04e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 59.49  E-value: 7.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCI--------------RIDGQDIS 609
Cdd:PLN03073  509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLS 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 610 Q------------VTQASLRSHIGvvpqdtvlfndtiadniRYGrvTAGNdeveaaaqaagihdaiMAFPEGYrtqvger 677
Cdd:PLN03073  589 SnpllymmrcfpgVPEQKLRAHLG-----------------SFG--VTGN----------------LALQPMY------- 626
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1169100883 678 glKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PLN03073  627 --TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
565-712 1.67e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 55.63  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 565 FTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHIGVVPQDTVLFNDTIADNIRYG 641
Cdd:PRK13543   32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmAYLGHLPGLKADLSTLENLHFLCGLHG 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 642 RvtagndeveAAAQAAGIHDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PRK13543  112 R---------RAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
217-515 1.95e-08

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 56.69  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGlerALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQgggTGSTGFVSNLRTFLWIRVQqfTS 296
Cdd:cd18549     5 FLDLFCAVLIA---ALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILR---TLLNYFVTYWGHVMGARIE--TD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELliFSHLHELSLRWHLGRRTGEVLriadrgtSSVTGLLSYlvfnvIPTLA-----DIIIGIIYFS------MFFNA 365
Cdd:cd18549    77 MRRDL--FEHLQKLSFSFFDNNKTGQLM-------SRITNDLFD-----ISELAhhgpeDLFISIITIIgsfiilLTINV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 366 WFGLIVFLCMSLYLTLTIvvtewrtKFRRAMNTQENATR-------ARAVDSLLNFETVKYYNAESYEVERYREAIIKYQ 438
Cdd:cd18549   143 PLTLIVFALLPLMIIFTI-------YFNKKMKKAFRRVRekigeinAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 439 GLEWKS-------SASLVLLNQTQNLVIGLGLlagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNwfgtyyRMIqtN 511
Cdd:cd18549   216 ESKKKAykamayfFSGMNFFTNLLNLVVLVAG-------GYFIIKGEITLGDLVAFLLYVNVFIKPIR------RLV--N 280

                  ....
gi 1169100883 512 FIDM 515
Cdd:cd18549   281 FTEQ 284
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
544-762 2.08e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 55.95  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDIS------------ 609
Cdd:PRK09580    2 LSIKDLHVS-VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLelspedragegi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 610 -------------------QVTQASLRSHIGVVPQDTVLFNDTIADNIRygrvtagndeveaaaqaagihdaIMAFPEGY 670
Cdd:PRK09580   81 fmafqypveipgvsnqfflQTALNAVRSYRGQEPLDRFDFQDLMEEKIA-----------------------LLKMPEDL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 671 RTQVGERGlkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKV-CANRTTIVVAH--RLSTVVNADQ 747
Cdd:PRK09580  138 LTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLrDGKRSFIIVTHyqRILDYIKPDY 215
                         250
                  ....*....|....*
gi 1169100883 748 ILVIKDGCIVERGRH 762
Cdd:PRK09580  216 VHVLYQGRIVKSGDF 230
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
222-440 2.99e-08

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 55.95  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRRVEL 301
Cdd:cd18576     1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQA-------VFSFFRIYLFARVGERVVADLRK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 302 LIFSHLHELSLRWHLGRRTGEVL-RIadrgTSSVTGLLSYLVFNVIPTLADIIIGIIyfsmffnawfGLIVFLCMSLYLT 380
Cdd:cd18576    74 DLYRHLQRLPLSFFHERRVGELTsRL----SNDVTQIQDTLTTTLAEFLRQILTLIG----------GVVLLFFISWKLT 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 381 L--------TIVVTEWRTKFRRAMNTQENATRARAV----DSLLNFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:cd18576   140 LlmlatvpvVVLVAVLFGRRIRKLSKKVQDELAEANtiveETLQGIRVVKAFTREDYEIERYRKALERVVKL 211
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
538-737 5.24e-08

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: 56.33  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 538 RFQKGRIEFEnVH-----------FSYADGRETLQDVSFTVMPGQ-----TLALVGPSGAGKSTILRLLfrfydisSGCI 601
Cdd:COG1245   319 RIRDEPIEFE-VHaprrekeeetlVEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVL 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 602 RIDGQDISqvtqASLRshIGVVPQ----DtvlFNDTIADNIRygrvTAGNDEVEAAAqaagihdaimafpegYRTQVGER 677
Cdd:COG1245   391 KPDEGEVD----EDLK--ISYKPQyispD---YDGTVEEFLR----SANTDDFGSSY---------------YKTEIIKP 442
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 678 -GLK---------LSGGEKQRVAIARTILKAPGIILLDEATSALDtSNERAIQAS-LAKVCANR--TTIVVAH 737
Cdd:COG1245   443 lGLEklldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRLAVAKaIRRFAENRgkTAMVVDH 514
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
514-758 5.92e-08

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 55.95  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 514 DMENMFDLLKEETEVKDlpgagplrfQKGRIEFENVhFSYADGRetLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:PRK09700  245 ELQNRFNAMKENVSNLA---------HETVFEVRNV-TSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQ-ASLRSHIGVVPQ---DTVLF-NDTIADNI---------RYGRVTAGNDEVEAAAQAAGI 659
Cdd:PRK09700  313 DKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQ 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 660 HDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAHR 738
Cdd:PRK09700  393 RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSE 468
                         250       260
                  ....*....|....*....|.
gi 1169100883 739 LSTVVNA-DQILVIKDGCIVE 758
Cdd:PRK09700  469 LPEIITVcDRIAVFCEGRLTQ 489
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
219-512 6.66e-08

