|
Name |
Accession |
Description |
Interval |
E-value |
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-557 |
0e+00 |
|
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: 693.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 1 MWDVRKHLRRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALS 80
Cdd:COG4618 11 LRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 81 LDKHFGEDAFIASISSP--KAAMGDIQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMIL 158
Cdd:COG4618 91 LDRRLGPRVFDAAFRAAlrGGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGLLALVGALVLVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 159 MVVASHYATRSAAGKAQEAAVAANLLAQAFTRNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRM 238
Cdd:COG4618 171 LALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 239 VLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVIASGKGhRADRLILPEPEG 318
Cdd:COG4618 251 LLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPA-EPERMPLPRPKG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLFWAPTHARadtsAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLG 398
Cdd:COG4618 330 RLSVENLTVVPPGSK----RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 399 GYIGYLAQDVQLLPGSIAENIARFdAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFG 478
Cdd:COG4618 406 RHIGYLPQDVELFDGTIAENIARF-GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 479 NPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSGAKPR 557
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-551 |
0e+00 |
|
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: 571.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 8 LRRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGE 87
Cdd:TIGR01842 4 VKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 88 DAFIASISSPKAAM--GDIQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVASHY 165
Cdd:TIGR01842 84 PIFAASFSATLRRGsgDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 166 ATRSAAGKAQEAAVAANLLAQAFTRNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVLQLAIL 245
Cdd:TIGR01842 164 ATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 246 GTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVIASGKGhRADRLILPEPEGRLTVKNL 325
Cdd:TIGR01842 244 GLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPS-RDPAMPLPEPEGHLSVENV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 326 FWAPTHARADTsaaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLA 405
Cdd:TIGR01842 323 TIVPPGGKKPT----LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 406 QDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLIL 485
Cdd:TIGR01842 399 QDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 486 DEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRL 551
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-550 |
3.72e-135 |
|
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: 410.38 E-value: 3.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 6 KHLRRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHF 85
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 86 GeDAFIASISS------PKAAMGDI-QPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMIL 158
Cdd:COG2274 232 S-SRFFRHLLRlplsffESRSVGDLaSRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 159 MVVASHYATRSAAGK-AQEAAVAANLLAQAFtRNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLR 237
Cdd:COG2274 311 LGLLFQPRLRRLSREeSEASAKRQSLLVETL-RGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 238 MVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVIA--SGKGHRADRLILPE 315
Cdd:COG2274 390 QLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDlpPEREEGRSKLSLPR 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 316 PEGRLTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRK 395
Cdd:COG2274 470 LKGDIELENV----SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARA 475
Cdd:COG2274 546 SLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARA 625
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
9-296 |
3.66e-103 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, 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 PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 313.39 E-value: 3.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AFIASISSPKAAMG---DIQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVASHY 165
Cdd:cd18586 81 VFRAVLELPLESRPsgyWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 166 ATRSAAGKAQEAAVAANLLAQAFTRNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVLQLAIL 245
Cdd:cd18586 161 ATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLIL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 246 GTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18586 241 GVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-550 |
4.15e-97 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 307.48 E-value: 4.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 4 VRKHLRRAWVeVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVA----- 78
Cdd:COG1132 16 LRPYRGLLIL-ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAqrvva 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 79 ----------LSLDKHFGEDAFIASISSpkAAMGDIQPLRDLATTrsfvaskGLANLIDLPFAPIFA-VILYCIHPVLCL 147
Cdd:COG1132 95 dlrrdlfehlLRLPLSFFDRRRTGDLLS--RLTNDVDAVEQFLAH-------GLPQLVRSVVTLIGAlVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 148 VTVAGAAVMILMVVASHYATRSAAGKAQEAAVAANLLAQAFTRNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINA 227
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 228 IFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVIA--SGKG 305
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDepPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 306 HRADRLILPEPEGRLTVKNLfwaptHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALD 385
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFENV-----SFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 386 GADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGG 465
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 466 TRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAkAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPAS 545
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
....*
gi 517342213 546 EILQR 550
Cdd:COG1132 560 ELLAR 564
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-538 |
1.64e-70 |
|
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: 224.40 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWAPtharADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG 399
Cdd:cd03246 1 LEVENVSFRY----PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQDVQLLPGSIAENIarfdagvsdaniteaasraqahalitglkqgyqttmeaaggsLSGGTRQRIGLARAFFGN 479
Cdd:cd03246 77 HVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 480 PKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
133-550 |
2.26e-64 |
|
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: 220.79 E-value: 2.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 133 IFAVILYCIHPVLCLVTVAGAAVmiLMVVASHYATRSAAGKAQEAAVAANLLAQAFTrnrETVQGMG--MIGHVTERWGR 210
Cdd:COG4987 145 AAVAFLAFFSPALALVLALGLLL--AGLLLPLLAARLGRRAGRRLAAARAALRARLT---DLLQGAAelAAYGALDRALA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 211 RFADAANLQDGASAINAIFAGSSRTLRMVLQ----LAILGTGAVLVLQGQMTAGMI--FASSTISgrALQPIDQLVAGWR 284
Cdd:COG4987 220 RLDAAEARLAAAQRRLARLSALAQALLQLAAglavVAVLWLAAPLVAAGALSGPLLalLVLAALA--LFEALAPLPAAAQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 285 QIVDARKAWKRLGSVIASGKGHRADRLILPEPEG-RLTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSG 363
Cdd:COG4987 298 HLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGpSLELEDV----SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 364 KSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHAL 443
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDW 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 444 ITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAkAGGTTVIIVTHRPAI 523
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAG 532
|
410 420
....*....|....*....|....*..
gi 517342213 524 VLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG4987 533 LERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
234-550 |
1.03e-60 |
|
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: 210.77 E-value: 1.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 234 RTLRM------VLQL-AILGTGAVLV------LQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVI 300
Cdd:COG4988 236 KVLRVaflssaVLEFfASLSIALVAVyigfrlLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 301 AS--GKGHRADRLILPEPEGRLTVKNLfwaptHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPT 378
Cdd:COG4988 316 DApePAAPAGTAPLPAAGPPSIELEDV-----SFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 379 GGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAA 458
Cdd:COG4988 391 SGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEG 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 459 GGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAkAGGTTVIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRI 549
|
330
....*....|..
gi 517342213 539 DAFGPASEILQR 550
Cdd:COG4988 550 VEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-536 |
7.15e-57 |
|
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: 188.75 E-value: 7.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGS 414
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIarfdagvsdaniteaasraqahalitglkqgyqttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03228 92 IRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 495 EGEAALERALLQAkAGGTTVIIVTHRPAIVLKCDKALVLRNG 536
Cdd:cd03228 130 ETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-550 |
9.23e-57 |
|
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: 190.51 E-value: 9.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03254 98 RLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 500 LERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03254 178 IQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
318-542 |
2.97e-55 |
|
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: 186.26 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 318 GRLTVKNL-FWAPTHARADtsaaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQ 396
Cdd:cd03245 1 GRIEFRNVsFSYPNQEIPA-----LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 LGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAF 476
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 477 FGNPKLLILDEPNSNLDAEGEAALERAlLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFG 542
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
340-550 |
1.73e-52 |
|
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: 179.66 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03249 98 RYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 500 LERALLQAkAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03249 178 VQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
317-538 |
7.66e-52 |
|
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: 177.28 E-value: 7.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 317 EGRLTVKNL-FWAPThaRADTSaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRK 395
Cdd:cd03248 9 KGIVKFQNVtFAYPT--RPDTL--VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARA 475
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
143-550 |
1.76e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 188.39 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 143 PVLCLVTVAgaAVMILMVVASHYATR--SAAGKAQEAAVAANLLAQAFTRNRETVQGMGMIGHVTERWGRRFADAANLQD 220
Cdd:TIGR00958 301 PRLTMVTLI--NLPLVFLAEKVFGKRyqLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 221 GASAINAIFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAG-----MIFASSTisGRALQpidQLVAGWRQIVDARKAWKR 295
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGnlvsfLLYQEQL--GEAVR---VLSYVYSGMMQAVGASEK 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 296 LGSVIASGKGHRADRLILPEP-EGRLTVKNL-FWAPTHAradtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAG 373
Cdd:TIGR00958 454 VFEYLDRKPNIPLTGTLAPLNlEGLIEFQDVsFSYPNRP----DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 374 VAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQT 453
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 454 TMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERAllqAKAGGTTVIIVTHRPAIVLKCDKALVL 533
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVL 686
|
410
....*....|....*..
gi 517342213 534 RNGAVDAFGPASEILQR 550
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMED 703
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-550 |
2.80e-51 |
|
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: 176.14 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 333 RADtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLP 412
Cdd:cd03252 11 KPD-GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 GSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:cd03252 90 RSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 493 DAEGEAALERAlLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03252 170 DYESEHAIMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-550 |
1.38e-50 |
|
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: 174.34 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGS 414
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03253 91 IGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 495 EGEAALERALLQAkAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03253 171 HTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-550 |
2.15e-50 |
|
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: 173.96 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGS 414
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 495 EGEAALERALLQAKAGGTTvIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03251 172 ESERLVQAALERLMKNRTT-FVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
274-533 |
2.45e-50 |
|
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: 182.10 E-value: 2.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 274 QPIDQLVAGWRQIVDARKAWKRLGSVIASGKGHRADRLILPE-PEGRLTVKNLfwapTHARADTSAAIiKDVSFDLKPGH 352
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAaPASSLEFSGV----SVAYPGRRPAL-RPVSFTVPPGE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 353 VLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANIT 432
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIR 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 433 EAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAkAGGT 512
Cdd:TIGR02857 430 EALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGR 508
|
250 260
....*....|....*....|.
gi 517342213 513 TVIIVTHRPAIVLKCDKALVL 533
Cdd:TIGR02857 509 TVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
144-550 |
4.76e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 176.69 E-value: 4.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 144 VLCLV-TVAGAAVM-----ILMVVASHYATRSAAGKAQEAAVAanlLAQAFTRNRETVQGMgmighvterwgRRFADaaN 217
Cdd:PRK13657 164 VLGIVyTLITTLVMrktkdGQAAVEEHYHDLFAHVSDAIGNVS---VVQSYNRIEAETQAL-----------RDIAD--N 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 218 LQDG----------ASAINAIfagsSRTLRMvlqLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIV 287
Cdd:PRK13657 228 LLAAqmpvlswwalASVLNRA----ASTITM---LAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVF 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 288 DARKAWKRLGSVIASgKGHRADRLILPEPE---GRLTVKNLFWapthaRADTSAAIIKDVSFDLKPGHVLAILGPSGSGK 364
Cdd:PRK13657 301 MAAPKLEEFFEVEDA-VPDVRDPPGAIDLGrvkGAVEFDDVSF-----SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 365 SSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALI 444
Cdd:PRK13657 375 STLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFI 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 445 TGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIvTHRPAIV 524
Cdd:PRK13657 455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII-AHRLSTV 533
|
410 420
....*....|....*....|....*.
gi 517342213 525 LKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
14-296 |
1.95e-47 |
|
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: 167.76 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 14 EVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGEDAFIAS 93
Cdd:cd18566 6 QVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 94 ISSP-----KAAMGD-IQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVASHYAT 167
Cdd:cd18566 86 LSLPlsffeREPSGAhLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 168 RSAAGKAQEAAVAA-NLLAQAFTrNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVLQLAILG 246
Cdd:cd18566 166 RRALKERSRADERRqNFLIETLT-GIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 517342213 247 TGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18566 245 FGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-551 |
1.23e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwapTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGG 399
Cdd:COG1131 1 IEVRGL----TKRYGDKTA--LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQDVQLLPG-SIAENIaRFDAGVSDANITEAASRAQAHALITGLKqgyqttmEAAG---GSLSGGTRQRIGLARA 475
Cdd:COG1131 74 RIGYVPQEPALYPDlTVRENL-RFFARLYGLPRKEARERIDELLELFGLT-------DAADrkvGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQRL 551
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
340-538 |
6.95e-44 |
|
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: 165.38 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:COG5265 453 AYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 517342213 500 LERALLQAKAGGTTVIIvTHRPAIVLKCDKALVLRNGAV 538
Cdd:COG5265 533 IQAALREVARGRTTLVI-AHRLSTIVDADEILVLEAGRI 570
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-538 |
9.25e-44 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 155.34 E-value: 9.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG 399
Cdd:cd03255 1 IELKNLSK--TYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 Y----IGYLAQDVQLLPG-SIAENIA---RFdAGVSDANIteaasRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIG 471
Cdd:cd03255 79 FrrrhIGFVFQSFNLLPDlTALENVElplLL-AGVPKKER-----RERAEELLERV--GLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 472 LARAFFGNPKLLILDEPNSNLDAE-GEAALEraLLQ--AKAGGTTVIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSEtGKEVME--LLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
133-550 |
2.05e-43 |
|
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: 163.35 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 133 IFAVILYcIHPVLCLVTVAGAAVMILMVVASHYATRSAAGKAQeaavaaNLLAQAFTRNRETVQGMGMI----GHVTERw 208
Cdd:TIGR02203 145 LFIVLLY-YSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQ------NSMGQVTTVAEETLQGYRVVklfgGQAYET- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 209 gRRFADAAN-LQDGASAINAIFAGSSRTLRMVLQLA---ILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQL--VAG 282
Cdd:TIGR02203 217 -RRFDAVSNrNRRLAMKMTSAGSISSPITQLIASLAlavVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLtnVNA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 283 WRQ--IVDARKAWKRLGSVIASGKGHRAdrliLPEPEGRLTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPS 360
Cdd:TIGR02203 296 PMQrgLAAAESLFTLLDSPPEKDTGTRA----IERARGDVEFRNV----TFRYPGRDRPALDSISLVIEPGETVALVGRS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 361 GSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFD-AGVSDANITEAASRAQ 439
Cdd:TIGR02203 368 GSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAY 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 440 AHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIvTH 519
Cdd:TIGR02203 448 AQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AH 526
|
410 420 430
....*....|....*....|....*....|.
gi 517342213 520 RPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-536 |
4.25e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 4.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWAPTHARadtsaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWD----RK 395
Cdd:COG4619 1 LELEGLSFRVGGKP------ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QlggyIGYLAQDVQLLPGSIAENIaRFDAGVSDANITEAASRAQAHALitGLKQGYqttMEAAGGSLSGGTRQRIGLARA 475
Cdd:COG4619 75 Q----VAYVPQEPALWGGTVRDNL-PFPFQLRERKFDRERALELLERL--GLPPDI---LDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-550 |
6.46e-43 |
|
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: 163.76 E-value: 6.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 15 VIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRA----VYCQRVA----LSLDKHFG 86
Cdd:TIGR01193 161 IVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIfllnVLGQRLSidiiLSYIKHLF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 87 EdaFIASISSPKAAMGDIQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVAshyA 166
Cdd:TIGR01193 241 E--LPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIIL---F 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 167 TRSAAGKAQEAAVAANLLAQAFTRNRETVQGMGMIGHVTERWGR---RFADAAN----LQDGASAINAIFAGssrtLRMV 239
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidsEFGDYLNksfkYQKADQGQQAIKAV----TKLI 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 240 LQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVI----ASGKGHRADRLILPE 315
Cdd:TIGR01193 392 LNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYlvdsEFINKKKRTELNNLN 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 316 peGRLTVKNLFWAPTHARAdtsaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRK 395
Cdd:TIGR01193 472 --GDIVINDVSYSYGYGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGGYIGYLAQDVQLLPGSIAEN-IARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLAR 474
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENlLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALAR 624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAggTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
341-488 |
1.32e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 149.72 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPG-SIAENI 419
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 420 ARfdaGVSDANITEAASRAQAHALITGLKQGYQ--TTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
322-536 |
1.33e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 151.85 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 322 VKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYI 401
Cdd:cd03225 2 LKNL----SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 402 GYLAQ--DVQLLPGSIAENIArFDA---GVSDANITEAASRAQAHALITGLKqgyqttmEAAGGSLSGGTRQRIGLARAF 476
Cdd:cd03225 78 GLVFQnpDDQFFGPTVEEEVA-FGLenlGLPEEEIEERVEEALELVGLEGLR-------DRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 477 FGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-550 |
5.31e-42 |
|
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: 150.95 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwapTHARADTSAAIiKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG 399
Cdd:COG1122 1 IELENL----SFSYPGGTPAL-DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQ--DVQLLPGSIAENIArF---DAGVSDAnitEAASRAQAHALITGLkQGYqttMEAAGGSLSGGTRQRIGLAR 474
Cdd:COG1122 76 KVGLVFQnpDDQLFAPTVEEDVA-FgpeNLGLPRE---EIRERVEEALELVGL-EHL---ADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
117-521 |
1.62e-40 |
|
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: 154.44 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 117 VASKGLANLIDLPFAPIFAVILycihpvlcLVTVAGAAVMILMVVASHYATRsAAGKAQEAAVAANLLA-----QAFTRN 191
Cdd:TIGR02868 142 AAAVAAIAVLSVPAALILAAGL--------LLAGFVAPLVSLRAARAAEQAL-ARLRGELAAQLTDALDgaaelVASGAL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 192 RETVQGMGMIGHVTERWGRRFADAANLQDGASAInaiFAGSSrtlrmVLQLAILGTGAVLvlQGQMTAGMIFASSTISGR 271
Cdd:TIGR02868 213 PAALAQVEEADRELTRAERRAAAATALGAALTLL---AAGLA-----VLGALWAGGPAVA--DGRLAPVTLAVLVLLPLA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 272 ALQPIDQLVAGWRQIVDARKAWKRLGSVI------ASGKGHRADRLILPEPegRLTVKNLfwaptHARADTSAAIIKDVS 345
Cdd:TIGR02868 283 AFEAFAALPAAAQQLTRVRAAAERIVEVLdaagpvAEGSAPAAGAVGLGKP--TLELRDL-----SAGYPGAPPVLDGVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 346 FDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAG 425
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 426 VSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALL 505
Cdd:TIGR02868 436 ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
410
....*....|....*.
