|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-571 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 736.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 1 MLRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHM 80
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 81 LGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLT 160
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 161 FFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALN 240
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 241 SSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDIVDS 320
Cdd:COG1132 248 FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 321 KDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDM 400
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 401 TLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAI 480
Cdd:COG1132 408 TLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 481 ARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGG 560
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGL 567
|
570
....*....|.
gi 446867357 561 YSRLYEAQFSS 571
Cdd:COG1132 568 YARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-568 |
1.59e-179 |
|
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: 523.63 E-value: 1.59e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 2 LRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHML 81
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 82 GVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLtNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTF 161
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 162 FVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNE-----RFEKDQFAVNNARFRTTKLMAyki 236
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAEsrfrrRWENLLAKYLNARFKLRRLSN--- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 237 maLNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPD 316
Cdd:COG2274 380 --LLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 317 IVDSKDAMEVKHVHGDIQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGI 395
Cdd:COG2274 458 REEGRSKLSLPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 396 DTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQK 475
Cdd:COG2274 538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 476 QRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
570
....*....|...
gi 446867357 556 EQGGGYSRLYEAQ 568
Cdd:COG2274 698 ARKGLYAELVQQQ 710
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
13-307 |
1.60e-158 |
|
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: 454.60 E-value: 1.60e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQK 92
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 93 LFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLAL 172
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 173 YFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVT 252
Cdd:cd18549 161 YFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 253 LFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRY 307
Cdd:cd18549 241 LVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFERF 295
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-569 |
3.31e-154 |
|
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: 453.79 E-value: 3.31e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 3 RKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLG 82
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 83 VNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLmeigEIAHHGPEDLFIAV----MTLVGAFSFMMMINWKLAL 158
Cdd:TIGR02203 83 NKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDS----EQVASAATDAFIVLvretLTVIGLFIVLLYYSWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 159 LTFFVIPFLLWLALYFNKKmtgtFRRLFSDV----ADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAY 234
Cdd:TIGR02203 159 IVVVMLPVLSILMRRVSKR----LRRISKEIqnsmGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 235 KIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETE 314
Cdd:TIGR02203 235 SAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 315 PDIVDSKDAMEvkHVHGDIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQID 393
Cdd:TIGR02203 315 PEKDTGTRAIE--RARGDVEFRNVTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 394 GIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLK-ASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSG 472
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 473 GQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHE 552
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHN 552
|
570
....*....|....*..
gi 446867357 553 ELIEQGGGYSRLYEAQF 569
Cdd:TIGR02203 553 ELLARNGLYAQLHNMQF 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-568 |
1.55e-144 |
|
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: 430.40 E-value: 1.55e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 1 MLRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNW-TLILWACFGLLAVY----ILNAGLQYV-- 73
Cdd:COG5265 20 LRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGaAALLVVPVGLLLAYgllrLLSVLFGELrd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 74 -----VTywghmlgvniETDMRQ---KLFDHIQKLSFRFFDNNKTGHL---ISRLTND--------LMEIGeiahhgPED 134
Cdd:COG5265 100 alfarVT----------QRAVRRlalEVFRHLHALSLRFHLERQTGGLsrdIERGTKGiefllrflLFNIL------PTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 135 LFIAVMTLVGAFSFmmmiNWKLALLTFFVIPFLLWLALYFNKKMTGtFRRLFSDvADFNAcienNVGGI------RVVQA 208
Cdd:COG5265 164 LEIALVAGILLVKY----DWWFALITLVTVVLYIAFTVVVTEWRTK-FRREMNE-ADSEA----NTRAVdsllnyETVKY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 209 FGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIgfvlLTNIF----F 284
Cdd:COG5265 234 FGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFV----LVNAYliqlY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 285 RPIEKINAVIESYPKGIAGFKRYVELLETEPDIVDSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAF 364
Cdd:COG5265 310 IPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 365 VGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVK 444
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAAR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 445 RAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVI 524
Cdd:COG5265 470 AAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 446867357 525 AHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:COG5265 550 AHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-569 |
5.97e-138 |
|
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: 412.56 E-value: 5.97e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 2 LRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNA---GLQYVVTYWg 78
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLAlgtAARFYLVTW- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 79 hmLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHhgpEDLFIAV---MTLVGAFSFMMMINWK 155
Cdd:TIGR02204 85 --LGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIG---SSLSMALrnaLMCIGGLIMMFITSPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 156 LALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYK 235
Cdd:TIGR02204 160 LTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 236 IMA-LNSSISYMLMRLVTLfVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETE 314
Cdd:TIGR02204 240 TRAlLTAIVIVLVFGAIVG-VLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 315 PDIVDSKDAMEVKH-VHGDIQYSNVTFGYENK--EPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQ 391
Cdd:TIGR02204 319 PDIKAPAHPKTLPVpLRGEIEFEQVNFAYPARpdQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 392 IDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLS 471
Cdd:TIGR02204 399 LDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 472 GGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSH 551
Cdd:TIGR02204 479 GGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTH 558
|
570
....*....|....*...
gi 446867357 552 EELIEQGGGYSRLYEAQF 569
Cdd:TIGR02204 559 AELIAKGGLYARLARLQF 576
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-565 |
1.39e-133 |
|
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: 388.51 E-value: 1.39e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:cd03251 1 VEFKNVTFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPIL 491
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 492 ILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLY 565
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-570 |
1.81e-129 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 390.92 E-value: 1.81e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 3 RKFFSYYKPYK-GLFI----LDFSCAVVAGLLELGFPLIVNQFidkllpGQ-NWTLILWACFGLLAVYILNAGLQYVVTY 76
Cdd:PRK11176 14 RRLWPTIAPFKaGLIVagvaLILNAASDTFMLSLLKPLLDDGF------GKaDRSVLKWMPLVVIGLMILRGITSFISSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 77 WGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHgpedlfiAVMTLV-------GAFSFM 149
Cdd:PRK11176 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSG-------ALITVVregasiiGLFIMM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 150 MMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAV--NNARFR 227
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKvsNRMRQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 228 TTKLMAykimalNSSISYMLMRLVT----LFVLICGTWFVLQGELTYGGFIgfVLLTNIF--FRPIEKINAVIESYPKGI 301
Cdd:PRK11176 241 GMKMVS------ASSISDPIIQLIAslalAFVLYAASFPSVMDTLTAGTIT--VVFSSMIalMRPLKSLTNVNAQFQRGM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 302 AGFKRYVELLETEPDIVDSKdaMEVKHVHGDIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLP 380
Cdd:PRK11176 313 AACQTLFAILDLEQEKDEGK--RVIERAKGDIEFRNVTFTYPGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 381 RFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYG-NLKASEAEIWQAVKRAQLEDLIYSQPDGL 459
Cdd:PRK11176 391 RFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNGL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 460 DTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVV 539
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILV 550
|
570 580 590
....*....|....*....|....*....|.
gi 446867357 540 VNKDGIAEQGSHEELIEQGGGYSRLYEAQFS 570
Cdd:PRK11176 551 VEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-559 |
2.94e-128 |
|
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: 387.19 E-value: 2.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 1 MLRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLL-PGQNWTLILWACFGLLAVYILNAGLQYVVTYWGH 79
Cdd:COG4988 4 LDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 80 MLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTndlmeigeiahHGPEDL-----------FIAVMTLVGAFSF 148
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT-----------EGVEALdgyfarylpqlFLAALVPLLILVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 149 MMMINWKLA---LLTFFVIPFLLWLALYFNKKMT----GTFRRLFSDVADfnacienNVGGIRVVQAFGNERFEKDQFAV 221
Cdd:COG4988 153 VFPLDWLSGlilLVTAPLIPLFMILVGKGAAKASrrqwRALARLSGHFLD-------RLRGLTTLKLFGRAKAEAERIAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 222 NNARFR--TTKLMAykiMALNSS-----ISYMLMRLVTLFVLicgtWFVLQGELTYGGFIGFVLLTNIFFRPIekiNAVI 294
Cdd:COG4988 226 ASEDFRkrTMKVLR---VAFLSSavlefFASLSIALVAVYIG----FRLLGGSLTLFAALFVLLLAPEFFLPL---RDLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 295 ESY---PKGIAGFKRYVELLETEPDIVDSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAG 371
Cdd:COG4988 296 SFYharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 372 KTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDL 451
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 452 IYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATI 531
Cdd:COG4988 456 VAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL 535
|
570 580
....*....|....*....|....*...
gi 446867357 532 KNADRIVVVNKDGIAEQGSHEELIEQGG 559
Cdd:COG4988 536 AQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
333-568 |
1.67e-124 |
|
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: 365.40 E-value: 1.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILI 492
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 493 LDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-569 |
4.84e-123 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 374.68 E-value: 4.84e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 7 SYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQN-W-TLILWACFGLLAVyilnagLQYVVtywghmlgVN 84
Cdd:PRK13657 12 QYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDiFpLLAAWAGFGLFNI------IAGVL--------VA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 85 IETDM---RQKL------FDHIQKLSFRFFDNNKTGHLIS---RLTNDL--MEIGEIAHHgpedlFIAVMTLVGAFSFMM 150
Cdd:PRK13657 78 RHADRlahRRRLavlteyFERIIQLPLAWHSQRGSGRALHtllRGTDALfgLWLEFMREH-----LATLVALVVLLPLAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 151 MINWKLALLTF-FVIPFLLWLALYFNKKMTGT------FRRLFSDVADfnacienNVGGIRVVQAFGNERFEkdqfaVNN 223
Cdd:PRK13657 153 FMNWRLSLVLVvLGIVYTLITTLVMRKTKDGQaaveehYHDLFAHVSD-------AIGNVSVVQSYNRIEAE-----TQA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 224 ARFRTTKLMAYKI-----MALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEK----INAVI 294
Cdd:PRK13657 221 LRDIADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQvvafINQVF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 295 ESYPKgiagFKRYVELLETEPDIVDSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTT 374
Cdd:PRK13657 301 MAAPK----LEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKST 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 375 LCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYS 454
Cdd:PRK13657 377 LINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 455 QPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNA 534
Cdd:PRK13657 457 KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA 536
|
570 580 590
....*....|....*....|....*....|....*
gi 446867357 535 DRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQF 569
Cdd:PRK13657 537 DRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-568 |
1.92e-114 |
|
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: 339.90 E-value: 1.92e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE--PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIG 410
Cdd:cd03249 1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 491 LILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
87-566 |
1.31e-112 |
|
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: 346.75 E-value: 1.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 87 TDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDlmeIGEIAHH-----GPedLFIAVMTLVGAFSFMMMINWKLAL--- 158
Cdd:COG4987 88 ADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD---VDALDNLylrvlLP--LLVALLVILAAVAFLAFFSPALALvla 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 159 ----LTFFVIPFLLWLAlyfnkkMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAY 234
Cdd:COG4987 163 lgllLAGLLLPLLAARL------GRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 235 KIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETE 314
Cdd:COG4987 237 RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 315 PDIVDSKDAMEVKHvHGDIQYSNVTFGYEN-KEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQID 393
Cdd:COG4987 317 PAVTEPAEPAPAPG-GPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 394 GIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGG 473
Cdd:COG4987 396 GVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 474 QKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEE 553
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
490
....*....|...
gi 446867357 554 LIEQGGGYSRLYE 566
Cdd:COG4987 556 LLAQNGRYRQLYQ 568
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-564 |
3.40e-112 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 350.18 E-value: 3.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 1 MLRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLL-----PGQNWTLILWACFGLLAVyiLNAGLQ---Y 72
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGgdkgpPALASAIFFMCLLSIASS--VSAGLRggsF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 73 VVTYwGHmlgvnIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMI 152
Cdd:TIGR00958 226 NYTM-AR-----INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 153 NWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRT---T 229
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQlnkR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 230 KLMAYKIMALNSSISYMLMRLVtlfVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVE 309
Cdd:TIGR00958 380 KALAYAGYLWTTSVLGMLIQVL---VLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 310 LLETEPDIVDSKDAMEvKHVHGDIQYSNVTFGYENK--EPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSS 387
Cdd:TIGR00958 457 YLDRKPNIPLTGTLAP-LNLEGLIEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 388 GSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERG 467
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 468 VKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAelSVGRTTLVIAHRLATIKNADRIVVVNKDGIAE 547
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
570
....*....|....*..
gi 446867357 548 QGSHEELIEQGGGYSRL 564
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKHL 710
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-559 |
1.81e-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: 329.19 E-value: 1.81e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIG 410
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 491 LILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGG 559
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
22-564 |
3.89e-91 |
|
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: 294.93 E-value: 3.89e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIvnqFIDKLLPG--QNWTLILWAcfGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQK 99
Cdd:TIGR03796 165 LLVLPGLVIPAFSQI---FVDEILVQgrQDWLRPLLL--GMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 100 LSFRFFDNNKTGHLISRL-TNDlmeigEIAHHGPEDLFIAVMTLVGAFSF---MMMINWKLALLTFfVIPFLLWLALYFN 175
Cdd:TIGR03796 240 LPVRFFAQRHAGDIASRVqLND-----QVAEFLSGQLATTALDAVMLVFYallMLLYDPVLTLIGI-AFAAINVLALQLV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKM-TGTFRRLFSDVADFNACIennVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYM---LMRLV 251
Cdd:TIGR03796 314 SRRrVDANRRLQQDAGKLTGVA---ISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLptlLTSLN 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 252 TLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDIV------DSKDAME 325
Cdd:TIGR03796 391 SALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLleepegSAATSEP 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 326 VKHVHGDIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSS 404
Cdd:TIGR03796 471 PRRLSGYVELRNITFGYSPLEpPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMF 484
Cdd:TIGR03796 551 LANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARAL 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELsvGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRL 564
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
6-567 |
3.55e-89 |
|
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: 286.79 E-value: 3.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 6 FSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNW--TLILWACFGllavyILNAGLQYVVTYWGHMLGV 83
Cdd:TIGR01192 11 LSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVlpTLALWAGFG-----VFNTIAYVLVAREADRLAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 84 NIETDMRQKLFDHIQKLSFRFFDNNKTG---HLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAfsfMMMINWKLAL-L 159
Cdd:TIGR01192 86 GRRATLLTEAFGRIISMPLSWHQQRGTSnalHTLLRATETLFGLWLEFMRQHLATFVALFLLIPT---AFAMDWRLSIvL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 160 TFFVIPFLLWLALYFNKKMTGT------FRRLFSDVADfnacienNVGGIRVVQAFgnERFEKDQFAVNNarfRTTKLMA 233
Cdd:TIGR01192 163 MVLGILYILIAKLVMQRTKNGQaavehhYHNVFKHVSD-------SISNVSVVHSY--NRIEAETSALKQ---FTNNLLS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 234 --YKIM---ALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYV 308
Cdd:TIGR01192 231 aqYPVLdwwALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 309 ELLETEPDIVDSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSG 388
Cdd:TIGR01192 311 DLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 389 SIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGV 468
Cdd:TIGR01192 391 QILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 469 KLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQ 548
Cdd:TIGR01192 471 RLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEK 550
|
570
....*....|....*....
gi 446867357 549 GSHEELIEQGGGYSRLYEA 567
Cdd:TIGR01192 551 GSFQELIQKDGRFYKLLRR 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-568 |
2.54e-88 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 284.69 E-value: 2.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 2 LRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWAcfGLLAVYI----LNAGLQYVVTYW 77
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVA--GLAAAYVglqlLAAGLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 78 GHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIgeiahhgpEDLFIAV-------MTLVGAFSF-M 149
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVI--------RDLYVTVvatvlrsAALIGAMLVaM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 150 MMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGN-----ERFEKDQFAVNNA 224
Cdd:PRK10790 161 FSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQqarfgERMGEASRSHYMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 225 RFRTTKLMAYKIMALNSSISYMLMrlvtlfvliCGtwFVLQGELTYGGFIGFVLLTnIFFRPIEKIN-AVIESYPKG--- 300
Cdd:PRK10790 241 RMQTLRLDGFLLRPLLSLFSALIL---------CG--LLMLFGFSASGTIEVGVLY-AFISYLGRLNePLIELTTQQsml 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 301 ----IAGfKRYVELLE-TEPDIVDSKDAMEvkhvHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTL 375
Cdd:PRK10790 309 qqavVAG-ERVFELMDgPRQQYGNDDRPLQ----SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 376 CSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNlKASEAEIWQAVKRAQLEDLIYSQ 455
Cdd:PRK10790 384 ASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 456 PDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNAD 535
Cdd:PRK10790 463 PDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEAD 542
|
570 580 590
....*....|....*....|....*....|...
gi 446867357 536 RIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-568 |
7.55e-88 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 285.70 E-value: 7.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 23 AVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSF 102
Cdd:TIGR03797 145 GLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 103 RFFDNNKTGHLISRLtndlMEIGEIAHHGPEDLFIAVMT-LVGAFSFMMMI--NWKLAL----LTFFVIPFLLWLALYfn 175
Cdd:TIGR03797 225 SFFRQYSTGDLASRA----MGISQIRRILSGSTLTTLLSgIFALLNLGLMFyySWKLALvavaLALVAIAVTLVLGLL-- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 kkMTGTFRRLFSDVADFNACIENNVGGI---RVVQAfgnerfEKDQFAV---NNARFRTTKLMAYKIMALNSSISYMLMR 249
Cdd:TIGR03797 299 --QVRKERRLLELSGKISGLTVQLINGIsklRVAGA------ENRAFARwakLFSRQRKLELSAQRIENLLTVFNAVLPV 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 250 LVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKI-NAVIESYpKGIAGFKRYVELLETEPDIVDSKdaMEVKH 328
Cdd:TIGR03797 371 LTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLsNTLISIL-AVIPLWERAKPILEALPEVDEAK--TDPGK 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 329 VHGDIQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRK 407
Cdd:TIGR03797 448 LSGAIEVDRVTFRYrPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 408 QIGIVQQDVFLFSGTIRENIAYGNLKASEaEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRK 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAELSVGRttLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEA 567
Cdd:TIGR03797 607 PRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARR 684
|
.
gi 446867357 568 Q 568
Cdd:TIGR03797 685 Q 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-567 |
1.43e-87 |
|
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: 285.48 E-value: 1.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 2 LRKFFSYYKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHML 81
Cdd:TIGR01193 144 LLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 82 GVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTnDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTF 161
Cdd:TIGR01193 224 GQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 162 FVIPFLLWLALYFNKkmtgTFRRLFSDV----ADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIM 237
Cdd:TIGR01193 303 LSIPVYAVIIILFKR----TFNKLNHDAmqanAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 238 ALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDI 317
Cdd:TIGR01193 379 QGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEF 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 318 VDSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT 397
Cdd:TIGR01193 459 INKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 398 KDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNL-KASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQ 476
Cdd:TIGR01193 539 KDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQ 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 477 RLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSvGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
570
....*....|.
gi 446867357 557 QGGGYSRLYEA 567
Cdd:TIGR01193 698 RNGFYASLIHN 708
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-568 |
1.01e-86 |
|
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: 268.59 E-value: 1.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEP-ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPIL 491
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 492 ILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-542 |
2.56e-86 |
|
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: 265.02 E-value: 2.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSGTIRENIaygnlkaseaeiwqavkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPPIL 491
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 492 ILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNK 542
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-540 |
3.58e-83 |
|
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: 269.16 E-value: 3.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIVNQFIDKLL-PGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKL 100
Cdd:TIGR02857 11 LGVLGALLIIAQAWLLARVVDGLIsAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 101 SFRFFDNNKTGHLISRLTN--DLMEiGEIAHHGPEdLFIAVMTLVGAFSFMMMINWKLA---LLTFFVIPFLLWLALYF- 174
Cdd:TIGR02857 91 GPRWLQGRPSGELATLALEgvEALD-GYFARYLPQ-LVLAVIVPLAILAAVFPQDWISGlilLLTAPLIPIFMILIGWAa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 175 ---NKKMTGTFRRLFSDVADFnaciennVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSIsymLMRLV 251
Cdd:TIGR02857 169 qaaARKQWAALSRLSGHFLDR-------LRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAV---LELFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 252 TLFVLICGTWF---VLQGELTY-GGFigFVL-LTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDIVDSKDAMEV 326
Cdd:TIGR02857 239 TLSVALVAVYIgfrLLAGDLDLaTGL--FVLlLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 327 KHVHGdIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLR 406
Cdd:TIGR02857 317 APASS-LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLK 486
Cdd:TIGR02857 396 DQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVV 540
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-550 |
6.43e-82 |
|
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: 255.50 E-value: 6.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQI 409
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSGTIRENIAYGNlKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGS 550
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-568 |
1.14e-80 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 263.88 E-value: 1.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 24 VVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFG-LLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSF 102
Cdd:PRK10789 5 IIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGtMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 103 RFFDNNKTGHLISRLTNDLMEIGEIAHHGpedlfiaVMTLV-----GAFSFMMM---INWKLALLTFFVIPFLLWLALYF 174
Cdd:PRK10789 85 EFYLRHRTGDLMARATNDVDRVVFAAGEG-------VLTLVdslvmGCAVLIVMstqISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 175 NKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLF 254
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 255 VLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDIVDSKDAmeVKHVHGDIQ 334
Cdd:PRK10789 238 AIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEP--VPEGRGELD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 335 YSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQ 413
Cdd:PRK10789 316 VNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 QDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILIL 493
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 494 DEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-306 |
1.71e-79 |
|
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: 251.70 E-value: 1.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 256 LICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
331-549 |
8.07e-78 |
|
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: 244.81 E-value: 8.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQI 409
Cdd:cd03245 1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQG 549
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
301-566 |
1.21e-69 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 234.72 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 301 IAGFKRYVELLETEPDIVDSKDAmEVKHVHGDIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLL 379
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTS-TAAADQVSLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 380 PRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIySQPDGL 459
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 460 DTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVV 539
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*..
gi 446867357 540 VNKDGIAEQGSHEELIEQGGGYSRLYE 566
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-557 |
4.05e-69 |
|
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: 233.10 E-value: 4.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 2 LRKFFSYYkpykgLFILDFSCAVvaGLLELGFPLIVNQFIDKLLPGQNwTLILWACFGL-LAVYILNAGLQYVVtywGHM 80
Cdd:COG4618 15 LRACRRAF-----LSVGLFSFFI--NLLMLTPPLYMLQVYDRVLTSRS-VDTLLMLTLLaLGLYAVMGLLDAVR---SRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 81 L---GVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLisrltNDLMEI-GEIAHHGPE---DLFIAVMTLVGAFsfmmMIN 153
Cdd:COG4618 84 LvrvGARLDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLrQFLTGPGLFalfDLPWAPIFLAVLF----LFH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 154 WKLALLTFFVIPFLLWLALyFNKKMTgtfRRLFSDVADF----NACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTT 229
Cdd:COG4618 155 PLLGLLALVGALVLVALAL-LNERLT---RKPLKEANEAairaNAFAEAALRNAEVIEAMGMLPALRRRWQRANARALAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 230 KLMAYKIMALNSSISymlmRLVTLF----VLICGTWFVLQGELTYGGFI------GFVLltniffRPIEKINAVIESYPK 299
Cdd:COG4618 231 QARASDRAGGFSALS----KFLRLLlqsaVLGLGAYLVIQGEITPGAMIaasilmGRAL------APIEQAIGGWKQFVS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 300 GIAGFKRYVELLETEPDivdSKDAMEVKHVHGDIQYSNVTFGYEN-KEPILNDISLKIHAGETVAFVGPSGAGKTTLCSL 378
Cdd:COG4618 301 ARQAYRRLNELLAAVPA---EPERMPLPRPKGRLSVENLTVVPPGsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 379 LPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIA-YGNlkASEAEIWQAVKRAQLEDLIYSQPD 457
Cdd:COG4618 378 LVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGD--ADPEKVVAAAKLAGVHEMILRLPD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 458 GLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKNADR 536
Cdd:COG4618 456 GYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDK 535
|
570 580
....*....|....*....|..
gi 446867357 537 IVVVnKDG-IAEQGSHEELIEQ 557
Cdd:COG4618 536 LLVL-RDGrVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-528 |
2.41e-68 |
|
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: 230.33 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 2 LRKFFSYYKPYKGLFILdfscAVVAGLLELGFPLIVnQFIDKLLPGQNWTL-----ILWACFGLLAVYILNAGLQYVVTY 76
Cdd:TIGR02868 1 LLRILPLLKPRRRRLAL----AVLLGALALGSAVAL-LGVSAWLISRAAEMppvlyLSVAAVAVRAFGIGRAVFRYLERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 77 WGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKL 156
Cdd:TIGR02868 76 VGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 157 A-------LLTFFVIPFL-LWLAlyfnkKMTGtfRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRT 228
Cdd:TIGR02868 156 AlilaaglLLAGFVAPLVsLRAA-----RAAE--QALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 229 TKLMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYV 308
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 309 ELLETEP--DIVDSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQS 386
Cdd:TIGR02868 309 EVLDAAGpvAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 387 SGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGER 466
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 467 GVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRL 528
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
16-306 |
3.37e-68 |
|
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: 222.31 E-value: 3.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 256 LICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAER 291
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
327-542 |
3.83e-68 |
|
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: 220.03 E-value: 3.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 327 KHVHGDIQYSNVTFGYENK--EPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSS 404
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMF 484
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNK 542
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-306 |
6.53e-67 |
|
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: 218.94 E-value: 6.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQN-WTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLF 94
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKsLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 95 DHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYF 174
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 175 NKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLF 254
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 255 VLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAER 292
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-557 |
3.54e-64 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 219.53 E-value: 3.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 11 PYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMR 90
Cdd:TIGR01842 3 KVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 91 QKLFDHiqklSFRFFDNNKTGHlISRLTNDLMEIGE-IAHHGPEDLFIAVMT---LVGAFSFMMMINWkLALLTFFVIPF 166
Cdd:TIGR01842 83 QPIFAA----SFSATLRRGSGD-GLQALRDLDQLRQfLTGPGLFAFFDAPWMpiyLLVCFLLHPWIGI-LALGGAVVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 167 LLWLALYFNKK---MTGTF---RRLFSDVADFNACIENNVGGIRVVQAFGNERfekdqfavnNARFRTTKLMAYKIMALN 240
Cdd:TIGR01842 157 LALLNNRATKKplkEATEAsirANNLADSALRNAEVIEAMGMMGNLTKRWGRF---------HSKYLSAQSAASDRAGML 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 241 SSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDivdS 320
Cdd:TIGR01842 228 SNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPS---R 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 321 KDAMEVKHVHGDIQYSNVTFGYEN-KEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKD 399
Cdd:TIGR01842 305 DPAMPLPEPEGHLSVENVTIVPPGgKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 400 MTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLA 479
Cdd:TIGR01842 385 WDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
308-568 |
6.27e-64 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 219.72 E-value: 6.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 308 VELLETEPDIVDSKDamevKHVHGD----IQYSN-VTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRF 382
Cdd:PRK11174 325 VTFLETPLAHPQQGE----KELASNdpvtIEAEDlEILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 383 --YEqssGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLD 460
Cdd:PRK11174 400 lpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 461 TVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVV 540
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVM 556
|
250 260
....*....|....*....|....*...
gi 446867357 541 NKDGIAEQGSHEELIEQGGGYSRLYEAQ 568
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
16-306 |
2.59e-63 |
|
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: 209.59 E-value: 2.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 256 LICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAER 291
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
16-291 |
1.33e-60 |
|
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: 202.62 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQ--NWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKL 93
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGqgDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 94 FDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALY 173
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 174 FNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTL 253
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446867357 254 FVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPI----EKIN 291
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIrdlaEKFN 282
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-557 |
1.27e-56 |
|
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: 189.85 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVF--LFSGTIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMF 484
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIA-HRLATI-KNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
16-287 |
1.56e-55 |
|
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: 189.22 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270
....*....|....*....|....*....|..