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 54.78  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQgggtgstgFVSNlrtFLWIRVQQFTSRR 298
Cdd:cd18545     2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVN--------WVAS---RLRIYLMAKVGQR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLI----FSHLHELSLRWHLGRRTGEVL-R-IADrgTSSVTGLLSYLVFNVIPTLAdIIIGIIYFSMFFNAWFGLIVF 372
Cdd:cd18545    71 ILYDLrqdlFSHLQKLSFSFFDSRPVGKILsRvIND--VNSLSDLLSNGLINLIPDLL-TLVGIVIIMFSLNVRLALVTL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLyltLTIVVTEWRTKFRRA----------MNT--QENATRARavdsllnfeTVKYYNAESYEVERYREAIIKYQGl 440
Cdd:cd18545   148 AVLPL---LVLVVFLLRRRARKAwqrvrkkisnLNAylHESISGIR---------VIQSFAREDENEEIFDELNRENRK- 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 441 EWKSSASLV-LLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNF 512
Cdd:cd18545   215 ANMRAVRLNaLFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAM 287
GguA NF040905
sugar ABC transporter ATP-binding protein;
548-712 9.42e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 55.57  E-value: 9.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF-RFY--DISsGCIRIDGQ--DISQVTQA-------- 614
Cdd:NF040905  264 TVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgrNIS-GTVFKDGKevDVSTVSDAidaglayv 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 -SLRSHIGVVPQDTVLFNDTIA--DNIRYGRVTAGNDEVEAAaqaagihdaimafpEGYRTQ-------VGERGLKLSGG 684
Cdd:NF040905  343 tEDRKGYGLNLIDDIKRNITLAnlGKVSRRGVIDENEEIKVA--------------EEYRKKmniktpsVFQKVGNLSGG 408
                         170       180
                  ....*....|....*....|....*...
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:NF040905  409 NQQKVVLSKWLFTDPDVLILDEPTRGID 436
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
538-737 1.06e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.59  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 538 RFQKGRIEFE----------NVHFSYADGRETLQDVSFTVMPGQ-----TLALVGPSGAGKSTILRLLfrfydisSGCIR 602
Cdd:PRK13409  318 RIRPEPIEFEerpprdeserETLVEYPDLTKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLL-------AGVLK 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 603 IDGQDISqvtqASLRshIGVVPQ-------DTV-LFNDTIADNIR---YgrvtagNDEVeaaAQAAGIHDaIMafpegyr 671
Cdd:PRK13409  391 PDEGEVD----PELK--ISYKPQyikpdydGTVeDLLRSITDDLGssyY------KSEI---IKPLQLER-LL------- 447
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 672 tqvgERGLK-LSGGEKQRVAIARTILKAPGIILLDEATSALDtSNERAIQAS-LAKVCANR--TTIVVAH 737
Cdd:PRK13409  448 ----DKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRLAVAKaIRRIAEEReaTALVVDH 512
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
569-741 1.33e-07

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: 55.18  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLL-----------------------FR-------FYDISSGCIRIdgqdiSQVTQaslrs 618
Cdd:COG1245    98 KGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlkrFRgtelqdyFKKLANGEIKV-----AHKPQ----- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQdtvLFNDTIADnirygrVTAGNDE---VEAAAQAAGIhDAIMafpegyrtqvgERGLK-LSGGEKQRVAIART 694
Cdd:COG1245   168 YVDLIPK---VFKGTVRE------LLEKVDErgkLDELAEKLGL-ENIL-----------DRDISeLSGGELQRVAIAAA 226
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 695 ILKAPGIILLDEATSALDTsNER-----AIQaSLAKvcANRTTIVVAHRLST 741
Cdd:COG1245   227 LLRDADFYFFDEPSSYLDI-YQRlnvarLIR-ELAE--EGKYVLVVEHDLAI 274
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
558-754 1.55e-07

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 54.67  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV-TQASLRSHIGVVPQD---TVLFNDT 633
Cdd:PRK15439  277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLPEDrqsSGLYLDA 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 -IADNI---RYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:PRK15439  357 pLAWNVcalTHNRRGFWIKPARENAVLERYRRAL-----NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1169100883 709 SALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK15439  432 RGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQG 479
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
566-739 1.95e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.43  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 566 TVMPGQTLALVGPSGAGKSTILRLL-----------------------FR-------FYDISSGCIRIdgqdiSQVTQas 615
Cdd:PRK13409   95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlkrFRgtelqnyFKKLYNGEIKV-----VHKPQ-- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 lrsHIGVVPQdtvLFNDTIADNIRygrvtaGNDEveaaaqaAGIHDAImafpegyrtqVGERGLK---------LSGGEK 686
Cdd:PRK13409  168 ---YVDLIPK---VFKGKVRELLK------KVDE-------RGKLDEV----------VERLGLEnildrdiseLSGGEL 218
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALDTsNER-----AIQaSLAKvcaNRTTIVVAHRL 739
Cdd:PRK13409  219 QRVAIAAALLRDADFYFFDEPTSYLDI-RQRlnvarLIR-ELAE---GKYVLVVEHDL 271
PLN03073 PLN03073
ABC transporter F family; Provisional
544-790 2.22e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.48  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILR--LLFRFYDISSGCI------RIDGQDISqVTQAS 615
Cdd:PLN03073  178 IHMENFSISVG-GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQilhveqEVVGDDTT-ALQCV 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHI---------------------------GVVPQDTVLFNDTIADNIR--YGRVTAgNDEVEAAAQAAGIHDAIMAF 666
Cdd:PLN03073  256 LNTDIertqlleeeaqlvaqqrelefetetgkGKGANKDGVDKDAVSQRLEeiYKRLEL-IDAYTAEARAASILAGLSFT 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 667 PEGYRtqvgERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKvcANRTTIVVAHR---LSTVV 743
Cdd:PLN03073  335 PEMQV----KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK--WPKTFIVVSHArefLNTVV 408
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 744 N-----ADQILVIKDGC--IVERGRHEALLSrggvyadmwqlQQGQEETSEDTK 790
Cdd:PLN03073  409 TdilhlHGQKLVTYKGDydTFERTREEQLKN-----------QQKAFESNERSR 451
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
278-487 2.49e-07