gi 517342213 506 QAKAgGTTVIIVTHRP 521
Cdd:TIGR02868 516 AALS-GRTVVLITHHL 530
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
340-546 |
2.75e-40 |
|
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: 146.42 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL----GGYIGYLAQDVQLLPGSI 415
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 A-ENIA----RfdAGVSDAniteaasRAQAHALIT--GLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:COG4181 107 AlENVMlpleL--AGRRDA-------RARARALLErvGLGH----RLDHYPAQLSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 489 NSNLD-AEGEAALEraLLQA--KAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASE 546
Cdd:COG4181 174 TGNLDaATGEQIID--LLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
330-538 |
9.21e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.80 E-value: 9.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 330 THARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL----GGYIGYLA 405
Cdd:COG1136 13 SYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 406 QDVQLLPG-SIAENIA---RFdagvsdANITEAASRAQAHALIT--GLKqgyqttmEAAG---GSLSGGTRQRIGLARAF 476
Cdd:COG1136 93 QFFNLLPElTALENVAlplLL------AGVSRKERRERARELLErvGLG-------DRLDhrpSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 477 FGNPKLLILDEPNSNLDAE-GEAALEraLLQ--AKAGGTTVIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKtGEEVLE--LLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
335-543 |
1.11e-39 |
|
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: 144.17 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGS 414
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAgVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03244 94 IRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517342213 495 EGEAALERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGP 543
Cdd:cd03244 173 ETDALIQKTIREAFK-DCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
340-536 |
1.56e-39 |
|
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: 142.15 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyPTWDRKQLGGYIGYLAQDVQLLPG-SIAEN 418
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-IKKEPEEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IarfdagvsdaniteaasraqahalitglkqgyqttmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEA 498
Cdd:cd03230 94 L-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 517342213 499 ALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:cd03230 133 EFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
342-550 |
1.30e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.29 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTW----DRKqlggyIGYLAQDVQLLPG-SIA 416
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlpprERR-----VGFVFQHYALFPHmTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArfdAGVSDANITEAASRAQAHALI-----TGLKQGY--QttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:COG1118 94 ENIA---FGLRVRPPSKAEIRARVEELLelvqlEGLADRYpsQ---------LSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 490 SNLDAEGEAALERAL--LQAKAGGTTvIIVTHRP--AIVLkCDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG1118 162 GALDAKVRKELRRWLrrLHDELGGTT-VFVTHDQeeALEL-ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-536 |
1.35e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 139.30 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQdvqllpgsiaeni 419
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 arfdagvsdaniteaasraqahalitglkqgyqttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 517342213 500 LERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:cd00267 119 LLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-548 |
1.36e-38 |
|
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: 142.49 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwaptHARADtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLG 398
Cdd:COG1120 1 MLEAENL-----SVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 399 GYIGYLAQDVQLLPG-SIAENIA-------RFDAGVSDANItEAASRAqahalitglkqgyqttMEAAG---------GS 461
Cdd:COG1120 75 RRIAYVPQEPPAPFGlTVRELVAlgryphlGLFGRPSAEDR-EAVEEA----------------LERTGlehladrpvDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 462 LSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVD 539
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNLAARyADRLVLLKDGRIV 217
|
....*....
gi 517342213 540 AFGPASEIL 548
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
320-576 |
1.96e-38 |
|
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: 148.51 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTG---GTIALDGADYPTWDRKQ 396
Cdd:COG1123 5 LEVRDL----SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 LGGYIGYLAQD--VQLLPGSIAENIArfdagvsDANITEAASRAQAHALITGL--KQGYQTTMEAAGGSLSGGTRQRIGL 472
Cdd:COG1123 81 RGRRIGMVFQDpmTQLNPVTVGDQIA-------EALENLGLSRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 473 ARAFFGNPKLLILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260
....*....|....*....|....*.
gi 517342213 551 LSGAKPRPVNANRVSVRNKSETADAP 576
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-538 |
4.00e-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: 140.33 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwAPTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL-- 397
Cdd:cd03257 2 LEVKNL--SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 398 -GGYIGYLAQDvqllPGS-------IAENIARFDAGVSDANITEAASRAQAHALIT-GLKQGYqttMEAAGGSLSGGTRQ 468
Cdd:cd03257 80 rRKEIQMVFQD----PMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEV---LNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 469 RIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
340-552 |
8.46e-38 |
|
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: 139.99 E-value: 8.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQlggyIGYLAQDVQLLPG-SI 415
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkEPREARRQ----IGVLPDERGLYDRlTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIARFDA--GVSDANITEAASR-AQAHALITGLKQGYQTtmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:COG4555 92 RENIRYFAElyGLFDEELKKRIEElIELLGLEEFLDRRVGE--------LSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 493 DAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQRLS 552
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
337-542 |
1.14e-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: 138.42 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKqlggyIGYLAQDVQLLPG 413
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgvPPERRN-----IGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIArF---DAGVSDANITEAASRAQAHALITGLKQGYQTTmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:cd03259 87 lTVAENIA-FglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 490 SNLDAEGEAALeRALLQA--KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFG 542
Cdd:cd03259 159 SALDAKLREEL-REELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-521 |
1.29e-37 |
|
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: 138.00 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwapTHARADTsaAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyPTWDRKQLG 398
Cdd:COG4133 2 MLEAENL----SCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 399 GYIGYLAQDVQLLPG-SIAENIaRFDAGVSDAniteAASRAQAHALIT--GLkQGYqttMEAAGGSLSGGTRQRIGLARA 475
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENL-RFWAALYGL----RADREAIDEALEavGL-AGL---ADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRP 521
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
294-550 |
1.93e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.43 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 294 KRLGSVIASGKGHRADRLILPEPEGRLTVKNL-FWAPTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLA 372
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEPLLEVRNLsKRYPVRGKGGVRA--VDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 373 GVAEPTGGTIALDGADYPTW---DRKQLGGYIGYLAQD--VQLLPG-SIAENIARfdAGVSDANITEAASRAQAHALIT- 445
Cdd:COG1123 313 GLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDpySSLNPRmTVGDIIAE--PLRLHGLLSRAERRERVAELLEr 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 446 -GLKQGYqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERAL--LQAKAgGTTVIIVTHRPA 522
Cdd:COG1123 391 vGLPPDL---ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLrdLQREL-GLTYLFISHDLA 466
|
250 260
....*....|....*....|....*....
gi 517342213 523 IVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG1123 467 VVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
316-536 |
2.83e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.07 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 316 PEGRLTVKNLfwAPTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAdyptwDRK 395
Cdd:COG1116 4 AAPALELRGV--SKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGGYIGYLAQDVQLLP-GSIAENIArfdAGVSDANITEAASRAQAHALI--TGLKqgyqttmEAAG---GSLSGGTRQR 469
Cdd:COG1116 77 GPGPDRGVVFQEPALLPwLTVLDNVA---LGLELRGVPKAERRERARELLelVGLA-------GFEDaypHQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 470 IGLARAFFGNPKLLILDEPNSNLDaegeaALERALLQA------KAGGTTVIIVTH--RPAIVLkCDKALVLRNG 536
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALD-----ALTRERLQDellrlwQETGKTVLFVTHdvDEAVFL-ADRVVVLSAR 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-542 |
5.67e-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: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLpgsiaeNI 419
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQALELL------GL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFdagvSDANITEaasraqahalitglkqgyqttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03214 88 AHL----ADRPFNE----------------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517342213 500 LERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFG 542
Cdd:cd03214 136 LLELLRRlARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
340-550 |
9.73e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.23 E-value: 9.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKqlggyIGYLAQDVQLLPG-SI 415
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglPPEKRN-----VGMVFQDYALFPHlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA---RFDaGVSDAnitEAASRAqAHAL-ITGLkQGYQTTMEAAggsLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:COG3842 95 AENVAfglRMR-GVPKA---EIRARV-AELLeLVGL-EGLADRYPHQ---LSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 492 LDAE--GEAALE-RALLQAKagGTTVIIVTHRP--AIVLkCDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG3842 166 LDAKlrEEMREElRRLQREL--GITFIYVTHDQeeALAL-ADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
340-542 |
8.69e-36 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 133.43 E-value: 8.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyPTWDRKQlggyIGYLAQDVQL---LPGSIA 416
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-LEKERKR----IGYVPQRRSIdrdFPISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIARfdAGVSDANITEAASRAQAHALITGLKqgyqtTMEAAG------GSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:cd03235 89 DVVLM--GLYGHKGLFRRLSKADKAKVDEALE-----RVGLSEladrqiGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLrNGAVDAFG 542
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-552 |
1.02e-35 |
|
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: 134.16 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwAPTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG 399
Cdd:COG1124 2 LEVRNL--SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQD-------VQLLPGSIAE--NIARFDAgvSDANITEAASRaqahaliTGLKQGYqttMEAAGGSLSGGTRQRI 470
Cdd:COG1124 80 RVQMVFQDpyaslhpRHTVDRILAEplRIHGLPD--REERIAELLEQ-------VGLPPSF---LDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 471 GLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKA-GGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
....
gi 517342213 549 QRLS 552
Cdd:COG1124 228 AGPK 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
340-538 |
3.08e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG-SI 415
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrIGVVFQDFRLLPDrTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA---RFdAGVSDANIteaasRAQAHALIT--GLK-QGYQTTMEaaggsLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:COG2884 97 YENVAlplRV-TGKSRKEI-----RRRVREVLDlvGLSdKAKALPHE-----LSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 490 SNLDAegEAALE--RALLQAKAGGTTVIIVTHRPAIVLKCDK-ALVLRNGAV 538
Cdd:COG2884 166 GNLDP--ETSWEimELLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-549 |
4.48e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYptwdrKQLGGYIGYLAQDVQL---LPGSIA 416
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYVPQRAEVdwdFPITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIA-------RFDAGVSdaniteAASRAQAHALITglkqgyqtTMEAAG------GSLSGGTRQRIGLARAFFGNPKLL 483
Cdd:COG1121 96 DVVLmgrygrrGLFRRPS------RADREAVDEALE--------RVGLEDladrpiGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 484 ILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVdAFGPASEILQ 549
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPEEVLT 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
340-549 |
7.93e-35 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 131.64 E-value: 7.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDvqllpG--- 413
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLFQG-----Galf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 ---SIAENIA---RFDAGVSDANITEAASRAQAHAlitGLKqgyqttmEAAG---GSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:COG1127 95 dslTVFENVAfplREHTDLSEAEIRELVLEKLELV---GLP-------GAADkmpSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 485 LDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-538 |
4.00e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 136.90 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAePTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFD 423
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 424 AGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERA 503
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190
....*....|....*....|....*....|....*
gi 517342213 504 LLQAKAGGTTvIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:PRK11174 528 LNAASRRQTT-LMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-547 |
9.56e-34 |
|
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: 128.07 E-value: 9.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAG-----VAEPTGGTIALDGADYPTWD--RKQLGGYIGYLAQDVQLL 411
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 412 PGSIAENIA-------RFDAGVSDANITEAASRAqahALITGLKQgyqttmEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:cd03260 94 PGSIYDNVAyglrlhgIKLKEELDERVEEALRKA---ALWDEVKD------RLHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 485 LDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKC-DKALVLRNGAVDAFGPASEI 547
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-538 |
1.61e-33 |
|
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: 126.99 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKqlgGYIGYLAQDV--QLLPGSIAE 417
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQDVdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIARFDAGVSDANiteaasrAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:cd03226 92 ELLLGLKELDAGN-------EQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 498 AALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
340-536 |
2.09e-33 |
|
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: 125.76 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY--PTWDRKQLGGYIGYLAQDVQLLPG-SIA 416
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIARfdagvsdaniteaasraqahalitglkqgyqttmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:cd03229 95 ENIAL---------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 497 EAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:cd03229 136 RREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
318-550 |
2.54e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 134.38 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 318 GRLTVKNLFWapTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL 397
Cdd:PRK11176 340 GDIEFRNVTF--TYPGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 398 GGYIGYLAQDVQLLPGSIAENIA-RFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAF 476
Cdd:PRK11176 416 RNQVALVSQNVHLFNDTIANNIAyARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 477 FGNPKLLILDEPNSNLDAEGEAALERAL--LQAKaggTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALdeLQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
324-536 |
8.01e-33 |
|
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: 124.89 E-value: 8.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 324 NLFWAPthaRADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadyptwdrkQLGGYIGY 403
Cdd:cd03250 7 SFTWDS---GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 404 LAQDVQLLPGSIAENI---ARFDAGVSDANIteaasraQAHALITGLKQ---GYQTTMEAAGGSLSGGTRQRIGLARAFF 477
Cdd:cd03250 71 VSQEPWIQNGTIRENIlfgKPFDEERYEKVI-------KACALEPDLEIlpdGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 478 GNPKLLILDEPNSNLDAEGEAAL-ERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNG 536
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
340-535 |
1.47e-32 |
|
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: 124.51 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAdyptwDRKQLGGYIGYLAQDVQLLP-GSIAEN 418
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDRGYVFQQDALLPwLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IArfdAGVSDANITEAASRAQAHALI--TGLKqgyqttmEAAG---GSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:cd03293 94 VA---LGLELQGVPKAEARERAEELLelVGLS-------GFENaypHQLSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517342213 494 AEGEAALERALLQAKAG-GTTVIIVTH--RPAIVLkCDKALVLRN 535
Cdd:cd03293 164 ALTREQLQEELLDIWREtGKTVLLVTHdiDEAVFL-ADRVVVLSA 207
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
9-281 |
1.78e-32 |
|
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: 126.40 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AF-----IASISSPKAAMGDIQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVAS 163
Cdd:cd18587 81 LFervlgLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 164 HYATRSAAGKAQEAAVAAN-LLAQAFTrNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVLQL 242
Cdd:cd18587 161 QKPLRRLVEESMRESAQKNaLLVESLS-GLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTV 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 517342213 243 AILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVA 281
Cdd:cd18587 240 AIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAG 278
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
340-549 |
2.78e-32 |
|
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: 124.15 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG-SI 415
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA---RFDAGVSDANITEAAsRAQAHALitGLKqGYQTTMEAaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:cd03261 95 FENVAfplREHTRLSEEEIREIV-LEKLEAV--GLR-GAEDLYPA---ELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 493 DAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:cd03261 168 DPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
340-536 |
3.09e-32 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 123.62 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG----YIGYLAQDVQLLPG-S 414
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQFHHLLPDfT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIArFDAGVSDANITEAASRAQAHALITGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:TIGR02211 100 ALENVA-MPLLIGKKSVKEAKERAYEMLEKVGLEH----RINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 495 EGEAALERALLQA-KAGGTTVIIVTHRPAIVLKCDKALVLRNG 536
Cdd:TIGR02211 175 NNAKIIFDLMLELnRELNTSFLVVTHDLELAKKLDRVLEMKDG 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
341-548 |
4.09e-32 |
|
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: 123.70 E-value: 4.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQLGgyIGYLAQDVQLLPG-SIA 416
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARLG--IGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENI---ARFDAGVSDANI----TEAASRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:cd03219 94 ENVmvaAQARTGSGLLLArarrEEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 490 SNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:cd03219 172 AGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
318-550 |
9.21e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.96 E-value: 9.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 318 GRLTVKNLfwapTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDR 394
Cdd:COG3839 2 ASLELENV----SKSYGGVEA--LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 395 KqlggyIGYLAQDVQLLPG-SIAENIA---RFdAGVSDANITEAASRAqAHAL-ITGL-----KQgyqttmeaaggsLSG 464
Cdd:COG3839 76 N-----IAMVFQSYALYPHmTVYENIAfplKL-RKVPKAEIDRRVREA-AELLgLEDLldrkpKQ------------LSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 465 GTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALeRALLQA--KAGGTTVIIVTHRP--AIVLkCDKALVLRNGAVDA 540
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEM-RAEIKRlhRRLGTTTIYVTHDQveAMTL-ADRIAVMNDGRIQQ 214
|
250
....*....|
gi 517342213 541 FGPASEILQR 550
Cdd:COG3839 215 VGTPEELYDR 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
340-549 |
2.37e-31 |
|
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: 121.39 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQLGgyIGYLAQDVQLLPG-SI 415
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitgLPPHERARAG--IGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENI-----ARFDAGVsdaniteAASRAQAHALITGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNs 490
Cdd:cd03224 93 EENLllgayARRRAKR-------KARLERVYELFPRLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 491 nldaEGEA-----ALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:cd03224 161 ----EGLApkiveEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
340-542 |
2.79e-31 |
|
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: 119.73 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDrKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 arfdagvsdaniteaasraqahalitglkqgyqttmeaaGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03247 96 ---------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 500 LERALLQAkAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFG 542
Cdd:cd03247 137 LLSLIFEV-LKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
340-542 |
4.32e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 120.38 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGhVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGYLPQEFGVYPNFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDA---GVSDANITEAASRAQAHaliTGLKQGYQTTMeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:cd03264 93 LDYIAwlkGIPSKEVKARVDEVLEL---VNLGDRAKKKI----GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517342213 497 EAALeRALLQAKAGGTTVIIVTHrpaIV----LKCDKALVLRNGAVDAFG 542
Cdd:cd03264 166 RIRF-RNLLSELGEDRIVILSTH---IVedveSLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
15-296 |
4.90e-31 |
|
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: 122.62 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 15 VIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGEDAFIASI 94
Cdd:cd18555 7 ILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 95 SSP-----KAAMGDI-QPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVASHYATR 168
Cdd:cd18555 87 KLPysffeNRSSGDLlFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 169 saagKAQEAAVAANLLAQAFT----RNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVLQLAI 244
Cdd:cd18555 167 ----KLNQEEIVAQTKVQSYLtetlYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 245 LGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18555 243 LWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
206-550 |
5.53e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 127.25 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 206 ERWGRRFADAANLQDGASAInAIFAGSSrTLRMVLQLAILGTGAVlVLQGQMTAGMIFASSTiSGRALQPIdqlvAGwrq 285
Cdd:PRK11160 231 QQWLAAQRRQANLTGLSQAL-MILANGL-TVVLMLWLAAGGVGGN-AQPGALIALFVFAALA-AFEALMPV----AG--- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 286 ivdarkAWKRLGSVIASGKghRADRLILPEPE-------------GRLTVKNL-FWAPtharaDTSAAIIKDVSFDLKPG 351
Cdd:PRK11160 300 ------AFQHLGQVIASAR--RINEITEQKPEvtfpttstaaadqVSLTLNNVsFTYP-----DQPQPVLKGLSLQIKAG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 352 HVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFDAGVSDANI 431
Cdd:PRK11160 367 EKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEAL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 432 TEAASRAQAHALITGlKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEgeaaLER---ALLQAK 508
Cdd:PRK11160 447 IEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE----TERqilELLAEH 521
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517342213 509 AGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK11160 522 AQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
340-549 |
1.24e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.22 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQL-LPGSIAEN 418
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IA--RFDAGVSDANITEAASRAQAHALITGLKQG-YQTtmeaaggsLSGGTRQRIGLARAF-------FGNPKLLILDEP 488
Cdd:COG4559 96 VAlgRAPHGSSAAQDRQIVREALALVGLAHLAGRsYQT--------LSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 489 NSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIV-LKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAaQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
336-524 |
1.76e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 118.50 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 336 TSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQ---LGGYIGYLAQDVQLLP 412
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlplLRRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 G-SIAENIArFDAGVSDANITEAASRAQAHALITGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:TIGR02673 93 DrTVYENVA-LPLEVRGKKEREIQRRVGAALRQVGLEH----KADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGN 167
|
170 180 190
....*....|....*....|....*....|...