gi 446867357 256 LICGTWFVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPI 273
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-542 |
2.05e-53 |
|
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: 179.33 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSGTIRENIaygnlkaseaeiwqavkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPPIL 491
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 492 ILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKNADRIVVVNK 542
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLED 170
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-287 |
2.81e-53 |
|
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: 182.46 E-value: 2.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNW---TLILWACFgLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQK 92
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetqALNVYSLA-LLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 93 LFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLAL 172
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 173 YFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVT 252
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 446867357 253 LFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
330-550 |
4.21e-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: 179.92 E-value: 4.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 330 HGDIQYSNVTFGYE-NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQ 408
Cdd:cd03369 4 HGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSGTIRENIAYGNlKASEAEIWQAVKraqledliysqpdgldtvIGERGVKLSGGQKQRLAIARMFLKNP 488
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 489 PILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGS 550
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-563 |
1.45e-52 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 194.09 E-value: 1.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 3 RKFFSYYKpykGLFILDFSCAVVAGLLELgFPLIVNQFIDKLLPGQNwtliLWACFGLLAVYILNAGLQYVVT-----YW 77
Cdd:PTZ00265 818 REIFSYKK---DVTIIALSILVAGGLYPV-FALLYAKYVSTLFDFAN----LEANSNKYSLYILVIAIAMFISetlknYY 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 78 GHMLGVNIETDMRQKLFDHI--QKLSFRFFDNNKTGHLISRLTND--LMEIGEIAHhgpedlfiavmtlVGAFSFMMMIN 153
Cdd:PTZ00265 890 NNVIGEKVEKTMKRRLFENIlyQEISFFDQDKHAPGLLSAHINRDvhLLKTGLVNN-------------IVIFTHFIVLF 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 154 WKLALLTFFVIPFLLWLalyfnkkMTGT---FRRLFSDVADFNACIE------NNVGGIRVVQAfGNERFEKDQFAVNNA 224
Cdd:PTZ00265 957 LVSMVMSFYFCPIVAAV-------LTGTyfiFMRVFAIRARLTANKDvekkeiNQPGTVFAYNS-DDEIFKDPSFLIQEA 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 225 RFRTTKLMAY---------------------KIMALNSSISYMLMRLVTLFVLICGTWF----VLQGELTYGGFIGfVLL 279
Cdd:PTZ00265 1029 FYNMNTVIIYgledyfcnliekaidysnkgqKRKTLVNSMLWGFSQSAQLFINSFAYWFgsflIRRGTILVDDFMK-SLF 1107
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 280 TNIFFRPIE-KINAVIESYPKGIAGFKRYVELLeTEPDIVDSKD--AMEVKH---VHGDIQYSNVTFGYENKE--PILND 351
Cdd:PTZ00265 1108 TFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLI-IRKSNIDVRDngGIRIKNkndIKGKIEIMDVNFRYISRPnvPIYKD 1186
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 352 ISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE----------------------------------------------- 384
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 385 -------QSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPD 457
Cdd:PTZ00265 1267 gedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPN 1346
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 458 GLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKNAD 535
Cdd:PTZ00265 1347 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSD 1426
|
650 660 670
....*....|....*....|....*....|....
gi 446867357 536 RIVVVN---KDG--IAEQGSHEELIE-QGGGYSR 563
Cdd:PTZ00265 1427 KIVVFNnpdRTGsfVQAHGTHEELLSvQDGVYKK 1460
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-541 |
9.28e-52 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 191.78 E-value: 9.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 5 FFSYYK----PYKGLFILDFSCAVVAGLlelGFPLIVNQF---IDKLLPGQNWTLILwacFGLLAVYILNAGLQYVVTYW 77
Cdd:PTZ00265 47 FFLPFKclpaSHRKLLGVSFVCATISGG---TLPFFVSVFgviMKNMNLGENVNDII---FSLVLIGIFQFILSFISSFC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 78 GHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTghliSRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAF----SFMMMIN 153
Cdd:PTZ00265 121 MDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTKFITIFTYASAFlglyIWSLFKN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 154 WKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMA 233
Cdd:PTZ00265 197 ARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 234 YKIMALNssisymlMRLVTLFVLIC---GTWF---VLQGELT--------YGGFIGFVLL---TNIFFRPIEKINavIES 296
Cdd:PTZ00265 277 NFMESLH-------IGMINGFILASyafGFWYgtrIIISDLSnqqpnndfHGGSVISILLgvlISMFMLTIILPN--ITE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 297 YPKGIAGFKRYVELLETEPDIVDSKDAMEVKHVHgDIQYSNVTFGYENKE--PILNDISLKIHAGETVAFVGPSGAGKTT 374
Cdd:PTZ00265 348 YMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKST 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 375 LCSLLPRFYEQSSGSIQI-DGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYG--NLKASEA-------------- 437
Cdd:PTZ00265 427 ILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlySLKDLEAlsnyynedgndsqe 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 438 -----------------------------------------EIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQ 476
Cdd:PTZ00265 507 nknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQ 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 477 RLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKNADRIVVVN 541
Cdd:PTZ00265 587 RISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVLS 653
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
16-306 |
4.63e-51 |
|
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: 177.21 E-value: 4.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQ------NWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDM 89
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 90 RQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLW 169
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 170 LALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKImalnSSISYMLMR 249
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY----SGLLMPIMN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 250 LVT--LFVLIC--GTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18547 237 FINnlGYVLVAvvGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
89-559 |
6.83e-51 |
|
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: 189.00 E-value: 6.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 89 MRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAhhgPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPF-- 166
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMI---PPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLgl 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 167 LLWLALYFNKKMTGTFRRLFS-----DVADFNacieNNVGGIRVVQAFG-NERFEKdqfaVNNARFRTTKLMAYKIMALN 240
Cdd:TIGR00957 1117 LYFFVQRFYVASSRQLKRLESvsrspVYSHFN----ETLLGVSVIRAFEeQERFIH----QSDLKVDENQKAYYPSIVAN 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 241 SSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIG----FVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPD 316
Cdd:TIGR00957 1189 RWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGlsvsYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPW 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 317 IVDSKDAMEVKHVHGDIQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGI 395
Cdd:TIGR00957 1269 QIQETAPPSGWPPRGRVEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 396 DTKDMTLSSLRKQIGIVQQDVFLFSGTIRENI-AYGNLkaSEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQ 474
Cdd:TIGR00957 1349 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQ 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 475 KQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
....*
gi 446867357 555 IEQGG 559
Cdd:TIGR00957 1507 LQQRG 1511
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
58-567 |
8.53e-51 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 188.65 E-value: 8.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 58 FGLLAVYILNaglqyvvTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFI 137
Cdd:PLN03232 961 FGQVAVTFTN-------SFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMN 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 138 AVMTLVGAFSFMMMINwKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDV-----ADFNACIeNNVGGIRVVQAFGNE 212
Cdd:PLN03232 1034 QLWQLLSTFALIGTVS-TISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTrspiyAQFGEAL-NGLSSIRAYKAYDRM 1111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 213 RFEKDQFAVNNARFRttklmaykiMALNSSISYMLMRLVTL---FVLICGTWFVLQ-----GELTYGGFIGFVL--LTNI 282
Cdd:PLN03232 1112 AKINGKSMDNNIRFT---------LANTSSNRWLTIRLETLggvMIWLTATFAVLRngnaeNQAGFASTMGLLLsyTLNI 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 283 --FFRPIEKINAVIESYPKGIAGFKRYVELLETEPDIVDSKDAMEVKHVHGDIQYSNVTFGYENK-EPILNDISLKIHAG 359
Cdd:PLN03232 1183 ttLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPS 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 360 ETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYGNlKASEAEI 439
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADL 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 440 WQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGR 519
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446867357 520 TTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIE-QGGGYSRLYEA 567
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVHS 1470
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
16-306 |
1.25e-50 |
|
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: 176.06 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQ-NWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLF 94
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 95 DHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYF 174
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 175 NKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLF 254
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 255 VLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKR 292
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-306 |
2.46e-50 |
|
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: 175.78 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 34 PLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHL 113
Cdd:cd18564 34 PLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 114 ISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFN 193
Cdd:cd18564 114 LSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 194 ACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGF 273
Cdd:cd18564 194 SVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL 273
|
250 260 270
....*....|....*....|....*....|...
gi 446867357 274 IGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18564 274 LVFLAYLKNLYKPVRDLAKLTGRIAKASASAER 306
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-288 |
2.60e-50 |
|
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: 175.39 E-value: 2.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLL----PGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQ 91
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 92 KLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLA 171
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 172 LYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLV 251
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446867357 252 TLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIE 288
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQ 277
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
58-560 |
4.25e-50 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 186.87 E-value: 4.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 58 FGLLAVYILNaglqyvvTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIgeiahhgpeDLFI 137
Cdd:PLN03130 964 FGQVLVTLLN-------SYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDI---------DRNV 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 138 AVmtlvgaFSFMMMINWKLALLTFFVIPFL----LWLA-----------LYFN------KKMTGTFRrlfSDV-ADFNAC 195
Cdd:PLN03130 1028 AV------FVNMFLGQIFQLLSTFVLIGIVstisLWAImpllvlfygayLYYQstarevKRLDSITR---SPVyAQFGEA 1098
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 196 IeNNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLmaykimalnSSISYMLMRLVTL---FVLICGTWFVLQGE----- 267
Cdd:PLN03130 1099 L-NGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNM---------SSNRWLAIRLETLgglMIWLTASFAVMQNGraenq 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 268 ----------LTYGGFIGfVLLTNIFfrpieKINAVIESYPKGIAGFKRYVELLETEPDIVDSKDAMEVKHVHGDIQYSN 337
Cdd:PLN03130 1169 aafastmgllLSYALNIT-SLLTAVL-----RLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFED 1242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 338 VTFGYE-NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDV 416
Cdd:PLN03130 1243 VVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAP 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFSGTIRENIAYGNlKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEA 496
Cdd:PLN03130 1323 VLFSGTVRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 497 TSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGG 560
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-542 |
1.12e-49 |
|
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: 170.73 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQ 414
Cdd:cd03225 3 KNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 --DVFLFSGTIRENIAYG--NLKASEAEIWQAVKRA----QLEDLiysqpdgLDTVIGErgvkLSGGQKQRLAIARMFLK 486
Cdd:cd03225 83 npDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEAlelvGLEGL-------RDRSPFT----LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIA-HRLATIKN-ADRIVVVNK 542
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLED 209
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
16-307 |
2.88e-48 |
|
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: 169.59 E-value: 2.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEdLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 256 LICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRY 307
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
314-557 |
1.47e-47 |
|
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: 173.55 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 314 EPDIVDSKDAMEVKHVHgdiqysnVTFGYENKE--PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQ 391
Cdd:COG1123 251 APAAAAAEPLLEVRNLS-------KRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 392 IDGIDTKDMT---LSSLRKQIGIVQQDVF--LFSG-TIRENIAYG---NLKASEAEIWQAVKRAqLEDLiysqpdGLDTV 462
Cdd:COG1123 324 FDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRERVAEL-LERV------GLPPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 463 IGER-GVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIV 538
Cdd:COG1123 397 LADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVA 476
|
250
....*....|....*....
gi 446867357 539 VVNKDGIAEQGSHEELIEQ 557
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-554 |
8.02e-47 |
|
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: 163.51 E-value: 8.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQ-----SSGSIQIDG--IDTKDMTLSSL 405
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGkdIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 406 RKQIGIVQQDVFLFSGTIRENIAYG-------NLKASEAEIWQAVKRAQLEDLIYSQPDGLDtvigergvkLSGGQKQRL 478
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-498 |
8.52e-47 |
|
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: 160.89 E-value: 8.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSG-TIRENI 427
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 428 AYGNL------KASEAEIWQAVKRAQLEDLiysqpdgLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:pfam00005 81 RLGLLlkglskREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-549 |
4.35e-46 |
|
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: 160.17 E-value: 4.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGI 411
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSGTIRENIaygnlkaseaeiwqavkraqledliysqpdgldtvigerGVKLSGGQKQRLAIARMFLKNPPIL 491
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 492 ILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQG 549
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
16-306 |
4.96e-46 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) 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: 349990 [Multi-domain] Cd Length: 292 Bit Score: 163.81 E-value: 4.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 256 LICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18546 241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEK 291
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
22-287 |
1.41e-45 |
|
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: 162.27 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLS 101
Cdd:cd18576 4 LLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 102 FRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGT 181
Cdd:cd18576 84 LSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 182 FRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICGTW 261
Cdd:cd18576 164 SKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGR 243
|
250 260
....*....|....*....|....*.
gi 446867357 262 FVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:cd18576 244 LVLAGELTAGDLVAFLLYTLFIAGSI 269
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-545 |
1.59e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.60 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSGTIRENIAYGNLKASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVK-LSGGQKQRLAIARMFLKNPPIL 491
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRERALEL-LERL------GLPPDILDKPVErLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 492 ILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGI 545
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
331-560 |
4.86e-44 |
|
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: 157.38 E-value: 4.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGYENK-EPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQI 409
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSGTIRENIAyGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGG 560
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
333-544 |
8.34e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.59 E-value: 8.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY---ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLL-----PrfyeqSSGSIQIDGIDTKDMT--- 401
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrP-----TSGEVLIDGQDISSLSere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLRKQ-IGIVQQDVFLFSG-TIRENIA----YGNLKASEAEIW--QAVKRAQLEDLIYSQPDgldtvigergvKLSGG 473
Cdd:COG1136 80 LARLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERarELLERVGLGDRLDHRPS-----------QLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 474 QKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKNADRIVVVnKDG 544
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRL-RDG 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-544 |
1.14e-43 |
|
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: 154.16 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE----PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslrkQ 408
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSGTIRENIAYGNlKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNP 488
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGK-PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 489 PILILDEATSALDTET-----ELAIQKSLAElsvGRTTLVIAHRLATIKNADRIVVVnKDG 544
Cdd:cd03250 147 DIYLLDDPLSAVDAHVgrhifENCILGLLLN---NKTRILVTHQLQLLPHADQIVVL-DNG 203
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-306 |
4.68e-43 |
|
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: 156.19 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 40 FIDKLLPGQNWTLiLWACFGLLAV-YILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLT 118
Cdd:cd18565 40 VPASLGPADPRGQ-LWLLGGLTVAaFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 119 NDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIEN 198
Cdd:cd18565 119 NDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLEN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 199 NVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQG------ELTYGG 272
Cdd:cd18565 199 NLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGT 278
|
250 260 270
....*....|....*....|....*....|....
gi 446867357 273 FIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18565 279 LVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKR 312
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
333-555 |
1.58e-42 |
|
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: 152.45 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAY--GNLKASEAEIWQAVKraQLEDLIYSQPDGLdtviGER-GVKLSGGQKQRLAIARMFLKNP 488
Cdd:cd03295 81 IQQIGLFPHmTVEENIALvpKLLKWPKEKIRERAD--ELLALVGLDPAEF----ADRyPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 489 PILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
333-554 |
1.64e-42 |
|
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: 153.35 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDM-TLSSLRKQIG 410
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPdgldtvigergVKLSGGQKQRLAIAR 482
Cdd:TIGR04520 81 MVFQnpDNQFVGATVEDDVAFGleNLGVPREEMRKRVDEAlklvGMEDFRDREP-----------HLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
333-559 |
2.88e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 151.93 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSsLRKQIGIV 412
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAY------GNLKASEAEIWQAVKRAQLEDLiysqpdgLDTVIGErgvkLSGGQKQRLAIARMFL 485
Cdd:COG4555 80 PDERGLYDRlTVRENIRYfaelygLFDEELKKRIEELIELLGLEEF-------LDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQGG 559
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-557 |
2.91e-42 |
|
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: 158.91 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCS----LLPRFYEQSsGSIQIDGIDTKDMTLSSLRK 407
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALalmgLLPHGGRIS-GEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 408 QIGIVQQDVF--LFSGTIRENIAYG--NLKASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARM 483
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAleNLGLSRAEARARVLEL-LEAV------GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 484 FLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
16-306 |
3.56e-42 |
|
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: 152.97 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQ-NWTLILWACFGLLAVYILNAGLQYVVTYWGHmlgvNIETDMRQKLF 94
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGsSGGLLALLVALFLLQAVLSALSSYLLGRTGE----RVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 95 DHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYF 174
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 175 NKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLF 254
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 255 VLICGTWFVLQGELTYGGFIGFVL-LTNIFFrPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18551 237 VLGVGGARVASGALTVGTLVAFLLyLFQLIT-PLSQLSSFFTQLQKALGALER 288
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-541 |
7.56e-42 |
|
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: 148.49 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDMTLSSLRKQIG 410
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSG-TIRENIAYGnlkaseaeiwqavkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 490 ILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA-TIKNADRIVVVN 541
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLR 175
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
13-290 |
1.60e-41 |
|
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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 151.48 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQK 92
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 93 LFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLAL 172
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 173 YFNKKMTGTF---RRLFSDV-ADFNACIEnnvgGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLM 248
Cdd:cd18540 161 YFQKKILKAYrkvRKINSRItGAFNEGIT----GAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446867357 249 RLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKI 290
Cdd:cd18540 237 SIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQL 278
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-557 |
1.81e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGIV 412
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAY-GNLK-ASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfARLYgLPRKEARERIDEL-LELF------GLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSVGRTTLVIA-HRLATI-KNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
16-306 |
3.80e-41 |
|
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: 150.24 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFV 255
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 256 LICGTWFVLQGELTYGGFIGFV-LLTNIFFrPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFInYLMQILM-SLMMLSMVFVMLPRASASAKR 291
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-287 |
5.96e-41 |
|
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: 149.94 E-value: 5.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN 175
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 176 KKMTGTFRRLFSDVADFNACIEN--NVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTL 253
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270
....*....|....*....|....*....|....
gi 446867357 254 FVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPL 274
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-544 |
5.98e-41 |
|
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: 147.64 E-value: 5.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY---ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLL-----PrfyeqSSGSIQIDGIDTKDMT--- 401
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrP-----TSGEVRVDGTDISKLSeke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLR-KQIGIVQQDVFLFSG-TIRENIA----YGNLKASEAEIW--QAVKRAQLEDLIYSQPDgldtvigergvKLSGG 473
Cdd:cd03255 76 LAAFRrRHIGFVFQSFNLLPDlTALENVElpllLAGVPKKERRERaeELLERVGLGDRLNHYPS-----------ELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 474 QKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAH--RLAtiKNADRIVVVnKDG 544
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHdpELA--EYADRIIEL-RDG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
333-554 |
6.18e-41 |
|
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: 148.03 E-value: 6.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT---LSSLRKQI 409
Cdd:cd03261 1 IELRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSG-TIRENIAYG---NLKASEAEIWQAVkRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFL 485
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIV-LEKLEAV------GLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEEL 554
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-557 |
1.20e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdMTLSSLRKQIGIV 412
Cdd:COG1121 7 IELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQ-------------DVFLfSGTIRENIAYGNLKASE-AEIWQAVKRAQLEDLIYSQpdgldtvIGErgvkLSGGQKQRL 478
Cdd:COG1121 81 PQraevdwdfpitvrDVVL-MGRYGRRGLFRRPSRADrEAVDEALERVGLEDLADRP-------IGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATI-KNADRIVVVNKDGIAEqGSHEELIE 556
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPPEEVLT 227
|
.
gi 446867357 557 Q 557
Cdd:COG1121 228 P 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
333-557 |
2.43e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 146.29 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVT--FGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDMTLSSLRKQ 408
Cdd:COG1126 2 IEIENLHksFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSG-TIRENIAYG---NLKASEAEiwqAVKRAqlEDLiysqpdgLDTV-IGERGVK----LSGGQKQRLA 479
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLApikVKKMSKAE---AEERA--MEL-------LERVgLADKADAypaqLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 480 IAR---MflkNPPILILDEATSALDTET--E-LAIQKSLAELsvGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHE 552
Cdd:COG1126 147 IARalaM---EPKVMLFDEPTSALDPELvgEvLDVMRDLAKE--GMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPE 221
|
....*
gi 446867357 553 ELIEQ 557
Cdd:COG1126 222 EFFEN 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
337-555 |
3.87e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 146.34 E-value: 3.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDV 416
Cdd:COG1120 6 NLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FL-FSGTIRENIAYGNL----------KASEAEIWQAVKRAQLEDLIysqpdgldtvigERGV-KLSGGQKQRLAIARMF 484
Cdd:COG1120 85 PApFGLTVRELVALGRYphlglfgrpsAEDREAVEEALERTGLEHLA------------DRPVdELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAH--RLAtIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHdlNLA-ARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-542 |
4.96e-40 |
|
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: 142.77 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 334 QYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQ 413
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 QdvflfsgtireniaygnlkaseaeiwqavkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILIL 493
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 494 DEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKNA-DRIVVVNK 542
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKD 155
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
333-544 |
8.18e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.42 E-value: 8.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT---LSSLRKQI 409
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDV-FLFSGTIRENIAYGnLKA---SEAEIWQAVKRA----QLEDLIYSQPDgldtvigergvKLSGGQKQRLAIA 481
Cdd:COG2884 82 GVVFQDFrLLPDRTVYENVALP-LRVtgkSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 482 RMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIA-HRLATIKNADRIVVVNKDG 544
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKRVLELEDG 213
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
20-306 |
4.02e-39 |
|
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: 144.63 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 20 FSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQK 99
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 100 LSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMT 179
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 180 GTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICG 259
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446867357 260 TWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASER 288
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-539 |
6.85e-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: 141.84 E-value: 6.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE---PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdMTLSSLRKQI 409
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFS-GTIRENIAYGnLKA---SEAEIwQAVKRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFL 485
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-LELqgvPKAEA-RERAEELLELV------GLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA-TIKNADRIVV 539
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVV 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
325-549 |
1.55e-38 |
|
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: 141.10 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 325 EVKHVhgdiqysNVTFG-YENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT-- 401
Cdd:cd03257 3 EVKNL-------SVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 -LSSLRKQIGIVQQDVFL---FSGTIRENIA-----YGNLKASEAEiwqavKRAQLEDLIYSQPDglDTVIGERGVKLSG 472
Cdd:cd03257 76 lRKIRRKEIQMVFQDPMSslnPRMTIGEQIAeplriHGKLSKKEAR-----KEAVLLLLVGVGLP--EEVLNRYPHELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 473 GQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRiVVVNKDG-IAEQ 548
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADR-VAVMYAGkIVEE 227
|
.
gi 446867357 549 G 549
Cdd:cd03257 228 G 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
332-554 |
1.93e-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: 144.47 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMT-LSSLRKQIG 410
Cdd:COG3842 5 ALELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVTgLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKRA----QLEDLiysqpdgldtviGERGVK-LSGGQKQRLAIAR 482
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFGlrMRGVPKAEIRARVAELlelvGLEGL------------ADRYPHqLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA---TIknADRIVVVNKDGIAEQGSHEEL 554
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-542 |
5.04e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 137.91 E-value: 5.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDmTLSSLRKQIGIV 412
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIaygnlkaseaeiwqavkraqledliysqpdgldtvigergvKLSGGQKQRLAIARMFLKNPPIL 491
Cdd:cd03230 79 PEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 492 ILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKN-ADRIVVVNK 542
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNN 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
333-555 |
6.62e-38 |
|
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: 139.64 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYEN---KEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSL---R 406
Cdd:cd03258 2 IELKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKR----AQLEDLIYSQPDgldtvigergvKLSGGQKQRLA 479
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPleIAGVPKAEIEERVLEllelVGLEDKADAYPA-----------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELI 555
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
13-290 |
1.02e-37 |
|
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: 141.04 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQK 92
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 93 LFDHIQKLSFRFFDNNKTGHLISRLtNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLAL 172
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 173 YFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVT 252
Cdd:cd18570 160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 446867357 253 LFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKI 290
Cdd:cd18570 240 LLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENL 277
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
336-546 |
1.41e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 138.05 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMtlsslRKQIGIV-QQ 414
Cdd:cd03235 3 EDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVpQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DVFL--FSGTIRENIAYGNL----------KASEAEIWQAVKRAQLEDLIYSQpdgldtvIGErgvkLSGGQKQRLAIAR 482
Cdd:cd03235 77 RSIDrdFPISVRDVVLMGLYghkglfrrlsKADKAKVDEALERVGLSELADRQ-------IGE----LSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATI-KNADRIVVVNKDGIA 546
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-549 |
1.97e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 137.65 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHgdiqysnVTFGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMT-L 402
Cdd:cd03259 1 LELKGLS-------KTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG---RDVTgV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 403 SSLRKQIGIVQQDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVKLSGGQKQRLA 479
Cdd:cd03259 68 PPERRNIGMVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVREL-LELV------GLEGLLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQG 549
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
325-554 |
4.40e-37 |
|
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: 138.01 E-value: 4.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 325 EVKHVHgdiqysnVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLS 403
Cdd:COG1124 3 EVRNLS-------VSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 404 SLRKQIGIVQQDVFL-----FS--GTIRENIAYGNLKASEAEIWQAVKRAQL-EDLIYSQPDgldtvigergvKLSGGQK 475
Cdd:COG1124 76 AFRRRVQMVFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPH-----------QLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 476 QRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHE 552
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
..
gi 446867357 553 EL 554
Cdd:COG1124 225 DL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
336-549 |
4.49e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 135.64 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVqqd 415
Cdd:cd03214 3 ENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 vflfsgtireniaygnlkaseaeiWQAVKRAQLEDLIysqpdgldtvigERGVK-LSGGQKQRLAIARMFLKNPPILILD 494
Cdd:cd03214 79 ------------------------PQALELLGLAHLA------------DRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 495 EATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQG 549
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
333-556 |
6.30e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 6.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQ----AVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARM 483
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGleNKKVPPKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 484 FLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLV-IAHRLATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-558 |
6.71e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.22 E-value: 6.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQ--DVFLFSGTIRENIAYG--NLKASEAE----IWQAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARM 483
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 484 FLKNPPILILDEATSALDT---ETELAIQKSLAELSvGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQG 558
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPrgrREVLETVRQLKEQK-GITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-556 |
1.50e-36 |
|
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: 136.26 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT---LSSLRKQI 409
Cdd:COG1127 6 IEVRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSG-TIRENIAYG---NLKASEAEIWQAVkRAQLEDLiysqpdGLDTVI----GErgvkLSGGQKQRLAIA 481
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV-LEKLELV------GLPGAAdkmpSE----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 482 RMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-545 |
2.38e-35 |
|
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: 131.61 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSLRKQIGIVQQDV 416
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 --FLFSGTIRENIAYGNLKASEAeiwQAVKRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAG---NEQAETVLKDL------DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 495 EATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATIKN-ADRIVVVNKDGI 545
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-538 |
3.24e-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: 131.50 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDMTLSSLRKQIG 410
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSG-TIRENIAYG-----NLKASEAE--IWQAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIAR 482
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikvkGMSKAEAEerALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 483 MFLKNPPILILDEATSALDTET--E-LAIQKSLAElsVGRTTLVIAHRLATIKN-ADRIV 538
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELvgEvLDVMKDLAE--EGMTMVVVTHEMGFAREvADRVI 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
333-557 |
3.33e-35 |
|
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: 132.36 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMT-LSSLRKQIGI 411
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG---KDITnLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMF 484
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlrLKKLPKAEIKERVAEAldlvQLEGYANRKPS-----------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
331-554 |
3.77e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.59 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMT-LSSLRKQI 409
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTdLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLF-SGTIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPDGldtvigergvkLSGGQKQRLAIAR 482
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAaellGLEDLLDRKPKQ-----------LSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 483 MFLKNPPILILDEATSALD------TETELA-IQKSLaelsvGRTTLVIAHRLA---TIknADRIVVVNkDGIAEQ-GSH 551
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDaklrveMRAEIKrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMN-DGRIQQvGTP 218
|
...