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 52.98  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 278 GFVSNLRTFLWIrvqqFTSRRVEL----LIFSHLHELSLRWHLGRRTGEVL-RIADRGTssvtgLLSYLVFNVIPTLADI 352
Cdd:cd18782    56 AVLTALRTYLFT----DTANRIDLelggTIIDHLLRLPLGFFDKRPVGELStRISELDT-----IRGFLTGTALTTLLDV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 353 IIGIIYFS-MFFNAWF-GLIVFLCMSLYLTLTIVVTE-WRTKFRRAMnTQENATRARAVDSLLNFETVKYYNAESYEVER 429
Cdd:cd18782   127 LFSVIYIAvLFSYSPLlTLVVLATVPLQLLLTFLFGPiLRRQIRRRA-EASAKTQSYLVESLTGIQTVKAQNAELKARWR 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 430 YREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLF 487
Cdd:cd18782   206 WQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
219-509 4.49e-07

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 52.42  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGGGTgstgFVSNlrtFLWIRVQQFTSRR 298
Cdd:cd18552     1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLAS----YLQT---YLMAYVGQRVVRD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVL-RI---ADRGTSSVTGLLSYLVFNVIptladIIIGIIYFSMFFNAWFGLIVFLC 374
Cdd:cd18552    74 LRNDLFDKLLRLPLSFFDRNSSGDLIsRItndVNQVQNALTSALTVLVRDPL-----TVIGLLGVLFYLDWKLTLIALVV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 375 MSLyltLTIVVTEWRTKFRR-AMNTQENATR--ARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKS---SASL 448
Cdd:cd18552   149 LPL---AALPIRRIGKRLRKiSRRSQESMGDltSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIaraRALS 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 449 VLLNQTQN-----LVIGLGllagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQ 509
Cdd:cd18552   226 SPLMELLGaiaiaLVLWYG--------GYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQ 283
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
217-510 6.10e-07

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 51.77  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGLeraLNVLVPIFYRNIVNLLTE-KAPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNlrtflwiRVQQFT 295
Cdd:cd18778     2 ILTLLCALLSTL---LGLVPPWLIRELVDLVTIgSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNH-------VAEQKV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 296 SRRVELLIFSHLHELSLRWHLGRRTGEVL-RIADrGTSSVTGLLSYLVFNVIPT-LADIIIGIIYFSMffNAWFGLIVFL 373
Cdd:cd18778    72 VADLRSDLYDKLQRLSLRYFDDRQTGDLMsRVIN-DVANVERLIADGIPQGITNvLTLVGVAIILFSI--NPKLALLTLI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 374 CMSLYLTLTIVVTEW-RTKFRR------AMNtqenatrARAVDSLLNFETVKYYNAESYEVERYREAIIKYQ-------- 438
Cdd:cd18778   149 PIPFLALGAWLYSKKvRPRYRKvrealgELN-------ALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRkaqlramk 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 439 -------GLEWKSSASLVLlnqtqnlVIGLGllagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQT 510
Cdd:cd18778   222 lwaifhpLMEFLTSLGTVL-------VLGFG--------GRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQR 285
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
560-736 8.58e-07

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 52.80  E-value: 8.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLL----FRFYDISSGCIRIDG---QDISQ------VTQASLRSHIGVVP-Q 625
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKKhyrgdvVYNAETDVHFPHLTvG 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  626 DTVLFndtiADNIRygrvTAGN-----DEVEAAAQAAGIHDAIMAFPEGYRTQVGE---RGLklSGGEKQRVAIARTILK 697
Cdd:TIGR00956  157 ETLDF----AARCK----TPQNrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1169100883  698 APGIILLDEATSALDTSNERAIQASLaKVCAN--RTTIVVA 736
Cdd:TIGR00956  227 GAKIQCWDNATRGLDSATALEFIRAL-KTSANilDTTPLVA 266
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
231-498 1.60e-06