gi 517342213 492 LDAEGEAALERALLQAKAGGTTVIIVTHRPAIV 524
Cdd:TIGR02673 168 LDPDLSERILDLLKRLNKRGTTVIVATHDLSLV 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
343-542 |
1.82e-30 |
|
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: 118.55 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLkPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA---------DYPTWDRKqlggyIGYLAQDVQLLPG 413
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkiNLPPQQRK-----IGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQttmeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 493 DAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFG 542
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
319-542 |
1.83e-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: 118.04 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLFWAPTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTG--GTIALDGadYPTwDRKQ 396
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING--RPL-DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 LGGYIGYLAQDVQLLPG-SIAENIaRFDAGVSdaniteaasraqahalitglkqgyqttmeaaggSLSGGTRQRIGLARA 475
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETL-MFAAKLR---------------------------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPA--IVLKCDKALVLRNGAVDAFG 542
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
337-548 |
4.17e-30 |
|
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: 118.07 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG 413
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKArrrIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIArFD---AGVSDANITEaasraQAHALIT--GLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:cd03258 97 rTVFENVA-LPleiAGVPKAEIEE-----RVLELLElvGLED----KADAYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 488 PNSNLDAEGEAALERALLQA-KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:cd03258 167 ATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
343-538 |
7.98e-30 |
|
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: 116.74 E-value: 7.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG-SIAEN 418
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIGVVFQDFRLLPDrNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IArFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEA 498
Cdd:cd03292 99 VA-FALEVTGVPPREIRKRVPAALELVGLSHKHRALPA----ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517342213 499 ALERALLQAKAGGTTVIIVTHRPAIVLKCDK-ALVLRNGAV 538
Cdd:cd03292 174 EIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
340-560 |
8.77e-30 |
|
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: 117.88 E-value: 8.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPG-HVlAILGPSGSGKSSLARLLAGVAEPT-GGTIALDGADYPTWD----RKQlggyIGYLAQDVQL-LP 412
Cdd:COG1119 18 ILDDISWTVKPGeHW-AILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDvwelRKR----IGLVSPALQLrFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 GSI-AENI---ARFDA-GVSDaNITEAAsRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:COG1119 93 RDEtVLDVvlsGFFDSiGLYR-EPTDEQ-RERARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 488 PNSNLDAEGEAALeRALLQ--AKAGGTTVIIVTHRPAIVLKC-DKALVLRNGAVDAFGPASEIL--QRLSGAKPRPVN 560
Cdd:COG1119 169 PTAGLDLGARELL-LALLDklAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLtsENLSEAFGLPVE 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
341-550 |
9.17e-30 |
|
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: 117.40 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPG-SIAENI 419
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDA--GVSDANIteaasRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:cd03295 97 ALVPKllKWPKEKI-----RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 498 AALERALLQ-AKAGGTTVIIVTH--RPAIVLKcDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03295 172 DQLQEEFKRlQQELGKTIVFVTHdiDEAFRLA-DRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
341-547 |
9.61e-30 |
|
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: 117.44 E-value: 9.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGgyIGYLAQDVQLLPG-SIAENI 419
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ArFDAGV--SDANITEAASRAQAHAL-----ITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:cd03296 96 A-FGLRVkpRSERPPEAEIRAKVHELlklvqLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 493 DAEGEAALERAL--LQAKAGGTTViIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:cd03296 168 DAKVRKELRRWLrrLHDELHVTTV-FVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-547 |
2.05e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP---TWDRKQLGgyIGYLAQDVQLLPG-SIAE 417
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsPRDAQAAG--IAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NI------ARFdaGVSDanitEAASRAQAHALITGLKQGYQTTMEAagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:COG1129 99 NIflgrepRRG--GLID----WRAMRRRARELLARLGLDIDPDTPV--GDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 492 LDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
341-550 |
2.52e-29 |
|
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: 115.90 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKqlggyIGYLAQDVQLLPG-SIA 416
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnLPPEKRD-----ISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIA------RFDAGVSDANITEAASRAQahalITGLKQGYQTTmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:cd03299 90 KNIAyglkkrKVDKKEIERKVLEIAEMLG----IDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 491 NLDAEGEAALERALLQA-KAGGTTVIIVTH--RPAIVLKcDKALVLRNGAVDAFGPASEILQR 550
Cdd:cd03299 159 ALDVRTKEKLREELKKIrKEFGVTVLHVTHdfEEAWALA-DKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-538 |
5.33e-29 |
|
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: 112.91 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQlggyigylaqdvqllpgsiaeniAR 421
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-----------------------AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 422 fDAGVsdaniteaasraqahALItglkqgYQttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALE 501
Cdd:cd03216 74 -RAGI---------------AMV------YQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 517342213 502 RALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:cd03216 123 KVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
341-549 |
7.25e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 115.52 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKQLGgyigyLA---QDVQLLPG- 413
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARLG-----IArtfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENI-----ARFDAGVSDANI-------TEAASRAQAHALI--TGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGN 479
Cdd:COG0411 95 TVLENVlvaahARLGRGLLAALLrlprarrEEREARERAEELLerVGLAD----RADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 480 PKLLILDEPNSNLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
9-296 |
7.49e-29 |
|
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: 116.15 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AFIASISSP-----KAAMGDIQP-LRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMI-LMVV 161
Cdd:cd18782 81 IIDHLLRLPlgffdKRPVGELSTrISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLlLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 162 ASHYATRSAAGKAQEAAVAANLLAQAFTrNRETVQGMGMIGHVTERWGRRFADAanLQDG--ASAINAIFAGSSRTLRMV 239
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLT-GIQTVKAQNAELKARWRWQNRYARS--LGEGfkLTVLGTTSGSLSQFLNKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 240 LQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18782 238 SSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
337-549 |
7.54e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 7.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQL-LPGSI 415
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA--RFDAGVSDANITEAASRAQAHALITGLKQ-GYQTtmeaaggsLSGGTRQRIGLARAF------FGNPKLLILD 486
Cdd:PRK13548 94 EEVVAmgRAPHGLSRAEDDALVAAALAQVDLAHLAGrDYPQ--------LSGGEQQRVQLARVLaqlwepDGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 487 EPNSNLD-AEGEAALERALLQAKAGGTTVIIVTHRPAI-VLKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK13548 166 EPTSALDlAHQHHVLRLARQLAHERGLAVIVVLHDLNLaARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
340-542 |
8.36e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.89 E-value: 8.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGgyIGYLAQDVQLLPG-SIAEN 418
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAMVFQNYALYPHmTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IArFD---AGVSDANITEAASRAqAHAL-ITGLKQGYQTTmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03301 93 IA-FGlklRKVPKDEIDERVREV-AELLqIEHLLDRKPKQ-------LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 495 EGEAALERAL--LQAKAgGTTVIIVTH--RPAIVLKcDKALVLRNGAVDAFG 542
Cdd:cd03301 164 KLRVQMRAELkrLQQRL-GTTTIYVTHdqVEAMTMA-DRIAVMNDGQIQQIG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-547 |
1.09e-28 |
|
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: 114.59 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG-S 414
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMIFQQFNLIERlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENI-----ARFDAGVSDANITEAASRAQAHALIT--GL-KQGYQTTmeaagGSLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:cd03256 95 VLENVlsgrlGRRSTWRSLFGLFPKEEKQRALAALErvGLlDKAYQRA-----DQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 487 EPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
341-549 |
1.23e-28 |
|
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: 115.05 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL----GGYIGYLAQDVQLLPG-SI 415
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIArfdAGVSDANITEAASRAQA-HAL-ITGLKqGYQTTMEaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:cd03294 120 LENVA---FGLEVQGVPRAEREERAaEALeLVGLE-GWEHKYP---DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 494 A--EGEAALERALLQAKAGGTTVIIvTHRPAIVLKC-DKALVLRNGAVDAFGPASEILQ 549
Cdd:cd03294 193 PliRREMQDELLRLQAELQKTIVFI-THDLDEALRLgDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
316-542 |
1.25e-28 |
|
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: 113.28 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 316 PE-GRLTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDR 394
Cdd:cd03369 2 PEhGEIEVENL----SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 395 KQLGGYIGYLAQDVQLLPGSIAENIARFDAgVSDANITEAASraqahalitgLKQGyqttmeaaGGSLSGGTRQRIGLAR 474
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNLDPFDE-YSDEEIYGALR----------VSEG--------GLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERAlLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFG 542
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKT-IREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-519 |
1.41e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.78 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadyptwdrkqlGGYIGYLAQDVQLLPG-SIAEN 418
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IARFDAGVSDANIT-EAASRAQAHALITGLKQG-YQTTMEAAGG--------------------------SLSGGTRQRI 470
Cdd:COG0488 82 VLDGDAELRALEAElEELEAKLAEPDEDLERLAeLQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517342213 471 GLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAggtTVIIVTH 519
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSH 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
340-533 |
1.65e-28 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 112.71 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQ----LGGYIGYLAQDVQLLPG-S 414
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfRREKLGYLFQNFALIENeT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIarfDAGVSDANITEAASRaqaHALITGLKQ-GYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:TIGR03608 93 VEENL---DLGLKYKKLSKKEKR---EKKKEALEKvGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517342213 494 AEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVL 533
Cdd:TIGR03608 167 PKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
340-542 |
1.95e-28 |
|
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: 112.76 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQlggyIGYLAQDVQLLPGSIAENI 419
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVE----ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517342213 500 LERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFG 542
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
340-547 |
2.83e-28 |
|
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: 113.10 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG---ADYPTWDRKqlggyIGYLAQDVQLLPG-SI 415
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdiTNLPPHKRP-----VNTVFQNYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIArFD---AGVSDANITEAASRAQAhalITGLKqGYQTTMEAaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:cd03300 90 FENIA-FGlrlKKLPKAEIKERVAEALD---LVQLE-GYANRKPS---QLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 493 DAEGEAALERAL--LQaKAGGTTVIIVTH--RPAIVLKcDKALVLRNGAVDAFGPASEI 547
Cdd:cd03300 162 DLKLRKDMQLELkrLQ-KELGITFVFVTHdqEEALTMS-DRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-547 |
3.65e-28 |
|
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: 112.21 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGG 399
Cdd:cd03263 1 LQIRNL----TKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQDVQLLPG-SIAENIaRFDAGVSDANITEAASRAQAHALITGLKQgYQTTMeaaGGSLSGGTRQRIGLARAFFG 478
Cdd:cd03263 76 SLGYCPQFDALFDElTVREHL-RFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKR---ARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 479 NPKLLILDEPNSNLDAEGEAALERALLQAKaGGTTVIIVTHRP--AIVLkCDKALVLRNGAVDAFGPASEI 547
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMdeAEAL-CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
340-519 |
9.74e-28 |
|
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: 110.70 E-value: 9.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRK--QLGGYIGYLAQDVQLLPG-SIA 416
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArfDAGVSDANITEAASRAQAHALITglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:cd03262 95 ENIT--LAPIKVKGMSKAEAEERALELLE--KVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180
....*....|....*....|...
gi 517342213 497 EAALERALLQAKAGGTTVIIVTH 519
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
242-549 |
1.22e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 117.12 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 242 LAIlGTGAVLVLQGQMTAGMIFASSTISGRALQPIdqLVAGWR-QIVD-ARKAWKRLGSVIASGKGHRADRLILPEPEGR 319
Cdd:PRK10789 237 LAI-GGGSWMVVNGSLTLGQLTSFVMYLGLMIWPM--LALAWMfNIVErGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVK-NLFWAPTHARAdtsaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLG 398
Cdd:PRK10789 314 LDVNiRQFTYPQTDHP-----ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 399 GYIGYLAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFG 478
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 479 NPKLLILDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
343-551 |
1.82e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 113.66 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---------PTWDRKqlggyIGYLAQDVQLLPG 413
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargiflPPHRRR-----IGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIarfDAGVSDANITE-AASRAQAHAL--ITGLkqgyqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:COG4148 92 lSVRGNL---LYGRKRAPRAErRISFDEVVELlgIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 490 SNLDAEGEAA----LERalLQAKAgGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQRL 551
Cdd:COG4148 162 AALDLARKAEilpyLER--LRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
340-548 |
4.21e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQ--DVQLLPGSIAE 417
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQnpDNQFIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIA------RFDAGVSDANITEAASRAQAHALitgLKQGYQttmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:PRK13632 104 DIAfglenkKVPPKKMKDIIDDLAKKVGMEDY---LDKEPQ--------NLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 492 LDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK13632 173 LDPKGKREIKKIMVDlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
341-536 |
4.38e-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: 108.84 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY--PTWDRKQLGGYIGYlaqdvqllPG----- 413
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqkNIEALRRIGALIEA--------PGfypnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIARFDA--GVSDANITEAAsraqahaLITGLKQ-GYQTTmeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:cd03268 88 TARENLRLLARllGIRKKRIDEVL-------DVVGLKDsAKKKV-----KGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPA-IVLKCDKALVLRNG 536
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSeIQKVADRIGIINKG 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
340-519 |
4.64e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 109.70 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYpTWDRKQLGGY---IGYLAQDVQLLPG-SI 415
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLrrkVGMVFQQFNLFPHlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIArfDAGVSDANITEAASRAQAHALIT--GLKqgyqttmEAAG---GSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:COG1126 95 LENVT--LAPIKVKKMSKAEAEERAMELLErvGLA-------DKADaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
|
170 180 190
....*....|....*....|....*....|.
gi 517342213 491 NLDAE--GEaaLERALLQAKAGGTTVIIVTH 519
Cdd:COG1126 166 ALDPElvGE--VLDVMRDLAKEGMTMVVVTH 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
345-550 |
5.00e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.46 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 345 SFDL--KPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKqlggyIGYLAQDVQLLPG-SIAEN 418
Cdd:COG3840 17 RFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltaLPPAERP-----VSMLFQENNLFPHlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IArfdAGVSDA-NITEAASRAQAHAL----ITGLKQGYQttmeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:COG3840 92 IG---LGLRPGlKLTAEQRAQVEQALervgLAGLLDRLP-------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 494 aegeAALERALLQ-----AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG3840 162 ----PALRQEMLDlvdelCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-549 |
7.97e-27 |
|
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: 108.00 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwaptHARADtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVA--EPTGGTIALDGAD---YPTWDR 394
Cdd:cd03217 1 LEIKDL-----HVSVG-GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDitdLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 395 KQLGGYIGYlaqdvqllpgsiaENIARFDaGVSDANiteaasraqahaLITGLKQGyqttmeaaggsLSGGTRQRIGLAR 474
Cdd:cd03217 75 ARLGIFLAF-------------QYPPEIP-GVKNAD------------FLRYVNEG-----------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIV--LKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
340-548 |
1.36e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 108.15 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQLGgyIGYLAQDVQLLPG-SI 415
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHRIARLG--IGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENI-----ARFDAGVSDANITEA-------ASRaqahalitgLKQgyqttmeaAGGSLSGGTRQRIGLARAFFGNPKLL 483
Cdd:COG0410 96 EENLllgayARRDRAEVRADLERVyelfprlKER---------RRQ--------RAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 484 ILDEPNsnldaEGEA-----ALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:COG0410 159 LLDEPS-----LGLApliveEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
341-558 |
1.39e-26 |
|
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: 107.94 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG--ADYPTWDRKqlggyigYLAQDVQLLPG-SIAE 417
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqITEPGPDRM-------VVFQNYSLLPWlTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIA-RFDAGVSDANITEAASRAQAHALITGLKQGyqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:TIGR01184 74 NIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEA----ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 497 EAALERALLQ-AKAGGTTVIIVTHrpaivlKCDKALVLRNGAVD-AFGPASEILQRLSGAKPRP 558
Cdd:TIGR01184 150 RGNLQEELMQiWEEHRVTVLMVTH------DVDEALLLSDRVVMlTNGPAANIGQILEVPFPRP 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-550 |
1.77e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.43 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQlggyIGYLAQDVQLLPG-SIAENI 419
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IGYLPEERGLYPKmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDA--GVSdanitEAASRAQAHALIT--GLKQGYQTTMEaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:COG4152 93 VYLARlkGLS-----KAEAKRRADEWLErlGLGDRANKKVE----ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 496 GEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG4152 164 NVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-538 |
5.60e-26 |
|
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: 104.82 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwaptharadTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTW---DRK 395
Cdd:cd03215 4 VLEVRGL----------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRsprDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGgyIGYLAQDVQ----LLPGSIAENIArfdagvsdaniteaasraqahalitglkqgyqttmeaAGGSLSGGTRQRIG 471
Cdd:cd03215 74 RAG--IAYVPEDRKreglVLDLSVAENIA-------------------------------------LSSLLSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 472 LARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIV-THRPAIVLKCDKALVLRNGAV 538
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLIsSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-550 |
9.10e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.02 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG---ADYPTWD-RKQlggyIGYLAQ--DV 408
Cdd:PRK13635 17 DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlSEETVWDvRRQ----VGMVFQnpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 409 QLLPGSIAENIA---------------RFDAGVSDANITEAASRAQAHalitglkqgyqttmeaaggsLSGGTRQRIGLA 473
Cdd:PRK13635 93 QFVGATVQDDVAfglenigvpreemveRVDQALRQVGMEDFLNREPHR--------------------LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 474 RAFFGNPKLLILDEPNSNLDAEG-EAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGrREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
339-533 |
2.07e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 105.20 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadyptwdRKQLGGYIGYLAQDVQL---LPGSI 415
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLdttLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 aENIARFDAGVSDANITEAASRAQAHALItglkqgyqttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:PRK09544 87 -NRFLRLRPGTKKEDILPALKRVQAGHLI-----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517342213 496 GEAALERALLQAKAG-GTTVIIVTHRPAIVL-KCDKALVL 533
Cdd:PRK09544 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
340-549 |
2.29e-25 |
|
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: 104.55 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQLGgyIGYLAQDVQLLPG-SI 415
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitkLPMHKRARLG--IGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIarfDAGVSDANITEAASRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:cd03218 93 EENI---LAVLEIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 496 GEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
9-296 |
2.77e-25 |
|
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: 106.04 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AFIASISSPKA-----AMGDI-QPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILM--V 160
Cdd:cd18588 81 LFRHLLRLPLSyfesrQVGDTvARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLslL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 161 VASHYATRSAAgKAQEAAVAANLLAQAFTrNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVL 240
Cdd:cd18588 161 VTPILRRRLEE-KFQRGAENQSFLVETVT-GIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 241 QLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18588 239 TLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
343-551 |
2.83e-25 |
|
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: 107.51 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLkPGH-VLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG---------ADYPTWDRKqlggyIGYLAQDVQLLP 412
Cdd:TIGR02142 15 DADFTL-PGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgIFLPPEKRR-----IGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 G-SIAENI--ARFDAGVSDANITEAAsraqahalITGLkQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:TIGR02142 89 HlSVRGNLryGMKRARPSERRISFER--------VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 490 SNLD----AEGEAALERalLQAKAgGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQRL 551
Cdd:TIGR02142 160 AALDdprkYEILPYLER--LHAEF-GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
281-545 |
3.30e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 281 AGWRQIVDarkawkRLGS----VIASGKGHRADRLILPEPEGRLTVKNLfwapTHARADtSAAIIKDVSFDLKPGHVLAI 356
Cdd:COG4178 326 AEWRATVD------RLAGfeeaLEAADALPEAASRIETSEDGALALEDL----TLRTPD-GRPLLEDLSLSLKPGERLLI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 357 LGPSGSGKSSLARLLAGVAEPTGGTIAL-DGADyptwdrkqlggyIGYLAQDVQLLPGSIAENIA--RFDAGVSDANITE 433
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR------------VLFLPQRPYLPLGTLREALLypATAEAFSDAELRE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 434 AASRAQAHALITGLKQGYQTTMEaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERaLLQAKAGGTT 513
Cdd:COG4178 463 ALEAVGLGHLAERLDEEADWDQV-----LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-LLREELPGTT 536
|
250 260 270
....*....|....*....|....*....|..