gi 446867357 552 EEL 554
Cdd:COG3839 219 EEL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
325-555 |
4.43e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.82 E-value: 4.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 325 EVKHVHgdiqysnVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTL--C-SLLPRFyeqSSGSIQIDGIDTKDM 400
Cdd:COG1135 3 ELENLS-------KTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLirCiNLLERP---TSGSVLVDGVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 401 T---LSSLRKQIGIVQQDVFLFSG-TIRENIAYGnLK---ASEAEIWqavKRAQ-------LEDLIYSQPDgldtviger 466
Cdd:COG1135 73 SereLRAARRKIGMIFQHFNLLSSrTVAENVALP-LEiagVPKAEIR---KRVAellelvgLSDKADAYPS--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 467 gvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKD 543
Cdd:COG1135 140 --QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|..
gi 446867357 544 GIAEQGSHEELI 555
Cdd:COG1135 218 RIVEQGPVLDVF 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
333-556 |
4.66e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.14 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVT--FGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKD--MTLSSLRKQ 408
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSG-TIRENIAYGNLK---ASEAEiwqavKRAQLEDLiysqpdgLDTV-IGERG----VKLSGGQKQRLA 479
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLRvrgASKEE-----AEKQAREL-------LAKVgLAERAhhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 480 IARMFLKNPPILILDEATSALDTETE---LAIQKSLAElsVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAE--EGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
.
gi 446867357 556 E 556
Cdd:PRK09493 225 K 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
333-553 |
1.92e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 131.71 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGID--TKDMTLSSLR 406
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQAVKRA-QLEDLIYsqpdglDTVIGERGVKLSGGQKQRLAIA 481
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAmNIVGLDY------EDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 482 RMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEE 553
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
333-557 |
2.42e-34 |
|
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: 130.00 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT---KDMTLSSLRKQI 409
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSG-TIRENIAYGNLKA-----------SEAEIWQAvkRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQR 477
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRA--LAALERV------GLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHR--LATiKNADRIVVVnKDG-IAEQGSHE 552
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQvdLAR-EYADRIVGL-KDGrIVFDGPPA 230
|
....*
gi 446867357 553 ELIEQ 557
Cdd:cd03256 231 ELTDE 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-557 |
2.45e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 132.96 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENkEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTkDMTLSSLRKQIGIV 412
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAYG--NLKASEAEIWQAV----KRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMFL 485
Cdd:COG1118 81 FQHYALFPHmTVAENIAFGlrVRPPSKAEIRARVeellELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH------RLatiknADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
333-539 |
3.17e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.21 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE---PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdMTLSSLRKQI 409
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-----KPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIV-QQDVfLFs-gTIRENIAYG--NLKASEAEiwqavKRAQLEDLiysqpdgLDTViGERGVK------LSGGQKQRLA 479
Cdd:COG1116 83 GVVfQEPA-LLpwlTVLDNVALGleLRGVPKAE-----RRERAREL-------LELV-GLAGFEdayphqLSGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH------RLatiknADRIVV 539
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVV 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
320-569 |
4.90e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 132.76 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 320 SKDAMEVKHVhgdIQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKD 399
Cdd:PRK09452 5 NKQPSSLSPL---VELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG---QD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 400 MT-LSSLRKQIGIVQQDVFLFSG-TIRENIAYGnL---KASEAEIWQAVKRA----QLEDLIYSQPDgldtvigergvKL 470
Cdd:PRK09452 78 IThVPAENRHVNTVFQSYALFPHmTVFENVAFG-LrmqKTPAAEITPRVMEAlrmvQLEEFAQRKPH-----------QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 471 SGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNKDGIAE 547
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALqrKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQ 225
|
250 260
....*....|....*....|..
gi 446867357 548 QGSHEELIEQGggySRLYEAQF 569
Cdd:PRK09452 226 DGTPREIYEEP---KNLFVARF 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
331-557 |
8.54e-34 |
|
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: 129.59 E-value: 8.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYeQSSGSIQIDGIDTKDMTLSSLRKQI 409
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSGTIRENI-AYGnlKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNP 488
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 489 PILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
333-555 |
1.26e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.95 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKepILNdISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMT-LSSLRKQIGI 411
Cdd:COG3840 2 LRLDDLTYRYGDF--PLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---QDLTaLPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENIAYG---NLKASEAE---IWQAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMF 484
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlrpGLKLTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 485 LKNPPILILDEATSALD----TETeLAIQKSLAElSVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELI 555
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEM-LDLVDELCR-ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
333-554 |
1.88e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.87 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT---KDMTLSSLRKQI 409
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIV-QQ-------DVFlfsgtirENIAYGNL-----------KASEAEI---WQAVKRAQLEDLIYSQPDgldtvigerg 467
Cdd:COG3638 83 GMIfQQfnlvprlSVL-------TNVLAGRLgrtstwrsllgLFPPEDReraLEALERVGLADKAYQRAD---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 468 vKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRIVVVNK-- 542
Cdd:COG3638 146 -QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDgr 224
|
250
....*....|....*
gi 446867357 543 ---DGIAEQGSHEEL 554
Cdd:COG3638 225 vvfDGPPAELTDAVL 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-536 |
2.78e-33 |
|
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: 126.37 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT---KDMTLSSLRKQI 409
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSG-TIRENIAYGnLKASEAEIWQAVKR-AQLEDLIysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFA-LEVTGVPPREIRKRvPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADR 536
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTR 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
314-524 |
2.97e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.46 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 314 EPDIVDSKDAMEVKHVhgdiqysNVTFGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE-----QSSG 388
Cdd:COG1117 2 TAPASTLEPKIEVRNL-------NVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 389 SIQIDGID--TKDMTLSSLRKQIGIVQQDVFLFSGTIRENIAYG---NLKASEAEIWQAV----KRAQLEDLIYsqpDGL 459
Cdd:COG1117 72 EILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSELDEIVeeslRKAALWDEVK---DRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 460 DtvigERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSvGRTTLVI 524
Cdd:COG1117 149 K----KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVI 208
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-495 |
5.14e-33 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 133.00 E-value: 5.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 9 YKPYKGLFILDFSCAVVAGLLELGFPLIVNQFIDKllPGQNWTLILWACFGLLAVYIL-NAGLQYVVTYwghmLGVNIET 87
Cdd:COG4615 8 LRESRWLLLLALLLGLLSGLANAGLIALINQALNA--TGAALARLLLLFAGLLVLLLLsRLASQLLLTR----LGQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 88 DMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEdLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFL 167
Cdd:COG4615 82 RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 168 LWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVqAFGNER---FEKDQFAVNNARFRTTKLMAYKIMALNSSIS 244
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKEL-KLNRRRrraFFDEDLQPTAERYRDLRIRADTIFALANNWG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 245 YMLMrlvtlFVLICGTWFVLQ--GELTYGGFIGFVLlTNIFFR-PIEKINAVIESYPKGIAGFKRYVEL---LETEPDIV 318
Cdd:COG4615 240 NLLF-----FALIGLILFLLPalGWADPAVLSGFVL-VLLFLRgPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 319 DSKDAMEVKHVHGDIQYSNVTFGYENKEP----ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG 394
Cdd:COG4615 314 ADAAAPPAPADFQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 395 IDTKDMTLSSLRKQIGIVQQDVFLFsgtirENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVigergvKLSGGQ 474
Cdd:COG4615 394 QPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLERLELDHKVSVEDGRFSTT------DLSQGQ 462
|
490 500
....*....|....*....|.
gi 446867357 475 KQRLAIARMFLKNPPILILDE 495
Cdd:COG4615 463 RKRLALLVALLEDRPILVFDE 483
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
349-557 |
7.42e-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: 126.99 E-value: 7.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSL----RKQIGIVQQDVFLFSG-TI 423
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAYG------NLKASEAEIWQAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMFLKNPPILILDEAT 497
Cdd:cd03294 120 LENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 498 SALDTETELAIQKSLAELS--VGRTTLVIAHRLA-TIKNADRIVVVnKDGIAEQ-GSHEELIEQ 557
Cdd:cd03294 189 SALDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIM-KDGRLVQvGTPEEILTN 251
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
23-306 |
1.07e-32 |
|
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: 127.15 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 23 AVVAGLLELG----FPLIVNQFIDKLLPGQNWT-------LILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQ 91
Cdd:cd18554 4 TIVIGLVRFGipllLPLILKYIVDDVIQGSSLTldekvykLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 92 KLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLA 171
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 172 LYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLV 251
Cdd:cd18554 164 KYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 252 TLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKR 306
Cdd:cd18554 244 PLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDR 298
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
79-557 |
1.30e-32 |
|
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: 133.88 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 79 HMLgVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLAL 158
Cdd:TIGR01271 951 HTL-LTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFI 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 159 LTFFVIPFLLWLALYFnKKMTGTFRRLFSDVAD--FNACIeNNVGGIRVVQAFGNERFEKDQF--AVNnarFRTTKLMAY 234
Cdd:TIGR01271 1030 AAIPVAVIFIMLRAYF-LRTSQQLKQLESEARSpiFSHLI-TSLKGLWTIRAFGRQSYFETLFhkALN---LHTANWFLY 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 235 KimalnSSISYMLMRLVTLFVL--ICGTWFVLQGELTYGGFIGFV--LLTNIFFRPIEKINAVI--ESYPKGIAGFKRYV 308
Cdd:TIGR01271 1105 L-----STLRWFQMRIDIIFVFffIAVTFIAIGTNQDGEGEVGIIltLAMNILSTLQWAVNSSIdvDGLMRSVSRVFKFI 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 309 ELLETEPD--------------IVDSKDAMEVKHVHGDIQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKT 373
Cdd:TIGR01271 1180 DLPQEEPRpsggggkyqlstvlVIENPHAQKCWPSGGQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKS 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 374 TLCSLLPRFYeQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRENI-AYGnlKASEAEIWQAVKRAQLEDLI 452
Cdd:TIGR01271 1260 TLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYE--QWSDEEIWKVAEEVGLKSVI 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 453 YSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIK 532
Cdd:TIGR01271 1337 EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
490 500
....*....|....*....|....*
gi 446867357 533 NADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:TIGR01271 1417 ECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-549 |
2.44e-32 |
|
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: 123.46 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETvAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGIV 412
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAY-GNLKA-SEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYiAWLKGiPSKEVKARVDEV-LELV------NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQG 549
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
331-556 |
3.25e-32 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 132.60 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGYENKEP-ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQI 409
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSGTIRENIAyGNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 490 ILIL-DEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PTZ00243 1466 GFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-566 |
5.24e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 132.02 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 25 VAGLLELGF-------PLIVNQFIDKLLPGQNwtlilwACFGLLAVYILNAGLQYVV----TYWGHMLGVNIEtdMRQKL 93
Cdd:PLN03232 305 LGGIFKIGHdlsqfvgPVILSHLLQSMQEGDP------AWVGYVYAFLIFFGVTFGVlcesQYFQNVGRVGFR--LRSTL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 94 FDHIQKLSFRF-------FDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPF 166
Cdd:PLN03232 377 VAAIFHKSLRLthearknFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 167 LlwlALYFNKkmtgtFRRLFSD---VADFNACIENNV-GGIRVVQAFGNER-FEKDQFAVNNAR---FRTTKLMAykimA 238
Cdd:PLN03232 457 Q---TLIVRK-----MRKLTKEglqWTDKRVGIINEIlASMDTVKCYAWEKsFESRIQGIRNEElswFRKAQLLS----A 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 239 LNSSISYMLMRLVTLFVLicGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELLETEPDIV 318
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERIL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 319 DSKDAMEVKHVHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCS-LLPRFYEQSSGSIQIdgidt 397
Cdd:PLN03232 603 AQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI----- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 398 kdmtlsslRKQIGIVQQDVFLFSGTIRENIAYGNLKASEaEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQR 477
Cdd:PLN03232 678 --------RGSVAYVPQVSWIFNATVRENILFGSDFESE-RYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQR 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKS-LAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
570
....*....|
gi 446867357 557 QGGGYSRLYE 566
Cdd:PLN03232 829 SGSLFKKLME 838
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
333-548 |
8.63e-32 |
|
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: 121.98 E-value: 8.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDmtLSSLRKQIGIV 412
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAYGnLK---ASEAEIWQAVKRA----QLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMF 484
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFG-LKlrkVPKDEIDERVREVaellQIEHLLDRKPK-----------QLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNkDGIAEQ 548
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLqqRLGTTTIYVTHdQVEAMTMADRIAVMN-DGQIQQ 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
333-557 |
1.09e-31 |
|
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: 122.83 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSslRKQIGIV 412
Cdd:cd03296 3 IEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSG-TIRENIAYG------NLKASEAEIWQAVKraQLEDLIysQPDGLdtviGER-GVKLSGGQKQRLAIARMF 484
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlrvkprSERPPEAEIRAKVH--ELLKLV--QLDWL----ADRyPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
345-556 |
1.29e-31 |
|
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: 122.44 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 345 KEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMT-LSSLRKQIGIVQQDVFLFSG-T 422
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITnLPPEKRDISYVPQNYALFPHmT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIAYG--NLKASEAEIWQAVKRAQlEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSAL 500
Cdd:cd03299 88 VYKNIAYGlkKRKVDKKEIERKVLEIA-EML------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 501 DTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:cd03299 161 DVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
301-544 |
2.41e-31 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 128.39 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 301 IAGFKRYVELLETEPDIVDSKDAMEvkhvHGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTL----C 376
Cdd:COG4178 335 LAGFEEALEAADALPEAASRIETSE----DGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLlraiA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 377 SLLPRfyeqSSGSIQI-DGIDTkdMTLSslrkqigivqQDVFLFSGTIRENIAYGNL--KASEAEIWQAVKRAQLEDLIy 453
Cdd:COG4178 411 GLWPY----GSGRIARpAGARV--LFLP----------QRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLA- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 454 sqpDGLDTViGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKN 533
Cdd:COG4178 474 ---ERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAF 549
|
250
....*....|.
gi 446867357 534 ADRIVVVNKDG 544
Cdd:COG4178 550 HDRVLELTGDG 560
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
333-550 |
3.42e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 124.14 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI---LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT---KDMTLSSLR 406
Cdd:PRK11153 2 IELKNISKVFPQGGRTihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQDVFLFSG-TIRENIAYGnLKA---SEAEIWQAV----KRAQLEDLIYSQPdgldtvigergVKLSGGQKQRL 478
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALP-LELagtPKAEIKARVtellELVGLSDKADRYP-----------AQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGS 550
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINreLGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
336-539 |
8.26e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.12 E-value: 8.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPRfyeqSSGSIQIDGIDTKDmTLSSLRKQIGI 411
Cdd:COG4133 6 ENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLlrilAGLLPP----SAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENIAY----GNLKASEAEIWQAVKRAQLEDLiysqpdgLDTVIGergvKLSGGQKQRLAIARMFLK 486
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAE-LSVGRTTLVIAHRLATIKNADRIVV 539
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
24-279 |
1.27e-30 |
|
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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 121.05 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 24 VVAGLLELGFPLIVNQFIDKLLPGQNWTLI---LWACFGLLAVYILNAGLQYVVTYWghmLGVNIETDMRQKLFDHIQKL 100
Cdd:cd18575 6 LIAAAATLALGQGLRLLIDQGFAAGNTALLnraFLLLLAVALVLALASALRFYLVSW---LGERVVADLRKAVFAHLLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 101 SFRFFDNNKTGHLISRLTNDLMEIGEIAHHGpedLFIA---VMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKK 177
Cdd:cd18575 83 SPSFFETTRTGEVLSRLTTDTTLIQTVVGSS---LSIAlrnLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 178 MtgtfRRLFSD----VADFNACIENNVGGIRVVQAFGNERFEKDQF--AVNNArFRTTK--------LMAYKIMALNSSI 243
Cdd:cd18575 160 V----RRLSRAsqdrLADLSAFAEETLSAIKTVQAFTREDAERQRFatAVEAA-FAAALrriraralLTALVIFLVFGAI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446867357 244 SYMLmrlvtlfvlicgtWF----VLQGELTYGGFIGFVLL 279
Cdd:cd18575 235 VFVL-------------WLgahdVLAGRMSAGELSQFVFY 261
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
13-297 |
2.30e-30 |
|
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: 120.39 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQK 92
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 93 LFDHIQKLSFRFFDNNKTGHLISRLtNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLAL 172
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 173 YFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVT 252
Cdd:cd18782 160 LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSS 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446867357 253 LFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESY 297
Cdd:cd18782 240 LLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQF 284
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-557 |
3.94e-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: 124.41 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPrfyeqSSGSIQIDGIDTKDMT---LSSLRKQIGIVQQDVFlfsG 421
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 ------TIRENIAYG----NLKASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGV-KLSGGQKQRLAIAR-MFLKnPP 489
Cdd:COG4172 374 slsprmTVGQIIAEGlrvhGPGLSAAERRARVAEA-LEEV------GLDPAARHRYPhEFSGGQRQRIAIARaLILE-PK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 490 ILILDEATSALDteteLAIQKS----LAELSV--GRTTLVIAHRLATIKN-ADRIVVVnKDG-IAEQGSHEELIEQ 557
Cdd:COG4172 446 LLVLDEPTSALD----VSVQAQildlLRDLQRehGLAYLFISHDLAVVRAlAHRVMVM-KDGkVVEQGPTEQVFDA 516
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
325-557 |
4.46e-30 |
|
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: 120.16 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 325 EVKHVHgdiqysnVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE---QSSGSIQIDGIDTKDM 400
Cdd:COG0444 3 EVRNLK-------VYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 401 TLSSLR----KQIGIVQQD-------VFlfsgTIRENIAYG---NLKASEAEIWQAVKRAqLEDLiysqpdGLDTVigER 466
Cdd:COG0444 76 SEKELRkirgREIQMIFQDpmtslnpVM----TVGDQIAEPlriHGGLSKAEARERAIEL-LERV------GLPDP--ER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 467 GVK-----LSGGQKQRLAIARMFLKNPPILILDEATSALDteteLAIQKS----LAEL--SVGRTTLVIAHRLATIKN-A 534
Cdd:COG0444 143 RLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQilnlLKDLqrELGLAILFITHDLGVVAEiA 218
|
250 260
....*....|....*....|...
gi 446867357 535 DRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG0444 219 DRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
332-549 |
4.66e-30 |
|
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: 116.50 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLP--RFYEQSSGSIQIDGIDtkdMTLSSLRKQI 409
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRP---LDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQ-DVFLFSGTIRENIAYGnlkaseaeiwqavkrAQLedliysqpdgldtvigeRGvkLSGGQKQRLAIARMFLKNP 488
Cdd:cd03213 85 GYVPQdDILHPTLTVRETLMFA---------------AKL-----------------RG--LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 489 PILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLAT--IKNADRIVVVNKDGIAEQG 549
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
349-550 |
1.18e-29 |
|
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: 116.24 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIH---AGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG---IDT-KDMTLSSLRKQIGIVQQDVFLFSG 421
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 -TIRENIAYGNLKASEAEIWQAVkrAQLEDLIysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSAL 500
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISV--DELLDLL-----GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 501 DTETELAIQKSLAEL--SVGRTTLVIAHRLATI-KNADRIVVVnKDGIAEQGS 550
Cdd:cd03297 163 DRALRLQLLPELKQIkkNLNIPVIFVTHDLSEAeYLADRIVVM-EDGRLQYIG 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
353-555 |
1.61e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.22 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 353 SLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSslRKQIGIVQQDVFLFSG-TIRENIAYG- 430
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 431 --NLKASEAEiwqavkRAQLEDlIYSQPdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAI 508
Cdd:PRK10771 97 npGLKLNAAQ------REKLHA-IARQM-GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 509 QKSLAELSVGR--TTLVIAHRL---ATIknADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK10771 169 LTLVSQVCQERqlTLLMVSHSLedaARI--APRSLVVADGRIAWDGPTDELL 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
202-562 |
2.65e-29 |
|
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: 123.90 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 202 GIRVVQAFGNE-RFEKDQFAVNNARFRTTKLMAYkiMALNSSISYM----LMRLVTLFVLI-CGTWFVLQGELTYGGfig 275
Cdd:TIGR00957 505 GIKVLKLYAWElAFLDKVEGIRQEELKVLKKSAY--LHAVGTFTWVctpfLVALITFAVYVtVDENNILDAEKAFVS--- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 276 fVLLTNIFFRPIEKINAVIESYPKGIAGFKRYVELL---ETEPDIVDSKdamEVKHVHGD-IQYSNVTFGYENKEP-ILN 350
Cdd:TIGR00957 580 -LALFNILRFPLNILPMVISSIVQASVSLKRLRIFLsheELEPDSIERR---TIKPGEGNsITVHNATFTWARDLPpTLN 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslrkQIGIVQQDVFLFSGTIRENIAYG 430
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFG 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 431 nlKASEAEIWQAVKRA-----QLEDLiysqPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTEte 505
Cdd:TIGR00957 723 --KALNEKYYQQVLEAcallpDLEIL----PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-- 794
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 506 laIQKSLAELSVG-------RTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYS 562
Cdd:TIGR00957 795 --VGKHIFEHVIGpegvlknKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
333-555 |
3.23e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.63 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT-LSSLRKQIGI 411
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 V-QQDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARM 483
Cdd:PRK13644 82 VfQNPETQFVGrTVEEDLAFGpeNLCLPPIEIRKRVDRAlaeiGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 484 FLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
348-538 |
1.29e-28 |
|
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: 113.68 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLL-----PrfyeqSSGSIQIDGIDtkdmtLSSL---------RKQIGIVQ 413
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLagldrP-----TSGTVRLAGQD-----LFALdedararlrARHVGFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 QDVFLFSG-TIRENIAygnLKASEAEIWQAVKRAQledliysqpDGLDTV-IGERG----VKLSGGQKQRLAIARMFLKN 487
Cdd:COG4181 97 QSFQLLPTlTALENVM---LPLELAGRRDARARAR---------ALLERVgLGHRLdhypAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAELSVGR-TTLVIA-HRLATIKNADRIV 538
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVL 217
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
20-281 |
2.27e-28 |
|
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: 114.56 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 20 FSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNA---GLQYVVTywgHMLGVNIETDMRQKLFDH 96
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGlfsGLRGGCF---SYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 97 IQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNK 176
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 177 KMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDqfavnnaRFRTTKLMAYKIM-------ALNSSISYMLMR 249
Cdd:cd18572 159 YYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREAR-------RYERALDKALKLSvrqalayAGYVAVNTLLQN 231
|
250 260 270
....*....|....*....|....*....|..
gi 446867357 250 LVTLFVLICGTWFVLQGELTYGGFIGFVLLTN 281
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQ 263
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
333-554 |
2.61e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 115.95 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVT--FGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMtlSSLRKQIG 410
Cdd:PRK10851 3 IEIANIKksFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSG-TIRENIAYG------NLKASEAEIWQAVKR----AQLEDLIYSQPdgldtvigergVKLSGGQKQRLA 479
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlprRERPNAAAIKAKVTQllemVQLAHLADRYP-----------AQLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-557 |
2.96e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.13 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY-ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSL-----LPRfyEQSSGSIQIDGIDTKDMTLSSLR 406
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingllLPD--DNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIAR 482
Cdd:PRK13640 84 EKVGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEMIKIVRDV-LADV------GMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
333-554 |
6.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDMTLSSLRKQIG 410
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQ--DVFLFSGTIRENIAYG--NLKASEAEIW----QAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIAR 482
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGplNLGLSKEEVEkrvkEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIA-HRLATI-KNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
226-566 |
1.39e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 118.30 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 226 FRTTKLMAykimALNSSISYMLMRLVTlfVLICGTWFVLQGELTYG-GFIGFVLLTNIFFrPIEKINAVIESYPKGIAGF 304
Cdd:PLN03130 516 FRKAQLLS----AFNSFILNSIPVLVT--VVSFGVFTLLGGDLTPArAFTSLSLFAVLRF-PLFMLPNLITQAVNANVSL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 305 KRYVELLETE-------PDIVDSKDAMEVKhvhgdiqysNVTFGYENK--EPILNDISLKIHAGETVAFVGPSGAGKTTL 375
Cdd:PLN03130 589 KRLEELLLAEervllpnPPLEPGLPAISIK---------NGYFSWDSKaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSL 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 376 CS-LLPRFYEQSSGSIQIdgidtkdmtlsslRKQIGIVQQDVFLFSGTIRENIAYGnLKASEAEIWQAVKRAQLEDLIYS 454
Cdd:PLN03130 660 ISaMLGELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDL 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 455 QPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAI-QKSLAELSVGRTTLVIAHRLATIKN 533
Cdd:PLN03130 726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQ 805
|
330 340 350
....*....|....*....|....*....|...