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 50.49  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEK-APWNSLAWTVTSYVFLKFLQGGGTgstgfvsnlrtFLWiRVQQF-TSRRVELL----IF 304
Cdd:cd18541    13 LLQLLIPRIIGRAIDALTAGtLTASQLLRYALLILLLALLIGIFR-----------FLW-RYLIFgASRRIEYDlrndLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 305 SHLHELSLRWHLGRRTGEVlrIAdRGTSSVTGLLSYLVFNVIpTLADII---IGIIYFSMFFNAWFGLIVFLCMSLyltL 381
Cdd:cd18541    81 AHLLTLSPSFYQKNRTGDL--MA-RATNDLNAVRMALGPGIL-YLVDALflgVLVLVMMFTISPKLTLIALLPLPL---L 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 382 TIVVTEW----RTKFRRAMNTQENATrARAVDSLLNFETVKYYNAESYEVERYREAIIKYQglewKSSASLV----LLNQ 453
Cdd:cd18541   154 ALLVYRLgkkiHKRFRKVQEAFSDLS-DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYV----EKNLRLArvdaLFFP 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1169100883 454 TQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18541   229 LIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPM 273
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
231-494 2.11e-06

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 50.25  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRRVELLIFSHLHEL 310
Cdd:cd18557    10 AAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQS-------VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 311 SLRWHLGRRTGEVL-RIA-DRGT--SSVTGLLSYLVFNVIptladIIIGIIYFsMFFNAW-FGLIVFLCMSLYLTLTIVV 385
Cdd:cd18557    83 EIAFFDKHKTGELTsRLSsDTSVlqSAVTDNLSQLLRNIL-----QVIGGLII-LFILSWkLTLVLLLVIPLLLIASKIY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 386 TEWRTKFRRAMntQENATRARAV--DSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGL 463
Cdd:cd18557   157 GRYIRKLSKEV--QDALAKAGQVaeESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1169100883 464 LAGSLLCAYFVTEQKLQVGDYVLFGTYIIQL 494
Cdd:cd18557   235 LLVLWYGGYLVLSGQLTVGELTSFILYTIMV 265
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
543-715 2.68e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 50.78  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRL--------------LFrfydissGCIRIDGQDI 608
Cdd:PRK10938  260 RIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLF-------GRRRGSGETI 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 609 SQVTQaslrsHIGVVP-------------QDTVL--FNDTIadniryGRVTAGNDEVEAAAQA----AGIHDAIMAFPeg 669
Cdd:PRK10938  332 WDIKK-----HIGYVSsslhldyrvstsvRNVILsgFFDSI------GIYQAVSDRQQKLAQQwldiLGIDKRTADAP-- 398
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1169100883 670 YRTqvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSN 715
Cdd:PRK10938  399 FHS--------LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
560-749 3.91e-06

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 49.15  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTIL---------RLLFRFYDISSGCIRIDG-QDISQVTQASlRSHIGVVPQDTVL 629
Cdd:cd03271    11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGlEHIDKVIVID-QSPIGRTPRSNPA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 FNDTIADNIR--YGRVTAG---NDE------------------VEAAAQ----AAGIHDAIMAFPE---GYrTQVGERGL 679
Cdd:cd03271    90 TYTGVFDEIRelFCEVCKGkryNREtlevrykgksiadvldmtVEEALEffenIPKIARKLQTLCDvglGY-IKLGQPAT 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 680 KLSGGEKQRVAIARTILKA---PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVNADQIL 749
Cdd:cd03271   169 TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWII 242
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
217-510 5.12e-06

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 48.97  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGleRALNVLVPIFYRNIVNLLTEKAP-WNSLAWTVTSYVFLKFLQGGGT---GSTG--FVSNLRTFLWir 290
Cdd:cd18551     1 LILALLLSLLG--TAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSyllGRTGerVVLDLRRRLW-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 291 vqqftsrrvellifSHLHELSLRWHLGRRTGEVL-RIadrgtSSVTGLLSYLVFNVIPTLAD---IIIGIIYFSMFFNAW 366
Cdd:cd18551    77 --------------RRLLRLPVSFFDRRRSGDLVsRV-----TNDTTLLRELITSGLPQLVTgvlTVVGAVVLMFLLDWV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 367 FGLIVFLCMSLYLTLTIVVTewrTKFRRA-MNTQENATR--ARAVDSLLNFETVKYYNAESYEVERYREAI--IKYQGLe 441
Cdd:cd18551   138 LTLVTLAVVPLAFLIILPLG---RRIRKAsKRAQDALGElsAALERALSAIRTVKASNAEERETKRGGEAAerLYRAGL- 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 442 wKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQT 510
Cdd:cd18551   214 -KAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQK 281
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
217-499 8.67e-06

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 48.55  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGlerALNVLVPIFYRNIVNLLTEkaPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSN-LRTFLWIRVQQFT 295
Cdd:cd18547     2 ILVIILAIIST---LLSVLGPYLLGKAIDLIIE--GLGGGGGVDFSGLLRILLLLLGLYLLSALFSyLQNRLMARVSQRT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 296 SRRVELLIFSHLHELSLRWHLGRRTGEVL-RI---ADRGTSSVTGLLSYLVFNVIptladIIIGIIYFsMFF-NAWFGLI 370
Cdd:cd18547    77 VYDLRKDLFEKLQRLPLSYFDTHSHGDIMsRVtndVDNISQALSQSLTQLISSIL-----TIVGTLIM-MLYiSPLLTLI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 371 VFLCMSLYLTLTIVVTEW-RTKFRR------AMN--TQENATraravdsllNFETVKYYNAESYEVERYREAIIKYQGLE 441
Cdd:cd18547   151 VLVTVPLSLLVTKFIAKRsQKYFRKqqkalgELNgyIEEMIS---------GQKVVKAFNREEEAIEEFDEINEELYKAS 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 442 WKSS--ASLV-----LLNQTQNLVIglgllagSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLN 499
Cdd:cd18547   222 FKAQfySGLLmpimnFINNLGYVLV-------AVVGGLLVINGALTVGVIQAFLQYSRQFSQPIN 279
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
569-740 9.28e-06