gi 517342213 514 VIIVTHRPAIVLKCDKALVLRNGAVDAFGPAS 545
Cdd:COG4178 537 VISVGHRSTLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
340-519 |
3.54e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.94 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA--DYPTWDRkqlggyiGYLAQDVQLLPG-SIA 416
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvTGPGADR-------GVVFQKDALLPWlNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIA---RFdAGVSdanitEAASRAQAHALI--TGLkQGYQttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:COG4525 95 DNVAfglRL-RGVP-----KAERRARAEELLalVGL-ADFA---RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180
....*....|....*....|....*....
gi 517342213 492 LDAEGEAALERALLQAKAG-GTTVIIVTH 519
Cdd:COG4525 165 LDALTREQMQELLLDVWQRtGKGVFLITH 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
325-536 |
4.17e-25 |
|
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: 104.89 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 325 LFWAPTHAradtsaAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYigyl 404
Cdd:TIGR02769 17 LFGAKQRA------PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 405 AQDVQLL----PG------SIAENIARFDAGVSDANITEAASRAQAHALITGLKQgyqTTMEAAGGSLSGGTRQRIGLAR 474
Cdd:TIGR02769 87 RRDVQLVfqdsPSavnprmTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS---EDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERAL--LQAkAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQ-AFGTAYLFITHDLRLVQSfCQRVAVMDKG 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
339-536 |
4.20e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 103.71 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWD---RKQL-GGYIGYLAQDVQLLPGS 414
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLrAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAGVSDANitEAASRAQAHALITGLKQGYQTTMEAAggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK10584 104 NALENVELPALLRGES--SRQSRNGAKALLEQLGLGKRLDHLPA--QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 495 E-GEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNG 536
Cdd:PRK10584 180 QtGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
340-536 |
6.56e-25 |
|
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: 100.60 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadyptwdrkqlGGYIGYLAQdvqllpgsiaeni 419
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 arfdagvsdaniteaasraqahalitglkqgyqttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03221 71 ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190
....*....|....*....|....*....|....*...
gi 517342213 500 LERAlLQAKAGgtTVIIVTH-RPAIVLKCDKALVLRNG 536
Cdd:cd03221 109 LEEA-LKEYPG--TVILVSHdRYFLDQVATKIIELEDG 143
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
337-535 |
7.45e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.56 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP---TGGTIALDGAD---YPTWDRKqlggyIGYLAQDVQL 410
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltaLPAEQRR-----IGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPG-SIAENIArFDagvsdanITEAASRAQAHALItglkqgyQTTMEAAG---------GSLSGGTRQRIGLARAFFGNP 480
Cdd:COG4136 88 FPHlSVGENLA-FA-------LPPTIGRAQRRARV-------EQALEEAGlagfadrdpATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 481 KLLILDEPNSNLDAEGEAALeRALL--QAKAGGTTVIIVTHRPAIVLKCDKALVLRN 535
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQF-REFVfeQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-521 |
8.68e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.26 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwapTHARADtsAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLG 398
Cdd:PRK13539 2 MLEGEDL----ACVRGG--RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 399 GYIGYlaQDVQLLPGSIAENI---ARFdAGVSDANITEAASRAQAHAlITGLKQGYqttmeaaggsLSGGTRQRIGLARA 475
Cdd:PRK13539 76 HYLGH--RNAMKPALTVAENLefwAAF-LGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517342213 476 FFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRP 521
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-550 |
1.21e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.16 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG-SIAE 417
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAArrkIGMIFQHFNLLSSrTVAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIA---RFdAGVSDANIteaasRAQAHALI--TGL---KQGY--QttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:COG1135 102 NVAlplEI-AGVPKAEI-----RKRVAELLelVGLsdkADAYpsQ---------LSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 488 PNSNLDAEG-EAALEraLLQ---AKAgGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG1135 167 ATSALDPETtRSILD--LLKdinREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
341-548 |
2.06e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.99 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQ--LLP----GS 414
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPNtsLNPrlniGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAgvsdaNITEAASRAQahaLITGLKQ--------GYQTTMeaaggsLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:COG4167 109 ILEEPLRLNT-----DLTAEEREER---IFATLRLvgllpehaNFYPHM------LSSGQKQRVALARALILQPKIIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 487 EPNSNLDAEGEAALERALL--QAKAgGTTVIIVTHRPAIVLKC-DKALVLRNGAVDAFGPASEIL 548
Cdd:COG4167 175 EALAALDMSVRSQIINLMLelQEKL-GISYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVF 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-542 |
2.86e-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: 101.29 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGGYIGYLAQDVQLLPG-SIAENI 419
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFdAGVSDANiteaasRAQAHALITGLKQ--GYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:cd03266 100 EYF-AGLYGLK------GDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517342213 498 AALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFG 542
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
318-550 |
2.95e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 107.11 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 318 GRLTVKNLFWAPTHARAdtsaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL 397
Cdd:PRK10790 339 GRIDIDNVSFAYRDDNL-----VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 398 GGYIGYLAQDVQLLPGSIAENIArFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFF 477
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVT-LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 478 GNPKLLILDEPNSNLDAEGEAALERAlLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQA-LAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
310-541 |
2.99e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 310 RLILPEPE--GR--LTVKNLfwapTHARADTsaAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALd 385
Cdd:COG0488 302 EIRFPPPErlGKkvLELEGL----SKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 386 gadyptwdrkqlgGY---IGYLAQDVQLLPG--SIAENIARFDAGVSDANITEAA-----SRAQAHALItglkqgyqttm 455
Cdd:COG0488 375 -------------GEtvkIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLgrflfSGDDAFKPV----------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 456 eaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERAlLQAKAGgtTVIIVTH-RPAIVLKCDKALVLR 534
Cdd:COG0488 431 ----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA-LDDFPG--TVLLVSHdRYFLDRVATRILEFE 503
|
....*..
gi 517342213 535 NGAVDAF 541
Cdd:COG0488 504 DGGVREY 510
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-550 |
4.21e-24 |
|
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: 103.21 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwaptHARADTSAAIIK---DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP---TGGTIALDGADYPTWD 393
Cdd:COG0444 2 LEVRNL-----KVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 394 RKQL----GGYIGYLAQDvqllPGS-----------IAENIARFDagvsdaNITEAASRAQAHALIT--GLKQGyqttmE 456
Cdd:COG0444 77 EKELrkirGREIQMIFQD----PMTslnpvmtvgdqIAEPLRIHG------GLSKAEARERAIELLErvGLPDP-----E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 457 AAGGS----LSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA----LERalLQAKAgGTTVIIVTHRPAIVLK-C 527
Cdd:COG0444 142 RRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQilnlLKD--LQREL-GLAILFITHDLGVVAEiA 218
|
250 260
....*....|....*....|...
gi 517342213 528 DKALVLRNGAVDAFGPASEILQR 550
Cdd:COG0444 219 DRVAVMYAGRIVEEGPVEELFEN 241
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
320-551 |
8.07e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwaptHARADtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVA--EPTGGTIALDGAD---YPTWDR 394
Cdd:COG0396 1 LEIKNL-----HVSVE-GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDileLSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 395 KQLGgyIGYLAQDvqllPGSIAeniarfdaGVSDANITEAASRAQAHALITGLK--QGYQTTMEAAG-----------GS 461
Cdd:COG0396 75 ARAG--IFLAFQY----PVEIP--------GVSVSNFLRTALNARRGEELSAREflKLLKEKMKELGldedfldryvnEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 462 LSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIV--LKCDKALVLRNGAVD 539
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILdyIKPDFVHVLVDGRIV 220
|
250
....*....|..
gi 517342213 540 AFGPAsEILQRL 551
Cdd:COG0396 221 KSGGK-ELALEL 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-536 |
1.08e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWAPTHA---RADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQ 396
Cdd:PRK10419 4 LNVSGLSHHYAHGglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 LGGYigylAQDVQLL----PG------SIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYqttMEAAGGSLSGGT 466
Cdd:PRK10419 84 RKAF----RRDIQMVfqdsISavnprkTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSV---LDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 467 RQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERAL--LQAKaGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLkkLQQQ-FGTACLFITHDLRLVERfCQRVMVMDNG 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-550 |
1.47e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.99 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAE-----PTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLL 411
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 412 PG-SIAENIA---RFDAGVSD-----ANITEAASRAQahalitgLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKL 482
Cdd:PRK14247 95 PNlSIFENVAlglKLNRLVKSkkelqERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 483 LILDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKC-DKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
340-519 |
1.54e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG--ADYPTWDRkqlggyiGYLAQDVQLLP-GSIA 416
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAER-------GVVFQNEGLLPwRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArfdAGVSDANITEAASRAQAHALITglkqgyQTTMEAAGG----SLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:PRK11248 89 DNVA---FGLQLAGVEKMQRLEIAHQMLK------KVGLEGAEKryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 517342213 493 DAEGEAALERALLQAKAG-GTTVIIVTH 519
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQEtGKQVLLITH 187
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
318-587 |
1.71e-23 |
|
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: 100.31 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 318 GRLTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSL----ARLLAgvaepTGGTIALDGADYPTWD 393
Cdd:cd03289 1 GQMTVKDL----TAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 394 RKQLGGYIGYLAQDVQLLPGSIAENIARFDAGvSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLA 473
Cdd:cd03289 72 LQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKW-SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 474 RAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSG 553
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 517342213 554 AKPRPVNANRVSV---RNKSETADAPENRDAGLVEST 587
Cdd:cd03289 230 FKQAISPSDRLKLfprRNSSKSKRKPRPQIQALQEET 266
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
340-551 |
2.28e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.01 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY--PTWDRKQLGGYIGYLAQDVQLLPGSIA- 416
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPHLTAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIARFDAGVSDAniTEAASRAQAHALITglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:PRK09493 96 ENVMFGPLRVRGA--SKEEAEKQARELLA--KVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 497 EAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALV-LRNGAVDAFGPASEIL-----QRL 551
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIknppsQRL 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
343-521 |
2.63e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 97.95 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGG---YIGYLAQDVQLLpgSIAENI 419
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQdllYLGHQPGIKTEL--TALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 aRFDAGVSDANITEAASRAQAHAlitGLkQGYqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:PRK13538 96 -RFYQRLHGPGDDEALWEALAQV---GL-AGF---EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|..
gi 517342213 500 LERALLQAKAGGTTVIIVTHRP 521
Cdd:PRK13538 168 LEALLAQHAEQGGMVILTTHQD 189
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
356-547 |
3.06e-23 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 101.03 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 356 ILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRkqlggYIGYLAQDVQLLPG-SIAENIA---RFDaGVSD 428
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnvPPHLR-----HINMVFQSYALFPHmTVEENVAfglKMR-KVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 429 ANITEAASRAQAHALITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE--GEAALERALLQ 506
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPH-------QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 507 AKAgGTTVIIVTH--RPAIVLKcDKALVLRNGAVDAFGPASEI 547
Cdd:TIGR01187 148 EQL-GITFVFVTHdqEEAMTMS-DRIAIMRKGKIAQIGTPEEI 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-547 |
3.63e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwaptharadTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP---TWDRK 395
Cdd:COG1129 256 VLEVEGL----------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsPRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGgyIGYLAQDVQ----LLPGSIAENI--ARFDAGVSDANITEAASRAQAHALIT--GLKQGyqtTMEAAGGSLSGGTR 467
Cdd:COG1129 326 RAG--IAYVPEDRKgeglVLDLSIRENItlASLDRLSRGGLLDRRRERALAEEYIKrlRIKTP---SPEQPVGNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 468 QRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHR-PAIVLKCDKALVLRNGAVDAFGPASE 546
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIVGELDREE 480
|
.
gi 517342213 547 I 547
Cdd:COG1129 481 A 481
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-521 |
3.72e-23 |
|
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: 98.11 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 331 HARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP---TGGTIALDGADYptwDRKQLGGYIGYLAQD 407
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR---KPDQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 408 VQLLPGSIAENIARFDAGVSDANITEAASRaQAHALITGLKqgyQTTMEAAGGS----LSGGTRQRIGLARAFFGNPKLL 483
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLPRKSSDAIR-KKRVEDVLLR---DLALTRIGGNlvkgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 517342213 484 ILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRP 521
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
9-280 |
4.41e-23 |
|
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: 99.51 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AFIASISSP------KAAMGDIQPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVA 162
Cdd:cd18783 81 TFDRLLSLPidfferTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 163 S--HYATRSAAGKAQEAAVAANLlaqaftrnRETVQGMGMIGHVT------ERWGRRFADAANLQDGASAINAIFAGSSR 234
Cdd:cd18783 161 FlpPFRRRLQALYRAEGERQAFL--------VETVHGIRTVKSLAleprqrREWDERVARAIRARFAVGRLSNWPQTLTG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 517342213 235 TLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLV 280
Cdd:cd18783 233 PLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLA 278
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
340-536 |
5.27e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.96 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWD---RKQLGGY-IGYLAQDVQLLPGSI 415
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 A-ENIArFDAGVSDANITEAASRAQAHALITGL-KQGYQTTMEaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK11629 104 AlENVA-MPLLIGKKKPAEINSRALEMLAAVGLeHRANHRPSE-----LSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517342213 494 AEGEAALERALLQA-KAGGTTVIIVTHRPAIVLKCDKALVLRNG 536
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
340-549 |
6.71e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.79 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQLGgyIGYLAQDvqllpGSI- 415
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithLPMHKRARLG--IGYLPQE-----ASIf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 -----AENIArfdAGVSDANITEAASRAQAHAL-----ITGLKqgyqttmEAAGGSLSGGTRQRIGLARAFFGNPKLLIL 485
Cdd:COG1137 91 rkltvEDNIL---AVLELRKLSKKEREERLEELleefgITHLR-------KSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 486 DEPNSNLD--AEGEaaLERALLQAKAGGTTVIIVTHRpaiV---LK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:COG1137 161 DEPFAGVDpiAVAD--IQKIIRHLKERGIGVLITDHN---VretLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-556 |
7.53e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 103.84 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadyptwdrkQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ArFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:TIGR01271 508 I-FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 500 L-ERALLQAKAGGTTvIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEilqrLSGAKP 556
Cdd:TIGR01271 587 IfESCLCKLMSNKTR-ILVTSKLEHLKKADKILLLHEGVCYFYGTFSE----LQAKRP 639
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
343-493 |
7.88e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.81 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGyigyLAQDVQLL---P-GS---- 414
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRMQMVfqdPyASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 ------IAENIARFDAGvsdaniTEAASRAQAHALIT--GLKQgyqttmEAAG---GSLSGGTRQRIGLARAFFGNPKLL 483
Cdd:COG4608 112 mtvgdiIAEPLRIHGLA------SKAERRERVAELLElvGLRP------EHADrypHEFSGGQRQRIGIARALALNPKLI 179
|
170
....*....|
gi 517342213 484 ILDEPNSNLD 493
Cdd:COG4608 180 VCDEPVSALD 189
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
338-547 |
9.56e-23 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 98.39 E-value: 9.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 338 AAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadyptwdrkQLGGYIGYLAQDVQLLPGSIAE 417
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIArfdAGVS-DANITEAASRA-QAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:cd03291 117 NII---FGVSyDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 496 GEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEI 547
Cdd:cd03291 194 TEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
341-547 |
1.05e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRK---QLGgyIGYLAQDVQLLPG-SIA 416
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLG--IGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENI------ARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK09700 99 ENLyigrhlTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
314-519 |
1.47e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.41 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 314 PEPEGRLTVKNL--FWAPTHAradtsaaiIKDVSFDLKPGHVLAILGPSGSGKSSLAR-------LLAGVAepTGGTIAL 384
Cdd:COG1117 6 STLEPKIEVRNLnvYYGDKQA--------LKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 385 DGAD-Y-PTWD----RKQlggyIGYLAQDVQLLPGSIAENIArfdAGVSDANITeaaSRAQAHALI-TGLKQgyqttmeA 457
Cdd:COG1117 76 DGEDiYdPDVDvvelRRR----VGMVFQKPNPFPKSIYDNVA---YGLRLHGIK---SKSELDEIVeESLRK-------A 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 458 A------------GGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALErALLQAKAGGTTVIIVTH 519
Cdd:COG1117 139 AlwdevkdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIE-ELILELKKDYTIVIVTH 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
331-537 |
1.53e-22 |
|
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: 96.35 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 331 HARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI-------ALDGADYPTWD----RKQlgg 399
Cdd:COG4778 17 HLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREilalRRR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQDVQLLPGSIAENI---ARFDAGVSdanitEAASRAQAHALITGLK------QGYQTTmeaaggsLSGGTRQRI 470
Cdd:COG4778 94 TIGYVSQFLRVIPRVSALDVvaePLLERGVD-----REEARARARELLARLNlperlwDLPPAT-------FSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 471 GLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGA 537
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-550 |
1.71e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.49 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWaptHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG---ADYPTWDRKQ 396
Cdd:PRK13650 5 IEVKNLTF---KYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 LggyIGYLAQ--DVQLLPGSIAENIArFdaGVSDANIT--EAASRA-QAHALItglkqGYQTTMEAAGGSLSGGTRQRIG 471
Cdd:PRK13650 82 K---IGMVFQnpDNQFVGATVEDDVA-F--GLENKGIPheEMKERVnEALELV-----GMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 472 LARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
340-547 |
1.72e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.64 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRkqlggYIGYLAQDVQLLPG-SI 415
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithVPAENR-----HVNTVFQSYALFPHmTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIArFD---AGVSDANITEAASRAQAHALITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:PRK09452 104 FENVA-FGlrmQKTPAAEITPRVMEALRMVQLEEFAQRKPH-------QLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 493 DAE--GEAALERALLQAKAgGTTVIIVTH--RPAIVLKcDKALVLRNGAVDAFGPASEI 547
Cdd:PRK09452 176 DYKlrKQMQNELKALQRKL-GITFVFVTHdqEEALTMS-DRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
339-521 |
3.03e-22 |
|
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: 94.87 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIAL----DGADYPTWDRKQLggYIGYLAQDVQLLpgS 414
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpLDFQRDSIARGLL--YLGHAPGIKTTL--S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAGVSDANITEAASRAqahalitGLKqGYQttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARV-------GLN-GFE---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*..