gi 446867357 534 ADRIVVVNKDGIAEQGSHEELIEQGGGYSRLYE 566
Cdd:PLN03130 806 VDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
348-554 |
1.67e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.38 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQ-----IDG---IDTKDMTLSSLRKQIGIVQQDVFLF 419
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 SG-TIRENIAYGNLKASEAEIWQAVKRAQlEDLIYSQPDGLDTVIGERgvkLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:PRK11264 98 PHrTVLENIIEGPVIVKGEPKEEATARAR-ELLAKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 499 ALDTE---TELAIQKSLAELSvgRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK11264 174 ALDPElvgEVLNTIRQLAQEK--RTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-560 |
1.76e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI-LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQD---VFLFSgTIRENIAYG--NLKASEAEIWQAVKRAqLEDLiysqpDGLDTVIGERGvKLSGGQKQRLAIARMFLK 486
Cdd:PRK13648 88 VFQNpdnQFVGS-IVKYDVAFGleNHAVPYDEMHRRVSEA-LKQV-----DMLERADYEPN-ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAELSVGR--TTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGG 560
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
333-549 |
2.18e-27 |
|
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: 109.61 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDmtLSSLRKQIG-I 411
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSGTIRENIAYGNLKA--SEAEIwqavkrAQLEDLIysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLgiRKKRI------DEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 490 ILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQG 549
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
333-552 |
2.32e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG------IDTKDMTLSSLR 406
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQDVFLFSG-TIRENIAYGNLKASEAEIWQAVKRA-------QLEDLIYSQPdgldtvigergVKLSGGQKQRL 478
Cdd:PRK11124 82 RNVGMVFQQYNLWPHlTVQQNLIEAPCRVLGLSKDQALARAekllerlRLKPYADRFP-----------LHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHE 552
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAeTGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
337-549 |
2.53e-27 |
|
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: 109.50 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEPIlnDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSslRKQIGIVQQDV 416
Cdd:cd03298 4 DKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFSG-TIRENIAYG---NLKASEaEIWQAVKRAQLEDliysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILI 492
Cdd:cd03298 80 NLFAHlTVEQNVGLGlspGLKLTA-EDRQAIEVALARV-------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 493 LDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQG 549
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-542 |
3.83e-27 |
|
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: 109.13 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKdMTLSSLRKQIGI 411
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENIA-YGNLKASEAEIwqavkrAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPP 489
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLKGLPKSE------IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKN-ADRIVVVNK 542
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSD 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
333-552 |
4.05e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--------IDTKDMtlSS 404
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAI--RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQDVFLFSG-TIRENIAygnlkasEAEIW-------QAVKRAQ--LEDLiysqpdGLDTVIGERGVKLSGGQ 474
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHlTVMENLI-------EAPCKvlglskeQAREKAMklLARL------RLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 475 KQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHE 552
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDAS 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
349-557 |
7.51e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 111.36 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT---LSSLRKQIGIVQQDVFlfsG---- 421
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPY---Aslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 --TIRENIAYG---NLKASEAEiwqavKRAQLEDLiysqpdgLDTVigerGVK----------LSGGQKQRLAIARMFLK 486
Cdd:COG4608 111 rmTVGDIIAEPlriHGLASKAE-----RRERVAEL-------LELV----GLRpehadrypheFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 487 NPPILILDEATSALDteteLAIQKS----LAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG4608 175 NPKLIVCDEPVSALD----VSIQAQvlnlLEDLqdELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-541 |
8.72e-27 |
|
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: 108.68 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGIVQ--QDVFLFSG-TIRE 425
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 426 NIAYG------------NLKASEAEIWQAVKRAqLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILIL 493
Cdd:cd03219 95 NVMVAaqartgsglllaRARREEREARERAEEL-LERV------GLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 494 DEATSAL-DTETELAIQ--KSLAELsvGRTTLVIAHRLATIKN-ADRIVVVN 541
Cdd:cd03219 168 DEPAAGLnPEETEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLD 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
324-548 |
1.01e-26 |
|
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: 109.51 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVhGDIQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLS 403
Cdd:TIGR02769 3 LEVRDV-THTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 404 S---LRKQIGIVQQD---VFLFSGTIRENIA-----YGNLKASEaeiwQAVKRAQLEDLIYSQPDGLDtvigERGVKLSG 472
Cdd:TIGR02769 82 QrraFRRDVQLVFQDspsAVNPRMTVRQIIGeplrhLTSLDESE----QKARIAELLDMVGLRSEDAD----KLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 473 GQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQ 548
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
337-557 |
2.55e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVT--FGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSLR-KQIGIVQ 413
Cdd:PRK11432 11 NITkrFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQqRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 QDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKRA-QLEDLiysqpDGLdtviGERGV-KLSGGQKQRLAIARMFLKNP 488
Cdd:PRK11432 85 QSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEAlELVDL-----AGF----EDRYVdQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 489 PILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELqqQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
59-554 |
2.84e-26 |
|
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: 114.24 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 59 GLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGE---IAHHgpedL 135
Cdd:TIGR01271 127 GLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEglaLAHF----V 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 136 FIAVMTLVgafsFMMMINWKLALLTFFV-IPFLLWLALY---FNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFG- 210
Cdd:TIGR01271 203 WIAPLQVI----LLMGLIWELLEVNGFCgLGFLILLALFqacLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCw 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 211 NERFEKDQFAVNNARFRTTKLMAY------------------------------KIMALNSSISYML---MRLVTLFVLI 257
Cdd:TIGR01271 279 EEAMEKIIKNIRQDELKLTRKIAYlryfyssafffsgffvvflsvvpyalikgiILRRIFTTISYCIvlrMTVTRQFPGA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 258 CGTWFVLQGELT-YGGFIGF----VLLTNIFFRPIEKINaVIESYPKGIAgfkryvELLETEpdivdSKDAMEVKHVHGD 332
Cdd:TIGR01271 359 IQTWYDSLGAITkIQDFLCKeeykTLEYNLTTTEVEMVN-VTASWDEGIG------ELFEKI-----KQNNKARKQPNGD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 --IQYSNVTFgyeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslrkQIG 410
Cdd:TIGR01271 427 dgLFFSNFSL---YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RIS 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSGTIRENIAYGnLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:TIGR01271 491 FSPQTSWIMPGTIKDNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADL 569
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 491 LILDEATSALDTETELAI-QKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
333-559 |
3.77e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGY--ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIG 410
Cdd:PRK13650 5 IEVKNLTFKYkeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQ--DVFLFSGTIRENIAYG------NLKASEAEIWQAVKRAQLEDLIYSQPdgldtvigergVKLSGGQKQRLAIAR 482
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGG 559
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
344-549 |
4.03e-26 |
|
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: 106.59 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQS---SGSIQIDGidtKDMTLSSLRKQIGIV-QQDVFLF 419
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVrQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 SGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIYSQPDglDTVIGERGVK-LSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 499 ALDTETELAIQKSLAELSV-GRTTLVIAH--RLATIKNADRIVVVNKDGIAEQG 549
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-556 |
4.79e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSS----LRKQIGIVQQDVFLFSG-TI 423
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprdaQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAYGNLKASEAEI-WQAVKR---AQLEDLiysqpdGLD----TVIGErgvkLSGGQKQRLAIARMFLKNPPILILDE 495
Cdd:COG1129 97 AENIFLGREPRRGGLIdWRAMRRrarELLARL------GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 496 ATSAL-DTETE--LAIQKSLAELsvGRTTLVIAHRLATIKN-ADRIVVVnKDG-------IAEQgSHEELIE 556
Cdd:COG1129 167 PTASLtEREVErlFRIIRRLKAQ--GVAIIYISHRLDEVFEiADRVTVL-RDGrlvgtgpVAEL-TEDELVR 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
347-562 |
5.06e-26 |
|
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: 108.02 E-value: 5.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslrkQIGIVQQDVFLFSGTIREN 426
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 427 IAYGnLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETEL 506
Cdd:cd03291 118 IIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 507 AI-QKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIEQGGGYS 562
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFS 253
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
23-293 |
9.43e-26 |
|
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: 107.26 E-value: 9.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 23 AVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSF 102
Cdd:cd18568 11 SLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 103 RFFDNNKTGHLISRLtNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTF 182
Cdd:cd18568 91 SFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 183 RRLFSDVADFNACIENNVGGIRVVQAFGNERFE----KDQFAVN-NARFRTTKLmAYKIMALNSSISYmlmrLVTLFVLI 257
Cdd:cd18568 170 REIFQANAEQQSFLVEALTGIATIKALAAERPIrwrwENKFAKAlNTRFRGQKL-SIVLQLISSLINH----LGTIAVLW 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 446867357 258 CGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAV 293
Cdd:cd18568 245 YGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
332-554 |
1.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQI------DGIDTKDmt 401
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLRKQIGIVQQdvF----LFSGTIRENIAYG--NLKASEAEiwqAVKRA-QLEDLIysqpdGLDTVIGERG-VKLSGG 473
Cdd:PRK13634 80 LKPLRKKVGIVFQ--FpehqLFEETVEKDICFGpmNFGVSEED---AKQKArEMIELV-----GLPEELLARSpFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 474 QKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGS 550
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....
gi 446867357 551 HEEL 554
Cdd:PRK13634 230 PREI 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
333-555 |
2.05e-25 |
|
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: 105.17 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSG-SIQIDGIDTKDMTLSSLRKQIGI 411
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 V---QQDVFLFSGTIRENI---AYGNL----KASEAEIWQAvkRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIA 481
Cdd:COG1119 83 VspaLQLRFPRDETVLDVVlsgFFDSIglyrEPTDEQRERA--RELLELL------GLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 482 RMFLKNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLV-IAHRLATIKNADRIVVVNKDG-IAEQGSHEELI 555
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIPPGITHVLLLKDGrVVAAGPKEEVL 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-554 |
2.87e-25 |
|
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: 104.05 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYEnKEPILNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPRfyeqSSGSIQIDGidtKDMT-LSS---LRK 407
Cdd:cd03224 4 ENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLlktiMGLLPP----RSGSIRFDG---RDITgLPPherARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 408 QIGIVQQDVFLFSG-TIRENI---AYGNLKASEAEIWQAVKRA--QLEDLiYSQPDGLdtvigergvkLSGGQKQRLAIA 481
Cdd:cd03224 76 GIGYVPEGRRIFPElTVEENLllgAYARRRAKRKARLERVYELfpRLKER-RKQLAGT----------LSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 482 RMFLKNPPILILDEATSALD----TETELAIQKsLAELsvGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLApkivEEIFEAIRE-LRDE--GVTILLVEQNArFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
33-280 |
3.39e-25 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. 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.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 105.67 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 33 FPLIVNQFIDKLLPGQNWTLIL-----WACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDN 107
Cdd:cd18573 15 VPFAIGKLIDVASKESGDIEIFglslkTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 108 NKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFS 187
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 188 DVADFNACIENNVGGIRVVQAFGNERFEKDQFA--VNNArFRTTKLMAyKIMALNSSISYMLMRLVTLFVLICGTWFVLQ 265
Cdd:cd18573 175 ALADATKVAEERLSNIRTVRAFAAERKEVERYAkkVDEV-FDLAKKEA-LASGLFFGSTGFSGNLSLLSVLYYGGSLVAS 252
|
250
....*....|....*
gi 446867357 266 GELTYGGFIGFVLLT 280
Cdd:cd18573 253 GELTVGDLTSFLMYA 267
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
337-569 |
3.83e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENkEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMtlSSLRKQIGIVQQDV 416
Cdd:PRK11607 24 NLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFSG-TIRENIAYG--NLKASEAEIWQAVkrAQLEDLIYSQpdgldTVIGERGVKLSGGQKQRLAIARMFLKNPPILIL 493
Cdd:PRK11607 101 ALFPHmTVEQNIAFGlkQDKLPKAEIASRV--NEMLGLVHMQ-----EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 494 DEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNKDGIAEQGSHEELIEQGGgySRlYEAQF 569
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDIleRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT--TR-YSAEF 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-539 |
4.95e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSS----LRKQIGIVQQDVFLFSG-TI 423
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAYGNLKASEAEIWQAVKRAQLEDLI--YsqpdGL----DTVIGErgvkLSGGQKQRLAIARMFLKNPPILILDEAT 497
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRELSerY----GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446867357 498 SAL-DTETE--LAIQKSLAELsvGRTTLVIAHRLATIK-NADRIVV 539
Cdd:COG3845 170 AVLtPQEADelFEILRRLAAE--GKSIIFITHKLREVMaIADRVTV 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
333-559 |
5.78e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDV--FLFSGTIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPdgldtvigergVKLSGGQKQRLAIARMF 484
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEAlkavRMWDFRDKPP-----------YHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIA-HRL-ATIKNADRIVVVNKDGIAEQG-----SHEELIEQ 557
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVdLAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQ 233
|
..
gi 446867357 558 GG 559
Cdd:PRK13647 234 AG 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
342-537 |
6.57e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.70 E-value: 6.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 342 YENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE-----QSSGSIQIDG-------IDTKDmtlssLRKQI 409
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGhniysprTDTVD-----LRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSGTIRENIAYG------------------NLKAseAEIWQAVKraqleDLIYsqpdglDTVIGergvkLS 471
Cdd:PRK14239 89 GMVFQQPNPFPMSIYENVVYGlrlkgikdkqvldeavekSLKG--ASIWDEVK-----DRLH------DSALG-----LS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 472 GGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHrlaTIKNADRI 537
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
332-554 |
8.70e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.27 E-value: 8.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSslRKQIGI 411
Cdd:PRK11000 3 SVTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENIAYGnLK---ASEAEIWQAVKRA----QLEDLIYSQPDGldtvigergvkLSGGQKQRLAIARM 483
Cdd:PRK11000 80 VFQSYALYPHlSVAENMSFG-LKlagAKKEEINQRVNQVaevlQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 484 FLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH-RLATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
333-557 |
9.50e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:PRK13548 3 LEARNLSVRLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFL-FSGTIRENIAYG------NLKASEAEIWQAVKRAQLEDL---IYSQpdgldtvigergvkLSGGQKQRLAIAR 482
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGraphglSRAEDDALVAAALAQVDLAHLagrDYPQ--------------LSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 483 MFL------KNPPILILDEATSALD---TETELAIQKSLAElSVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGS-- 550
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDlahQHHVLRLARQLAH-ERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTpa 226
|
250
....*....|
gi 446867357 551 ---HEELIEQ 557
Cdd:PRK13548 227 evlTPETLRR 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
337-558 |
9.77e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDV 416
Cdd:PRK11231 7 NLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFSG-TIRENIAYG-----NL-----KASEAEIWQAVKRAQLEDLiysqpdgldtviGERGV-KLSGGQKQRLAIARMF 484
Cdd:PRK11231 86 LTPEGiTVRELVAYGrspwlSLwgrlsAEDNARVNQAMEQTRINHL------------ADRRLtDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELIEQG 558
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
333-557 |
1.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKE-----PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDM-TLSSLR 406
Cdd:PRK13633 5 IKCKNVSYKYESNEestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEIW----QAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRL 478
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIRervdESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 446867357 557 Q 557
Cdd:PRK13633 234 E 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
305-557 |
3.24e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 305 KRYVELLETEPDIVDSKDAMEV-------KHVhgdIQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCS 377
Cdd:COG0488 284 KALEKLEREEPPRRDKTVEIRFppperlgKKV---LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 378 LLPRFYEQSSGSIQIdGIDTKdmtlsslrkqIGIVQQDVFLFSG--TIRENIAYGNLKASEAEIwqavkRAQLEDLIYSq 455
Cdd:COG0488 360 LLAGELEPDSGTVKL-GETVK----------IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEV-----RGYLGRFLFS- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 456 PDGLDTVIGergvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSvGrTTLVIAH-R--LATIk 532
Cdd:COG0488 423 GDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV- 495
|
250 260
....*....|....*....|....*.
gi 446867357 533 nADRIVVVNKDGIAE-QGSHEELIEQ 557
Cdd:COG0488 496 -ATRILEFEDGGVREyPGGYDDYLEK 520
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
333-558 |
3.84e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGID----TKDMTLSS 404
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQ--DVFLFSGTIRENIAYGNlKASEAEIWQAVKRAQ--LEDLIYSQpdgldTVIGERGVKLSGGQKQRLAI 480
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGP-KNFKMNLDEVKNYAHrlLMDLGFSR-----DVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 481 ARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 446867357 558 G 558
Cdd:PRK13646 237 K 237
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-554 |
4.15e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI--LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIG 410
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQAVKRAQLE----DLIYSQPdgldtvigergVKLSGGQKQRLAIAR 482
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGmeNQGIPREEMIKRVDEALLAvnmlDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-549 |
7.22e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.75 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKqIGIVQQDVFLFSG-TIRENI 427
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 428 AY-GNLkaseaeiwQAVKRAQLEDLIYSQPDGLDT--VIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTET 504
Cdd:cd03266 100 EYfAGL--------YGLKGDELTARLEELADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446867357 505 ELAIQKSLAEL-SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQG 549
Cdd:cd03266 172 TRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
333-554 |
1.21e-23 |
|
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: 99.37 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPIlNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGID-TKDMTlsSLRKQIGI 411
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVREPR--EVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENIA-YGNLkaseaeiwQAVKRAQLEDLIYSQPDGLDtvIGERGVKL----SGGQKQRLAIARMFL 485
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiHARL--------YGVPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEEL 554
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
351-554 |
1.38e-23 |
|
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: 102.50 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGI----DTKDMTLSSLRKQIGIVQQDVFLFSG-TIRE 425
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 426 NIAYGNLKASEAEiwQAVKRAQLEDLIysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETE 505
Cdd:TIGR02142 95 NLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 506 LAIQKSLAELS--VGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:TIGR02142 168 YEILPYLERLHaeFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-544 |
2.64e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 96.73 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSS----LRKQIGIVQQdvflfsgt 422
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASprdaRRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 ireniaygnlkaseaeiwqavkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILILDEATSAL-D 501
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALtP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446867357 502 TETE--LAIQKSLAELsvGRTTLVIAHRLATIKN-ADRIVVVnKDG 544
Cdd:cd03216 116 AEVErlFKVIRRLRAQ--GVAVIFISHRLDEVFEiADRVTVL-RDG 158
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
337-567 |
2.76e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLL---PRfYEQSSGSIQIDGIDTKDMTLSSlRKQIGIvq 413
Cdd:COG0396 5 NLHVSVEGKE-ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDE-RARAGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 qdvFL-------FSG-TIRE--NIAYGNLKASEAEIWQAVKRAQ--LEDLiysqpdGLDTVIGERGV--KLSGGQKQRLA 479
Cdd:COG0396 80 ---FLafqypveIPGvSVSNflRTALNARRGEELSAREFLKLLKekMKEL------GLDEDFLDRYVneGFSGGEKKRNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 480 IARMFLKNPPILILDEATSALDTEtelAIQKsLAE-----LSVGRTTLVIAH--RLATIKNADRIVVVNKDGIAEQGSHE 552
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDID---ALRI-VAEgvnklRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
250
....*....|....*..
gi 446867357 553 --ELIEQgGGYSRLYEA 567
Cdd:COG0396 227 laLELEE-EGYDWLKEE 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
344-504 |
7.60e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.78 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLL-----PRFyeQSSGSIQIDGIDTKdmTLSSLRKQIGIVQQDVFL 418
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlsPAF--SASGEVLLNGRRLT--ALPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 FSG-TIRENIAYG-----NLKASEAEIWQAVKRAQLEDLiysqpdgldtviGERGVK-LSGGQKQRLAIARMFLKNPPIL 491
Cdd:COG4136 88 FPHlSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGF------------ADRDPAtLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|...
gi 446867357 492 ILDEATSALDTET 504
Cdd:COG4136 156 LLDEPFSKLDAAL 168
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
333-554 |
1.46e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDMTLSSLRKQIG 410
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQAVKRAQledliysQPDGLDTVIGERGVKLSGGQKQRLAIARMFLK 486
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNAL-------KRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRLATIK-NADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkeLGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
349-555 |
1.55e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.11 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSL----RKQIGIVQQDVFLFSG-TI 423
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAYG----NLKASE--AEIWQAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMFLKNPPILILDEAT 497
Cdd:PRK10070 124 LDNTAFGmelaGINAEErrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 498 SALDTETELAIQKSLAELSVG--RTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-541 |
1.71e-22 |
|
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: 97.03 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGIVQ--QDVFLFSG-TIRE 425
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 426 NIA-----------------YGNLKASEAEIWQAVkRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNP 488
Cdd:COG0411 99 NVLvaaharlgrgllaallrLPRARREEREARERA-EELLERV------GLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 489 PILILDEATSAL-DTETELAIQ--KSLAELSvGRTTLVIAHRLATIKN-ADRIVVVN 541
Cdd:COG0411 172 KLLLLDEPAAGLnPEETEELAEliRRLRDER-GITILLIEHDMDLVMGlADRIVVLD 227
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
13-297 |
1.87e-22 |
|
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: 97.58 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQK 92
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 93 LFDHIQKLSFRFFDNNKTGHLISRLtNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLAL 172
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 173 YFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNE---------RFEKdqfaVNNARFRTTKLMAYkIMALNSSI 243
Cdd:cd18555 160 LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEkniykkwenLFKK----QLKAFKKKERLSNI-LNSISSSI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 244 SYMLmrlvTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPiekINAVIESY 297
Cdd:cd18555 235 QFIA----PLLILWIGAYLVINGELTLGELIAFSSLAGSFLTP---IVSLINSY 281
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
333-559 |
1.87e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSlRKQIGIV 412
Cdd:PRK13536 42 IDLAGVSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQ-DVFLFSGTIREN-IAYG-----NLKASEAEIWQAVKRAQLEdliySQPDGldtvigeRGVKLSGGQKQRLAIARMFL 485
Cdd:PRK13536 120 PQfDNLDLEFTVRENlLVFGryfgmSTREIEAVIPSLLEFARLE----SKADA-------RVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSL-AELSVGRTTLVIAHRLATIKN-ADRIVVVNKD-GIAEQGSHEELIEQGG 559
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHALIDEHIG 265
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
349-566 |
2.28e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.77 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTL--C-----SLLPRFyeQSSGSIQIDG--IDTKDMTLSSLRKQIGIVQQDVFLF 419
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIlrCfnrlnDLIPGF--RVEGKVTFHGknLYAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 SGTIRENIAYG----NLKASEAEIWQ-AVKRAQLEDLIysqPDGLDtvigERGVKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:PRK14243 104 PKSIYDNIAYGarinGYKGDMDELVErSLRQAALWDEV---KDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 495 EATSALDTETELAIQKSLAELSVGRTTLVIAHRL-ATIKNADRIVVVNKdgiaeqgsheELIEQGGGYSRLYE 566
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFFNV----------ELTEGGGRYGYLVE 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-544 |
2.29e-22 |
|
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: 94.14 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslRKQIGIV 412
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSGTIRENIAYGnlkaseaeiWQAVkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILI 492
Cdd:cd03223 70 PQRPYLPLGTLREQLIYP---------WDDV--------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 493 LDEATSALDTETELAIQKSLAELSvgrTTLV-IAHRLATIKNADRIVVVNKDG 544
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELG---ITVIsVGHRPSLWKFHDRVLDLDGEG 164
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
336-556 |
2.53e-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: 95.67 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPRfyeqSSGSIQIDGID-TKDMTLSSLRKQIG 410
Cdd:TIGR03410 4 SNLNVYYGQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLlktlMGLLPV----KSGSIRLDGEDiTKLPPHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSG-TIRENIAYG--NLKASEAEIwqavkraqlEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTGlaALPRRSRKI---------PDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDE 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-554 |
4.14e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE-----QSSGSIQIDGIDTKDMTLSSLR 406
Cdd:PRK14247 5 EIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 407 KQIgivqQDVFLFSG-----TIRENIAYG--------NLKASEAEIWQAVKRAQLEDLIysqPDGLDTVIGergvKLSGG 473
Cdd:PRK14247 82 RRV----QMVFQIPNpipnlSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEV---KDRLDAPAG----KLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 474 QKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAH---RLATIknADRIVVVNKDGIAEQGS 550
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARI--SDYVAFLYKGQIVEWGP 228
|
....
gi 446867357 551 HEEL 554
Cdd:PRK14247 229 TREV 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-548 |
4.17e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 97.99 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG-----IDTKDmtlsslrK 407
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvneLEPAD-------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 408 QIGIVQQDVFLFSG-TIRENIAYG--NLKASEAEIWQAVKRA----QLEDLIYSQPdgldtvigeRgvKLSGGQKQRLAI 480
Cdd:PRK11650 77 DIAMVFQNYALYPHmSVRENMAYGlkIRGMPKAEIEERVAEAarilELEPLLDRKP---------R--ELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 481 ARMFLKNPPILILDEATSALDT----ETELAIQKSLAELSVgrTTLVIAH-RLATIKNADRIVVVNKdGIAEQ 548
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRLKT--TSLYVTHdQVEAMTLADRVVVMNG-GVAEQ 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-504 |
5.09e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslRKQIGIVQQD 415
Cdd:COG0488 2 ENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 VFLFSG-TIRENIAYGNlkaseAEIWQAVKR-AQLEDLIYSQPD-------------------------------GLDTV 462
Cdd:COG0488 70 PPLDDDlTVLDTVLDGD-----AELRALEAElEELEAKLAEPDEdlerlaelqeefealggweaearaeeilsglGFPEE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446867357 463 IGERGVK-LSGGQKQRLAIARMFLKNPPILILDEATSALDTET 504
Cdd:COG0488 145 DLDRPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
337-557 |
5.31e-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: 99.76 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKT----TLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRK---- 407
Cdd:COG4172 13 SVAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 408 QIGIVQQD-------VFlfsgTIRENIA-----YGNLKASEAeiwqavkRAQLEDLiysqpdgLDTViG----ERGVK-- 469
Cdd:COG4172 93 RIAMIFQEpmtslnpLH----TIGKQIAevlrlHRGLSGAAA-------RARALEL-------LERV-GipdpERRLDay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 ---LSGGQKQRLAIArMFLKN-PPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNK 542
Cdd:COG4172 154 phqLSGGQRQRVMIA-MALANePDLLIADEPTTALDVTVQAQILDLLKDLqrELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|....*
gi 446867357 543 DGIAEQGSHEELIEQ 557
Cdd:COG4172 233 GEIVEQGPTAELFAA 247
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
333-526 |
6.68e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMtlSSLRkqiGIV 412
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP--GAER---GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 -QQDVFLFSGTIRENIAYG-NLKASEAEIWQAVKRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK11248 76 fQNEGLLPWRNVQDNVAFGlQLAGVEKMQRLEIAHQMLKKV------GLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 446867357 491 LILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAH 526
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
333-569 |
8.29e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.31 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSS---- 404
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 --------------------LRKQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEiwqAVKRAQLedliYSQPDGLD 460
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAAK----YIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 461 TVIGERG-VKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKNADRIV 538
Cdd:PRK13651 156 ESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRT 235
|
250 260 270
....*....|....*....|....*....|.
gi 446867357 539 VVNKDGiaeqgsheELIEQGGGYSRLYEAQF 569
Cdd:PRK13651 236 IFFKDG--------KIIKDGDTYDILSDNKF 258
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
344-556 |
9.72e-22 |
|
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: 94.15 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSlRKQIGI--VQQDVFLFSG 421
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 -TIRENI--AYGNLKASEAEIWQAVKrAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:cd03218 90 lTVEENIlaVLEIRGLSKKEREEKLE-ELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 499 ALDTETELAIQKSLAELS-VGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKdRGIGVLITDHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
333-556 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.28 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG----IDTKDMTLSS 404
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEiwqavkrAQLEDLIYSQPDGLDT-VIGERGVKLSGGQKQRLA 479
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE-------AKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
323-526 |
1.43e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 323 AMEVKHVHgdIQYSnvtfGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTL 402
Cdd:COG4525 3 MLTVRHVS--VRYP----GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG---VPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 403 SSLRKqiGIV-QQDVFLFSGTIRENIAYGnLK---ASEAEiwqavKRAQLEDLIysQPDGLDTVIGERGVKLSGGQKQRL 478
Cdd:COG4525 74 PGADR--GVVfQKDALLPWLNVLDNVAFG-LRlrgVPKAE-----RRARAEELL--ALVGLADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLaeLSVGRTT----LVIAH 526
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELL--LDVWQRTgkgvFLITH 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
333-544 |
1.90e-21 |
|
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: 93.16 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSI----QIDGIDTKDMTLSSLRKQ 408
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSGTIRENIAYGNlkASEAEIWQAVKRA-QLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGS--PFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 488 PPILILDEATSALDTE-TELAIQKSLAEL--SVGRTTLVIAHRLATIKNADRIVVVnKDG 544
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAM-KDG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-556 |
3.25e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.31 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDgidtkdmtlsslrKQIGIVQQDVFLFSGTIRENI 427
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 428 AYGNlKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTET-EL 506
Cdd:PTZ00243 742 LFFD-EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446867357 507 AIQKSLAELSVGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
332-556 |
3.67e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.43 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKEP---ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPrFYE----QSSGSIQIDGidtKDMTLSS 404
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPrkhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSpkgvKGSGSVLLNG---MPIDAKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQ-DVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIysQPDGL----DTVIGERGVK--LSGGQKQR 477
Cdd:TIGR00955 97 MRAISAYVQQdDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVL--QALGLrkcaNTRIGVPGRVkgLSGGERKR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLAT--IKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQkGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
..