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: 48.13  E-value: 9.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLLfrfydisSG------CIRIDGQDISQVtqasLRSHIGVVPQD--TVLFNDTI------ 634
Cdd:cd03236    25 EGQVLGLVGPNGIGKSTALKIL-------AGklkpnlGKFDDPPDWDEI----LDEFRGSELQNyfTKLLEGDVkvivkp 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 --ADNIRygRVTAGN-DEVEAAAQAAGIHDAIMAFPEgyRTQVGERGL-KLSGGEKQRVAIARTILKAPGIILLDEATSA 710
Cdd:cd03236    94 qyVDLIP--KAVKGKvGELLKKKDERGKLDELVDQLE--LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1169100883 711 LDT----SNERAIQaSLAKvcANRTTIVVAHRLS 740
Cdd:cd03236   170 LDIkqrlNAARLIR-ELAE--DDNYVLVVEHDLA 200
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
294-487 9.87e-06

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 48.33  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 FTSRRVELLIFS----HLHELSLRWHLGRRTGEVL-RIADRGTssvtgLLSYLVFNVIPTLADIIIGIIYFSMFF--NAW 366
Cdd:cd18568    68 YFANRIDLSLLSdfykHLLSLPLSFFASRKVGDIItRFQENQK-----IRRFLTRSALTTILDLLMVFIYLGLMFyyNLQ 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 367 FGLIVFLCMSLYLTLTIVVtewrTKFRRAMNTQENATRARA----VDSLLNFETVKYYNAESYEVERYREAIIKYQGLEW 442
Cdd:cd18568   143 LTLIVLAFIPLYVLLTLLS----SPKLKRNSREIFQANAEQqsflVEALTGIATIKALAAERPIRWRWENKFAKALNTRF 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1169100883 443 KSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLF 487
Cdd:cd18568   219 RGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAF 263
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
560-752 1.10e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.79  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLrSHIGvvPQDTVLFNDTIADNIR 639
Cdd:PRK13541   16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 Y-GRVTAGNDEVEAAAQAAGIHDAImafpegyrtqvGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNeRA 718
Cdd:PRK13541   93 FwSEIYNSAETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-RD 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1169100883 719 IQASLAKVCANRTTIVV--AHRLSTVVNAdQILVIK 752
Cdd:PRK13541  161 LLNNLIVMKANSGGIVLlsSHLESSIKSA-QILQLD 195
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
679-754 1.30e-05

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: 46.41  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNE----RAIQASLAKvcANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03222    70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEE--GKKTALVVEHDLAVLDYLSDRIHVFEG 147
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
657-749 1.51e-05

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: 48.90  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883  657 AGIHdaIMAFPEGYRTQvgerGLK-LSGGEKQRVAIAR--TILK---APgIILLDEATSALDTSN-ERAiqASLAKVCAN 729
Cdd:TIGR02168 1071 AGIE--IFAQPPGKKNQ----NLSlLSGGEKALTALALlfAIFKvkpAP-FCILDEVDAPLDDANvERF--ANLLKEFSK 1141
                           90       100
                   ....*....|....*....|.
gi 1169100883  730 RTT-IVVAHRLSTVVNADQIL 749
Cdd:TIGR02168 1142 NTQfIVITHNKGTMEVADQLY 1162
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
223-515 3.45e-05

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 46.38  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 223 LGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLqgggtgsTGFVSNLRTFLWIRVQQFTSRRVELL 302
Cdd:cd18572     2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVL-------SGLFSGLRGGCFSYAGTRLVRRLRRD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 303 IFSHLHELSLRWHLGRRTGEVL-RI-ADrgTSSVTGLLSYLVFNVIPTLADIIIGIIYfsMFFNAWF-GLIVFLCMslyl 379
Cdd:cd18572    75 LFRSLLRQDIAFFDATKTGELTsRLtSD--CQKVSDPLSTNLNVFLRNLVQLVGGLAF--MFSLSWRlTLLAFITV---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 380 TLTIVVTEWRTKFRRAMNTQENATRAR----AVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQ 455
Cdd:cd18572   147 PVIALITKVYGRYYRKLSKEIQDALAEanqvAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVN 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 456 NLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFgtyiiQLYmpLNWFGTYYRMIQTNFIDM 515
Cdd:cd18572   227 TLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTF-----MLY--QQQLGEAFQSLGDVFSSL 279
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
547-723 5.48e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 46.70  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGciridgqdisqvTQASLRSHIGvvpqd 626
Cdd:PRK10636  316 EKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AG------------ELAPVSGEIG----- 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 tvlfndtIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPE------------GYR-TQVGERGLKLSGGEKQRVAIAR 693
Cdd:PRK10636  371 -------LAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQEleqklrdylggfGFQgDKVTEETRRFSGGEKARLVLAL 443
                         170       180       190
                  ....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASL 723
Cdd:PRK10636  444 IVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
352-498 9.03e-05

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 45.08  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 352 IIIGIIYFSMFFNAWFGLIVFLCMSLyLTLTIVVTEWRT--KFRR------AMN--TQENATRARavdsllnfeTVKYYN 421
Cdd:cd18548   126 MLIGAIIMAFRINPKLALILLVAIPI-LALVVFLIMKKAipLFKKvqkkldRLNrvVRENLTGIR---------VIRAFN 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 422 AESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18548   196 REDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
231-502 1.14e-04