gi 517342213 495 EGEAALERALLQAKAGGTTVIIVTHRP 521
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
341-552 |
3.72e-22 |
|
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: 100.26 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIA-------LDGADYPTWDRKQLGGYIGYLAQDVQLLP- 412
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 GSIAENIARfdaGVSDANITEAASRAQAHALIT-GLKQGY-QTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:TIGR03269 380 RTVLDNLTE---AIGLELPDELARMKAVITLKMvGFDEEKaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 491 NLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQRLS 552
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEELT 520
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
340-549 |
6.85e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQdVQLLPGSIA--E 417
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHLTPEGITvrE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIARfdaGVSDANITEAASRAQAHALITGLKQGYQTT--MEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:PRK11231 96 LVAY---GRSPWLSLWGRLSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 496 GEAALERALLQAKAGGTTVIIVTH------RpaivlKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK11231 173 HQVELMRLMRELNTQGKTVVTVLHdlnqasR-----YCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-519 |
1.01e-21 |
|
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: 98.85 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadyptwdRKQLGGYIGYLAQDVQLLP------- 412
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-----------RPQPGIKVGYLPQEPQLDPtktvren 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 -----GSIAENIARFDAgVSDAnitEAASRAQAHALITglKQG-YQTTMEAAGG------------------------SL 462
Cdd:TIGR03719 89 veegvAEIKDALDRFNE-ISAK---YAEPDADFDKLAA--EQAeLQEIIDAADAwdldsqleiamdalrcppwdadvtKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 463 SGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAggtTVIIVTH 519
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-538 |
1.03e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP---TWDRKQLGgyIGYLAQDVQLLPG-SIAE 417
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsPRDAIALG--IGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIArfdAGVSDANITeAASRAQAHALITGLkqgyqttMEAAG---------GSLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:COG3845 100 NIV---LGLEPTKGG-RLDRKAARARIREL-------SERYGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 489 NSNLDAEGEAALERALLQAKAGGTTVIIVTHRpaivLK-----CDKALVLRNGAV 538
Cdd:COG3845 169 TAVLTPQEADELFEILRRLAAEGKSIIFITHK----LRevmaiADRVTVLRRGKV 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
341-519 |
1.04e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKqlggyIGYLAQDVQLLPG-SIA 416
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQRP-----INMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArfdAGVSDANITEAASRAQAHALITGLKQgyQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA-- 494
Cdd:PRK11607 110 QNIA---FGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKkl 184
|
170 180 190
....*....|....*....|....*....|.
gi 517342213 495 ------EGEAALERAllqakagGTTVIIVTH 519
Cdd:PRK11607 185 rdrmqlEVVDILERV-------GVTCVMVTH 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
335-561 |
1.48e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.03 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG----YIGYLAQDVQL 410
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPGSIAENIARFDAGVsdANITEAASRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK10535 98 LSHLTAAQNVEVPAVY--AGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAfGPASEILQRLSGAKPRPVNA 561
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGGTEPVVNT 243
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
339-521 |
2.05e-21 |
|
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: 92.42 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGGYIGYLAQdvqlLPG----- 413
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGH----LPGlkpel 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIARFDAGVSDANITeaASRAQAHALITGLKQgyqttmeAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRT--IEDALAAVGLTGFED-------LPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*...
gi 517342213 494 AEGEAALERALLQAKAGGTTVIIVTHRP 521
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
337-533 |
2.27e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadyptwdrkqlGGYIGYLAQDVQL---LPG 413
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIA--RFDAGVSDANITEAASRAQAHAL----ITGLKqgyqttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:NF040873 73 TVRDLVAmgRWARRGLWRRLTRDDRAAVDDALervgLADLA-------GRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517342213 488 PNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVL 533
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
337-550 |
2.30e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.94 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPtwDRKQLGGYIGYLAQDVQLLPG-SI 415
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA---RFdAGVSDANITEAASRAQAHALITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:PRK11432 96 GENVGyglKM-LGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 493 DAEgeaaLERAL------LQAKAGGTTvIIVTHRPAIVLKC-DKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK11432 168 DAN----LRRSMrekireLQQQFNITS-LYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
340-561 |
2.35e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGvSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:PLN03232 1331 DPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 500 LERAlLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSGAKPRPVNA 561
Cdd:PLN03232 1410 IQRT-IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
319-549 |
2.92e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.03 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwapthARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRK 395
Cdd:PRK10895 3 TLTAKNL------AKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDislLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 396 QLGgyIGYLAQDvqllpGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTT--MEAAGGSLSGGTRQRIGLA 473
Cdd:PRK10895 77 RRG--IGYLPQE-----ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 474 RAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-547 |
4.44e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.57 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADypTWD--------RKQLGGYIGYlaQDVQLLP 412
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD--ITDkkvklsdiRKKVGLVFQY--PEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 GSIAENIArF---DAGVSDANITEAASRAQAhalITGLKqgYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:PRK13637 99 ETIEKDIA-FgpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 490 SNLDAEG-EAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK13637 173 AGLDPKGrDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
9-286 |
5.77e-21 |
|
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: 93.38 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AFIASISSPKA-----AMGDI-QPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVA 162
Cdd:cd18779 81 FLEHLLRLPYRffqqrSTGDLlMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 163 SHyatrsaagKAQEAAVAANLLAQAFTRNR--------ETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSR 234
Cdd:cd18779 161 TR--------RRVRELMARELAAQAEAQSYlvealsgiETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 235 TLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQI 286
Cdd:cd18779 233 TLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQL 284
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
340-519 |
6.61e-21 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 91.32 E-value: 6.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWD-------RKQLggyIGYLAQDVQLLP 412
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSysqkiilRREL---IGYIFQSFNLIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 G-SIAENIA-----RfdaGVSDANITEAASRAQAHALITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:NF038007 97 HlSIFDNVAlplkyR---GVAKKERIERVNQVLNLFGIDNRRNHKPM-------QLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190
....*....|....*....|....*....|...
gi 517342213 487 EPNSNLDAEGEAALERALLQAKAGGTTVIIVTH 519
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-517 |
7.87e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 319 RLTVKNLfwaptHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQ-- 396
Cdd:COG3845 257 VLEVENL-----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 -LGgyIGYLAQDVQ---LLPG-SIAENIA--RFDAG--VSDANITEAASRAQAHALItglkQGYQ---TTMEAAGGSLSG 464
Cdd:COG3845 332 rLG--VAYIPEDRLgrgLVPDmSVAENLIlgRYRRPpfSRGGFLDRKAIRAFAEELI----EEFDvrtPGPDTPARSLSG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517342213 465 GTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIV 517
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
9-296 |
8.22e-21 |
|
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: 92.89 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 ----------AFIASISSpkaamGDI-QPLRDLATTRSFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMI 157
Cdd:cd18570 81 yfkhllklplSFFETRKT-----GEIiSRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 158 LMVVASHYATRSAAGKAQE--AAVAANLLaqaftrnrETVQGMGMI------GHVTERWGRRFADAANLQDGASAINAIF 229
Cdd:cd18570 156 LIILLFNKPFKKKNREVMEsnAELNSYLI--------ESLKGIETIkslnaeEQFLKKIEKKFSKLLKKSFKLGKLSNLQ 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 230 AGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18570 228 SSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-523 |
9.61e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 89.52 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgaDYPTwdrkqlGGYIGYLAQDVQLLPGS 414
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPE------GEDLLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIArfdagvsdaniteaasraqahalitglkqgYQTTMEaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:cd03223 80 LREQLI------------------------------YPWDDV-----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*....
gi 517342213 495 EGEAALERALlqaKAGGTTVIIVTHRPAI 523
Cdd:cd03223 125 ESEDRLYQLL---KELGITVISVGHRPSL 150
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
340-545 |
1.53e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA--DYPTW----DRKQLGGYIGYLAQDVQLLPG 413
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKpsekAIRLLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIarFDAGVSDANITEAASRAQAHALITGLKqgYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:COG4161 97 lTVMENL--IEAPCKVLGLSKEQAREKAMKLLARLR--LTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517342213 493 DAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPAS 545
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-550 |
1.88e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 94.75 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVaEPTGGTIALDGADYPTWDRKQLGGyigyLAQDVQLL---P-GS--- 414
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRP----LRRRMQVVfqdPfGSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 -------IAENIARFDAGVSDANITEAASRAqahalitglkqgyqttMEAAGGS----------LSGGTRQRIGLARAFF 477
Cdd:COG4172 378 rmtvgqiIAEGLRVHGPGLSAAERRARVAEA----------------LEEVGLDpaarhrypheFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 478 GNPKLLILDEPNSNLDAEGEA---ALERAlLQAKAGGTTVIIvTHRPAIV--LkCDKALVLRNGAVDAFGPASEILQR 550
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAqilDLLRD-LQREHGLAYLFI-SHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
323-493 |
2.56e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.33 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 323 KNLFWAPTHARAdtsaaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQlgg 399
Cdd:PRK11308 19 RGLFKPERLVKA------LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkADPEAQKL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 yigyLAQDVQLL---P----------GSIAEniarfDAGVSDANITEAASRAQAHALIT--GLK-QGYQTT--Meaaggs 461
Cdd:PRK11308 90 ----LRQKIQIVfqnPygslnprkkvGQILE-----EPLLINTSLSAAERREKALAMMAkvGLRpEHYDRYphM------ 154
|
170 180 190
....*....|....*....|....*....|..
gi 517342213 462 LSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
340-548 |
2.89e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.58 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI-----ALDGADYPTWDR---KQLGGYIGYLAQDVQLL 411
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 412 PG-SIAENIarfdagVSDANITEAASRAQAHALITGL--KQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:PRK11264 98 PHrTVLENI------IEGPVIVKGEPKEEATARARELlaKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 489 NSNLDAE--GEA-ALERALLQAKaggTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK11264 172 TSALDPElvGEVlNTIRQLAQEK---RTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-553 |
3.05e-20 |
|
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: 90.74 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARfDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03288 116 DP-ECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517342213 500 LERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSG 553
Cdd:cd03288 195 LQKVVMTAFA-DRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
9-296 |
3.15e-20 |
|
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: 91.47 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVR----AVYCQRVALSLDKH 84
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRqyllDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 85 FGEDAF---IASISSPKAamGDIqplrdlaTTR--------SFVASKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAG- 152
Cdd:cd18568 81 FYKHLLslpLSFFASRKV--GDI-------ITRfqenqkirRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 153 AAVMILMVVASHYATRSAAGKAQEAAVAANLLAQAFTrNRETVQGMGMIGHVTERWGRRFADAANLQDGAS--AINAIFA 230
Cdd:cd18568 152 PLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALT-GIATIKALAAERPIRWRWENKFAKALNTRFRGQklSIVLQLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 231 GSsrTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18568 231 SS--LINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
340-553 |
3.31e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.48 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLL------------AGVAEPTG---------------------------- 379
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhiVFKNEHTNdmtneqdyqgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 380 --------------GTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI--ARFDAGVSDanITEAASRAQAHAL 443
Cdd:PTZ00265 1263 eggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIkfGKEDATRED--VKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 444 ITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAK-AGGTTVIIVTHRPA 522
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIA 1420
|
250 260 270
....*....|....*....|....*....|....*.
gi 517342213 523 IVLKCDKALVL----RNGA-VDAFGPASEILQRLSG 553
Cdd:PTZ00265 1421 SIKRSDKIVVFnnpdRTGSfVQAHGTHEELLSVQDG 1456
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
338-542 |
3.48e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.40 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 338 AAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA---DYPTWDRKqlggyIGYLAQDVQLLPG- 413
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG-----VGMVFQSYALYPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIArFDAGVSDANITEAASRAQAHALITGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK11000 91 SVAENMS-FGLKLAGAKKEEINQRVNQVAEVLQLAH----LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 494 aegeAAL------ERALLQAKAgGTTVIIVTHR--PAIVLkCDKALVLRNGAVDAFG 542
Cdd:PRK11000 166 ----AALrvqmriEISRLHKRL-GRTMIYVTHDqvEAMTL-ADKIVVLDAGRVAQVG 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
341-548 |
3.81e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDgaDYPTwdrkQLGGYiGYLAQDVQLL--PGSIAEN 418
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID--DHPL----HFGDY-SYRSQRIRMIfqDPSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IARFDAGVSDANI---TEAASRAQAHALITGLKQ--------GYQTTMeaaggsLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:PRK15112 102 PRQRISQILDFPLrlnTDLEPEQREKQIIETLRQvgllpdhaSYYPHM------LAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 488 PNSNLDAEGEAALERAL--LQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK15112 176 ALASLDMSMRSQLINLMleLQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
340-557 |
4.49e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALD----GADYPTWDR------------KQLGGYIGY 403
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELitnpyskkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 404 LAQ--DVQLLPGSIAENI--ARFDAGVSDaniTEAASRAQAHALITGLKQGYqttMEAAGGSLSGGTRQRIGLARAFFGN 479
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDImfGPVALGVKK---SEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 480 PKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI------LQRLS 552
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIftdqhiINSTS 274
|
....*
gi 517342213 553 GAKPR 557
Cdd:PRK13631 275 IQVPR 279
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
351-542 |
5.14e-20 |
|
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: 88.70 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 351 GHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKqlggyIGYLAQDVQLLPG-SIAENIarfDAGV 426
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaaPPADRP-----VSMLFQENNLFAHlTVEQNV---GLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 427 SDANITEAASRAQAHALITglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDaegeAALERALLQ 506
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALA--RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD----PALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 507 AKAG-----GTTVIIVTHRPAIVLKCDKALV-LRNGAVDAFG 542
Cdd:cd03298 170 LVLDlhaetKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-550 |
6.29e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRkQLGGYIGYLAQDVQLLPG-SIAEN 418
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVGVVPQFDNLDPDfTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IARFDAGVsdaniteAASRAQAHALITGLKQ--GYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:PRK13537 101 LLVFGRYF-------GLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 497 EAALERALLQAKAGGTTVIIVTH--RPAIVLkCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTHfmEEAERL-CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
341-547 |
1.06e-19 |
|
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: 88.20 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKQlggyIGYLAQDVQLLPGSIA- 416
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrePREVRRR----IGIVFQDLSVDDELTGw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIARFDA--GVSDANITEAASRAQAhalitglkqgYQTTMEAAG---GSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:cd03265 92 ENLYIHARlyGVPGAERRERIDELLD----------FVGLLEAADrlvKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 492 LDAEGEAALERALLQAKA-GGTTVIIVTH--RPAIVLkCDKALVLRNGAVDAFGPASEI 547
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEeFGMTILLTTHymEEAEQL-CDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-519 |
1.15e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 92.49 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP-TGGTIALDGADyptwdrkqlggyIGYLAQDVQLLP------ 412
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEfEGEARPAPGIK------------VGYLPQEPQLDPektvre 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 ------GSIAENIARFDAgVSDAnitEAASRAQAHALITglKQG-YQTTMEAAGG------------------------S 461
Cdd:PRK11819 90 nveegvAEVKAALDRFNE-IYAA---YAEPDADFDALAA--EQGeLQEIIDAADAwdldsqleiamdalrcppwdakvtK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 462 LSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERaLLQAKAGgtTVIIVTH 519
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ-FLHDYPG--TVVAVTH 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
318-577 |
1.16e-19 |
|
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: 93.82 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 318 GRLTVKNLfwapTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEpTGGTIALDGADYPTWDRKQL 397
Cdd:TIGR01271 1216 GQMDVQGL----TAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 398 GGYIGYLAQDVQLLPGSIAENIARFdAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFF 477
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSGTFRKNLDPY-EQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 478 GNPKLLILDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSGAKPR 557
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS-NCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQA 1448
|
250 260
....*....|....*....|....*
gi 517342213 558 PVNANRVSV-----RNKSETADAPE 577
Cdd:TIGR01271 1449 MSAADRLKLfplhrRNSSKRKPQPK 1473
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
9-280 |
1.28e-19 |
|
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: 89.44 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 9 RRAWVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGED 88
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 89 AFIASISSP-----KAAMGDI-------QPLRDLATTrSFVASkglanLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVM 156
Cdd:cd18567 81 LFRHLLRLPlsyfeKRHLGDIvsrfgslDEIQQTLTT-GFVEA-----LLDGLMAILTLVMMFLYSPKLALIVLAAVALY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 157 ILMVVASHYATRSAAGKAQEAAVAAN--LLaqaftrnrETVQGMGMI---GHVTER---WGRRFADAANLQDGASAINAI 228
Cdd:cd18567 155 ALLRLALYPPLRRATEEQIVASAKEQshFL--------ETIRGIQTIklfGREAERearWLNLLVDAINADIRLQRLQIL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 229 FAGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFA----SSTISGRALQPIDQLV 280
Cdd:cd18567 227 FSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAflayKDQFSSRASSLIDKLF 282
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-562 |
1.32e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP---TGGTIALDGADYptwDRKQLGGYIGYLAQDVQLLPGSIA 416
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIARFDAGVS-DANITEAASRAQAHALIT--GLKQGYQTTMEAAGG--SLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:TIGR00955 117 REHLMFQAHLRmPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 492 LDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKC--DKALVLRNGAVDAFGPASEILQRLS-GAKPRPVNAN 562
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSdLGHPCPENYN 270
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
341-548 |
2.96e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA--DYPTWDRKQLGGYIGYLAQ--DVQLLPGSIA 416
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQdpDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIA--RFDAGVSDANITEAASRAQAHALITGLKqgyqttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK13636 102 QDVSfgAVNLKLPEDEVRKRVDNALKRTGIEHLK-------DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 495 EGEAALERALLQ-AKAGGTTVIIVTHRPAIV-LKCDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK13636 175 MGVSEIMKLLVEmQKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-547 |
3.19e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP---TWDRKqlggyIGYLAQDVQLLPG-SI 415
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlhARDRK-----VGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA----------RFDAGVSDANITEAASRAQ-AHalitgLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK10851 92 FDNIAfgltvlprreRPNAAAIKAKVTQLLEMVQlAH-----LADRYPA-------QLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 485 LDEPNSNLDAEGEAALERAL--LQAKAGGTTViIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLrqLHEELKFTSV-FVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
341-548 |
3.27e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.09 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY----IGYLAQDVQLLPG-SI 415
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIArfdAGVSDANITEAASRAQAhalITGLKQ-GYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK10070 124 LDNTA---FGMELAGINAEERREKA---LDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 495 --EGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK10070 198 liRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
340-519 |
7.50e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.68 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRkqlGGYIGYLAQDVQLlpG--- 413
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKR---AKYIGRVFQDPMM--Gtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 --SIAENIA---------RFDAGVSDANiteaasRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKL 482
Cdd:COG1101 96 smTIEENLAlayrrgkrrGLRRGLTKKR------RELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517342213 483 LILDEPNSNLD---AEGEAALERALLQAKagGTTVIIVTH 519
Cdd:COG1101 170 LLLDEHTAALDpktAALVLELTEKIVEEN--NLTTLMVTH 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
317-550 |
8.93e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 317 EGRLTVKNLFWAPTHARADTSAAIiKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadYPTWdrkq 396
Cdd:COG1134 19 EPSRSLKELLLRRRRTRREEFWAL-KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 L----GGYIGYLaqdvqllpgSIAENIaRFDA---GVSDANITEAASRAQAHAlitGLKQGYQTTMeaagGSLSGGTRQR 469
Cdd:COG1134 92 LlelgAGFHPEL---------TGRENI-YLNGrllGLSRKEIDEKFDEIVEFA---ELGDFIDQPV----KTYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 470 IGLARAFFGNPKLLILDEpnsNL---DAE-GEAALERaLLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPA 544
Cdd:COG1134 155 LAFAVATAVDPDILLVDE---VLavgDAAfQKKCLAR-IRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
....*.