gi 446867357 555 IE 556
Cdd:TIGR00955 255 VP 256
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-554 |
4.61e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.26 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKD---MTLSSLRKQIGIVQQDVFLfS----- 420
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPYG-Slnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 421 --GTIRENIAYGNLKASEAEiwqavKRAQLEDLiysqpdgLDTVigerGVK----------LSGGQKQRLAIARMFLKNP 488
Cdd:PRK11308 110 kvGQILEEPLLINTSLSAAE-----RREKALAM-------MAKV----GLRpehydryphmFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 489 PILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLqqELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-554 |
4.63e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 342 YENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGI------DTKDMTLSSLRKQIGIVQQD 415
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 VFLFSG-TIRENIAYgNLKASEAEIWQAVKRAQLEDLiysQPDGLDTVIGER----GVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK14246 99 PNPFPHlSIYDNIAY-PLKSHGIKEKREIKKIVEECL---RKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 491 LILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-531 |
6.32e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSsGSIQIDG--------IDTKDMTLSS 404
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQDVFLFSGTIRENIAYG------NLKASEAEIWQ-AVKRAQLEDLIYSQpdgldtvIGERGVKLSGGQKQR 477
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVEsALKDADLWDEIKHK-------IHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGR--TTLVIAHRLATI 531
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQV 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-558 |
1.20e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKE---PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDM---TLSSLRKQ- 408
Cdd:PRK10535 8 KDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSG-TIRENIaygNLKASEAEIWQAVKRAQLEDLIysQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNV---EVPAVYAGLERKQRLLRAQELL--QRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 488 PPILILDEATSALDT---ETELAIQKSLAELsvGRTTLVIAHRLATIKNADRIVVVnKDG--IAEQGSHEELIEQG 558
Cdd:PRK10535 163 GQVILADEPTGALDShsgEEVMAILHQLRDR--GHTVIIVTHDPQVAAQAERVIEI-RDGeiVRNPPAQEKVNVAG 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
347-541 |
1.37e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 90.57 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTK-DMTLSS------LRKQ-IGIVQQdvFL 418
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvDLAQASpreilaLRRRtIGYVSQ--FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 fsgtiR-------ENIAYGNLKASEAEIWQAVKRAqlEDLiysqpdgLDTV-IGERgvkL--------SGGQKQRLAIAR 482
Cdd:COG4778 103 -----RviprvsaLDVVAEPLLERGVDREEARARA--REL-------LARLnLPER---LwdlppatfSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 483 MFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLV-IAHRLATIKN-ADRIVVVN 541
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVT 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
347-538 |
1.51e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslRKQIGIVQQDVFL---FSGTI 423
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAYGNL----------KASEAEIWQAVKRAQLEDLIYSQpdgLDTvigergvkLSGGQKQRLAIARMFLKNPPILIL 493
Cdd:NF040873 75 RDLVAMGRWarrglwrrltRDDRAAVDDALERVGLADLAGRQ---LGE--------LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446867357 494 DEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKNADRIV 538
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
333-557 |
1.88e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGI----DTKDMTLSS 404
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEiwqAVKRAQlEDLIYSqpdGLDTVIGERG-VKLSGGQKQRLA 479
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEE---AEALAR-EKLALV---GISESLFEKNpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 480 IARMFLKNPPILILDEATSALDTE--TEL-AIQKSLAELsvGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKgrKELmTLFKKLHQS--GMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIF 233
|
..
gi 446867357 556 EQ 557
Cdd:PRK13649 234 QD 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
333-557 |
2.14e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGI----DTKDMTLSS 404
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEIwQAVKRAQLEDLiysqpdGLDTVIGERG-VKLSGGQKQRLA 479
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKA-EKIAAEKLEMV------GLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 480 IARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-544 |
2.26e-20 |
|
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: 87.50 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslrkqigiv 412
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 qqdvflfsgtiRENIAYgnlkaseaeiwqavkraqledliYSQpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILI 492
Cdd:cd03221 62 -----------TVKIGY-----------------------FEQ--------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 493 LDEATSALDTETELAIQKSLAELSvgRTTLVIAHRLATIKN-ADRIVVVNKDG 544
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-556 |
3.30e-20 |
|
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: 89.66 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPRfyeqSSGSIQIDGIDTKDMTLSSL-RKQIG 410
Cdd:COG0410 7 ENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLlkaiSGLLPP----RSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQQDVFLFSG-TIRENI---AYGNLKASEAeiwqavkRAQLEDlIYSQ-PdgldtVIGER----GVKLSGGQKQRLAIA 481
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLllgAYARRDRAEV-------RADLER-VYELfP-----RLKERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 482 RMFLKNPPILILDEATSAldteteLA------IQKSLAEL-SVGRTTLVI---AHRLATIknADRIVVVNKDGIAEQGSH 551
Cdd:COG0410 149 RALMSRPKLLLLDEPSLG------LApliveeIFEIIRRLnREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTA 220
|
....*
gi 446867357 552 EELIE 556
Cdd:COG0410 221 AELLA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
3.65e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQ--DVFLFSGTIRENIAYG--NLKASEAEIW----QAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMF 484
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGpiNLGLDEETVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
337-558 |
3.79e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.12 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFyEQSSGSIQIDGidtkDMTLSSLRKQIGIVQQDV 416
Cdd:PRK11247 17 AVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAG----TAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFS-GTIRENIAYGnLKASeaeiWQAVKRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDE 495
Cdd:PRK11247 91 RLLPwKKVIDNVGLG-LKGQ----WRDAALQALAAV------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 496 ATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLA-TIKNADRIVvvnkdgiaeqgsheeLIEQG 558
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVL---------------LIEEG 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-564 |
4.85e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.30 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTT----LCSLL-PrfyeqSSGSIQIDGID-TKDMTlsSLRKQIGIV----QQ---- 414
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILvP-----TSGEVRVLGYVpFKRRK--EFARRIGVVfgqrSQlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 ----DVFLFSGTI--------RENIAYgnlkaseaeiwqAVKRAQLEDLIySQPdgldtvigergV-KLSGGQKQRLAIA 481
Cdd:COG4586 111 lpaiDSFRLLKAIyripdaeyKKRLDE------------LVELLDLGELL-DTP-----------VrQLSLGQRMRCELA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 482 RMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQG 558
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERF 246
|
....*.
gi 446867357 559 GGYSRL 564
Cdd:COG4586 247 GPYKTI 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
348-554 |
7.14e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 7.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG-----IDTKD--------MTLSSLRKQIGIVQQ 414
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDgqlkvadkNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DVFLFSG-TIRENIAYGNLKASEAEIWQAVKRAqledLIYSQPDGLD-TVIGERGVKLSGGQKQRLAIARMFLKNPPILI 492
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLGLSKQEARERA----VKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 493 LDEATSALDTE---TELAIQKSLAElsVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK10619 176 FDEPTSALDPElvgEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-542 |
1.47e-19 |
|
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: 86.33 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSLRKQI--GIV-------QQDVFLf 419
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIraGIAyvpedrkREGLVL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 SGTIRENIAYGNLkaseaeiwqavkraqledliysqpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILILDEATSA 499
Cdd:cd03215 92 DLSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446867357 500 LDTETELAIQKSLAELS-VGRTTLVIAHRLATI-KNADRIVVVNK 542
Cdd:cd03215 135 VDVGAKAEIYRLIRELAdAGKAVLLISSELDELlGLCDRILVMYE 179
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-542 |
1.49e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHgdiqysnVTF--GYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT 401
Cdd:COG1101 2 LELKNLS-------KTFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLRKQIGIVQQDVFL---FSGTIREN--IAY----------GNLKASEAEIwqavkRAQLEDLIYSQPDGLDTVIGer 466
Cdd:COG1101 75 EYKRAKYIGRVFQDPMMgtaPSMTIEENlaLAYrrgkrrglrrGLTKKRRELF-----RELLATLGLGLENRLDTKVG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 467 gvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTET-ELAIQksLAELSVGR---TTLVIAHRL--AtIKNADRIVVV 540
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTaALVLE--LTEKIVEEnnlTTLMVTHNMeqA-LDYGNRLIMM 222
|
..
gi 446867357 541 NK 542
Cdd:COG1101 223 HE 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
348-547 |
1.91e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.59 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDtkdmtLSSL--------RKQIGIVQQDVFlf 419
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP-----LAKLnraqrkafRRDIQMVFQDSI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 sG------TIRENIAYGN---LKASEAEiwQAVKRAQLEDLIYSQPDGLDtvigERGVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK10419 100 -SavnprkTVREIIREPLrhlLSLDKAE--RLARASEMLRAVDLDDSVLD----KRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 491 LILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRLATIKN-ADRIVVVNKDGIAE 547
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
28-287 |
2.60e-19 |
|
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: 88.71 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 28 LLELGFPLIVNQFIDKLLPGQNW-TLILWAcFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFD 106
Cdd:cd18588 16 LFALVTPLFFQVIIDKVLVHRSLsTLDVLA-IGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 107 NNKTGHLISRLtndlMEIGEIAHhgpedlFI---AVMTLV-GAFSF-----MMMINWKLALLTFFVIPFLLWLALYFNKK 177
Cdd:cd18588 95 SRQVGDTVARV----RELESIRQ------FLtgsALTLVLdLVFSVvflavMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 178 MTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLI 257
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILW 244
|
250 260 270
....*....|....*....|....*....|
gi 446867357 258 CGTWFVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:cd18588 245 FGAYLVMDGELTIGQLIAFNMLAGQVSQPV 274
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
341-553 |
2.99e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.69 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 341 GYE-NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLF 419
Cdd:PRK10247 14 GYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 SGTIRENIAYGnlkaseaeiWQAVKRAQ-----LEDLIYSqpdGLDTVIGERGV-KLSGGQKQRLAIAR--MFLknPPIL 491
Cdd:PRK10247 94 GDTVYDNLIFP---------WQIRNQQPdpaifLDDLERF---ALPDTILTKNIaELSGGEKQRISLIRnlQFM--PKVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 492 ILDEATSALDTE---------TELAIQKSLAELSVgrttlviAHRLATIKNADRIVVVNKDGIAEQGSHEE 553
Cdd:PRK10247 160 LLDEITSALDESnkhnvneiiHRYVREQNIAVLWV-------THDKDEINHADKVITLQPHAGEMQEARYE 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
349-540 |
4.12e-19 |
|
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: 86.37 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslrKQIG-------IVQQDVFLFSG 421
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG------------KQITepgpdrmVVFQNYSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 -TIRENIAYGnLKASEAEIWQAVKRAQLEDLIysQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSAL 500
Cdd:TIGR01184 69 lTVRENIALA-VDRVLPDLSKSERRAIVEEHI--ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446867357 501 DTETELAIQKSLAEL--SVGRTTLVIAHRL-ATIKNADRIVVV 540
Cdd:TIGR01184 146 DALTRGNLQEELMQIweEHRVTVLMVTHDVdEALLLSDRVVML 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
348-557 |
4.31e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmTLSSLrkqIGI---VQQDvflFSGtiR 424
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgagFHPE---LTG--R 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENI-----AYGnlkASEAEIWQAVKR----AQLEDLIYsQPdgldtvigergVK-LSGGQKQRLAIARMFLKNPPILILD 494
Cdd:COG1134 107 ENIylngrLLG---LSRKEIDEKFDEivefAELGDFID-QP-----------VKtYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 495 EATSALDTETelaIQKSLAEL----SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:COG1134 172 EVLAVGDAAF---QKKCLARIrelrESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
348-549 |
4.68e-19 |
|
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: 86.05 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmTLSSLrkqigivqqdVFLFSG-----T 422
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL----------LGLGGGfnpelT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIA-YGNLK-ASEAEIWQAVKR----AQLEDLIYSQpdgldtvigergVK-LSGGQKQRL--AIARMFlkNPPILIL 493
Cdd:cd03220 101 GRENIYlNGRLLgLSRKEIDEKIDEiiefSELGDFIDLP------------VKtYSSGMKARLafAIATAL--EPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 494 DEATSALDTETELAIQKSLAELSVGRTTLVIA-HRLATIKN-ADRIVVVNKDGIAEQG 549
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
331-554 |
4.71e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GDIQYSNVTFGYENKEPI----LNDISLKIHAGETVAFVGPSGAGKTTLCSL-----LPRFYEQSSGSIQIDGIDTKDMT 401
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLRKQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEIWQAVkrAQLEDLIySQPDgldTVIGERGVKLSGGQKQR 477
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYKKV--PELLKLV-QLPE---DYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkeYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
338-555 |
4.88e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 338 VTFGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVF 417
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 418 L-FSGTIRENIAYGNL----------KASEAEIWQAVKRAQLedliysqpdgldTVIGERGV-KLSGGQKQRLAIARMFL 485
Cdd:PRK09536 88 LsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGV------------AQFADRPVtSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVdDGKTAVAAIHDLdLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
325-559 |
8.84e-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: 84.89 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 325 EVKHVHGDIqysnvtfgyENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLL---PRfYEQSSGSIQIDGIDTKDMT 401
Cdd:cd03217 2 EIKDLHVSV---------GGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILFKGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSS-LRKQIGIVQQDVFLFSGtireniaygnlkaseaeiwqaVKraqLEDLIysqpdgldtvigeRGV--KLSGGQKQRL 478
Cdd:cd03217 71 PEErARLGIFLAFQYPPEIPG---------------------VK---NADFL-------------RYVneGFSGGEKKRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAH--RLATIKNADRIVVVNKDGIAEQGSHE--E 553
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaL 193
|
....*.
gi 446867357 554 LIEQGG 559
Cdd:cd03217 194 EIEKKG 199
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
6-317 |
9.01e-19 |
|
Six-transmembrane helical domain 2 (TMD2) 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: 350022 [Multi-domain] Cd Length: 317 Bit Score: 87.51 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 6 FSYYKPYKGLFILDFSCAVVAGLLelgFPL-------IVNQFIDKLLPGQNWTLILW-------ACFGLLAVYILNAGLQ 71
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAV---FPVfailfskLISVFSLPDDDELRSEANFWalmflvlAIVAGIAYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 72 YVvtywghmlGVNIETDMRQKLFDHI--QKLSFrfFD--NNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFS 147
Cdd:cd18578 78 IA--------GERLTRRLRKLAFRAIlrQDIAW--FDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 148 FMMMINWKLALLTFFVIPFLLwLALYFNKKMTGTF----RRLFSDVADFnACieNNVGGIRVVQAFGNERFEKDQFAVNN 223
Cdd:cd18578 148 IAFVYGWKLALVGLATVPLLL-LAGYLRMRLLSGFeeknKKAYEESSKI-AS--EAVSNIRTVASLTLEDYFLEKYEEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 224 ARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFigFVLLTNIFF--RPIEKINAVIESYPKGI 301
Cdd:cd18578 224 EEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMALIFgaQSAGQAFSFAPDIAKAK 301
|
330
....*....|....*.
gi 446867357 302 AGFKRYVELLETEPDI 317
Cdd:cd18578 302 AAAARIFRLLDRKPEI 317
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
348-536 |
9.74e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSS---LR-KQIGIVQQDVFLFSG-T 422
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIAY----GNLKASEAEiwqavKRAqLEDLiysQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:PRK11629 104 ALENVAMplliGKKKPAEIN-----SRA-LEML---AAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446867357 499 ALDTETELAIQKSLAELSVGRTT--LVIAHRLATIKNADR 536
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSR 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-549 |
1.61e-18 |
|
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: 84.25 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSlRKQIGIVQQDVFLFSG-TIREN 426
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 427 IAY-GNLK-------ASEAEIWqaVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:cd03269 91 LVYlAQLKglkkeeaRRRIDEW--LERLELSEYANKRVE-----------ELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 499 ALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQG 549
Cdd:cd03269 158 GLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-554 |
1.75e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYeQSSGSIQIDG-----IDTKDMTlsSLRKQIGIVQQDVFlfSG- 421
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGqplhnLNRRQLL--PVRHRIQVVFQDPN--SSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 ----TIRENIAYG------NLKASEAEiwQAVKRAQLEDliysqpdGLDTVIGER-GVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK15134 376 nprlNVLQIIEEGlrvhqpTLSAAQRE--QQVIAVMEEV-------GLDPETRHRyPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 491 LILDEATSALDTETE---LAIQKSLAE---LSVgrttLVIAHRLATIKNADRIVVVNKDG-IAEQGSHEEL 554
Cdd:PRK15134 447 IILDEPTSSLDKTVQaqiLALLKSLQQkhqLAY----LFISHDLHVVRALCHQVIVLRQGeVVEQGDCERV 513
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-554 |
1.78e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSG-----SIQIDG---IDTKDMTlsSLRKQ 408
Cdd:PRK14271 26 NLTLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGrsiFNYRDVL--EFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSGTIRENIAYG--NLKASEAEIWQAVKRAQLEDLiySQPDGLDTVIGERGVKLSGGQKQRLAIARMFLK 486
Cdd:PRK14271 103 VGMLFQRPNPFPMSIMDNVLAGvrAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
324-554 |
2.01e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKH--VHGDIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDM 400
Cdd:PRK15079 9 LEVADlkVHFDIKDGKQWFWQPPKTlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 401 T---LSSLRKQIGIVQQDVfLFS----GTIRENIA------YGNLkaSEAEIWQAVKRAQ-----LEDLIYSQPDgldtv 462
Cdd:PRK15079 89 KddeWRAVRSDIQMIFQDP-LASlnprMTIGEIIAeplrtyHPKL--SRQEVKDRVKAMMlkvglLPNLINRYPH----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 463 igergvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRLATIKN-ADRIVV 539
Cdd:PRK15079 161 ------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQreMGLSLIFIAHDLAVVKHiSDRVLV 234
|
250
....*....|....*
gi 446867357 540 VNKDGIAEQGSHEEL 554
Cdd:PRK15079 235 MYLGHAVELGTYDEV 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
125-542 |
5.56e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.53 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 125 GEIAHHgpEDLFIAVMTLVgAFSFMMMINWKLaLLTFF-----------VIPFLLWL----ALYFNKKMTGTFRR---LF 186
Cdd:TIGR01257 722 GRILHY--SDPFILFLFLL-AFSTATIMQCFL-LSTFFskaslaaacsgVIYFTLYLphilCFAWQDRMTADLKTavsLL 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 187 SDVA-----DFNACIENNVGGIRVVQaFGNERFEKDQFAVnnarfrttkLMAYKIMALNSSISYMLM-RLVTLFVLICGT 260
Cdd:TIGR01257 798 SPVAfgfgtEYLVRFEEQGLGLQWSN-IGNSPLEGDEFSF---------LLSMKMMLLDAALYGLLAwYLDQVFPGDYGT 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 261 ---WFVLQGELTYGGFIGFVLLTNiffRPIEKINAVIES-----YPKGI--AGFKRyvELLETEPDIVdSKDAMEVKHVH 330
Cdd:TIGR01257 868 plpWYFLLQESYWLGGEGCSTREE---RALEKTEPLTEEmedpeHPEGIndSFFER--ELPGLVPGVC-VKNLVKIFEPS 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 331 GD--IQYSNVTFgYENkepilndislkihagETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTkDMTLSSLRKQ 408
Cdd:TIGR01257 942 GRpaVDRLNITF-YEN---------------QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQS 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSG-TIRENIA-YGNLKASEAEIWQAVKRAQLEDliysqpDGLDTVIGERGVKLSGGQKQRLAIARMFLK 486
Cdd:TIGR01257 1005 LGMCPQHNILFHHlTVAEHILfYAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVG 1078
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRL--ATIKnADRIVVVNK 542
Cdd:TIGR01257 1079 DAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdeADLL-GDRIAIISQ 1135
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-556 |
8.93e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.39 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRF--YEQSSGSI-------------------- 390
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 391 -------------QIDGIDTKDMTLSSLRKQIGIVQQDVFLFSG--TIRENIAYGnLKASEAEIWQAVKRAQleDLIysQ 455
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEA-LEEIGYEGKEAVGRAV--DLI--E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 456 PDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN 533
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|....
gi 446867357 534 -ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
89-280 |
1.28e-17 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family 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. 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. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 83.45 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 89 MRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLL 168
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 169 WLALYFNKKMTgTFRRLFSD-VADFNACIENNVGGIRVVQAFGNERFEKDQFAVNnarFRTTKLMAYKIMALNSSISYML 247
Cdd:cd18780 157 IGAVIYGKYVR-KLSKKFQDaLAAASTVAEESISNIRTVRSFAKETKEVSRYSEK---INESYLLGKKLARASGGFNGFM 232
|
170 180 190
....*....|....*....|....*....|....*.
gi 446867357 248 MRLVTL---FVLICGTWFVLQGELTYGGFIGFVLLT 280
Cdd:cd18780 233 GAAAQLaivLVLWYGGRLVIDGELTTGLLTSFLLYT 268
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
333-536 |
1.70e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.85 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLL---PRfyeQSSGSIQIDGIDTKD-MTLSSLRKQ 408
Cdd:PRK11614 6 LSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDwQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 409 IGIVQQDVFLFSG-TIRENIAYGNLKASEAEIWQAVKRaqledlIYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLA--TIKNADR 536
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADR 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
347-542 |
1.89e-17 |
|
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: 82.00 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGIV----QQ-------- 414
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR-KKFLRRIGVVfgqkTQlwwdlpvi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DVFLFSGTIReNIAYGNLKASEAEIWQAVkraQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:cd03267 114 DSFYLLAAIY-DLPPARFKKRLDELSELL---DLEELLDTPVR-----------QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 495 EATSALDTETELAIQKSLAELSVGRTTLVI--AHRLATI-KNADRIVVVNK 542
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDK 229
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
15-297 |
2.16e-17 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins 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. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 82.89 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 15 LFILdfscAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQY----VVTYWGHMLGVNietdMR 90
Cdd:cd18567 7 ILLL----SLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSAlrswLVLYLSTSLNLQ----WT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 91 QKLFDHIQKLSFRFFDNNKTGHLISR----------LTNDLMEIgeiahhgpedlFIAVMTLVGAFSFMMMINWKLALLT 160
Cdd:cd18567 79 SNLFRHLLRLPLSYFEKRHLGDIVSRfgsldeiqqtLTTGFVEA-----------LLDGLMAILTLVMMFLYSPKLALIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 161 --FFVIPFLLWLALYfnkkmtGTFRRLFSDVADFNA-----CIEnNVGGIRVVQAFGNERFEKDQF-----AVNNARFRT 228
Cdd:cd18567 148 laAVALYALLRLALY------PPLRRATEEQIVASAkeqshFLE-TIRGIQTIKLFGREAEREARWlnllvDAINADIRL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 229 TKLmaykiMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFfrpIEKINAVIESY 297
Cdd:cd18567 221 QRL-----QILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQF---SSRASSLIDKL 281
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
351-554 |
2.60e-17 |
|
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: 83.61 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLL-----PrfyeqSSGSIQIDG---IDT-KDMTLSSLRKQIGIVQQDVFLFSG 421
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglerP-----DSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 -TIRENIAYGnLKASeaeiWQAVKRAQLEDLIysqpDGLDtvIG---ERGV-KLSGGQKQRLAIARMFLKNPPILILDEA 496
Cdd:COG4148 92 lSVRGNLLYG-RKRA----PRAERRISFDEVV----ELLG--IGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 497 TSALDTET-------------ELAI-----QKSLAELSvgrttlviahRLatiknADRIVVVNKDGIAEQGSHEEL 554
Cdd:COG4148 161 LAALDLARkaeilpylerlrdELDIpilyvSHSLDEVA----------RL-----ADHVVLLEQGRVVASGPLAEV 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
350-554 |
2.63e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 350 NDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlSSLRKQIGIVQ--QDVFLF-SGTIREN 426
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFrEMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 427 ------------IAYGNLKA-----SEAEiwqAVKRAQ--LEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKN 487
Cdd:PRK11300 101 llvaqhqqlktgLFSGLLKTpafrrAESE---ALDRAAtwLERV------GLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
22-271 |
2.71e-17 |
|
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: 82.52 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIVNQFIDKLLPGQNWTL--------ILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKL 93
Cdd:cd18577 7 AAIAAGAALPLMTIVFGDLFDAFTDFGSGESspdeflddVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 94 FDHIQKLSFRFFDNNKTGHLISRLTNDLMEI----GEIAHHgpedLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLW 169
Cdd:cd18577 87 LKALLRQDIAWFDKNGAGELTSRLTSDTNLIqdgiGEKLGL----LIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 170 LALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMR 249
Cdd:cd18577 163 VGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIF 242
|
250 260
....*....|....*....|..
gi 446867357 250 LVTLFVLICGTWFVLQGELTYG 271
Cdd:cd18577 243 AMYALAFWYGSRLVRDGEISPG 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-556 |
2.73e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE-----QSSGSIQIDGID--TKDMTLSSL 405
Cdd:PRK14267 5 IETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 406 RKQIGIVQQDVFLFSG-TIRENIAYG----NLKASEAEI-----WqAVKRAQLEDLIYSQpdgldtvIGERGVKLSGGQK 475
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVAIGvklnGLVKSKKELderveW-ALKKAALWDEVKDR-------LNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 476 QRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGKLIEVGPTRKV 235
|
..
gi 446867357 555 IE 556
Cdd:PRK14267 236 FE 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-556 |
3.01e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHA----------GETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDT-KDMTLSSLRKQIGIVQQ 414
Cdd:PRK10261 329 LLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DVFLfSGTIRENIAYG--------NLKASEAeiwqAVKR-AQLEDLIYSQPDGLDTVIGErgvkLSGGQKQRLAIARMFL 485
Cdd:PRK10261 409 DPYA-SLDPRQTVGDSimeplrvhGLLPGKA----AAARvAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PRK10261 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQrdFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
336-554 |
3.54e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENKEP----ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSS------- 404
Cdd:PRK13631 25 KNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 ---------LRKQIGIVQQ--DVFLFSGTIRENIAYG--NLKASEAEiwqAVKRAQLedliYSQPDGLDTVIGERG-VKL 470
Cdd:PRK13631 105 skkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKKSE---AKKLAKF----YLNKMGLDDSYLERSpFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 471 SGGQKQRLAIARMFLKNPPILILDEATSALDTETE-LAIQKSLAELSVGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQ 548
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKT 257
|
....*.
gi 446867357 549 GSHEEL 554
Cdd:PRK13631 258 GTPYEI 263
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
349-544 |
3.55e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLS-SLRKQIGIVQQDVFLFSG-TIREN 426
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 427 IAYGNL---KASEAEI--WQAVK-RAQLEDLIYSQPDGLDTVIGErgvkLSGGQKQRLAIARMFLKNPPILILDEATSAL 500
Cdd:PRK09700 101 LYIGRHltkKVCGVNIidWREMRvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446867357 501 -DTETE--LAIQKSLAelSVGRTTLVIAHRLATIKN-ADRIVVVnKDG 544
Cdd:PRK09700 177 tNKEVDylFLIMNQLR--KEGTAIVYISHKLAEIRRiCDRYTVM-KDG 221
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
22-271 |
5.08e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 81.82 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIVNQFID------KLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18574 4 SALAAALVNIQIPLLLGDLVNvisrslKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIQKLSFRFFDNNKTGHLISRLTNDLME----------IGeiahhgpedlFIAVMTLVGAFSFMMMINWKLALLTFFVIP 165
Cdd:cd18574 84 SLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcvsQG----------LRSVTQTVGCVVSLYLISPKLTLLLLVIVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 166 FLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQF--AVNNARFRTTKLmAYKI------- 236
Cdd:cd18574 154 VVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYeeEVEKAAKLNEKL-GLGIgifqgls 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 446867357 237 -MALNSsisymlmrlVTLFVLICGTWFVLQGELTYG 271
Cdd:cd18574 233 nLALNG---------IVLGVLYYGGSLVSRGELTAG 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
344-529 |
1.05e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSLRKQIGIV-QQDVFLFSGT 422
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLgHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIAYgnlkaseaeiWQAVK-------RAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDE 495
Cdd:PRK13539 90 VAENLEF----------WAAFLggeeldiAAALEAV------GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|....