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 44.78  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGGGTGstgfvsnLRTFLWIRVQQFTSRRVELLIFSHLHEL 310
Cdd:cd18543    13 LAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSF-------LRRYLAGRLSLGVEHDLRTDLFAHLQRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 311 SLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMffNAWFGLIVFLCMSLyltLTIVVTEWRT 390
Cdd:cd18543    86 DGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLVL--SPPLALVALASLPP---LVLVARRFRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 391 KFRRAMNT--QENATRARAVD-SLLNFETVKYYNAESYEVERYREAIIKYQGLEWKS-------SASLVLLNQ-TQNLVI 459
Cdd:cd18543   161 RYFPASRRaqDQAGDLATVVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAarlrarfWPLLEALPElGLAAVL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1169100883 460 GLGllagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFG 502
Cdd:cd18543   241 ALG--------GWLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
251-502 1.19e-04

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 44.86  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 251 APWNSLAWTVTS----YVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVL-- 324
Cdd:cd18565    37 LPLVPASLGPADprgqLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMsv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 325 ---------RIADRGTSSVTGLLSYLVFnviptladiiIGIIYFSMffNAWFGLIVFLCMSLyltlTIVVTEWrtkFRRA 395
Cdd:cd18565   117 lnndvnqleRFLDDGANSIIRVVVTVLG----------IGAILFYL--NWQLALVALLPVPL----IIAGTYW---FQRR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 396 MNTQENATR-------ARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEW---KSSASLVLLNQtqnLVIGLGLLA 465
Cdd:cd18565   178 IEPRYRAVReavgdlnARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWraiRLRAAFFPVIR---LVAGAGFVA 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1169100883 466 GSLLCAYFVTE------QKLQVGDYVLFGTYIIQLYMPLNWFG 502
Cdd:cd18565   255 TFVVGGYWVLDgpplftGTLTVGTLVTFLFYTQRLLWPLTRLG 297
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
681-749 1.31e-04

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: 43.47  E-value: 1.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 681 LSGGEKQRVAIARTILKAPG--IILLDEATSALDTSNERAIQASLAK-VCANRTTIVVAHRLSTVVNADQIL 749
Cdd:cd03238    88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWII 159
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
549-767 1.83e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 44.41  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 549 VHFSYADGRETLQD-VSFTVMPGQTLALVGPSGAGKSTILRLL--------------FRFYDISSGCI------RIDGQD 607
Cdd:PRK15093   11 IEFKTSDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDDIDLLRLsprerrKLVGHN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 608 ISQVTQAslrshigvvPQDTVLFNDTIADNIR------------YGRVTAGNDEVEAAAQAAGI--HDAIM-AFPegyrt 672
Cdd:PRK15093   91 VSMIFQE---------PQSCLDPSERVGRQLMqnipgwtykgrwWQRFGWRKRRAIELLHRVGIkdHKDAMrSFP----- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgergLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR-TTI-VVAHRLSTVVN-ADQIL 749
Cdd:PRK15093  157 ------YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTIlLISHDLQMLSQwADKIN 230
                         250
                  ....*....|....*...
gi 1169100883 750 VIKDGCIVERGRHEALLS 767
Cdd:PRK15093  231 VLYCGQTVETAPSKELVT 248
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
303-498 2.57e-04

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 43.95  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 303 IFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFS-MFFnawfgLIVFLCMSLYLTL 381
Cdd:cd18554    85 LFDHLQKLSLRYYANNRSGEII---SRVINDVEQTKDFITTGLMNIWLDMITIIIAICiMLV-----LNPKLTFVSLVIF 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 382 TIVVTEWRTKFRRAMNTQENATRARAVDSLLNFE------TVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQ 455
Cdd:cd18554   157 PFYILAVKYFFGRLRKLTKERSQALAEVQGFLHEriqgmsVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAV 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1169100883 456 NLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18554   237 NTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
217-510 6.21e-04

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 42.50  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGLErALNVLVPIFYRNIVN--LLTEKAPW-NSLAWTVTSYVFLKFLqgggtgstgfVSNLRTFLWIRVQQ 293
Cdd:cd18555     3 LLISILLLSLLLQ-LLTLLIPILTQYVIDnvIVPGNLNLlNVLGIGILILFLLYGL----------FSFLRGYIIIKLQT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 FTSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIadrgtSSVTGLLSYLVFNVIPTLADIIIGIIYFSM--FFNAWFGLI 370
Cdd:cd18555    72 KLDKSLMSDFFEHLLKLPYSFFENRSSGDLLfRA-----NSNVYIRQILSNQVISLIIDLLLLVIYLIYmlYYSPLLTLI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 371 VFLCMSLYLTLTIVVtewrTKFRRAMNTQENATRARA----VDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSA 446
Cdd:cd18555   147 VLLLGLLIVLLLLLT----RKKIKKLNQEEIVAQTKVqsylTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 447 SLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQT 510
Cdd:cd18555   223 LSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFIL 286
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
283-452 6.37e-04