gi 517342213 545 SEILQR 550
Cdd:COG1134 231 EEVIAA 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
335-547 |
9.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 9.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA--DYPTWD----RKQLGgyIGYLAQDV 408
Cdd:PRK13639 14 GTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSllevRKTVG--IVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 409 QLLPGSIAENIA--RFDAGVSDANITEAASRAqahalitgLK----QGYQttmEAAGGSLSGGTRQRIGLARAFFGNPKL 482
Cdd:PRK13639 90 QLFAPTVEEDVAfgPLNLGLSKEEVEKRVKEA--------LKavgmEGFE---NKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 483 LILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIV-LKCDKALVLRNGAVDAFGPASEI 547
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-555 |
1.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.29 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 323 KNLFWAPTHARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP----TWDRKQLG 398
Cdd:PRK13633 8 KNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 399 GYIgYLAQDVQLLPGSIAENIArF---DAGVSDANITEAASRAqahalitgLKQ-GYQTTMEAAGGSLSGGTRQRIGLAR 474
Cdd:PRK13633 88 GMV-FQNPDNQIVATIVEEDVA-FgpeNLGIPPEEIRERVDES--------LKKvGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSG 553
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEM 237
|
..
gi 517342213 554 AK 555
Cdd:PRK13633 238 MK 239
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-536 |
1.19e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGyIGYLAQ-DVQLLPGSIAE 417
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQfDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIARFDA--GVSDANITEAASRAQAHALItglkqgyQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:PRK13536 134 NLLVFGRyfGMSTREIEAVIPSLLEFARL-------ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 496 GEAALERALLQAKAGGTTVIIVTH--RPAIVLkCDKALVLRNG 536
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHfmEEAERL-CDRLCVLEAG 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
340-535 |
1.22e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIAL-DGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAEN 418
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 I----------------------ARFD------------AG-----------------------VSDANITEAASRAQAH 441
Cdd:PTZ00265 480 IkyslyslkdlealsnyynedgnDSQEnknkrnscrakcAGdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 442 ALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTV-IIVTHR 520
Cdd:PTZ00265 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHR 639
|
250
....*....|....*
gi 517342213 521 PAIVLKCDKALVLRN 535
Cdd:PTZ00265 640 LSTIRYANTIFVLSN 654
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
341-519 |
1.33e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.60 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAE-----PTGGTIALDGADY--PTWDRKQLGGYIGYLAQDVQLLPG 413
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIA---RFdAGVSDANITEAASRaqahaliTGLKQG-----YQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLIL 485
Cdd:PRK14239 101 SIYENVVyglRL-KGIKDKQVLDEAVE-------KSLKGAsiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....
gi 517342213 486 DEPNSNLDAEGEAALERALLQAKAgGTTVIIVTH 519
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKD-DYTMLLVTR 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-548 |
1.68e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.48 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA------DYPTWDRKQLGGYIGYLAQDVQLLP 412
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 G-SIAENIAR--FDAGVSDA----NITEAASRAqahaliTGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLIL 485
Cdd:PRK14246 104 HlSIYDNIAYplKSHGIKEKreikKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 486 DEPNSNLDAEGEAALERALLQAKaGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
344-554 |
1.82e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.80 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENIARFD 423
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 424 AGvSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERA 503
Cdd:PLN03130 1338 EH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 504 LLQA-KAggTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSGA 554
Cdd:PLN03130 1417 IREEfKS--CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSA 1466
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
340-549 |
2.23e-18 |
|
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: 89.62 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFdAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEaA 499
Cdd:TIGR00957 1381 DPF-SQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-N 1458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517342213 500 LERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
340-542 |
2.88e-18 |
|
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: 84.12 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDrkqLGGyiGYLAQdvqlLPGSiaENI 419
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG---LGG--GFNPE----LTGR--ENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 aRFDAGVSDANITEAASRAQAHALITGLKQGYQTTMeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:cd03220 106 -YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517342213 500 LERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFG 542
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
344-548 |
4.51e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.83 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAePTGGTIALDGADYPTWDRKQLGGYIGYLAQDVqllPGSIAENIARFD 423
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQ---TPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 424 AGVSDANITEAASRAQAHALITGLKqgYQTTMEAAGGSLSGGTRQRIGLARAFF-----GNP--KLLILDEPNSNLDAEG 496
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEVAEALG--LDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517342213 497 EAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
337-533 |
4.74e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 337 SAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIA 416
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArFDAGVSDaniteaaSRAQAHALITGLKQGY--QTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK10247 99 DNLI-FPWQIRN-------QQPDPAIFLDDLERFAlpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517342213 495 EGEAALERALLQ-AKAGGTTVIIVTHRPAIVLKCDKALVL 533
Cdd:PRK10247 171 SNKHNVNEIIHRyVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
346-538 |
5.60e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 82.99 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 346 FDL--KPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKqlggyIGYLAQDVQLLPG-SIAENI 419
Cdd:TIGR01277 17 FDLnvADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtglAPYQRP-----VSMLFQENNLFAHlTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ArfdAGVSDANITEAASRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA---EG 496
Cdd:TIGR01277 92 G---LGLHPGLKLNAEQQEKVVDAAQQV--GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPllrEE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 497 EAALERALLQAKAggTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:TIGR01277 167 MLALVKQLCSERQ--RTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
340-554 |
6.00e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD----------YPTWDRKQLGGYIGYLAQDVQ 409
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 410 LLP----GSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAaggSLSGGTRQRIGLARAFFGNPKLLIL 485
Cdd:PRK10619 100 HFNlwshMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPV---HLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 486 DEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALV-LRNGAVDAFGPASEIL---------QRLSGA 554
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIfLHQGKIEEEGAPEQLFgnpqsprlqQFLKGS 255
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
346-548 |
6.86e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 82.98 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 346 FDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRkqlggYIGYLAQDVQL---LPGSIAENIARF 422
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWR-----HIGYVPQRHEFawdFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 423 DAGVSD--ANITEAASRAQAHALITglkQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAAL 500
Cdd:TIGR03771 76 RTGHIGwlRRPCVADFAAVRDALRR---VGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517342213 501 ERALLQAKAGGTTVIIVTHR-PAIVLKCDKaLVLRNGAVDAFGPASEIL 548
Cdd:TIGR03771 153 TELFIELAGAGTAILMTTHDlAQAMATCDR-VVLLNGRVIADGTPQQLQ 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-538 |
1.56e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.67 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNL--FWAPTHAradtsaaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQL 397
Cdd:PRK11701 7 LSVRGLtkLYGPRKG--------CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 398 G------------GYIGYLAQDVQLLPGSIAENIARFDAGVSD---ANITEAASRAQAHALITGLKqgyqttMEAAGGSL 462
Cdd:PRK11701 79 SeaerrrllrtewGFVHQHPRDGLRMQVSAGGNIGERLMAVGArhyGDIRATAGDWLERVEIDAAR------IDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 463 SGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA---LERALLQAKagGTTVIIVTHRPAIV-LKCDKALVLRNGAV 538
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARlldLLRGLVREL--GLAVVIVTHDLAVArLLAHRLLVMKQGRV 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
320-557 |
2.00e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.51 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNL---FwapthARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKS----SLARLLAGVAEPTGGTIALDGADYPTW 392
Cdd:COG4172 7 LSVEDLsvaF-----GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 393 DRKQL----GGYIGYLAQDvqllPGS-----------IAENIARFDAgvsdanITEAASRAQAHALI--TGLKqgyqttm 455
Cdd:COG4172 82 SERELrrirGNRIAMIFQE----PMTslnplhtigkqIAEVLRLHRG------LSGAAARARALELLerVGIP------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 456 EAAG--GS----LSGGTRQRIGLARAFFGNPKLLILDEPNSNLD----AEGEAALERalLQAKAgGTTVIIVTHRPAIVL 525
Cdd:COG4172 145 DPERrlDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKD--LQREL-GMALLLITHDLGVVR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 517342213 526 K-CDKALVLRNGAVDAFGPASEIL--------QRLSGAKPR 557
Cdd:COG4172 222 RfADRVAVMRQGEIVEQGPTAELFaapqhpytRKLLAAEPR 262
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
342-547 |
2.00e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.70 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDVQLLPG-SIAE 417
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqIGMIFQHFNLLSSrTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIArFD---AGVSDANIteaasRAQAHAL-----ITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:PRK11153 102 NVA-LPlelAGTPKAEI-----KARVTELlelvgLSDKADRYPA-------QLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 490 SNLDAEgeaaLERALLQAKAG-----GTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK11153 169 SALDPA----TTRSILELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
341-524 |
2.56e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQ---LGGYIGYLAQDVQLL-PGSIA 416
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIA--RFDAGVSDANITEAASRAQAhalitglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK10908 98 DNVAipLIIAGASGDDIRRRVSAALD-------KVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190
....*....|....*....|....*....|
gi 517342213 495 EGEAALERALLQAKAGGTTVIIVTHRPAIV 524
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
310-550 |
3.85e-17 |
|
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: 85.77 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 310 RLILPEPEGRLTVKNLFWapTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAdy 389
Cdd:TIGR00957 627 RTIKPGEGNSITVHNATF--TWARDLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 390 ptwdrkqlggyIGYLAQDVQLLPGSIAENIarfdagVSDANITEAASRA--QAHALITGLK---QGYQTTMEAAGGSLSG 464
Cdd:TIGR00957 701 -----------VAYVPQQAWIQNDSLRENI------LFGKALNEKYYQQvlEACALLPDLEilpSGDRTEIGEKGVNLSG 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 465 GTRQRIGLARAFFGNPKLLILDEPNSNLDAE-GEAALERAL-LQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFG 542
Cdd:TIGR00957 764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
|
....*...
gi 517342213 543 PASEILQR 550
Cdd:TIGR00957 844 SYQELLQR 851
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-550 |
4.83e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGV--AEPT------------------------------GGTIALDGA 387
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTsgriiyhvalcekcgyverpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 388 DYptWD-----RKQLGGYIGYLAQDVQLLPG--SIAENIARfdaGVSDANITEAASRAQAHALITGLKQGYQTTMEAAgg 460
Cdd:TIGR03269 95 DF--WNlsdklRRRIRKRIAIMLQRTFALYGddTVLDNVLE---ALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIAR-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 461 SLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQA-KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
250
....*....|..
gi 517342213 539 DAFGPASEILQR 550
Cdd:TIGR03269 248 KEEGTPDEVVAV 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
345-493 |
6.92e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 345 SFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY---PTWDRKqlggyIGYLAQDVQLLPG-SIAENIA 420
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHtttPPSRRP-----VSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 421 rfdAGVSDANITEAASRAQAHALITglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK10771 94 ---LGLNPGLKLNAAQREKLHAIAR--QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
310-549 |
7.18e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 310 RLILPEPEGRLTVKNLfwaptharadtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD- 388
Cdd:PRK10762 248 RLDKAPGEVRLKVDNL-----------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEv 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 389 YPTWDRKQLGGYIGYLAQDVQ----LLPGSIAEN--IARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSL 462
Cdd:PRK10762 317 VTRSPQDGLANGIVYISEDRKrdglVLGMSVKENmsLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 463 SGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHR-PAIVLKCDKALVLRNGAVDAF 541
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGE 476
|
....*...
gi 517342213 542 GPASEILQ 549
Cdd:PRK10762 477 FTREQATQ 484
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
343-568 |
7.65e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG--ADYPTwDRKQLGGYIGYLAQDVQLLPG-SIAENI 419
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFAS-TTAALAAGVAIIYQELHLVPEmTVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ------ARFdaGVsdanITEAASRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK11288 101 ylgqlpHKG--GI----VNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 494 AEGEAALERALLQAKAGGTTVIIVTHR-PAIVLKCDKALVLRNGA-VDAFGPASEI-------------LQRLSGAKPRP 558
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSHRmEEIFALCDAITVFKDGRyVATFDDMAQVdrdqlvqamvgreIGDIYGYRPRP 252
|
250
....*....|
gi 517342213 559 VNANRVSVRN 568
Cdd:PRK11288 253 LGEVRLRLDG 262
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
344-549 |
1.13e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPG-SIAENIA-- 420
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGmTVRELVAig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 421 ---------RFdaGVSDANITEaasraQAHALItGLKQGYQTTMEaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:PRK10575 110 rypwhgalgRF--GAADREKVE-----EAISLV-GLKPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 492 LDAEGEA---ALERALLQAKagGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK10575 178 LDIAHQVdvlALVHRLSQER--GLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
340-523 |
1.13e-16 |
|
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: 83.64 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadypTWDRKqlgGYIGYLAQDVQLLPGSIAENI 419
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL--------TKPAK---GKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 A-------RFDAGVSDANITEAASRAQAHALITglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:TIGR00954 536 IypdssedMKRRGLSDKDLEQILDNVQLTHILE--REGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180 190
....*....|....*....|....*....|.
gi 517342213 493 DAEGEAALERAllqAKAGGTTVIIVTHRPAI 523
Cdd:TIGR00954 614 SVDVEGYMYRL---CREFGITLFSVSHRKSL 641
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
15-296 |
1.15e-16 |
|
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: 80.67 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 15 VIFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVA---------------L 79
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGqrvvfdlrrdlfrhlQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 80 SLDKHFGEDAFIASISSpkAAMGDIQPLRDLATTrsfvaskGLANLIDLPFAPIFA-VILYCIHPVLCLVTVAGAAVMIL 158
Cdd:cd07346 84 RLSLSFFDRNRTGDLMS--RLTSDVDAVQNLVSS-------GLLQLLSDVLTLIGAlVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 159 MVVASHYATRSAAGKAQEA-AVAANLLAQAFTrNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLR 237
Cdd:cd07346 155 ILRYFRRRIRKASREVRESlAELSAFLQESLS-GIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 238 MVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd07346 234 ALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
340-547 |
1.61e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY----PTwDRKQLGGYIgyLAQDVQLLPG-S 414
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPA-KAHQLGIYL--VPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIArfdagVSDANITEAASRAQahALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD- 493
Cdd:PRK15439 103 VKENIL-----FGLPKRQASMQKMK--QLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 494 AEGEAALE--RALLQAKAGgttVIIVTHR-PAIVLKCDKALVLRNGAVDAFGPASEI 547
Cdd:PRK15439 174 AETERLFSriRELLAQGVG---IVFISHKlPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
343-545 |
1.80e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGT--IALDGADY--PTWDRK--QLGGYIGYLAQDVQLLPG-SI 415
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFskTPSDKAirELRRNVGMVFQQYNLWPHlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIarFDAGVSDANITEAASRAQAHALITGLKQGyqttmEAAGG---SLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:PRK11124 100 QQNL--IEAPCRVLGLSKDQALARAEKLLERLRLK-----PYADRfplHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517342213 493 DAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPAS 545
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
340-547 |
3.49e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSS----LARLLAgvaepTGGTIALDGADYPTWDRKQLGGY---IGYLAQDvqllP 412
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVrhrIQVVFQD----P 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 GS-----------IAENIARFDAGVSDANITEAASRA-QAHALITGLKQGYQTtmeaaggSLSGGTRQRIGLARAFFGNP 480
Cdd:PRK15134 372 NSslnprlnvlqiIEEGLRVHQPTLSAAQREQQVIAVmEEVGLDPETRHRYPA-------EFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 481 KLLILDEPNSNLDAEGEA---ALERALLQAKagGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAqilALLKSLQQKH--QLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
341-536 |
4.77e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 77.76 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyPTWDRKQLGGYIGY-LAQDVQL---LPG--- 413
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-PWKRRKKFLRRIGVvFGQKTQLwwdLPVids 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIARFDAGVSDANITEAASRAQ-AHALITGLKQgyqttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:cd03267 116 fYLLAAIYDLPPARFKKRLDELSELLDlEELLDTPVRQ------------LSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517342213 492 LDAEGEAALERALLQA-KAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:cd03267 184 LDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEAlARRVLVIDKG 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
341-553 |
5.11e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.25 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQ--DVQLLpGSiaen 418
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQnpDNQFV-GS---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IARFDAGVSDANitEAASRAQAHALITGLKQGYQTTMEA--AGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:PRK13648 100 IVKYDVAFGLEN--HAVPYDEMHRRVSEALKQVDMLERAdyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 497 EAALERALLQAKA-GGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSG 553
Cdd:PRK13648 178 RQNLLDLVRKVKSeHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
340-538 |
6.19e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPtWDRKqlggyigylaqdvqllpGSIAENI 419
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-FGRE-----------------ASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAgVSDAniTEAASRAqahalitGLKQGYqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAA 499
Cdd:COG2401 107 GRKGD-FKDA--VELLNAV-------GLSDAV--LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 500 LERALLQ-AKAGGTTVIIVTHRPAIV--LKCDKALVLRNGAV 538
Cdd:COG2401 175 VARNLQKlARRAGITLVVATHHYDVIddLQPDLLIFVGYGGV 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
323-533 |
7.18e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 323 KNLFWAPtharADTSAAIiKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY-- 400
Cdd:PRK15079 24 KQWFWQP----PKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 401 -IGYLAQD--VQLLP----GSI-AENIARFDAGVSDANITEaasRAQAHALITGLkqgYQTTMEAAGGSLSGGTRQRIGL 472
Cdd:PRK15079 99 dIQMIFQDplASLNPrmtiGEIiAEPLRTYHPKLSRQEVKD---RVKAMMLKVGL---LPNLINRYPHEFSGGQCQRIGI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 473 ARAFFGNPKLLILDEPNSNLDAEGEAALERaLLQA--KAGGTTVIIVTHRPAIVLK-CDKALVL 533
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALDVSIQAQVVN-LLQQlqREMGLSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
340-546 |
8.58e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.69 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTG--GTIALDGADyPTwdrKQLGGYIGYLAQDVQL------- 410
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK-PT---KQILKRTGFVTQDDILyphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 ----------LPGSIA--ENIARFDAGVSDANITEAASRAQAHALITGLkqgyqttmeaaggslSGGTRQRIGLARAFFG 478
Cdd:PLN03211 159 etlvfcsllrLPKSLTkqEKILVAESVISELGLTKCENTIIGNSFIRGI---------------SGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 479 NPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPA--IVLKCDKALVLRNGAVDAFGPASE 546
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSsrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-549 |
8.84e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 321 TVKNLfwapTHARADTsaAIIKDVSFDLKPGHVLAILGPSGSGKSSL----ARLLagvaEPTGGTIALDGADYPTWDRKQ 396
Cdd:COG4604 3 EIKNV----SKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLlsmiSRLL----PPDSGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 397 LGGYIGYLAQDVQL---LpgSIAENIA--RFDAgvSDANITEAASRAQAHAL----ITGLKQGYQTTmeaaggsLSGGTR 467
Cdd:COG4604 73 LAKRLAILRQENHInsrL--TVRELVAfgRFPY--SKGRLTAEDREIIDEAIayldLEDLADRYLDE-------LSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 468 QRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTH------RPAivlkcDKALVLRNGAVDA 540
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADELGKTVVIVLHdinfasCYA-----DHIVAMKDGRVVA 216
|
....*....