gi 446867357 496 ATSALDTetelAIQKSLAELsvgrttlvIAHRLA 529
Cdd:PRK13539 154 PTAALDA----AAVALFAEL--------IRAHLA 175
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
349-544 |
1.17e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSS--GSIQIDGIDTKDMTLS-SLRKQIGIVQQDVFLFSG-TIR 424
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENIAYGNlkaseaEI-------WQAV-KRAQ--LEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:PRK13549 101 ENIFLGN------EItpggimdYDAMyLRAQklLAQL------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 495 EATSAL---DTETELAIQKSLAelSVGRTTLVIAHRLATIKN-ADRIVVVnKDG 544
Cdd:PRK13549 169 EPTASLtesETAVLLDIIRDLK--AHGIACIYISHKLNEVKAiSDTICVI-RDG 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-554 |
1.31e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHGdiQYSNVtfgyenkePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTlS 403
Cdd:PRK15439 12 LCARSISK--QYSGV--------EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 404 SLRKQIGI--VQQDVFLFSG-TIRENIAYGNLKASEAEiwqaVKRAQLEDLIYSQPDgLDTVIGergvKLSGGQKQRLAI 480
Cdd:PRK15439 81 AKAHQLGIylVPQEPLLFPNlSVKENILFGLPKRQASM----QKMKQLLAALGCQLD-LDSSAG----SLEVADRQIVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 481 ARMFLKNPPILILDEATSAL---DTETELAIQKSLAELSVGrtTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLtpaETERLFSRIRELLAQGVG--IVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
333-556 |
1.45e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.62 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGiDTKDMTLSSLRKQIGIV 412
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQ-DVFLFSGTIRENIA----YGNLKASEAE--IWQAVKRAQLEDliysqpdGLDTVIGErgvkLSGGQKQRLAIARMFL 485
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLvfgrYFGLSAAAARalVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
333-553 |
1.60e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT---KDMTLSSLRKQI 409
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDV-FLFSGTIRENIAygnlkaseaeIWQAVKRAQLEDLIYSQPDGLDTV-----IGERGVKLSGGQKQRLAIARM 483
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVA----------IPLIIAGASGDDIRRRVSAALDKVglldkAKNFPIQLSGGEQQRVGIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 484 FLKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATIKNADRIVVVNKDGIAEQGSHEE 553
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNrVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
337-555 |
1.68e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTL-SSLRKQIGIVQQD 415
Cdd:PRK10895 8 NLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 VFLFsgtiRENIAYGNLKASeAEIWQAVKRAQLEDL---------IYSQPDGLdtvigerGVKLSGGQKQRLAIARMFLK 486
Cdd:PRK10895 87 ASIF----RRLSVYDNLMAV-LQIRDDLSAEQREDRanelmeefhIEHLRDSM-------GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 487 NPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLrDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
349-569 |
2.17e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.11 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCS----LLPrfyeqSSGSIQIDGIDTKDMTLSSLRKQIG-IVQQDVFLFSGTI 423
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLArmagLLP-----GQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIA-YGNLKASEAEIWQAV----KRAQLEDLiysqpdgLDTVIGergvKLSGGQKQRLAIARMFLK-----NPP--IL 491
Cdd:COG4138 87 FQYLAlHQPAGASSEAVEQLLaqlaEALGLEDK-------LSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 492 ILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEELIEQgGGYSRLYEAQF 569
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTP-ENLSEVFGVKF 234
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
35-292 |
2.37e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 79.63 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 35 LIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLI 114
Cdd:cd18561 17 WLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 115 SRLTNDL--MEiGEIAHHGPEdLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADF 192
Cdd:cd18561 97 TTVVDGVeaLE-AYYGRYLPQ-LLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 193 NACIENNVGGIRVVQAFGNERFEKDQFAVNNARFR--TTKLMAykIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTY 270
Cdd:cd18561 175 SAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRqaTMKVLA--VSLLSSGIMGLATALGTALALGVGALRVLGGQLTL 252
|
250 260
....*....|....*....|..
gi 446867357 271 GGFIGFVLLTNIFFRPIEKINA 292
Cdd:cd18561 253 SSLLLILFLSREFFRPLRDLGA 274
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
316-554 |
3.63e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 316 DIVDSKDAMEVKHVhgdiqysNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG 394
Cdd:PRK10261 5 DELDARDVLAVENL-------NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 395 ----------IDTKDMTLSSLRKQIG-----IVQQ------DVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLIY 453
Cdd:PRK10261 78 mllrrrsrqvIELSEQSAAQMRHVRGadmamIFQEpmtslnPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 454 SQpdgldTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLA----ELSVGrtTLVIAHRLA 529
Cdd:PRK10261 158 AQ-----TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMG--VIFITHDMG 230
|
250 260
....*....|....*....|....*.
gi 446867357 530 TIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK10261 231 VVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
346-513 |
3.68e-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: 77.15 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 346 EPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIRE 425
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 426 NIAYGNLKASEAEIWQAVKRAQL---EDLIYSQpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILILDEATSALDT 502
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLngfEDRPVAQ--------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|.
gi 446867357 503 ETELAIQKSLA 513
Cdd:cd03231 159 AGVARFAEAMA 169
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
337-555 |
6.73e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDV 416
Cdd:PRK10253 12 QLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFSG-TIRENIAYGNL----------KASEAEIWQAVKRAQLEDLIYSQPDgldtvigergvKLSGGQKQRLAIARMFL 485
Cdd:PRK10253 91 TTPGDiTVQELVARGRYphqplftrwrKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAELS--VGRTTLVIAHRL-ATIKNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-542 |
7.60e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.45 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLprF--YEQSSGSIQIDGidtKDMTLSSLRKQI--GIV-------QQDVF 417
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDG---KPVRIRSPRDAIraGIAyvpedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 418 LfSGTIRENIAYGNLKA-------SEAEIWQAVKRaQLEDL-IysQPDGLDTVIGErgvkLSGGQKQRLAIARMFLKNPP 489
Cdd:COG1129 343 L-DLSIRENITLASLDRlsrggllDRRRERALAEE-YIKRLrI--KTPSPEQPVGN----LSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 490 ILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATI-KNADRIVVVNK 542
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAeGKAVIVISSELPELlGLSDRILVMRE 469
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
89-278 |
7.87e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 78.15 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 89 MRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAhhgPEDLFIAVMTLV---GAFSFMMMINWKLALLTFFVIP 165
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSV---ALNANVLLRSLVktlGMLGFMLSLSWQLTLLTLIEMP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 166 FLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFavNNARFRTTKLmaYKIMALNSSISY 245
Cdd:cd18590 148 LTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRY--SEALERTYNL--KDRRDTVRAVYL 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 446867357 246 MLMRLVTLFV----LICGTWFVLQGELTYGGFIGFVL 278
Cdd:cd18590 224 LVRRVLQLGVqvlmLYCGRQLIQSGHLTTGSLVSFIL 260
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
332-554 |
7.98e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKE-PILNDISLKIHAGETVAFVGPSGAGKT-TLCSLL------PRFYEQssGSIQIDG---IDTKDM 400
Cdd:PRK15134 7 AIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpspPVVYPS--GDIRFHGeslLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 401 TLSSLR-KQIGIVQQD------------------VFLFSGTIREniaygnlkASEAE---------IWQAVKRaqLEDLI 452
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEpmvslnplhtlekqlyevLSLHRGMRRE--------AARGEilncldrvgIRQAAKR--LTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 453 YsqpdgldtvigergvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLAT 530
Cdd:PRK15134 155 H---------------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqqELNMGLLFITHNLSI 219
|
250 260
....*....|....*....|....*
gi 446867357 531 IKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK15134 220 VRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
344-554 |
9.36e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFY--EQSSGS--------IQIDGIDTKDMTLSslRKQIG-IV 412
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgrtVQREGRLARDIRKS--RANTGyIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSGTIRENIAYGNLKASEaeIW--------QAVKRAQLEDLIYSqpdGLDTVIGERGVKLSGGQKQRLAIARMF 484
Cdd:PRK09984 93 QQFNLVNRLSVLENVLIGALGSTP--FWrtcfswftREQKQRALQALTRV---GMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRL-ATIKNADRIVVVNK-----DGIAEQGSHEEL 554
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVdYALRYCERIVALRQghvfyDGSSQQFDNERF 245
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
330-544 |
1.20e-15 |
|
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: 75.36 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 330 HGDIQYSNVTF---GYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQS--SGSIQIDGIDTKDmtlsS 404
Cdd:cd03232 1 GSVLTWKNLNYtvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 405 LRKQIGIV-QQDVFLFSGTIRENIAYGnlkaseaeiwqavkrAQLedliysqpdgldtvigeRGvkLSGGQKQRLAIARM 483
Cdd:cd03232 77 FQRSTGYVeQQDVHSPNLTVREALRFS---------------ALL-----------------RG--LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 484 FLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHR--LATIKNADRIVVVNKDG 544
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQpsASIFEKFDRLLLLKRGG 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
349-557 |
1.35e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG-----IDTKDmtlsSLRKQIGIVQQDVFLFSG-T 422
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTA----ALAAGVAIIYQELHLVPEmT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIAYGNLKAS----EAEIWQAVKRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:PRK11288 96 VAENLYLGQLPHKggivNRRLLNYEAREQLEHL------GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 499 AL---DTETELAIQKSL-AElsvGRTTLVIAHRLATI-KNADRIVVVnKDG--IA-----EQGSHEELIEQ 557
Cdd:PRK11288 170 SLsarEIEQLFRVIRELrAE---GRVILYVSHRMEEIfALCDAITVF-KDGryVAtfddmAQVDRDQLVQA 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
343-525 |
1.56e-15 |
|
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: 75.38 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 343 ENKEPILNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPRfYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFL 418
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEG-NVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 FSGTIRENIaygnlkaseaeiwQAVKRAQLEDLIysqpdgldtvigeRGVklSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:cd03233 96 PTLTVRETL-------------DFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180
....*....|....*....|....*...
gi 446867357 499 ALDTETELAIQKSLAELS-VGRTTLVIA 525
Cdd:cd03233 148 GLDSSTALEILKCIRTMAdVLKTTTFVS 175
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
347-501 |
1.70e-15 |
|
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: 75.09 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTIREN 426
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 427 IAYGN--LKASEAEIWQAVKRAQL---EDLIYSQpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILILDEATSALD 501
Cdd:TIGR01189 94 LHFWAaiHGGAQRTIEDALAAVGLtgfEDLPAAQ--------------LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
89-278 |
2.02e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 89 MRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLL 168
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 169 WLALYFNKkmtgTFRRLFSDV----ADFNACIENNVGGIRVVQAFGNERFEKDQFAvnNARFRTTKLMAYKIMALNSSIS 244
Cdd:cd18784 151 IVSKVYGD----YYKKLSKAVqdslAKANEVAEETISSIRTVRSFANEDGEANRYS--EKLKDTYKLKIKEALAYGGYVW 224
|
170 180 190
....*....|....*....|....*....|....*.
gi 446867357 245 YMLMRLVTLFVLIC--GTWFVLQGELTYGGFIGFVL 278
Cdd:cd18784 225 SNELTELALTVSTLyyGGHLVITGQISGGNLISFIL 260
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-569 |
2.45e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 352 ISLKIHAGETVAFVGPSGAGKTTLCS----LLPrfyeqSSGSIQIDGIDTKDMTLSSLRKQIG-IVQQ-------DVF-- 417
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLLP-----GSGSIQFAGQPLEAWSAAELARHRAyLSQQqtppfamPVFqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 418 --LFSGtireniAYGNLKASEAEIWQAVKRAQLEDLiysqpdgLDTVIGErgvkLSGGQKQRLAIARMFLK-----NP-- 488
Cdd:PRK03695 90 ltLHQP------DKTRTEAVASALNEVAEALGLDDK-------LGRSVNQ----LSGGEWQRVRLAAVVLQvwpdiNPag 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 489 PILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEELIEQgGGYSRLYE 566
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP-ENLAQVFG 231
|
...
gi 446867357 567 AQF 569
Cdd:PRK03695 232 VNF 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
293-557 |
2.78e-15 |
|
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: 78.69 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 293 VIESYPKGIAGFKRYVELlETEPDIVDSKDAMevKHvhgdiqYSNVTFGYENKepiLNDISLKIHAGETVAFVGPSGAGK 372
Cdd:TIGR03269 256 VVAVFMEGVSEVEKECEV-EVGEPIIKVRNVS--KR------YISVDRGVVKA---VDNVSLEVKEGEIFGIVGTSGAGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 373 TTLCSLLPRFYEQSSGSIQID-GIDTKDMT------LSSLRKQIGIVQQDVFLFS-GTIRENI--AYGNLKASEAEIWQA 442
Cdd:TIGR03269 324 TTLSKIIAGVLEPTSGEVNVRvGDEWVDMTkpgpdgRGRAKRYIGILHQEYDLYPhRTVLDNLteAIGLELPDELARMKA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 443 V---KRAQLEDliysqpDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSL--AELSV 517
Cdd:TIGR03269 404 VitlKMVGFDE------EKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEM 477
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446867357 518 GRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:TIGR03269 478 EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-559 |
6.77e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.53 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 325 EVKHVHgdIQYSNVTfgyenkepILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDmtl 402
Cdd:COG4152 3 ELKGLT--KRFGDKT--------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPED--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 403 sslRKQIG-------------IVQQDVFLfsGTIReniaygNLKASEAeiwqavkRAQLEDLIysqpDGLDtvIGERGVK 469
Cdd:COG4152 70 ---RRRIGylpeerglypkmkVGEQLVYL--ARLK------GLSKAEA-------KRRADEWL----ERLG--LGDRANK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 ----LSGGQKQRLAIARMFLKNPPILILDEATSALD---TETelaIQKSLAEL-SVGRTTLVIAHRLATI-KNADRIVVV 540
Cdd:COG4152 126 kveeLSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvnVEL---LKDVIRELaAKGTTVIFSSHQMELVeELCDRIVII 202
|
250
....*....|....*....
gi 446867357 541 NKDGIAEQGSHEELIEQGG 559
Cdd:COG4152 203 NKGRKVLSGSVDEIRRQFG 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
343-544 |
6.96e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 343 ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDgidtkdmtlsslrkqigiVQQDVFLFSGT 422
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIA-YGNLKASeAEIWQAVkraqledliysqpdGL-DTVIGERGVK-LSGGQKQRLAIARMFLKNPPILILDEATSA 499
Cdd:COG2401 102 LIDAIGrKGDFKDA-VELLNAV--------------GLsDAVLWLRRFKeLSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446867357 500 LDTETELAIQKSLAELS--VGRTTLVIAHRlATIKNA---DRIVVVNKDG 544
Cdd:COG2401 167 LDRQTAKRVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGG 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
343-526 |
1.06e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 343 ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT---LSSLR-KQIGIVQQDvFL 418
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRaKHVGFVFQS-FM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 FSGTI--RENIAYGNLKASEAEiWQAVKRAQ--LEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:PRK10584 99 LIPTLnaLENVELPALLRGESS-RQSRNGAKalLEQL------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....
gi 446867357 495 EATSALDTETELAIQKSLAELS--VGRTTLVIAH 526
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNreHGTTLILVTH 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
324-556 |
1.23e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHGDIQYS--NVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT 401
Cdd:PRK10575 1 MQEYTNHSDTTFAlrNVSFRVPGRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLRKQIGIVQQDVFLFSG-TIRENIAYGNLKaseaeiWQ-------AVKRAQLEDLIysqpdgldTVIG-----ERGV 468
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGmTVRELVAIGRYP------WHgalgrfgAADREKVEEAI--------SLVGlkplaHRLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 469 -KLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTTLVIAhRLATIKNA----DRIVVVNKD 543
Cdd:PRK10575 146 dSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGG 224
|
250
....*....|...
gi 446867357 544 GIAEQGSHEELIE 556
Cdd:PRK10575 225 EMIAQGTPAELMR 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
333-531 |
1.27e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKdmtlSSLRKQ-IGI 411
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQ--DVFLFSGTIRENIA----YGNL------KASEAEIW-QAVKRAQLEDLIYSQpdgldtvIGErgvkLSGGQKQRL 478
Cdd:PRK15056 83 VPQseEVDWSFPVLVEDVVmmgrYGHMgwlrraKKRDRQIVtAALARVDMVEFRHRQ-------IGE----LSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 479 AIARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATI 531
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSV 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
348-527 |
1.63e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSS--GSIQIDGIDTKDMTLsslrKQIGIVQQDVFLFSG-TIR 424
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENIAYGNLKASEAEIWQAVKRAQLEDLIYSQpdGL----DTVIGE---RGVklSGGQKQRLAIARMFLKNPPILILDEAT 497
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISEL--GLtkceNTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|.
gi 446867357 498 SALDTETELAIQKSLAELS-VGRTTLVIAHR 527
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAqKGKTIVTSMHQ 265
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
337-535 |
1.66e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.29 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENkEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGiDTKDMTLSSLRKQIGIVQQDv 416
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER-QSIKKDLCTYQKQLCFVGHR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 flfSG-----TIRENIAYG-NLKASEAEIWQAVKRAQLEDLIySQPDGLdtvigergvkLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK13540 83 ---SGinpylTLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446867357 491 LILDEATSALDTET-ELAIQKSLAELSVGRTTLVIAHRLATIKNAD 535
Cdd:PRK13540 149 WLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
344-556 |
1.78e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLcsllprFY------EQSSGSIQIDGIDtkdmtLSSL------RKQIGI 411
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGED-----ITHLpmhkraRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 412 VQQDVFLFSG-TIRENI--AYGNLKASEAEIwqavkRAQLEDLIysqpD--GLDTVIGERGVKLSGGQKQRLAIARMFLK 486
Cdd:COG1137 83 LPQEASIFRKlTVEDNIlaVLELRKLSKKER-----EERLEELL----EefGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 487 NPPILILDEATSALDTETELAIQK---SLAELSVG--------RTTLVIahrlatiknADRIVVVNKDGIAEQGSHEELI 555
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKiirHLKERGIGvlitdhnvRETLGI---------CDRAYIISEGKVLAEGTPEEIL 224
|
.
gi 446867357 556 E 556
Cdd:COG1137 225 N 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
333-554 |
2.17e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSL---RKQI 409
Cdd:PRK11831 8 VDMRGVSFTRGNR-CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 410 GIVQQDVFLFSG-TIRENIAYGNLKASE--AEIWQAVKRAQLEdliysqpdgldtVIGERGV------KLSGGQKQRLAI 480
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHSTVMMKLE------------AVGLRGAaklmpsELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446867357 481 ARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
333-547 |
2.29e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIV 412
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSGTIREniayGNLKASEAEIWQAVKRAQLEDLIysqpdgldTVIGER--GVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK10522 403 FTDFHLFDQLLGP----EGKPANPALVEKWLERLKMAHKL--------ELEDGRisNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 491 LILDEATSALDTE-TELAIQKSLAEL-SVGRTTLVIAHRLATIKNADRIVVVNKDGIAE 547
Cdd:PRK10522 471 LLLDEWAADQDPHfRREFYQVLLPLLqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-556 |
3.59e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSLRKQ----IGIVQQDVFLFSG-TI 423
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELNLIPQlTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAYGNlkaseaEIWQAVKRAQLEDLiYSQPDGL----------DTVIGErgvkLSGGQKQRLAIARMFLKNPPILIL 493
Cdd:PRK10762 97 AENIFLGR------EFVNRFGRIDWKKM-YAEADKLlarlnlrfssDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 494 DEATSAL-DTETElAIQKSLAEL-SVGRTTLVIAHRLATI-KNADRIVVVnKDG--IAEQG----SHEELIE 556
Cdd:PRK10762 166 DEPTDALtDTETE-SLFRVIRELkSQGRGIVYISHRLKEIfEICDDVTVF-RDGqfIAEREvadlTEDSLIE 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
347-554 |
3.96e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCS----LLPRFYEQSSGSIQIDGidtKDMTLSSLR-KQIGIVQQD------ 415
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAaalgILPAGVRQTAGRVLLDG---KPVAPCALRgRKIATIMQNprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 -VFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLiysqpdglDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:PRK10418 94 pLHTMHTHARETCLALGKPADDATLTAALEAVGLENA--------ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 495 EATSALDTETELAIQKSLAELSVGRT--TLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEEL 554
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
338-528 |
6.76e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 338 VTFGyenKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsSLRkqIGIVQQDVF 417
Cdd:PRK09544 12 VSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------KLR--IGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 418 LfSGTIRENIA-YGNLK--ASEAEIWQAVKRAQLEDLIySQPDGldtvigergvKLSGGQKQRLAIARMFLKNPPILILD 494
Cdd:PRK09544 78 L-DTTLPLTVNrFLRLRpgTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 446867357 495 EATSALDTETELAIQKSLAEL--SVGRTTLVIAHRL 528
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLrrELDCAVLMVSHDL 181
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
351-503 |
8.70e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDtkdmtlssLRKQIGIVQQDVfLFSG--------- 421
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--------IRRQRDEYHQDL-LYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 TIRENIAY---GNLKASEAEIWQAVKRAQL---EDLIYSQpdgldtvigergvkLSGGQKQRLAIARMFLKNPPILILDE 495
Cdd:PRK13538 90 TALENLRFyqrLHGPGDDEALWEALAQVGLagfEDVPVRQ--------------LSAGQQRRVALARLWLTRAPLWILDE 155
|
....*...
gi 446867357 496 ATSALDTE 503
Cdd:PRK13538 156 PFTAIDKQ 163
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
337-558 |
1.01e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.77 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENkEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIdgidtkdmtlsSLRKQIGIVQQDV 416
Cdd:PRK15064 324 NLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------SENANIGYYAQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 ---FLFSGTIRENIA-YGNLKASEaeiwQAVkRAQLEDLIYSQPDgldtvIGERGVKLSGGQKQRLAIARMFLKNPPILI 492
Cdd:PRK15064 392 aydFENDLTLFDWMSqWRQEGDDE----QAV-RGTLGRLLFSQDD-----IKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 493 LDEATSALDTETELAIQKSLaELSVGrTTLVIAH------RLATiknadRIVVVNKDGIAE-QGSHEE-LIEQG 558
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMAL-EKYEG-TLIFVSHdrefvsSLAT-----RIIEITPDGVVDfSGTYEEyLRSQG 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
349-544 |
1.81e-13 |
|
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: 72.94 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSS--GSIQIDGIDTKDMTLSSL-RKQIGIVQQDVFLFSG-TIR 424
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENIAYGN---LKASEAEIWQAVKRAQ--LEDLiysqpdGLDTVIGERGV-KLSGGQKQRLAIARMFLKNPPILILDEATS 498
Cdd:TIGR02633 97 ENIFLGNeitLPGGRMAYNAMYLRAKnlLREL------QLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446867357 499 AL---DTETELAIQKSLAELSVGrtTLVIAHRLATIKNADRIVVVNKDG 544
Cdd:TIGR02633 171 SLtekETEILLDIIRDLKAHGVA--CVYISHKLNEVKAVCDTICVIRDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
349-544 |
2.20e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSS--GSIQIDGI-----DTKDmtlsSLRKQIGIVQQDVFLFSG 421
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD----SEALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 -TIRENIAYGNLKASEAEI-WQAVKRAQLEDLiysQPDGL----DTVIGERGVklsgGQKQRLAIARMFLKNPPILILDE 495
Cdd:NF040905 93 lSIAENIFLGNERAKRGVIdWNETNRRARELL---AKVGLdespDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 496 ATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATI-KNADRIVVVnKDG 544
Cdd:NF040905 166 PTAALNEEDSAALLDLLLELkAQGITSIIISHKLNEIrRVADSITVL-RDG 215
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
333-532 |
3.48e-13 |
|
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: 72.47 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtkdmtlsslRKQIGIV 412
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDVFLFSGTIRENIAYGNLKA-------SEAEIWQAVKRAQLEDLIySQPDGLDTVIGERGVkLSGGQKQRLAIARMFL 485
Cdd:TIGR00954 521 PQRPYMTLGTLRDQIIYPDSSEdmkrrglSDKDLEQILDNVQLTHIL-EREGGWSAVQDWMDV-LSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAElsVGRTTLVIAHRLATIK 532
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
272-544 |
4.18e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 272 GFIGFVLLTNIFF----RPIEKINAVIeSYPKGIAgfKRYVELLETEP---------------DIVDSKDA------MEV 326
Cdd:TIGR00956 677 GFTVFFFFVYILLtefnKGAKQKGEIL-VFRRGSL--KRAKKAGETSAsnkndieagevlgstDLTDESDDvndekdMEK 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 327 KHVHGDIQYSNVTF--GYE-NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPrfyEQSSGsiqidGIDTKDMTL- 402
Cdd:TIGR00956 754 ESGEDIFHWRNLTYevKIKkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA---ERVTT-----GVITGGDRLv 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 403 ------SSLRKQIGIVQQ-DVFLFSGTIRENIAYGNLKASEAEIWQAVKRAQLEDLI--YSQPDGLDTVIGERGVKLSGG 473
Cdd:TIGR00956 826 ngrpldSSFQRSIGYVQQqDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 474 QKQRLAIARMFLKNPPILI-LDEATSALDTETELAIQKSLAELS-VGRTTLVIAHR-LATIKNA-DRIVVVNKDG 544
Cdd:TIGR00956 906 QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQpSAILFEEfDRLLLLQKGG 980
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
344-526 |
4.41e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 344 NKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKdmtlsslrkqigivqqdvflfSGTI 423
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---------------------RGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAY-GNLKASEAEIwqavkrAQLEDLIY----------SQPDGLDTVIGERGV------KLSGGQKQRLAIARMFLK 486
Cdd:PRK13543 81 SRFMAYlGHLPGLKADL------STLENLHFlcglhgrrakQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446867357 487 NPPILILDEATSALDTETELAIQKSL-AELSVGRTTLVIAH 526
Cdd:PRK13543 155 PAPLWLLDEPYANLDLEGITLVNRMIsAHLRGGGAALVTTH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
333-535 |
4.65e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.58 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLL----PRFY---------EQSSGSiqidgidtkd 399
Cdd:PRK10938 261 IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhPQGYsndltlfgrRRGSGE---------- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 400 mTLSSLRKQIGIVQQDVFL---FSGTIRENIAYGNLKAseAEIWQAVKRAQ-------LEDLiysqpdGLDTVIGERGVK 469
Cdd:PRK10938 330 -TIWDIKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDS--IGIYQAVSDRQqklaqqwLDIL------GIDKRTADAPFH 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 -LSGGQkQRLA-IARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLV------------IAHRLATIKNA 534
Cdd:PRK10938 401 sLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLfvshhaedapacITHRLEFVPDG 479
|
.
gi 446867357 535 D 535
Cdd:PRK10938 480 D 480
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-549 |
7.13e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSL---------RKQIGIVQQD------ 415
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHprdglr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 --VflfS--GTIRENIA------YGNLKASEAEIWQAVKRAqledliysqPDGLDtvigERGVKLSGGQKQRLAIARMFL 485
Cdd:PRK11701 104 mqV---SagGNIGERLMavgarhYGDIRATAGDWLERVEID---------AARID----DLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 486 KNPPILILDEATSALDteteLAIQKSLAEL------SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQG 549
Cdd:PRK11701 168 THPRLVFMDEPTGGLD----VSVQARLLDLlrglvrELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-559 |
8.48e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 336 SNVTFGYENkEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSI--QIDGIDTKDMTLSSLRKQIGIVQ 413
Cdd:PRK13638 5 SDLWFRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 QD--VFLFSGTIRENIAYG--NLKASEAEIWQAVKRAQledliysqpdgldTVIGERGVK------LSGGQKQRLAIARM 483
Cdd:PRK13638 84 QDpeQQIFYTDIDSDIAFSlrNLGVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 484 FLKNPPILILDEATSALDTETE---LAIQKSLAelSVGRTTLVIAHRLATIKN-ADRIVVVNKDGIAEQG------SHEE 553
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRtqmIAIIRRIV--AQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTE 228
|
....*.