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 42.49  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 283 LRTFLWIRvqqfTSRRVELL----IFSHLHELSLRWHLGRRTGEVL-RIadRGTSSVTgllSYLVFNVIPTLADIIIGII 357
Cdd:cd18588    61 LRTYLFSH----TTNRIDAElgarLFRHLLRLPLSYFESRQVGDTVaRV--RELESIR---QFLTGSALTLVLDLVFSVV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 358 YFS-MFFNAWF-GLIVFLCMSLYLTLTIVVTEwrtKFRRAMNTQ-ENATRARA--VDSLLNFETVKYYNAESYEVERYRE 432
Cdd:cd18588   132 FLAvMFYYSPTlTLIVLASLPLYALLSLLVTP---ILRRRLEEKfQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEE 208
                         170       180
                  ....*....|....*....|
gi 1169100883 433 AIIKYQglewKSSASLVLLN 452
Cdd:cd18588   209 LLARYV----KASFKTANLS 224
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
681-749 6.41e-04

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: 41.68  E-value: 6.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 681 LSGGEKQRVAIAR--TILK---APgIILLDEATSALDTSN-ERAiqASLAKVCANRT-TIVVAHRLSTVVNADQIL 749
Cdd:cd03278   114 LSGGEKALTALALlfAIFRvrpSP-FCVLDEVDAALDDANvERF--ARLLKEFSKETqFIVITHRKGTMEAADRLY 186
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
555-613 7.42e-04

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: 41.61  E-value: 7.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 555 DGRETLQDVsftvMPGQTLALVGPSGAGKSTILRLLFrfydissGCIRIDGQDISQVTQ 613
Cdd:cd01854    74 EGLDELREL----LKGKTSVLVGQSGVGKSTLLNALL-------PELVLATGEISEKLG 121
PRK01889 PRK01889
GTPase RsgA; Reviewed
569-604 1.28e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.84  E-value: 1.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRID 604
Cdd:PRK01889  194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
ABC_6TM_NdvA_beta-glucan_exporter_like cd18562
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ...
231-434 1.40e-03

Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350006 [Multi-domain]  Cd Length: 289  Bit Score: 41.46  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEkapWNSLAWTVTSYVFLKFLqggGTGSTGFVSNLRTFLWIRvqqftsRRVELLI--FSHLH 308
Cdd:cd18562    13 GVQFAEPVLFGRVVDALSS---GGDAFPLLALWAALGLF---SILAGVLVALLADRLAHR------RRLAVMAsyFEHVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 309 ELSLRWHLGRRTGEVLRIADRGTSSVTGL-LSYLVFNvIPTLADIIIgIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTE 387
Cdd:cd18562    81 TLPLSFHSQRGSGRLLRIMLRGTDALFGLwLGFFREH-LAALVSLIV-LLPVALWMNWRLALLLVVLAAVYAALNRLVMR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1169100883 388 wRTKFR-RAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAI 434
Cdd:cd18562   159 -RTKAGqAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGIT 205
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
298-499 1.52e-03

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 41.31  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 298 RVELliFSHLHELSLRWHLGRRTGEVL-RIA-DRG--TSSVTGLLSYLVFNVIPTLADIIIgiiyfsMFFNAW-FGLIVF 372
Cdd:cd18550    75 RVQL--YAHLQRMSLAFFTRTRTGEIQsRLNnDVGgaQSVVTGTLTSVVSNVVTLVATLVA------MLALDWrLALLSL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEWRTKFRRAmnTQE-NATRARAVDSLLN---FETVKYYNAESYEVERYREAIIKYQGLEWKSSASL 448
Cdd:cd18550   147 VLLPLFVLPTRRVGRRRRKLTRE--QQEkLAELNSIMQETLSvsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAG 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 449 VLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLN 499
Cdd:cd18550   225 RWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLT 275
aroK PRK00131
shikimate kinase; Reviewed
568-617 1.73e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 40.17  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 568 MPGQTLALVGPSGAGKSTILRLL-----FRFYDissgcirIDgQDISQVTQASLR 617
Cdd:PRK00131    2 LKGPNIVLIGFMGAGKSTIGRLLakrlgYDFID-------TD-HLIEARAGKSIP 48
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
669-749 2.03e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 41.92  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 669 GYrTQVGERGLKLSGGEKQRVAIARTILK---APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV-AHRLSTVVN 744
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKT 897

                  ....*
gi 1169100883 745 ADQIL 749
Cdd:TIGR00630 898 ADYII 902
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
543-754 2.14e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 40.28  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHfSYADgretlqDVSFTVMPGQTLaLVGPSGAGKSTILR-LLFRFYDISSGCIRIDGQDISQVTQASLRSHIg 621
Cdd:cd03240     3 KLSIRNIR-SFHE------RSEIEFFSPLTL-IVGQNGAGKTTIIEaLKYALTGELPPNSKGGAHDPKLIREGEVRAQV- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 vvpqdTVLFNDTIADNIRYGRvtagndEVEAAAQAAGIH----DAIMAFPEGYrtqvgerglkLSGGEKQ------RVAI 691
Cdd:cd03240    74 -----KLAFENANGKKYTITR------SLAILENVIFCHqgesNWPLLDMRGR----------CSGGEKVlasliiRLAL 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNeraIQASLA------KVCANRTTIVVAHRLSTVVNADQIL-VIKDG 754
Cdd:cd03240   133 AETFGSNCGILALDEPTTNLDEEN---IEESLAeiieerKSQKNFQLIVITHDEELVDAADHIYrVEKDG 199
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
219-509 2.25e-03