gi 517342213 541 FGPASEILQ 549
Cdd:COG4604 217 QGTPEEIIT 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
343-536 |
9.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.95 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG----ADYPTWDRKQLGGYIGYLAQ--DVQLLPGSIA 416
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQfpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIarfDAGVSDANITEAASRAQAHALI--TGLKQgyqTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK13641 105 KDV---EFGPKNFGFSEDEAKEKALKWLkkVGLSE---DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 495 EGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHG 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
340-577 |
1.60e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.59 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadyptWDRKQlggyIGYLAQDVQLLPGSIAENI 419
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS----IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGvSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE-GEA 498
Cdd:PTZ00243 742 LFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 499 ALERALLQAKAGGTTViIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSGAKPRPVNANRVSVRNKSETADAPE 577
Cdd:PTZ00243 821 VVEECFLGALAGKTRV-LATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKDSKEGDADAEVAE 898
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-548 |
1.85e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwapTHARADTSaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGG 399
Cdd:PRK09536 4 IDVSDL----SVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIGYLAQDVQLLPGSIAENI---------ARFDAGVS--DANITEAASRAQAHALItglkqgyqttmEAAGGSLSGGTRQ 468
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVvemgrtphrSRFDTWTEtdRAAVERAMERTGVAQFA-----------DRPVTSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 469 RIGLARAFFGNPKLLILDEPNSNLDAEGEA---ALERALLQAkagGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPA 544
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVrtlELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPP 223
|
....
gi 517342213 545 SEIL 548
Cdd:PRK09536 224 ADVL 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
340-550 |
2.04e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGgyIGYLAQDVQLLPG-SIAEN 418
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IAMVFQNYALYPHmSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IA-----RfdaGVSDANITEaasRAQAHALITGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK11650 97 MAyglkiR---GMPKAEIEE---RVAEAARILELEP----LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 494 AEGEAA-------LERALlqakagGTTVIIVTHR--PAIVLkCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK11650 167 AKLRVQmrleiqrLHRRL------KTTSLYVTHDqvEAMTL-ADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-519 |
2.99e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 330 THARADTsaAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQ 409
Cdd:PRK13543 18 AFSRNEE--PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 410 LLpgSIAENIaRFDAGVSDANITEAASRAQAhalITGLKqGYQTTMEAaggSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:PRK13543 96 DL--STLENL-HFLCGLHGRRAKQMPGSALA---IVGLA-GYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190
....*....|....*....|....*....|
gi 517342213 490 SNLDAEGEAALERALLQAKAGGTTVIIVTH 519
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
341-548 |
3.09e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQ--DVQLLPGSIAEN 418
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IArfdAGVSDANIT-EAASRAQAHALITGLKQGYQTTMEAaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:PRK13642 103 VA---FGMENQGIPrEEMIKRVDEALLAVNMLDFKTREPA---RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 498 AALERALLQAKAG-GTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK13642 177 QEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-552 |
3.21e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP---TGGTIALDGADY---PTWD-RKQLGgyIGYLAQD 407
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLtakTVWDiREKVG--IVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 408 VQLLPGSIAENIArF---DAGVSDANITEAASRAQAHAlitglkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK13640 95 NQFVGATVGDDVA-FgleNRAVPRPEMIKIVRDVLADV-------GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 485 LDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLS 552
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
320-557 |
3.70e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.69 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNL---FWAPtharaDTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP---TGGTIALDGADYPTWD 393
Cdd:PRK09473 13 LDVKDLrvtFSTP-----DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 394 RKQLGGY----IGYLAQD-----------------VQLLPGSIAENIArFDAGVS--DA-NITEAASRaqahalitglkq 449
Cdd:PRK09473 88 EKELNKLraeqISMIFQDpmtslnpymrvgeqlmeVLMLHKGMSKAEA-FEESVRmlDAvKMPEARKR------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 450 gyqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-C 527
Cdd:PRK09473 155 -----MKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGiC 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 517342213 528 DKALVLRNGAVDAFGPASEILQR--------LSGAKPR 557
Cdd:PRK09473 230 DKVLVMYAGRTMEYGNARDVFYQpshpysigLLNAVPR 267
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
341-519 |
3.96e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLAR-------LLAGV-AEptgGTIALDGADY--PTWDRKQLGGYIGYLAQDVQL 410
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFrVE---GKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPGSIAENIArFDAGVS--DANITEAASRA--QAhALITGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:PRK14243 103 FPKSIYDNIA-YGARINgyKGDMDELVERSlrQA-ALWDEVKD----KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|...
gi 517342213 487 EPNSNLDAEGEAALERALLQAKAgGTTVIIVTH 519
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKE-QYTIIIVTH 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-549 |
4.41e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAE-----PTGGTIALDGADYPTWD------RKQLGGYIGYLAQDV 408
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDvdpievRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 409 QLlpgSIAENIA---RFDAGV-SDANITEAASRAQAHAlitGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK14267 99 HL---TIYDNVAigvKLNGLVkSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 485 LDEPNSNLDAEGEAALERALLQAKAgGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
340-538 |
4.49e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.48 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaLDGADYPTWDRKQlggyIGYLAQDVQLLP-GSIAEN 418
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARED----TRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IArfdAGVSdANITEAASRAqahalitglkqgyqttMEAAG---------GSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:PRK11247 102 VG---LGLK-GQWRDAALQA----------------LAAVGladranewpAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 490 SNLDA----EGEAALERALLQAkagGTTVIIVTH--RPAIVLkCDKALVLRNGAV 538
Cdd:PRK11247 162 GALDAltriEMQDLIESLWQQH---GFTVLLVTHdvSEAVAM-ADRVLLIEEGKI 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-550 |
6.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 336 TSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQ--DVQLLPG 413
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIArfdAGVSDANITEAASraqAHALITGLKQ-GYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:PRK13652 95 TVEQDIA---FGPINLGLDEETV---AHRVSSALHMlGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 493 DAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13652 169 DPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
343-551 |
6.39e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIAL-DGADYPTWDRKQLGGY---IGYLAQ--DVQLLPGSIA 416
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVrkkVGVVFQfpESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArfdAGVSDANIT-EAASRAQAHAL-ITGLKQGYqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDA 494
Cdd:PRK13643 104 KDVA---FGPQNFGIPkEKAEKIAAEKLeMVGLADEF---WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 495 EGEAALERALLQAKAGGTTVIIVTH-RPAIVLKCDKALVLRNGAVDAFGPASEILQRL 551
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
343-552 |
6.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.17 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG----ADYPTWDRKQLGGYIGYLAQ--DVQLLPGSIA 416
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIKQIRKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIArF---DAGVSdanITEAASRAQAHALITGLKQgyqTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK13649 105 KDVA-FgpqNFGVS---QEEAEALAREKLALVGISE---SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 494 AEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQRLS 552
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQDVD 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
343-547 |
1.32e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALD---------GADYPTWDRKqlggyIGYLAQDVQLLP- 412
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekGICLPPEKRR-----IGYVFQDARLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 ---------GSIAENIARFDAGVSDANITEAASRAQAhalitglkqgyqttmeaaggSLSGGTRQRIGLARAFFGNPKLL 483
Cdd:PRK11144 91 ykvrgnlryGMAKSMVAQFDKIVALLGIEPLLDRYPG--------------------SLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 484 ILDEPNSNLDA----EGEAALERAllqAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK11144 151 LMDEPLASLDLprkrELLPYLERL---AREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
343-537 |
1.81e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVaEPTG---GTIALDGA-----DYPtwDRKQLGgyIGYLAQDVQLLPG- 413
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGEvcrfkDIR--DSEALG--IVIIHQELALIPYl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENI------ARFdaGVSDANitEAASRAQAHALITGLKQGYQTTMeaagGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:NF040905 94 SIAENIflgnerAKR--GVIDWN--ETNRRARELLAKVGLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 488 PNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGA 537
Cdd:NF040905 166 PTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
329-548 |
2.01e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.35 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 329 PTHARAdtsaaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY------------------- 389
Cdd:PRK13651 17 PTELKA------LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktkekekvleklviq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 390 PTWDRK-----QLGGYIGYLAQ--DVQLLPGSIAENIArFDA---GVSDAnitEAASRAQAHALITGLKQGYqttMEAAG 459
Cdd:PRK13651 91 KTRFKKikkikEIRRRVGVVFQfaEYQLFEQTIEKDII-FGPvsmGVSKE---EAKKRAAKYIELVGLDESY---LQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 460 GSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDK-ALVLRNGAV 538
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKrTIFFKDGKI 243
|
250
....*....|
gi 517342213 539 DAFGPASEIL 548
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-516 |
3.45e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDgadyPTWDrkqlggyIGYLAQDVQLLPG--SIAE 417
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVK-------LAYVDQSRDALDPnkTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIarfdagvSDAN--IT----EAASRAQAHALitGLKQGYQttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:TIGR03719 406 EI-------SGGLdiIKlgkrEIPSRAYVGRF--NFKGSDQ---QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
170 180
....*....|....*....|....*
gi 517342213 492 LDAEGEAALERALLqaKAGGTTVII 516
Cdd:TIGR03719 474 LDVETLRALEEALL--NFAGCAVVI 496
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
322-550 |
4.29e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.85 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 322 VKNLFWaptHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYI 401
Cdd:PRK13647 7 VEDLHF---RYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 402 GYLAQDV--QLLPGSIAENIA--RFDAGVSDANI---TEAASRAQahalitglkqGYQTTMEAAGGSLSGGTRQRIGLAR 474
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAfgPVNMGLDKDEVerrVEEALKAV----------RMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 475 AFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGpASEILQR 550
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG-DKSLLTD 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-548 |
5.51e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGG-----TIALDGADYPTW-DRKQLGGYIGYLAQDVQLLPG 413
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIArfdAGVSDANIT---EAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK14271 116 SIMDNVL---AGVRAHKLVprkEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 491 NLDAEGEAALERaLLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK14271 193 ALDPTTTEKIEE-FIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
340-519 |
6.29e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 72.14 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIAL-----------DGADYPTwDRKQLGGYIGYLA--- 405
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirlkpdrDGELVPA-DRRQLQRIRTRLGmvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 406 QDVQLLPG-SIAENIarFDAGVSDANITEAASRAQAHALITglKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:COG4598 102 QSFNLWSHmTVLENV--IEAPVHVLGRPKAEAIERAEALLA--KVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 517342213 485 LDEPNSNLDAE--GEA-ALERALLQAkagGTTVIIVTH 519
Cdd:COG4598 178 FDEPTSALDPElvGEVlKVMRDLAEE---GRTMLVVTH 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-550 |
7.82e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.36 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALdGADYPTWDRKQ-----LGGYIGYLAQ--DVQLLPG 413
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkpLRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIArF---DAGVSDAnitEAASRAQAHALITGLKQGYqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK13634 102 TVEKDIC-FgpmNFGVSEE---DAKQKAREMIELVGLPEEL---LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 491 NLDAEGEAALERALLQA-KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
340-548 |
9.93e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQlLPGSIA--E 417
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT-TPGDITvqE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIARfdaGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGG--SLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:PRK10253 101 LVAR---GRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 496 GEAALERALLQA-KAGGTTVIIVTHRPAIVLKCDKALV-LRNGAVDAFGPASEIL 548
Cdd:PRK10253 178 HQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
339-537 |
1.05e-13 |
|
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: 70.44 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI----ALDGADYPTWDRKQLGGYIGYLAQDVQLLPGS 414
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIA--------RFDAgvsdanITEAASraqAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:cd03290 95 VEENITfgspfnkqRYKA------VTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 487 EPNSNLDAEgeaaLERALLQA------KAGGTTVIIVTHRPAIVLKCDKALVLRNGA 537
Cdd:cd03290 166 DPFSALDIH----LSDHLMQEgilkflQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-552 |
1.16e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADypTWDRKQLGG---YIGYLAQ--DVQLLPGSI 415
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGirkLVGIVFQnpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIArF---DAGVSDANITEAASRAQAHaliTGLKQgYQttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:PRK13644 96 EEDLA-FgpeNLCLPPIEIRKRVDRALAE---IGLEK-YR---HRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 493 DAE-GEAALERaLLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLS 552
Cdd:PRK13644 168 DPDsGIAVLER-IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
341-540 |
1.65e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADY----PTWDRKQLGGYIGYLAQDVQLLPG-SI 415
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprsPLDAVKKGMAYITESRRDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIA--RF--DAGVSDA----NITEAASRAQAHALITGLKqgyQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:PRK09700 359 AQNMAisRSlkDGGYKGAmglfHEVDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517342213 488 PNSNLDAEGEAALERALLQAKAGGTTVIIVTHR-PAIVLKCDKALVLRNGAVDA 540
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQ 489
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-550 |
3.69e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 338 AAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA--DYPTWDRKQLGGYIGYLAQD--VQLLPG 413
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpeQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIArF---DAGVSDANITeaasRAQAHALITGLKQGYQttmEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK13638 94 DIDSDIA-FslrNLGVPEAEIT----RRVDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
341-538 |
3.85e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP---------------TWDRKQLGGYiGYLa 405
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneainhgfalvTEERRSTGIY-AYL- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 406 qDVQLlpGSIAENIARFDAGVSDANITEAASRAQAhaLITGLK---QGYQTTMeaagGSLSGGTRQRIGLARAFFGNPKL 482
Cdd:PRK10982 342 -DIGF--NSLISNIRNYKNKVGLLDNSRMKSDTQW--VIDSMRvktPGHRTQI----GSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 483 LILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
248-574 |
5.31e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 248 GAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRLGSVIASgkghrADRLILPEPEGR-----LTV 322
Cdd:PLN03232 543 GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLS-----EERILAQNPPLQpgapaISI 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 323 KNLFWApthARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALdgadyptwdrkqLGGYIG 402
Cdd:PLN03232 618 KNGYFS---WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 403 YLAQDVQLLPGSIAENIArFDAGVSDANITEAAS-RAQAHALitGLKQGYQ-TTMEAAGGSLSGGTRQRIGLARAFFGNP 480
Cdd:PLN03232 683 YVPQVSWIFNATVRENIL-FGSDFESERYWRAIDvTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 481 KLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQRLSGAKPRPVN 560
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
330
....*....|....
gi 517342213 561 ANRVSVRNKSETAD 574
Cdd:PLN03232 840 AGKMDATQEVNTND 853
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
343-547 |
7.33e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAePTG---GTIALDGAD---YPTWDRKQLGgyIGYLAQDVQLLPG-SI 415
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEElqaSNIRDTERAG--IAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 416 AENIarF------DAGVSDANiteaASRAQAHALITGLKQG---YQTTMEaaggsLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:PRK13549 100 LENI--FlgneitPGGIMDYD----AMYLRAQKLLAQLKLDinpATPVGN-----LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 487 EPNSNLDAEGEAALERALLQAKAGGTTVIIVTHR----PAIvlkCDKALVLRNGAVDAFGPASEI 547
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIYISHKlnevKAI---SDTICVIRDGRHIGTRPAAGM 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
340-542 |
8.78e-13 |
|
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: 67.29 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTG---GTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIA 416
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIarfdagvsdanitEAASRAQAHALITGlkqgyqttmeaaggsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAeg 496
Cdd:cd03233 102 ETL-------------DFALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS-- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 497 EAALE---RALLQAKAGGTTVIIVTHRPA--IVLKCDKALVLRNGAVDAFG 542
Cdd:cd03233 152 STALEilkCIRTMADVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
340-550 |
9.45e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.73 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFdagvsdaniTEAASRAQAHAL-ITGLK-------QGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLIL-DEPNS 490
Cdd:PTZ00243 1405 DPF---------LEASSAEVWAALeLVGLRervasesEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 491 NLDaegeAALER---ALLQAKAGGTTVIIVTHRPAIVLKCDKALVLRNGAVDAFGPASEILQR 550
Cdd:PTZ00243 1476 NID----PALDRqiqATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-519 |
9.81e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.20 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 347 DLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyptwdrkqlggyIGYLAQDVQL-LPGSIAENIARFDAG 425
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYIKAdYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 426 VSDAN--ITEAASRAQAHALitglkqgyqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE----GEAA 499
Cdd:cd03237 89 FYTHPyfKTEIAKPLQIEQI-----------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKV 157
|
170 180
....*....|....*....|
gi 517342213 500 LERALLQAKAggtTVIIVTH 519
Cdd:cd03237 158 IRRFAENNEK---TAFVVEH 174
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-536 |
1.08e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 350 PGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRK--QLGGyIGYLAQDVQLLPG-SIAENI------- 419
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssQEAG-IGIIHQELNLIPQlTIAENIflgrefv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAgvsdanITEAASRAQAHALIT--GLKQGYQTTMeaagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL-DAEG 496
Cdd:PRK10762 108 NRFGR------IDWKKMYAEADKLLArlNLRFSSDKLV----GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517342213 497 EaALERALLQAKAGGTTVIIVTHRpaivLK-----CDKALVLRNG 536
Cdd:PRK10762 178 E-SLFRVIRELKSQGRGIVYISHR----LKeifeiCDDVTVFRDG 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
340-536 |
1.32e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.50 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAG--VAEPTGGTIALDGadYPTwdRKQLGGYIGYLAQDVQLLPGSIAE 417
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING--RPL--DKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 418 NIARFdagvsdaniteaasraqaHALITGLkqgyqttmeaaggslSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:cd03232 98 EALRF------------------SALLRGL---------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517342213 498 AALERALLQAKAGGTTVIIVTHRPAIVL--KCDKALVLRNG 536
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
344-538 |
1.33e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGV----------AEPTGGTIALDGAdyPTWDRKQLGGYIGYLAQDVQLLPG 413
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGR--LARDIRKSRANTGYIFQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 -SIAENIARFDAGVSDANIT--EAASRAQA-HALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPN 489
Cdd:PRK09984 101 lSVLENVLIGALGSTPFWRTcfSWFTREQKqRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 490 SNLDAEGEAALERALLQA-KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:PRK09984 181 ASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-585 |
1.68e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyPTWDRKQLGGYIGY-LAQDVQLLpgsiaeni 419
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-PFKRRKEFARRIGVvFGQRSQLW-------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 arFDAGVSDA--------NITEAASRAQAHALITGLKQG---YQTTMEaaggsLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:COG4586 109 --WDLPAIDSfrllkaiyRIPDAEYKKRLDELVELLDLGellDTPVRQ-----LSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 489 NSNLDAEGEAALeRALLQA--KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV--DafGPASEILQRLSGAKprpvnanR 563
Cdd:COG4586 182 TIGLDVVSKEAI-REFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIiyD--GSLEELKERFGPYK-------T 251
|
250 260
....*....|....*....|..