gi 446867357 554 LIEQGG 559
Cdd:PRK13638 229 AMEQAG 234
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
85-299 |
9.42e-13 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain] Cd Length: 289 Bit Score: 69.04 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 85 IETDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVI 164
Cdd:cd18589 67 IHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 165 PFLLWLAlyfnkKMTGTFRRLFS-----DVADFNACIENNVGGIRVVQAFGNERFEKDQFAV---NNARFRTTKLMAYKI 236
Cdd:cd18589 147 PLLLLVP-----KFVGKFQQSLAvqvqkSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQrlqKTYRLNKKEAAAYAV 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 237 MALNSSISYMLMRLVTLFVlicGTWFVLQGELTYGGFIGFVLLTNIFFRPIEkinAVIESYPK 299
Cdd:cd18589 222 SMWTSSFSGLALKVGILYY---GGQLVTAGTVSSGDLVTFVLYELQFTSAVE---VLLSYYPS 278
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
351-553 |
1.37e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG---IDT-KDMTLSSLRKQIGIVQQDVFLFSG-TIRE 425
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFPHyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 426 NIAYGNLKASEAEIWQAVKRAQLEDLIYSQPdgldtvigergVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETE 505
Cdd:PRK11144 96 NLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446867357 506 LAIQKSLAELS--VGRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEE 553
Cdd:PRK11144 165 RELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
337-533 |
2.31e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDgidTKdmtlsslrkqigivqQDV 416
Cdd:PRK11147 324 NVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG---TK---------------LEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLF---------SGTIRENIAYGNlkaSEAEIwQAVKR---AQLEDLIYS-----QPdgldtvigergVK-LSGGQKQRL 478
Cdd:PRK11147 385 AYFdqhraeldpEKTVMDNLAEGK---QEVMV-NGRPRhvlGYLQDFLFHpkramTP-----------VKaLSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 479 AIARMFLKNPPILILDEATSALDTET-ELaiqksLAELSVGR--TTLVIAHRLATIKN 533
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETlEL-----LEELLDSYqgTVLLVSHDRQFVDN 502
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
13-297 |
4.36e-12 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 67.16 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNW-TLILwACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQ 91
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYsTLYV-LTIGVVIALLFEGILGYLRRYLLLVATTRIDARLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 92 KLFDHIQKLSFRFFDNNKTGhlisRLTNDLMEIGEIAHHGPEDLFIAV---MTLVGAFSFMMMINWKLALLTF-FVIPFL 167
Cdd:cd18783 80 RTFDRLLSLPIDFFERTPAG----VLTKHMQQIERIRQFLTGQLFGTLldaTSLLVFLPVLFFYSPTLALVVLaFSALIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 168 LWLALYFNkkmtgTFRRLFSDV----ADFNACIENNVGGIRVVQAFGNE---RFEKDQFAVN--NARFRTTKLMAYkIMA 238
Cdd:cd18783 156 LIILAFLP-----PFRRRLQALyraeGERQAFLVETVHGIRTVKSLALEprqRREWDERVARaiRARFAVGRLSNW-PQT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 239 LNSSISyMLMRLVTLFVlicGTWFVLQGELTYGGFIGFVLLTNIFFRPIEKINAVIESY 297
Cdd:cd18783 230 LTGPLE-KLMTVGVIWV---GAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEY 284
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-546 |
4.98e-12 |
|
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: 66.28 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAG-----ETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDT--KDMTLSSlrKQIGIVQQdvFLFSG 421
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsyKPQYIKA--DYEGTVRD--LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 TIReniaYGNLKASEAEIwqaVKRAQLEDLIysqpdgldtvigERGV-KLSGGQKQRLAIARMFLKNPPILILDEATSAL 500
Cdd:cd03237 86 TKD----FYTHPYFKTEI---AKPLQIEQIL------------DREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 501 DTETELAIQKSLAE--LSVGRTTLVIAHRLATIKN-ADRIVVVN----KDGIA 546
Cdd:cd03237 147 DVEQRLMASKVIRRfaENNEKTAFVVEHDIIMIDYlADRLIVFEgepsVNGVA 199
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
28-280 |
6.78e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents 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: 350010 [Multi-domain] Cd Length: 294 Bit Score: 66.45 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 28 LLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDN 107
Cdd:cd18566 16 ILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 108 NKTGHLISRLtNDLMEIGEIaHHGPedLFIAVMTLVGAFSF---MMMINWKLALLTFFVIPFLLWLALYFNKKMtgtfRR 184
Cdd:cd18566 96 EPSGAHLERL-NSLEQIREF-LTGQ--ALLALLDLPFVLIFlglIWYLGGKLVLVPLVLLGLFVLVAILLGPIL----RR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 185 LFSDVADFNA-----CIEnNVGGIRVVQAFGNE-----RFEKDQFAVNNARFRTTklmayKIMALNSSISYMLMRLVTLF 254
Cdd:cd18566 168 ALKERSRADErrqnfLIE-TLTGIHTIKAMAMEpqmlrRYERLQANAAYAGFKVA-----KINAVAQTLGQLFSQVSMVA 241
|
250 260
....*....|....*....|....*.
gi 446867357 255 VLICGTWFVLQGELTYGGFIGFVLLT 280
Cdd:cd18566 242 VVAFGALLVINGDLTVGALIACTMLS 267
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
349-542 |
8.84e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE-QSSGSIQIDG--IDTKDmTLSSLRKQIGIVQQDV----FLFSG 421
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRN-PAQAIRAGIAMVPEDRkrhgIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 TIRENIAYGNLK-----------ASEAEIWQAVKRAQLEDliySQPDgldTVIGergvKLSGGQKQRLAIARMFLKNPPI 490
Cdd:TIGR02633 355 GVGKNITLSVLKsfcfkmridaaAELQIIGSAIQRLKVKT---ASPF---LPIG----RLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446867357 491 LILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKN-ADRIVVVNK 542
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGE 478
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
299-530 |
9.85e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 299 KGIAGFKRYVELLETEpdivdSKDAMEVKHVH-------GD--IQYSNVTFGYENKePILNDISLKIHAGETVAFVGPSG 369
Cdd:TIGR03719 285 KSKARLARYEELLSQE-----FQKRNETAEIYippgprlGDkvIEAENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 370 AGKTTLCSLLPRFYEQSSGSIQIDgiDTKdmtlsslrkQIGIVQQdvflfsgtIRENIAYGNlkaseaEIWQAVKraqle 449
Cdd:TIGR03719 359 AGKSTLFRMITGQEQPDSGTIEIG--ETV---------KLAYVDQ--------SRDALDPNK------TVWEEIS----- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 450 dliysqpDGLDTV-IGERGV---------------------KLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELA 507
Cdd:TIGR03719 409 -------GGLDIIkLGKREIpsrayvgrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
250 260
....*....|....*....|....*....
gi 446867357 508 IQKSLaeLSVGRTTLVIAH------RLAT 530
Cdd:TIGR03719 482 LEEAL--LNFAGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
40-288 |
1.20e-11 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 65.58 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 40 FIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKTGHLISRL-T 118
Cdd:cd18569 28 FIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVqS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 119 ND---LMEIGEIAhhgpeDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNAC 195
Cdd:cd18569 108 NDrvaNLLSGQLA-----TTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 196 IENNVGGIRVVQAFGNER--FEK---DQFAVNNARFRTTKlmaykIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTY 270
Cdd:cd18569 183 TMSGLQMIETLKASGAESdfFSRwagYQAKVLNAQQELGR-----TNQLLGALPTLLSALTNAAILGLGGLLVMDGALTI 257
|
250
....*....|....*...
gi 446867357 271 GGFIGFVLLTNIFFRPIE 288
Cdd:cd18569 258 GMLVAFQSLMASFLAPVN 275
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
327-539 |
1.45e-11 |
|
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: 67.12 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 327 KHVHGDIQYSNVTFGYENKEPILNDISL-----KIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIqidgidtkDMT 401
Cdd:COG1245 329 VHAPRREKEEETLVEYPDLTKSYGGFSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LS-SLRKQigIVQQDvflFSGTIRENIAYGNLKASEAEIWQA--VKRAQLEDLIysqpdgldtvigERGVK-LSGGQKQR 477
Cdd:COG1245 401 LKiSYKPQ--YISPD---YDGTVEEFLRSANTDDFGSSYYKTeiIKPLGLEKLL------------DKNVKdLSGGELQR 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKS---LAElSVGRTTLVIAHRLATIKN-ADRIVV 539
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAirrFAE-NRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-526 |
1.81e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPrfyeqssgsiqidGIDtKDMT---LSSLRKQIGIVQ 413
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFNgeaRPQPGIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 QDVFL-FSGTIRENIAYGnlkasEAEIWQAVKR----------------------AQLEDLIYSQpDG--LDTVI----- 463
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEG-----VAEIKDALDRfneisakyaepdadfdklaaeqAELQEIIDAA-DAwdLDSQLeiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 464 ------GERGV-KLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSvGrTTLVIAH 526
Cdd:TIGR03719 149 alrcppWDADVtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP-G-TVVAVTH 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
348-561 |
2.07e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQS--------SGSIQIDG-----IDTkdMTLSSLRKQIGIVQQ 414
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGeplaaIDA--PRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DVFLFSgtIRENI---------AYGNLKASEAEI-WQAVKRAqledliysqpdGLDTVIGERGVKLSGGQKQRLAIARMF 484
Cdd:PRK13547 94 PAFAFS--AREIVllgrypharRAGALTHRDGEIaWQALALA-----------GATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 485 LK---------NPPILILDEATSALDteteLAIQKSLAElSVGRTT-------LVIAH--RLATiKNADRIVVVNKDGIA 546
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALD----LAHQHRLLD-TVRRLArdwnlgvLAIVHdpNLAA-RHADRIAMLADGAIV 234
|
250 260
....*....|....*....|
gi 446867357 547 EQGS-----HEELIEQGGGY 561
Cdd:PRK13547 235 AHGApadvlTPAHIARCYGF 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
306-542 |
1.59e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 306 RYVELLETEPDIVDSKDAMEVKhvhgdiqysNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQ 385
Cdd:COG3845 240 REVLLRVEKAPAEPGEVVLEVE---------NLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 386 SSGSIQIDGIDTKDMTLSSLRKQ-IGIVQQD------VFLFSgtIRENIA---YGNLKASEAEI--WQAVkRAQLEDLI- 452
Cdd:COG3845 311 ASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrglVPDMS--VAENLIlgrYRRPPFSRGGFldRKAI-RAFAEELIe 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 453 -YS-QPDGLDTVIGergvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLA 529
Cdd:COG3845 388 eFDvRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDLD 463
|
250
....*....|....
gi 446867357 530 TIKN-ADRIVVVNK 542
Cdd:COG3845 464 EILAlSDRIAVMYE 477
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
350-501 |
1.91e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 350 NDISLKIHAGETVAFVGPSGAGKTT----LCSLLPrfyeQSSGSIQIDG--IDTKDMtlsSLRKQIGIVQQDVFLFSG-T 422
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLLP----ASEGEAWLFGqpVDAGDI---ATRRRVGYMSQAFSLYGElT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 IRENIA-----YGnLKASEAE--IWQAVKRAQLEDLIYSQPDGLdtvigergvklSGGQKQRLAIARMFLKNPPILILDE 495
Cdd:NF033858 356 VRQNLElharlFH-LPAAEIAarVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDE 423
|
....*.
gi 446867357 496 ATSALD 501
Cdd:NF033858 424 PTSGVD 429
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
349-539 |
2.21e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLK-----IHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQID----------GIDTkDMTLSSLRKQIGivq 413
Cdd:PRK13409 350 LGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyiKPDY-DGTVEDLLRSIT--- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 414 qdvflfsgtireniayGNLKAS--EAEIwqaVKRAQLEDLIysqpdgldtvigERGVK-LSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK13409 426 ----------------DDLGSSyyKSEI---IKPLQLERLL------------DKNVKdLSGGELQRVAIAACLSRDADL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446867357 491 LILDEATSALDTETELAIQK---SLAELSvGRTTLVIAHRLATIKN-ADRIVV 539
Cdd:PRK13409 475 YLLDEPSAHLDVEQRLAVAKairRIAEER-EATALVVDHDIYMIDYiSDRLMV 526
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
337-547 |
2.72e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 337 NVTfGYENKEpiLNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMT-LSSLRKQIGIV--- 412
Cdd:PRK09700 270 NVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYItes 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 -QQDVFLFSGTIRENIAY------GNLKAS--------EAEIWQAVKraqleDLIYSQPDGLDTVIGErgvkLSGGQKQR 477
Cdd:PRK09700 347 rRDNGFFPNFSIAQNMAIsrslkdGGYKGAmglfhevdEQRTAENQR-----ELLALKCHSVNQNITE----LSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATIKNA-DRIVVVNKDGIAE 547
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-504 |
2.72e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 342 YENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPrfyeqssgsiqidGIDTK---DMTLSSLRKqIGIVQQDVFL 418
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKEfegEARPAPGIK-VGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 -FSGTIRENIAYGnlkasEAEIWQAVKR----------------------AQLEDLIYSQ------------------PD 457
Cdd:PRK11819 82 dPEKTVRENVEEG-----VAEVKAALDRfneiyaayaepdadfdalaaeqGELQEIIDAAdawdldsqleiamdalrcPP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446867357 458 GlDTVIGergvKLSGGQKQRLAIARMFLKNPPILILDEATSALDTET 504
Cdd:PRK11819 157 W-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
324-555 |
3.82e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.96 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHGDIQYSNVTFGYENKEPIlNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDMT 401
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 402 LSSLRkqIGIVQQDVF-----------LFSGTIRENIAYgNLKASEAEIWQAVKRAQL-EDLIYSQPDgldtvigergvK 469
Cdd:PRK15112 84 YRSQR--IRMIFQDPStslnprqrisqILDFPLRLNTDL-EPEQREKQIIETLRQVGLlPDHASYYPH-----------M 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 LSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN-ADRIVVVNKDGIA 546
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
....*....
gi 446867357 547 EQGSHEELI 555
Cdd:PRK15112 230 ERGSTADVL 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
348-540 |
6.81e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYE-QSSGSIQIDG--IDTKDmTLSSLRKQIGIVQQD------VFL 418
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDrkrdgiVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 FSgtIRENIAYGNLK-----------ASEAEIWQAVKRAQLEDliySQPdglDTVIGergvKLSGGQKQRLAIARMFLKN 487
Cdd:PRK13549 356 MG--VGKNITLAALDrftggsriddaAELKTILESIQRLKVKT---ASP---ELAIA----RLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 488 PPILILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKN-ADRIVVV 540
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGlSDRVLVM 478
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
324-552 |
6.97e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHGDIqysnvtfgyeNKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLL---PRfYEQSSGSIQIDGIDTKDM 400
Cdd:CHL00131 8 LEIKNLHASV----------NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghPA-YKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 401 TlSSLRKQIGI------------VQQDVFLFSGTIRENIAYGNLKASEAEIWQAVKraQLEDLIysqpdGLDTVIGERGV 468
Cdd:CHL00131 77 E-PEERAHLGIflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIIN--EKLKLV-----GMDPSFLSRNV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 469 K--LSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAH--RLATIKNADRIVVVNKD 543
Cdd:CHL00131 149 NegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNG 228
|
....*....
gi 446867357 544 GIAEQGSHE 552
Cdd:CHL00131 229 KIIKTGDAE 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-531 |
8.78e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTL----CSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVFLFSGTI 423
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENIAY-------GNLKASEAEIWQAVKRAQLEDLIYSQPDGLDTVIGE---RGVklSGGQKQRLAIARMFLKNPPILIL 493
Cdd:TIGR00956 156 GETLDFaarcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 446867357 494 DEATSALDTETELAIQKSLaelsvgRTTLVIAHRLATI 531
Cdd:TIGR00956 234 DNATRGLDSATALEFIRAL------KTSANILDTTPLV 265
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
22-269 |
9.82e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 59.81 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIVNQFIDKL--LPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQK 99
Cdd:cd18579 5 LKLLEDLLSLAQPLLLGLLISYLssYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 100 LSFRFFDNNKTGHLISRLTNDLMEIGEIAHHGPeDLFIAVMTLVGAFSFM-MMINWkLALLTFFVIPFLLWLALYFNKKM 178
Cdd:cd18579 85 LSSSARQETSTGEIVNLMSVDVQRIEDFFLFLH-YLWSAPLQIIVALYLLyRLLGW-AALAGLGVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 179 tGTFRRLFSDVAD-----FNACIennvGGIRVVQAFGNER-FEKdqfAVNNARFRTTKLM--AYKIMALNSSISYMLMRL 250
Cdd:cd18579 163 -SKLRKKLMKATDervklTNEIL----SGIKVIKLYAWEKpFLK---RIEELRKKELKALrkFGYLRALNSFLFFSTPVL 234
|
250
....*....|....*....
gi 446867357 251 VTLFVLicGTWFVLQGELT 269
Cdd:cd18579 235 VSLATF--ATYVLLGNPLT 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-539 |
1.07e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 351 DISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSlRKQIGIV------QQDVFLFSGTIR 424
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENIAygNLKASEAEIWQAVKR--AQLEDliYSQPDGLDTVIGERGVK-LSGGQKQRLAIARMFLKNPPILILDEATSALD 501
Cdd:PRK15439 360 WNVC--ALTHNRRGFWIKPARenAVLER--YRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446867357 502 TETELAIQ---KSLAELSVGrtTLVIAHRLATI-KNADRIVV 539
Cdd:PRK15439 436 VSARNDIYqliRSIAAQNVA--VLFISSDLEEIeQMADRVLV 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
324-501 |
1.63e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 324 MEVKHVHGdiqysnvtfgyenkePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLS 403
Cdd:PRK10762 258 LKVDNLSG---------------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 404 SLRKQI--GIV------QQDVFLFSGTIRENI---AYGNLKASEAEIWQAVKRAQLEDLI----YSQPdGLDTVIGergv 468
Cdd:PRK10762 320 SPQDGLanGIVyisedrKRDGLVLGMSVKENMsltALRYFSRAGGSLKHADEQQAVSDFIrlfnIKTP-SMEQAIG---- 394
|
170 180 190
....*....|....*....|....*....|...
gi 446867357 469 KLSGGQKQRLAIARMFLKNPPILILDEATSALD 501
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
359-532 |
2.83e-09 |
|
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: 55.84 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 359 GETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIvqqdvflfsgtireniaygnlkaseae 438
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 439 iwqavkraqledliysqpdgldtviGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLA----- 513
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|
gi 446867357 514 -ELSVGRTTLVIAHRLATIK 532
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDL 129
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-540 |
3.59e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 359 GETVAFVGPSGAGKTTLCSLLprfyeqsSGSI-----QIDGIDTKDMTLSSLR-------------KQIGIVQ--QDVFL 418
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-------SGELipnlgDYEEEPSWDEVLKRFRgtelqnyfkklynGEIKVVHkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 419 ----FSGTIRENIAygnlKASEAEIWQAVkraqLEDLiysqpdGLDTVIgERGVK-LSGGQKQRLAIARMFLKNPPILIL 493
Cdd:PRK13409 172 ipkvFKGKVRELLK----KVDERGKLDEV----VERL------GLENIL-DRDISeLSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446867357 494 DEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKN-ADRIVVV 540
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
457-540 |
4.12e-09 |
|
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: 56.04 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 457 DGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATIKN- 533
Cdd:cd03222 59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYl 138
|
....*..
gi 446867357 534 ADRIVVV 540
Cdd:cd03222 139 SDRIHVF 145
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
348-554 |
5.38e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 348 ILNDISLKIHAGETVAFVGPSGAGKTTLC-SLLPRFYEQS-SGSIQIDG--IDTKDMT---------LSSLRKQIGIVQQ 414
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRNiSGTVFKDGkeVDVSTVSdaidaglayVTEDRKGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DvflfsgTIRENIAYGNLKA--------SEAEIWQAVK-RAQLEdlIYSqPDgldtvIGERGVKLSGGQKQRLAIARMFL 485
Cdd:NF040905 355 D------DIKRNITLANLGKvsrrgvidENEEIKVAEEyRKKMN--IKT-PS-----VFQKVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 486 KNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLAT-IKNADRIVVVNKDGI-----AEQGSHEEL 554
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVISSELPElLGMCDRIYVMNEGRItgelpREEASQERI 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
345-557 |
6.96e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 345 KEPIlndiSLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSL--------------RKQIG 410
Cdd:PRK11288 269 REPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPrdairagimlcpedRKAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 IVQqdvflfSGTIRENIA---------YGNLKASEAEIWQAvkRAQLEDLIYSQPDGlDTVIGergvKLSGGQKQRLAIA 481
Cdd:PRK11288 342 IIP------VHSVADNINisarrhhlrAGCLINNRWEAENA--DRFIRSLNIKTPSR-EQLIM----NLSGGNQQKAILG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 482 RMFLKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLA-TIKNADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK11288 409 RWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLPeVLGVADRIVVMREGRIAGELAREQATER 486
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-540 |
8.13e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.26 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 359 GETVAFVGPSGAGKTTLCSLLprfyeqsSGSI-----QIDGIDTKDMTLSSLRkqiGIVQQDVFlfsgtirENIAYGNLK 433
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKIL-------SGELkpnlgDYDEEPSWDEVLKRFR---GTELQDYF-------KKLANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 434 ASE-----AEIWQAVK------------RAQLEDLIysQPDGLDTVIgERGVK-LSGGQKQRLAIARMFLKNPPILILDE 495
Cdd:COG1245 162 VAHkpqyvDLIPKVFKgtvrellekvdeRGKLDELA--EKLGLENIL-DRDISeLSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446867357 496 ATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATI-KNADRIVVV 540
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAILdYLADYVHIL 285
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
340-538 |
9.87e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 340 FGYEnkePILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDgidtKDMTLSSLrkqigivQQD---- 415
Cdd:PRK11147 13 FSDA---PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARL-------QQDpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 416 VflfSGTIRENIAYGnlkasEAEIWQAVKR-AQLEDLIYSQPDG--------------------LDTVIGERGVK----- 469
Cdd:PRK11147 79 V---EGTVYDFVAEG-----IEEQAEYLKRyHDISHLVETDPSEknlnelaklqeqldhhnlwqLENRINEVLAQlgldp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 470 ------LSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLaeLSVGRTTLVIAHRLATIKN-ADRIV 538
Cdd:PRK11147 151 daalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQGSIIFISHDRSFIRNmATRIV 224
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-299 |
1.14e-08 |
|
Six-transmembrane helical domain 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: 350002 [Multi-domain] Cd Length: 312 Bit Score: 56.90 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 48 QNWTLILWACFGLLAVYILNAGLQyvVTYWGHMLGVNIETdMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEI 127
Cdd:cd18558 56 EEMTLYAYYYLIIGAIVLITAYIQ--GSFWGLAAGRQTKK-IRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 128 AHHGPEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQ 207
Cdd:cd18558 133 IGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 208 AFGNERFEKDQFAVNNARFRTTKLMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:cd18558 213 AFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSA 292
|
250
....*....|..
gi 446867357 288 EKINAVIESYPK 299
Cdd:cd18558 293 GQQVPSIEAFAN 304
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
16-279 |
1.87e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 55.97 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 16 FILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQN----WTLILWACFGLLAVyILNAGLQYVVTYWGhmlGVNIETDMRQ 91
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNsssgYYLGVYAALLVLAS-VLLVLLRWLLFVLA---GLRASRRLHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 92 KLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEI-GEIAHHGpEDLFIAVMTLVGAFSFMMMINWKLALLTFFVIPFLLWL 170
Cdd:cd18580 77 KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIdEELPLAL-LDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 171 ALYFNKkmtgT---FRRLFSD-----VADFNACIEnnvgGIRVVQAFG-NERFEKDQFAVNNARFRTTklmaykiMALNS 241
Cdd:cd18580 156 QRYYLR----TsrqLRRLESEsrsplYSHFSETLS----GLSTIRAFGwQERFIEENLRLLDASQRAF-------YLLLA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446867357 242 SISYMLMRL---VTLFVLICGTWFVLQGELTYGGFIGFVLL 279
Cdd:cd18580 221 VQRWLGLRLdllGALLALVVALLAVLLRSSISAGLVGLALT 261
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
333-530 |
2.56e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPIlNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIdGiDTKdmtlsslrkQIGIV 412
Cdd:PRK11819 325 IEAENLSKSFGDRLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETV---------KLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 413 QQDvflfsgtiRENIAygnlkaSEAEIWQAVKraqledliysqpDGLDTV-IGERGV---------------------KL 470
Cdd:PRK11819 393 DQS--------RDALD------PNKTVWEEIS------------GGLDIIkVGNREIpsrayvgrfnfkggdqqkkvgVL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 471 SGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSvGrTTLVIAH------RLAT 530
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP-G-CAVVISHdrwfldRIAT 510
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
52-277 |
2.76e-08 |
|
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: 55.61 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 52 LILWACFGLLAVYilnAGLQYVVTYwghmLGVNIETDMRQKL----FDHIQKLSFRFFDNNKTGHLISRLT-----NDLM 122
Cdd:cd18583 38 IGLYVLLRFLQSG---GGLGLLRSW----LWIPVEQYSYRALstaaFNHVMNLSMDFHDSKKSGEVLKAIEqgssiNDLL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 123 E--IGEIahhGPE--DLFIAvmtlVGAFSFMMmiNWKLALLTFFVIPFLLWLALYFNKKMTgTFRRLFSDvADFNaciEN 198
Cdd:cd18583 111 EqiLFQI---VPMiiDLVIA----IVYLYYLF--DPYMGLIVAVVMVLYVWSTIKLTSWRT-KLRRDMID-ADRE---ER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 199 NVG-----GIRVVQAFGNERFEKDQF--AVNNARFRTTKLMAYkimalnSSISYMLMRLVTLFVLICGTWF----VLQGE 267
Cdd:cd18583 177 SILtesllNWETVKYFNREPYEKERYreAVKNYQKAERKYLFS------LNLLNAVQSLILTLGLLAGCFLaayqVSQGQ 250
|
250
....*....|
gi 446867357 268 LTYGGFIGFV 277
Cdd:cd18583 251 ATVGDFVTLL 260
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
347-561 |
2.78e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLP--RFYEQSSGSIQIDGidtKDMTLSSLRKQIGivqQDVFLFSGTIR 424
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKG---KDLLELSPEDRAG---EGIFMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENIAYGN---LKASEAEIWQ-----AVKRAQLEDLIYSQPDGL----DTVIGERGVKLSGGQKQRLAIARMFLKNPPILI 492
Cdd:PRK09580 89 EIPGVSNqffLQTALNAVRSyrgqePLDRFDFQDLMEEKIALLkmpeDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 493 LDEATSALDTETELAIQKSLAELSVG-RTTLVIAH--RLATIKNADRIVVVNKDGIAEQGSH---EELIEQGGGY 561
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQGYGW 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
333-526 |
4.30e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 333 IQYSNVTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSI--------------QIDGID-T 397
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDlS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 398 KDMTLSSLRKQIGIVQQDVflfsgtireniaygnlkaseaeiwqavkRAQLEDLIYSQPDGLDTVigergVKLSGGQKQR 477
Cdd:PLN03073 589 SNPLLYMMRCFPGVPEQKL----------------------------RAHLGSFGVTGNLALQPM-----YTLSGGQKSR 635
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446867357 478 LAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGrtTLVIAH 526
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
343-527 |
4.58e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 343 ENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPR-----FYEqssGSIQIDGIDTKDMTLSSLRkqiGIVQQ-DV 416
Cdd:PLN03140 890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYIE---GDIRISGFPKKQETFARIS---GYCEQnDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 417 FLFSGTIRENIAYGNLKASEAEIWQAVKRA---QLEDLIysQPDGL-DTVIGERGVK-LSGGQKQRLAIARMFLKNPPIL 491
Cdd:PLN03140 964 HSPQVTVRESLIYSAFLRLPKEVSKEEKMMfvdEVMELV--ELDNLkDAIVGLPGVTgLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*..