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 40.83  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVN--LLTEKAPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSN---LRTFLWIRVQq 293
Cdd:cd18544     1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQklgQRIIYDLRRD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 ftsrrvellIFSHLHELSLRWHLGRRTGEVL-RIA-DrgTSSVTGLLSYLVFNVIptlADI--IIGIIYFSMFFNAWFGL 369
Cdd:cd18544    80 ---------LFSHIQRLPLSFFDRTPVGRLVtRVTnD--TEALNELFTSGLVTLI---GDLllLIGILIAMFLLNWRLAL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 370 IVFLCMSLYLTLTIVvtewrtkFRRAMNTQENATRAR--AVDSLLN-----FETVKYYNAESYEVERYRE---------- 432
Cdd:cd18544   146 ISLLVLPLLLLATYL-------FRKKSRKAYREVREKlsRLNAFLQesisgMSVIQLFNREKREFEEFDEinqeyrkanl 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 433 AIIKYQGL-----EWKSSASLVLLnqtqnLVIglgllagsllCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRM 507
Cdd:cd18544   219 KSIKLFALfrplvELLSSLALALV-----LWY----------GGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNI 283

                  ..
gi 1169100883 508 IQ 509
Cdd:cd18544   284 LQ 285
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
681-761 2.65e-03

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 40.32  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 LSGGEKQRVAIARTI-LKAPGII-LLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:cd03270   138 LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIGPGAGV 217

                  ....
gi 1169100883 758 ERGR 761
Cdd:cd03270   218 HGGE 221
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
681-749 3.69e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.97  E-value: 3.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883  681 LSGGEKQRVAIARTIL---KAPGIILLDEATSALDTSNERA-IQASLAKVCANRTTIVVAHRLSTVVNADQIL 749
Cdd:PRK00635   810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
557-712 3.69e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 40.92  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGCIRIDGQDISQVTQASLrshiGVVPQDTVLFN----D 632
Cdd:PRK10636   14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQL----AWVNQETPALPqpalE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 TIADNIRYGR-----VTAGNDEVE--AAAQAAGIHDAIMAFPEGYRTQVGERGL------------KLSGGEKQRVAIAR 693
Cdd:PRK10636   83 YVIDGDREYRqleaqLHDANERNDghAIATIHGKLDAIDAWTIRSRAASLLHGLgfsneqlerpvsDFSGGWRMRLNLAQ 162
                         170
                  ....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALD 712
Cdd:PRK10636  163 ALICRSDLLLLDEPTNHLD 181
ABC_6TM_McjD_like cd18556
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...
219-498 4.17e-03

Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.


Pssm-ID: 350000  Cd Length: 298  Bit Score: 39.93  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKA--PWNSLAWTVTSYVFL----KFLQgggtgstgFVSN-LRTFLWIRV 291
Cdd:cd18556     4 FFSILFISLLSSILISISPVILAKITDLLTSSSsdSYNYIVVLAALYVITisatKLLG--------FLSLyLQSSLRVEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 292 QQFTSRRVELLIFSHLHELSLRwhlgRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIV 371
Cdd:cd18556    76 IISISSSYFRYLYEQPKTFFVK----ENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 372 FLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIK---YQGLEWKSSASL 448
Cdd:cd18556   152 LLYAVLFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnSQKRYWKLTFKM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169100883 449 VLLNQTQNLVIGLGLLAGSLlcaYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18556   232 LILNSLLNVILFGLSFFYSL---YGVVNGQVSIGHFVLITSYILLLSTPI 278
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
231-436 4.38e-03

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 39.77  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNS----LAWTVTSYVFLKFLQGGGTGSTGFVSnlrTFLWIRVQQFTSRRVELLIFSH 306
Cdd:cd18577    13 AALPLMTIVFGDLFDAFTDFGSGESspdeFLDDVNKYALYFVYLGIGSFVLSYIQ---TACWTITGERQARRIRKRYLKA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 307 LHELSLRWHLGRRTGEVL-RIAD------RGTSSVTGLLsylvfnvIPTLADIIIGIIyFSMFFNAWFGLIVfLCMSLYL 379
Cdd:cd18577    90 LLRQDIAWFDKNGAGELTsRLTSdtnliqDGIGEKLGLL-------IQSLSTFIAGFI-IAFIYSWKLTLVL-LATLPLI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 380 TLTIVVTEWRTKfRRAMNTQENATRARAV--DSLLNFETVKYYNAESYEVERYREAIIK 436
Cdd:cd18577   161 AIVGGIMGKLLS-KYTKKEQEAYAKAGSIaeEALSSIRTVKAFGGEEKEIKRYSKALEK 218
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
555-590 4.58e-03

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: 38.68  E-value: 4.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1169100883 555 DGRETLQDVsftvMPGQTLALVGPSGAGKSTILRLL 590
Cdd:pfam03193  95 EGIEALKEL----LKGKTTVLAGQSGVGKSTLLNAL 126
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
544-610 5.67e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 40.11  E-value: 5.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 610
Cdd:NF033858    2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
AAA_22 pfam13401
AAA domain;
573-620 6.27e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 6.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1169100883 573 LALVGPSGAGKSTILRLLFRFYDI-SSGCIRIDGQdiSQVTQASLRSHI 620
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPEvRDSVVFVDLP--SGTSPKDLLRAL 54
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
575-595 8.35e-03

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 37.51  E-value: 8.35e-03
                          10        20
                  ....*....|....*....|.
gi 1169100883 575 LVGPSGAGKSTILRLLFRFYD 595
Cdd:cd00071     4 LSGPSGVGKSTLLKRLLEEFD 24
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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