gi 446867357 492 ILDEATSALDTETELAIQKSLAE-LSVGRTTLVIAHR 527
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQ 1078
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
353-557 |
6.29e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 353 SLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDgidTKDMTLSSLRKQIGIVQQDvFLFSGTIRENIAYGNL 432
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---FSHITRLSFEQLQKLVSDE-WQRNNTDMLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 433 KASEAEIWQ-AVKRAQLEDLiYSQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKS 511
Cdd:PRK10938 99 GRTTAEIIQdEVKDPARCEQ-LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446867357 512 LAELSVGRTTLV-IAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQ 557
Cdd:PRK10938 178 LASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
363-551 |
7.56e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.99 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 363 AFVGPSGAGKTTL--CSLLPRFYEQSSGSIQIDGiDTKDMTLSSLRKQIGIVqqdvflFSGTIRENIAygnlkaseaeiw 440
Cdd:cd03240 26 LIVGQNGAGKTTIieALKYALTGELPPNSKGGAH-DPKLIREGEVRAQVKLA------FENANGKKYT------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 441 qaVKR--AQLEDLIYSQPDGLDTVIGERGVKLSGGQKQ------RLAIARMFLKNPPILILDEATSALDTETelaIQKSL 512
Cdd:cd03240 87 --ITRslAILENVIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446867357 513 AEL------SVGRTTLVIAHRLATIKNADRIVVVNKDGiaEQGSH 551
Cdd:cd03240 162 AEIieerksQKNFQLIVITHDEELVDAADHIYRVEKDG--RQKSR 204
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
332-557 |
7.62e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKEPI-LNDISLKIHAGETVAFVGPSGAGKT----TLCSLLPRfYEQSSGSIQIDG---IDTKDMTLS 403
Cdd:PRK09473 14 DVKDLRVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGreiLNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 404 SLR-KQIGIVQQDV------FLFSGTIRENIAYGNLKASEAEIWQ-------AVKRAQLEDLIYSQPDgldtvigergvK 469
Cdd:PRK09473 93 KLRaEQISMIFQDPmtslnpYMRVGEQLMEVLMLHKGMSKAEAFEesvrmldAVKMPEARKRMKMYPH-----------E 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 LSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL--SVGRTTLVIAHRLATIKN-ADRIVVVNKDGIA 546
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkrEFNTAIIMITHDLGVVAGiCDKVLVMYAGRTM 241
|
250
....*....|.
gi 446867357 547 EQGSHEELIEQ 557
Cdd:PRK09473 242 EYGNARDVFYQ 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-544 |
9.74e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDG--IDTKDmTLSSLRKQIGIVQQDVFLF-SGTIRE 425
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALENGISMVHQELNLVlQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 426 NIAYGN--LKA---SEAEIWQAVKrAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSAL 500
Cdd:PRK10982 93 NMWLGRypTKGmfvDQDKMYRDTK-AIFDEL------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446867357 501 dTETEL----AIQKSLAELSVGrtTLVIAHRLATI-KNADRIVVVnKDG 544
Cdd:PRK10982 166 -TEKEVnhlfTIIRKLKERGCG--IVYISHKMEEIfQLCDEITIL-RDG 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
338-554 |
2.31e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 338 VTFGYEnKEPI--LNDISLKIHAGETVAFVGPSGAGKT----TLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIG- 410
Cdd:PRK11022 11 VHFGDE-SAPFraVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 411 ---IVQQD-------VFLFSGTIRENIAY---GNLKAseaeiwqavKRAQLEDLI--YSQPDG---LDTVIGErgvkLSG 472
Cdd:PRK11022 90 evaMIFQDpmtslnpCYTVGFQIMEAIKVhqgGNKKT---------RRQRAIDLLnqVGIPDPasrLDVYPHQ----LSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 473 GQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELSVGRTT--LVIAHRLATI-KNADRIVVVNKDGIAEQG 549
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
....*
gi 446867357 550 SHEEL 554
Cdd:PRK11022 237 KAHDI 241
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
22-229 |
2.43e-07 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 52.41 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 22 CAVVAGLLELGFPLIVNQFIDKL-LPGQNWTLILWACFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKL 100
Cdd:cd18584 4 LGLLAALLIIAQAWLLARIIAGVfLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 101 SFRFFDNNKTGHLISRLTNDLmeigeiahhgpEDL------FIAVMTLVGAFSFMMMI-----NWK---LALLTFFVIPF 166
Cdd:cd18584 84 GPALLRRQSSGELATLLTEGV-----------DALdgyfarYLPQLVLAAIVPLLILVavfplDWVsalILLVTAPLIPL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 167 LLWLALYFNKKMT----GTFRRL---FSDVadfnaciennVGGIRVVQAFGNERFEKDQFAVNNARFRTT 229
Cdd:cd18584 153 FMILIGKAAQAASrrqwAALSRLsghFLDR----------LRGLPTLKLFGRARAQAARIARASEDYRRR 212
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
20-286 |
2.66e-07 |
|
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: 52.61 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 20 FSCAVVAGLLELGFPLIVNQFIDKLLPGQN------WTLILWACFGLLAVYILNAGLQYVVTYwghmLGVNIETDMRQKL 93
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNALTLAKVkdlesaVTLILLYALLRFSSKLLKELRSLLYRR----VQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 94 FDHIQKLSFRFFDNNKTGHLISRL------TNDLMEIGeiahhgpedLFIAVMTLVGAFS----FMMMINWKLALLTFFV 163
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMdrgtesANTLLSYL---------VFYLVPTLLELIVvsvvFAFHFGAWLALIVFLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 164 ipfllwLALYFNKKMTGT-----FRRLFSDvadfnacIENNVGGIRV--------VQAFGNERFEKDQFavnnarfrTTK 230
Cdd:cd18560 149 ------VLLYGVFTIKVTewrtkFRRAANK-------KDNEAHDIAVdsllnfetVKYFTNEKYEVDRY--------GEA 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 231 LMAYKIMALNSSISYML--------MRLVTLFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRP 286
Cdd:cd18560 208 VKEYQKSSVKVQASLSLlnvgqqliIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQP 271
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
470-558 |
4.42e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 LSGGQKQRLAIAR-MFLKNPPIL-ILDEATSALDTETELAIQKSLAEL-SVGRTTLVIAHRLATIKNADRIVVVNKdGIA 546
Cdd:cd03238 88 LSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWIIDFGP-GSG 166
|
90
....*....|..
gi 446867357 547 EQGSHeeLIEQG 558
Cdd:cd03238 167 KSGGK--VVFSG 176
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
470-555 |
4.99e-07 |
|
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: 52.71 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 LSGGQKQRLAIARMFLK---NPPILILDEATSAL---DTETELAIQKSLAELsvGRTTLVIAHRLATIKNADRIVVVNKD 543
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK--GNTVVVIEHNLDVIKTADYIIDLGPE 907
|
90
....*....|....*...
gi 446867357 544 G------IAEQGSHEELI 555
Cdd:TIGR00630 908 GgdgggtVVASGTPEEVA 925
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
349-532 |
8.83e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIGIVQQDVF--LFSGTIREN 426
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFkmLCMGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 427 IaygnlKASEAEIwqaVKRAQLEDLIYsQPDGldtvigergvKLSGGQKQRLAIARMFLKNPPILILDEATSALDtetEL 506
Cdd:PRK13546 120 I-----KAMTPKI---IEFSELGEFIY-QPVK----------KYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177
|
170 180 190
....*....|....*....|....*....|
gi 446867357 507 AIQKSLAEL----SVGRTTLVIAHRLATIK 532
Cdd:PRK13546 178 FAQKCLDKIyefkEQNKTIFFVSHNLGQVR 207
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
28-287 |
1.09e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 50.62 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 28 LLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYVVtywGHMLGV---NIETDMRQKLFDHIQKLSFRF 104
Cdd:cd18779 16 LLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLR---SHLLLRlrtRLDTQLTLGFLEHLLRLPYRF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 105 FDNNKTGHLISRLTNDLMeIGEIahhgpedLFIAVMTLV-------GAFSFMMMINWKLALLTFFVIPFLLWLALYFNKK 177
Cdd:cd18779 93 FQQRSTGDLLMRLSSNAT-IREL-------LTSQTLSALldgtlvlGYLALLFAQSPLLGLVVLGLAALQVALLLATRRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 178 MTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNE-----RFEKDQFAVNNARFRTTKLmaykiMALNSSISYMLMRLVT 252
Cdd:cd18779 165 VRELMARELAAQAEAQSYLVEALSGIETLKASGAEdraldRWSNLFVDQLNASLRRGRL-----DALVDALLATLRLAAP 239
|
250 260 270
....*....|....*....|....*....|....*
gi 446867357 253 LFVLICGTWFVLQGELTYGGFIGFVLLTNIFFRPI 287
Cdd:cd18779 240 LVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPL 274
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
349-501 |
1.22e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLLP--RFYEQssGSIQIDGidtKDMTLSSLRKQIG--IvqqdVFLFSG--- 421
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQQ--GRVEVLG---GDMADARHRRAVCprI----AYMPQGlgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 422 ------TIRENIAY-GNL---KASEaeiwqavKRAQLEDLIYSQpdGLDTvIGER--GvKLSGGQKQRLAIARMFLKNPP 489
Cdd:NF033858 88 nlyptlSVFENLDFfGRLfgqDAAE-------RRRRIDELLRAT--GLAP-FADRpaG-KLSGGMKQKLGLCCALIHDPD 156
|
170
....*....|..
gi 446867357 490 ILILDEATSALD 501
Cdd:NF033858 157 LLILDEPTTGVD 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
345-556 |
1.59e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 345 KEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGidtKDMTLSSLRKQIgivQQDVFLFSGTIR 424
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAI---NHGFALVTEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 425 ENIAYGNLKASEAEIWQAVKRaqledliYSQPDGL--------DT--VIGERGVK----------LSGGQKQRLAIARMF 484
Cdd:PRK10982 334 STGIYAYLDIGFNSLISNIRN-------YKNKVGLldnsrmksDTqwVIDSMRVKtpghrtqigsLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446867357 485 LKNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATIKN-ADRIVVVNKD---GIAE--QGSHEELIE 556
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGlvaGIVDtkTTTQNEILR 485
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
347-528 |
2.09e-06 |
|
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: 51.17 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 347 PILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQSSGSIQIDGiDTKDMTLSSLRKQIGIVQQ-DVF--LFSGti 423
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-KSILTNISDVHQNMGYCPQfDAIddLLTG-- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 424 RENI-AYGNLKASEAEIWQAVKRAQLEDLiysqpdGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDT 502
Cdd:TIGR01257 2030 REHLyLYARLRGVPAEEIEKVANWSIQSL------GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180
....*....|....*....|....*..
gi 446867357 503 ETELAIQKSLAE-LSVGRTTLVIAHRL 528
Cdd:TIGR01257 2104 QARRMLWNTIVSiIREGRAVVLTSHSM 2130
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
468-538 |
2.36e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 2.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 468 VKLSGGQKQRLAIARMF----LKNPPILILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLATIKNADRIV 538
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITHLPELAELADKLI 151
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
458-538 |
2.87e-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: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 458 GLDTV-IGERGVKLSGGQKQRLAIARMFLK---NPPILILDEATSAL---DTETELAIQKSLAELsvGRTTLVIAHRLAT 530
Cdd:cd03271 157 GLGYIkLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK--GNTVVVIEHNLDV 234
|
....*...
gi 446867357 531 IKNADRIV 538
Cdd:cd03271 235 IKCADWII 242
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
352-555 |
3.14e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 352 ISLKIHAGETVAFVGPSGAGKT----TLCSLLPRFYEQSSGSIQIDGIDTKDMTLSSLRKQIG-----IVQQDVFLFSGT 422
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsmIFQEPQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 423 irENIAYGNLKA-----SEAEIWQAV---KRAQLEDL----IYSQPDgldtVIGERGVKLSGGQKQRLAIARMFLKNPPI 490
Cdd:PRK15093 106 --ERVGRQLMQNipgwtYKGRWWQRFgwrKRRAIELLhrvgIKDHKD----AMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446867357 491 LILDEATSALDTETELAIQKSLAELSV--GRTTLVIAHRLATI-KNADRIVVVNKDGIAEQGSHEELI 555
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
23-280 |
3.45e-06 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 48.97 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 23 AVVAGLLELGFPLIVNQFIDKLLPGQNwTLILWA-CFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQ--K 99
Cdd:cd18587 11 ALLINLFALASPLFVMNVYDRVVPNNA-IETLWVlAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSRLFERVLglR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 100 LSFRffdNNKTGHLISRLtNDLMEIGEiahhgpedlFIAVMTLVGA----FSF-----MMMINWKLALLTFFVIPFLLWL 170
Cdd:cd18587 90 LEAR---PASVGSFANNL-REFESVRD---------FFTSATLTALidlpFVLlflavIALIGGPLALVPLVAIPLVLLY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 171 ALYFNKKMTGTFRRLFSDVADFNACIENNVGGIRVVQAFGNE-----RFEK--DQFAVNNARFRttklmayKIMALNSSI 243
Cdd:cd18587 157 GLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEgrmqrRWEEavAALARSSLKSR-------LLSSSATNF 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 446867357 244 SYMLMRLVTLFVLICGTWFVLQGELTYGGFIGFVLLT 280
Cdd:cd18587 230 AQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILS 266
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
18-269 |
6.64e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 48.26 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 18 LDFSCAVVAGLLELGFPLIVNQFIDKL-LPGQNWTLILWA-CFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFD 95
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVwVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 96 HIqkLSFRFF-----------------DNNKTGHLISRLTN----DLMEIGEIAHHGPeDLFIAVMTLVGAFSFMMMINW 154
Cdd:cd18596 81 KA--LRRRDKsgssksseskkkdkeedEDEKSSASVGKINNlmsvDANRISEFAAFLH-LLVSAPLQIVIAIVFLYRLLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 155 KLALLTFFVIPFLLWLALYFNKKMTGTFRRL--FSD--VADFNACIennvGGIRVVQAFGNERFEKDQfaVNNAR----- 225
Cdd:cd18596 158 WSALVGLAVMVLLLPLNGYLAKRYSRAQKELmkARDarVQLVTEVL----QGIRMIKFFAWERKWEER--ILEAReeelk 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446867357 226 -FRTTKLMAYKIMALNSSISYMLMrLVTLFVLIcgtwFVLQGELT 269
Cdd:cd18596 232 wLRKRFLLDLLLSLLWFLIPILVT-VVTFATYT----LVMGQELT 271
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
349-538 |
1.01e-05 |
|
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: 46.87 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 349 LNDISLKIHAGETVAFVGPSGAGKTTLCSLL-----PRFYEQSSGSI---QIDGIDTKDMT-LSSLRKQIGIVQQdvfLF 419
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTiyaegQRRYVESLSAYarqFLGQMDKPDVDsIEGLSPAIAIDQK---TT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 420 S-------GTIRENIAYGNLKASEAEIwqavkRAQLEDLIYSqpdGLDTVIGERGVK-LSGGQKQRLAIARMFLKNPP-- 489
Cdd:cd03270 88 SrnprstvGTVTEIYDYLRLLFARVGI-----RERLGFLVDV---GLGYLTLSRSAPtLSGGEAQRIRLATQIGSGLTgv 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446867357 490 ILILDEATSAL---DTETELAIQKSLAELsvGRTTLVIAHRLATIKNADRIV 538
Cdd:cd03270 160 LYVLDEPSIGLhprDNDRLIETLKRLRDL--GNTVLVVEHDEDTIRAADHVI 209
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-529 |
1.07e-05 |
|
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: 47.36 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 359 GETVAFVGPSGAGKTTLCSLLprfyeqsSGSIQ-----IDGIDTKDMTLSSLRkqiGIVQQDVFlfsgtirENIAYGNLK 433
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKIL-------AGKLKpnlgkFDDPPDWDEILDEFR---GSELQNYF-------TKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 434 AseaeiwqaVKRAQLEDLIYSQPDG--------------LDTVIG--------ERGV-KLSGGQKQRLAIARMFLKNPPI 490
Cdd:cd03236 89 V--------IVKPQYVDLIPKAVKGkvgellkkkdergkLDELVDqlelrhvlDRNIdQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446867357 491 LILDEATSALDTETELAIQKSLAELSV-GRTTLVIAHRLA 529
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
92-274 |
1.71e-05 |
|
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: 46.72 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 92 KLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEIGEIAHH-----GPEDLFIAVMTLVGAFSFmmmiNWKLALLTFFVIPF 166
Cdd:cd18582 76 RVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFllfniLPTILELLLVCGILWYLY----GWSYALITLVTVAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 167 LLWLALYFNKKMTgTFRRLFSDVadfnaciENNVGGIRV--------VQAFGNERFEKDQFAVNNARFRTTKLMAYKIMA 238
Cdd:cd18582 152 YVAFTIKVTEWRT-KFRREMNEA-------DNEANAKAVdsllnyetVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 446867357 239 LNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFI 274
Cdd:cd18582 224 LLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFV 259
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
470-555 |
3.74e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 LSGGQKQRLAIARMFL---KNPPILILDEATSALDTETELAIQKSLAELS-VGRTTLVIAHRLATIKNADRIVVVNKDGI 545
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLELGPEGG 889
|
90
....*....|....*.
gi 446867357 546 AEQG------SHEELI 555
Cdd:PRK00635 890 NLGGyllascSPEELI 905
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
87-269 |
9.53e-05 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 44.39 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 87 TDMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDlmeIGEIAHhgpedLF--------IAVMTLVGAFSFMMMINWKLAL 158
Cdd:cd18585 68 SNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVAD---IDTLDN-----LYlrvlsppvVALLVILATILFLAFFSPALAL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 159 LTF-------FVIPFLLWLAlyfnKKMTGtfRRLFSDVADFNACIENNVGGIRVVQAFG-NERFEKDQFAVNNARFRTTK 230
Cdd:cd18585 140 ILLaglllagVVIPLLFYRL----GKKIG--QQLVQLRAELRTELVDGLQGMAELLIFGaLERQRQQLEQLSDALIKEQR 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 446867357 231 LMAyKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELT 269
Cdd:cd18585 214 RLA-RLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
437-551 |
2.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 437 AEIWQAVKRAQ--LEDLIYSqpdGLDTV-IGERGVKLSGGQKQRLAIAR-MFL--KNPPILILDEATSALDTETELAIQK 510
Cdd:PRK00635 1667 AETFPFLKKIQkpLQALIDN---GLGYLpLGQNLSSLSLSEKIAIKIAKfLYLppKHPTLFLLDEIATSLDNQQKSALLV 1743
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446867357 511 SLAEL-SVGRTTLVIAHRLATIKNADRIVVVNKdGIAEQGSH 551
Cdd:PRK00635 1744 QLRTLvSLGHSVIYIDHDPALLKQADYLIEMGP-GSGKTGGK 1784
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
454-544 |
3.97e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 454 SQPDGLDTvigergvkLSGGQKQ------RLAIARMFLKNPPILILDEATSALDTE--TELA--IQKSLAELSVGRTTLV 523
Cdd:PRK01156 794 GMVEGIDS--------LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDrrTNLKdiIEYSLKDSSDIPQVIM 865
|
90 100
....*....|....*....|.
gi 446867357 524 IAHRLATIKNADRIVVVNKDG 544
Cdd:PRK01156 866 ISHHRELLSVADVAYEVKKSS 886
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
338-556 |
4.00e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 338 VTFGYENKEPILNDISLKIHAGETVAFVGPSGAGKTTLCSLLPRFYEQS---SGSIQIDGIDTKDMTlsSLRKQIGIVQQ 414
Cdd:PLN03140 170 INLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFV--PRKTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 415 DVFLFSGTIRENIAYGNL---KASEAEIWQAVKRAQLEDLIYSQPD--------------------------GLD----T 461
Cdd:PLN03140 248 DVHVGVMTVKETLDFSARcqgVGTRYDLLSELARREKDAGIFPEAEvdlfmkatamegvksslitdytlkilGLDickdT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 462 VIGE---RGVklSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAELsVGRTTLVIAHRL-----ATIKN 533
Cdd:PLN03140 328 IVGDemiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI-VHLTEATVLMSLlqpapETFDL 404
|
250 260
....*....|....*....|...
gi 446867357 534 ADRIVVVNKDGIAEQGSHEELIE 556
Cdd:PLN03140 405 FDDIILLSEGQIVYQGPRDHILE 427
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
445-560 |
4.54e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 445 RAQLEDLIysQPDGLDTVIGERGVKLSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLAEL-SVGRTTLV 523
Cdd:NF000106 122 RARADELL--ERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLL 199
|
90 100 110
....*....|....*....|....*....|....*...
gi 446867357 524 IAHRLATIKN-ADRIVVVNKDGIAEQGSHEELIEQGGG 560
Cdd:NF000106 200 TTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGG 237
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
470-540 |
6.08e-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: 41.30 E-value: 6.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446867357 470 LSGGQKQRLAIA---RMFLKNP-PILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIVVV 540
Cdd:cd03278 114 LSGGEKALTALAllfAIFRVRPsPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYGV 188
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
13-274 |
1.41e-03 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 40.89 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 13 KGLFILDFSCAVVAGLLELGFPLIVNQFIDKLLPGQNWTLILWACFGLLAVYILNAGLQYV----VTYWGHMLGVNIETD 88
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIrswiLLHISSRINISIISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 89 MRQKLFdhiqKLSFRFFDNNKTGHLISR----------LTNDLMEIgeiahhgpedlFIAVMTLVgAFSFMMMI-NWKLa 157
Cdd:cd18571 81 FLIKLM----RLPISFFDTKMTGDILQRindhsriesfLTSSSLSI-----------LFSLLNLI-VFSIVLAYyNLTI- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 158 LLTFFV--IPFLLWLALYFNKKMTGTFRRlFSDVADFNACIENNVGGIRVVQAFGNERFEKDQFAVNNARFRTTKLMAYK 235
Cdd:cd18571 144 FLIFLIgsVLYILWILLFLKKRKKLDYKR-FDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLK 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 446867357 236 IMALNSSISYMLMRLVTLFVLICGTWFVLQGELTYGGFI 274
Cdd:cd18571 223 LDQYQQIGALFINQLKNILITFLAAKLVIDGEITLGMML 261
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
470-538 |
2.21e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446867357 470 LSGGQKQRLAIARMF---LKNP-PILILDEATSALDTETELAIQKSLAELSVGRTTLVIAHRLATIKNADRIV 538
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqKYKPaPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
362-517 |
2.54e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 362 VAFVGPSGAGKTTLCSLLpRF--YEQSSGSIQIDG---------------IDTKDMTLSSLRKQiGivQQDVFLFS---- 420
Cdd:COG0419 26 NLIVGPNGAGKSTILEAI-RYalYGKARSRSKLRSdlinvgseeasveleFEHGGKRYRIERRQ-G--EFAEFLEAkpse 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 421 ---------GTIRENIAYGNLKASEAEIWQAVKRA----QLEDLIYSQPDGLDTVigergVKLSGGQKQRLAIARMFLkn 487
Cdd:COG0419 102 rkealkrllGLEIYEELKERLKELEEALESALEELaelqKLKQEILAQLSGLDPI-----ETLSGGERLRLALADLLS-- 174
|
170 180 190
....*....|....*....|....*....|
gi 446867357 488 ppiLILDeaTSALDTETELAIQKSLAELSV 517
Cdd:COG0419 175 ---LILD--FGSLDEERLERLLDALEELAI 199
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
34-257 |
4.60e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 39.15 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 34 PLIVNQFIDKLLPGQNWTL---ILWAcFGLLAVYILNAGLQYVVTYWGHMLGVNIETDMRQKLFDHIQKLSFRFFDNNKT 110
Cdd:cd18594 17 PLLLGRLVAYFVPDSTVTKteaYLYA-LGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 111 GHLISRLTNDLMEIGEI---AHHgpedLFIAVMTLVGafsfMMMINWKL----ALLTFFVIPFLLWLALYFNKKMtGTFR 183
Cdd:cd18594 96 GHIVNLLSNDVQKFDEVlvyLHF----LWIAPLQVIV----LTGLLWREigpsSLAGLGVLLLLLPLQAYLGKLF-AKYR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446867357 184 RLFSDVADFNACIENNV-GGIRVVQAFGNER-FEKDQFAVNNARFRTTKLMAYkIMALNSSISYMLMRLVTLFVLI 257
Cdd:cd18594 167 RKTAGLTDERVKIMNEIiSGMRVIKMYTWEEsFAKLIENIRKKELKLIRKAAY-IRAFNMAFFFFSPTLVSFATFV 241
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
59-278 |
4.61e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 39.37 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 59 GLLAVYILNAGLQYVVTYWGHMLGVNIetdMRQKLFDHIQKLSFRFFDNNKTGHLISRLTNDLMEI-GEIAHHGpEDLFI 137
Cdd:cd18604 51 LISLLSVLLGTLRYLLFFFGSLRASRK---LHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIdSELADSL-SSLLE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 138 AVMTLVGAFSFMMMINWKLALLTFFVIPFLLWLALYFN------KKMTGTFRR-LFSdvaDFNACIEnnvgGIRVVQAFG 210
Cdd:cd18604 127 STLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLrasrelKRLESVARSpILS---HFGETLA----GLVTIRAFG 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446867357 211 NERFEKDQFAV---NNARfrttklMAYKIMALNSSISYMLMRLVTLFVLICGTWFVLQGELTyGGFIGFVL 278
Cdd:cd18604 200 AEERFIEEMLRridRYSR------AFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPGID-AGLAGFSL 263
|
|
| MobB |
cd03116 |
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ... |
362-385 |
6.48e-03 |
|
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.
Pssm-ID: 349770 [Multi-domain] Cd Length: 157 Bit Score: 37.62 E-value: 6.48e-03
10 20
....*....|....*....|....*
gi 446867357 362 VAFVGPSGAGKTTLCS-LLPRFYEQ 385
Cdd:cd03116 3 VGVVGKSGSGKTTLIEkLIPELKAR 27
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
358-375 |
6.65e-03 |
|
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: 38.15 E-value: 6.65e-03
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
470-545 |
7.09e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 470 LSGGQKQRLAIA---RMFLKNP-PILILDEATSALD---TETELAIQKSLAElsvgRTT-LVIAHRLATIKNADRI--VV 539
Cdd:TIGR02168 1090 LSGGEKALTALAllfAIFKVKPaPFCILDEVDAPLDdanVERFANLLKEFSK----NTQfIVITHNKGTMEVADQLygVT 1165
|
....*.
gi 446867357 540 VNKDGI 545
Cdd:TIGR02168 1166 MQEKGV 1171
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
359-375 |
7.30e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 7.30e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
332-526 |
8.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 332 DIQYSNVTFGYENKEpILNDISLKIHAGETVAFVGPSGAGKTTL---------------CSLLprFYEQssgsiQIDGID 396
Cdd:PLN03073 177 DIHMENFSISVGGRD-LIVDASVTLAFGRHYGLVGRNGTGKTTFlrymamhaidgipknCQIL--HVEQ-----EVVGDD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446867357 397 TKDM--TLSSLRKQIGIVQQDVFLFS--GTIRENIAYGNLK-ASEAEIWQAVKRAQLEDlIYSQPDGLDTVIGE------ 465
Cdd:PLN03073 249 TTALqcVLNTDIERTQLLEEEAQLVAqqRELEFETETGKGKgANKDGVDKDAVSQRLEE-IYKRLELIDAYTAEaraasi 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446867357 466 ------------RGVK-LSGGQKQRLAIARMFLKNPPILILDEATSALDTETELAIQKSLaeLSVGRTTLVIAH 526
Cdd:PLN03073 328 laglsftpemqvKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
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