gi 517342213 564 VSVRNKSETADAPENRDAGLVE 585
Cdd:COG4586 252 IVLELAEPVPPLELPRGGEVIE 273
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-536 |
2.40e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 342 KDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD---YPTWDRKQLGgyIGYLAQDVQ----LLPGS 414
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEinaLSTAQRLARG--LVYLPEDRQssglYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIARFDAGVSDANITEAASRA---QAHALItGLKqgyQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSN 491
Cdd:PRK15439 358 LAWNVCALTHNRRGFWIKPARENAvleRYRRAL-NIK---FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517342213 492 LDAEGEAALERALLQAKAGGTTVI-IVTHRPAIVLKCDKALVLRNG 536
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
320-550 |
2.76e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWAPTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA----------DY 389
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAA--VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 390 PTWDRKQL----GGYIGYLAQD-------VQLLPGSIAENIaRFDAGVSDANITEAASRAQAHALITglkqGYQTTMEAA 458
Cdd:PRK10261 91 SEQSAAQMrhvrGADMAMIFQEpmtslnpVFTVGEQIAESI-RLHQGASREEAMVEAKRMLDQVRIP----EAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 459 GGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEA---ALERALLQAKAGGttVIIVTHRPAIVLK-CDKALVLR 534
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilQLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|....*.
gi 517342213 535 NGAVDAFGPASEILQR 550
Cdd:PRK10261 244 QGEAVETGSVEQIFHA 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
344-547 |
6.28e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadyptwdrKQLGGYIGYLA---------QDVQLLPG- 413
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG--------QHIEGLPGHQIarmgvvrtfQHVRLFREm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENI---------ARFDAGVSDaniTEAASRAQAHAL---ITGLKQ-GYQTTMEAAGGSLSGGTRQRIGLARAFFGNP 480
Cdd:PRK11300 96 TVIENLlvaqhqqlkTGLFSGLLK---TPAFRRAESEALdraATWLERvGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 481 KLLILDEPNSNLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
292-549 |
8.63e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 292 AWKRLgsviaSGKGHRADRLILPepegrlTVKNLFWAPTHA--------RADTSAAIIKDVSFDLKPGHVLAILGPSGSG 363
Cdd:TIGR00956 31 AYKNL-----SAYGVAADSDYQP------TFPNALLKILTRgfrklkkfRDTKTFDILKPMDGLIKPGELTVVLGRPGSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 364 KSSLARLLA----GVAEPTGGTIALDGADyPTWDRKQLGGYIGYLAQ-DVQLLPGSIAENI---ARFDA------GVSDA 429
Cdd:TIGR00956 100 CSTLLKTIAsntdGFHIGVEGVITYDGIT-PEEIKKHYRGDVVYNAEtDVHFPHLTVGETLdfaARCKTpqnrpdGVSRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 430 niTEAASRAQAHALITGLKQGYQTTM--EAAGGsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAegEAALE--RAL- 504
Cdd:TIGR00956 179 --EYAKHIADVYMATYGLSHTRNTKVgnDFVRG-VSGGERKRVSIAEASLGGAKIQCWDNATRGLDS--ATALEfiRALk 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 517342213 505 LQAKAGGTTVIIVTHRPA--IVLKCDKALVLRNGAVDAFGPASEILQ 549
Cdd:TIGR00956 254 TSANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-516 |
8.72e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALdGadyPTWDrkqlggyIGYLAQDVQLLPG--SIAEN 418
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---ETVK-------LAYVDQSRDALDPnkTVWEE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IarfdagvSDAN--IT----EAASRAQAHALitGLKQGYQttmEAAGGSLSGGTRQRIGLARAFF--GNpkLLILDEPNS 490
Cdd:PRK11819 409 I-------SGGLdiIKvgnrEIPSRAYVGRF--NFKGGDQ---QKKVGVLSGGERNRLHLAKTLKqgGN--VLLLDEPTN 474
|
170 180
....*....|....*....|....*.
gi 517342213 491 NLDAEGEAALERALLQakAGGTTVII 516
Cdd:PRK11819 475 DLDVETLRALEEALLE--FPGCAVVI 498
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
341-548 |
8.79e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.18 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAG-VAEPTGGTIALDGADYPTWDR----KQLGGYIGYLAQ--DVQLLPG 413
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGlIISETGQTIVGDYAIPANLKKikevKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIARfdagvsdANITEAASRAQAHALITGLKQGYQTTMEAAGGS---LSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK13645 107 TIEKDIAF-------GPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 491 NLDAEGEAALERALLQA-KAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK13645 180 GLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
285-538 |
9.06e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 285 QIVDARKAWKRLGSVIASgkghrADRLILPEP-----EGRLTVKN--LFWAPTHARADTSaaiikDVSFDLKPGHVLAIL 357
Cdd:PLN03130 580 QAVNANVSLKRLEELLLA-----EERVLLPNPplepgLPAISIKNgyFSWDSKAERPTLS-----NINLDVPVGSLVAIV 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 358 GPSGSGKSSLARLLAGVAEPTGGTIALdgadyptwdrkqLGGYIGYLAQDVQLLPGSIAENI---ARFDAGVSDANItEA 434
Cdd:PLN03130 650 GSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNIlfgSPFDPERYERAI-DV 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 435 ASRAQAHALITGlkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE-GEAALERAlLQAKAGGTT 513
Cdd:PLN03130 717 TALQHDLDLLPG---GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKC-IKDELRGKT 792
|
250 260
....*....|....*....|....*
gi 517342213 514 VIIVTHRPAIVLKCDKALVLRNGAV 538
Cdd:PLN03130 793 RVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
340-547 |
1.02e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.56 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLggyigYLA-QDVQLLpgsiaen 418
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL-----YTVrKRMSML------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 iarFDAGV--SDANITEAAS---RAQAHALITGLKQGYQTTMEAAG---------GSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK11831 90 ---FQSGAlfTDMNVFDNVAyplREHTQLPAPLLHSTVMMKLEAVGlrgaaklmpSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 485 LDEPNSNLDAEGEAALERALLQA-KAGGTTVIIVTHR-PAIVLKCDKALVLRNGAVDAFGPASEI 547
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
352-519 |
1.29e-11 |
|
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: 68.12 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 352 HVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGGYIGYLAQDVQLLPG-SIAENIArFDAGVSDAN 430
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHIL-FYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 431 ITEAASRAQAHALITGLKqgYQTTMEAAggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAg 510
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTGLH--HKRNEEAQ--DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS- 1109
|
....*....
gi 517342213 511 GTTVIIVTH 519
Cdd:TIGR01257 1110 GRTIIMSTH 1118
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-538 |
1.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGAD--YPTWDR--KQLGGYIGYLAQ--DVQLLPGS 414
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITitHKTKDKyiRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENIArFDAGVSDANITEAASRaqAHALITGLkqGY-QTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLD 493
Cdd:PRK13646 103 VEREII-FGPKNFKMNLDEVKNY--AHRLLMDL--GFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517342213 494 AEGEAALERAL--LQAKAgGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:PRK13646 178 PQSKRQVMRLLksLQTDE-NKTIILVSHDMNEVARyADEVIVMKEGSI 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
341-524 |
1.87e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGY---IGYLAQDV-------QL 410
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPyasldprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPGSIAENIARFDAGVSDAniteAASRAQAHALITGLKQGYQTTMEAAggsLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKA----AAARVAWLLERVGLLPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|....*
gi 517342213 491 NLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIV 524
Cdd:PRK10261 493 ALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVV 527
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
333-550 |
2.34e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 333 RADTSAAIIKDVSFDLKPGHVLAILGPSGSGKS-----SLARLLAGVAEpTGGTIALDGadyptwdrkqlggyigylaqd 407
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDG--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 408 VQLLPGSIaeniarfdAGVSDANITEAASRA-------QAHALITGLKQGYQTT-------MEAAG------------GS 461
Cdd:PRK10418 69 KPVAPCAL--------RGRKIATIMQNPRSAfnplhtmHTHARETCLALGKPADdatltaaLEAVGlenaarvlklypFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 462 LSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEA---ALERALLQAKAGGttVIIVTHRPAIVLKC-DKALVLRNGA 537
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQArilDLLESIVQKRALG--MLLVTHDMGVVARLaDDVAVMSHGR 218
|
250
....*....|...
gi 517342213 538 VDAFGPASEILQR 550
Cdd:PRK10418 219 IVEQGDVETLFNA 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
344-538 |
2.41e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLggyigyLAQDVQLLPgsiaENIARFD 423
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI------MREAVAIVP----EGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 424 AGVSDANITEA---ASRAQAHALITGLKQGYQTTME---AAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:PRK11614 94 RMTVEENLAMGgffAERDQFQERIKWVYELFPRLHErriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 498 AALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-519 |
6.89e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTG-----GTIALDGADypTWDRK----QLGGYIGYLAQDVQL 410
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQN--IYERRvnlnRLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPGSIAENIAR------FDAGVSDANITEAASRAqahaliTGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK14258 100 FPMSVYDNVAYgvkivgWRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 517342213 485 LDEPNSNLDAEGEAALErALLQAKA--GGTTVIIVTH 519
Cdd:PRK14258 174 MDEPCFGLDPIASMKVE-SLIQSLRlrSELTMVIVSH 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-536 |
7.90e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLfwaptHARADTSAaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGvaEP----TGGTIALDGA---DYPTW 392
Cdd:CHL00131 8 LEIKNL-----HASVNENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGEsilDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 393 DRKQLGGYIGYlaQdvqlLPGSIaeniarfdAGVSDANITEAA--SRAQAHAL-----------------ITGLKQGYQT 453
Cdd:CHL00131 80 ERAHLGIFLAF--Q----YPIEI--------PGVSNADFLRLAynSKRKFQGLpeldplefleiineklkLVGMDPSFLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 454 TMEAAGgsLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIV--LKCDKAL 531
Cdd:CHL00131 146 RNVNEG--FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLdyIKPDYVH 223
|
....*
gi 517342213 532 VLRNG 536
Cdd:CHL00131 224 VMQNG 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-536 |
8.00e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNL-FWAPTHARADtsaaIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEptG---GTIALDG--------A 387
Cdd:PRK13549 260 LEVRNLtAWDPVNPHIK----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGkpvkirnpQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 388 D-------YPTWDRKQLGgyigylaqdvqLLPG-SIAENIA-----RFDAGvsdANITEAASRAQAHALITGLKqgYQT- 453
Cdd:PRK13549 334 QaiaqgiaMVPEDRKRDG-----------IVPVmGVGKNITlaaldRFTGG---SRIDDAAELKTILESIQRLK--VKTa 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 454 TMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHR-PAIVLKCDKALV 532
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLV 477
|
....
gi 517342213 533 LRNG 536
Cdd:PRK13549 478 MHEG 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
340-575 |
9.41e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadyptwdrkqlGGYIGYLAQ-DVQLLPG--SIA 416
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-----------GIKLGYFAQhQLEFLRAdeSPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENIARfdagvsdanITEAASRAQAHALITGLK-QGYQTTMEAagGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:PRK10636 396 QHLAR---------LAPQELEQKLRDYLGGFGfQGDKVTEET--RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 496 GEAALERALLQAKagGTTVIIVTHRPAIVLKCDKALVLRNGAVDAF-GPASEILQRLSG---------AKPRPVNANRVS 565
Cdd:PRK10636 465 MRQALTEALIDFE--GALVVVSHDRHLLRSTTDDLYLVHDGKVEPFdGDLEDYQQWLSDvqkqenqtdEAPKENNANSAQ 542
|
250
....*....|
gi 517342213 566 VRNKSETADA 575
Cdd:PRK10636 543 ARKDQKRREA 552
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
341-536 |
1.15e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVaEPTG---GTIALDGADYPTW---DRKQLGgyIGYLAQDVQLLPG- 413
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASnirDTERAG--IVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIARFDAGVSDANITE-AASRAQAHALITGLKQGYQTTMEAAGgSLSGGTRQRIGLARAFFGNPKLLILDEPNSNL 492
Cdd:TIGR02633 94 SVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517342213 493 DAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
341-540 |
1.22e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPT-GGTIALDGADYPTWDRKQLggyigyLAQDVQLLPGSIAENI 419
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQA------IRAGIAMVPEDRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGVSDaNITEAA-----------SRAQAHALITGLKQGYQTTMEA--AGGSLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:TIGR02633 350 IVPILGVGK-NITLSVlksfcfkmridAAAELQIIGSAIQRLKVKTASPflPIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 487 EPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDA 540
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKG 483
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-543 |
2.28e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIG----------YLAQDVQL 410
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPqseevdwsfpVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPGSIAENIARFDAGVSDANITEAASRAqahalitglkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:PRK15056 103 MGRYGHMGWLRRAKKRDRQIVTAALARV-----------DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRnGAVDAFGP 543
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASGP 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-528 |
2.74e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTwDRKQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDAGVSDAN--ITEaasraqahaLITGLKQGYqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGE 497
Cdd:PRK13540 95 CLYDIHFSPGAvgITE---------LCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|.
gi 517342213 498 AALERALLQAKAGGTTVIIVTHRPAIVLKCD 528
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
339-538 |
8.47e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVA--EPTGGTIALDGADYPTWDRKQLGGYIGYLA-QDVQLLPG-- 413
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAfQYPVEIPGvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 ---------------SIAENIARFDAgvsdANITEAAsraqahalITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFG 478
Cdd:PRK09580 95 nqfflqtalnavrsyRGQEPLDRFDF----QDLMEEK--------IALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517342213 479 NPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIV--LKCDKALVLRNGAV 538
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILdyIKPDYVHVLYQGRI 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
347-519 |
1.26e-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: 60.95 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 347 DLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI--ALDGADYPtwdrkQlggyigYLAQDVqllPGSIAENIARFDA 424
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdeDLKISYKP-----Q------YISPDY---DGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 425 GVSDANI--TEAASRAQAHALitglkqgyqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALER 502
Cdd:COG1245 428 DDFGSSYykTEIIKPLGLEKL-----------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170
....*....|....*...
gi 517342213 503 ALLQ-AKAGGTTVIIVTH 519
Cdd:COG1245 497 AIRRfAENRGKTAMVVDH 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
330-488 |
1.26e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 330 THARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI-ALDG--ADypTWDRKQLGGYIGYLAQ 406
Cdd:NF033858 8 SHRYGKTVA--LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGdmAD--ARHRRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 407 DV--QLLPG-SIAENIARF------DAGVSDANITE--AAsraqahaliTGLkqgyQTTMEAAGGSLSGGTRQRIGLARA 475
Cdd:NF033858 84 GLgkNLYPTlSVFENLDFFgrlfgqDAAERRRRIDEllRA---------TGL----APFADRPAGKLSGGMKQKLGLCCA 150
|
170
....*....|...
gi 517342213 476 FFGNPKLLILDEP 488
Cdd:NF033858 151 LIHDPDLLILDEP 163
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-519 |
1.39e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadypTWDRKqlgGYIGYLAQDvqllpgsiaeNI 419
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN---ANIGYYAQD----------HA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDagvSDANITEAASRaqahalITGLKQGYQTTMEAAG-------------GSLSGGTRQRIGLARAFFGNPKLLILD 486
Cdd:PRK15064 393 YDFE---NDLTLFDWMSQ------WRQEGDDEQAVRGTLGrllfsqddikksvKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190
....*....|....*....|....*....|...
gi 517342213 487 EPNSNLDAEGEAALERALLQAKAggtTVIIVTH 519
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKYEG---TLIFVSH 493
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
350-534 |
2.16e-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: 56.23 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 350 PGHVLAILGPSGSGKSSLARLLAG-VAEPTGGTIALDGADYPTWDRKQLGGYIGYlaqdvqllpgsiaeniarfdagvsd 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 429 aniteaasraqahalitglkqgyqttmeAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERA----- 503
Cdd:smart00382 56 ----------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190
....*....|....*....|....*....|..
gi 517342213 504 -LLQAKAGGTTVIIVTHRPAIVLkcDKALVLR 534
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEKDLG--PALLRRR 137
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
340-562 |
3.43e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGvaEPTGGTIaldgadypTWDRKQLGGY---------IGYLAQ-DVQ 409
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI--------TGGDRLVNGRpldssfqrsIGYVQQqDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 410 LLPGSIAENIaRFDA------GVSDA----------NITEAASRAQAhalITGLkqgyqttmeaAGGSLSGGTRQRIGLA 473
Cdd:TIGR00956 848 LPTSTVRESL-RFSAylrqpkSVSKSekmeyveeviKLLEMESYADA---VVGV----------PGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 474 RAFFGNPKLLI-LDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVL--KCDKALVL-RNGAVDAFGPASEILQ 549
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILfeEFDRLLLLqKGGQTVYFGDLGENSH 993
|
250
....*....|....*....
gi 517342213 550 RL------SGAKPRPVNAN 562
Cdd:TIGR00956 994 TIinyfekHGAPKCPEDAN 1012
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
344-547 |
3.53e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKS--SLArlLAGVAEPTGGTIA----LDGADYPTWDRKQ----LGGYIGYLAQD--VQLL 411
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLIDYPGRVMAekleFNGQDLQRISEKErrnlVGAEVAMIFQDpmTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 412 PG-----SIAENIARFDAGvsdaniTEAASRAQAHALIT--GLKQGyQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK11022 104 PCytvgfQIMEAIKVHQGG------NKKTRRQRAIDLLNqvGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 485 LDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEI 547
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
340-519 |
4.29e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI----ALDgadyptwdrkqlggyIGYLAQ-DVQLLP-G 413
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLE---------------VAYFDQhRAELDPeK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 414 SIAENIARfdaGVSDANITeAASRaqaHALitglkqGY-----------QTTMEAaggsLSGGTRQRIGLARAFFGNPKL 482
Cdd:PRK11147 399 TVMDNLAE---GKQEVMVN-GRPR---HVL------GYlqdflfhpkraMTPVKA----LSGGERNRLLLARLFLKPSNL 461
|
170 180 190
....*....|....*....|....*....|....*..
gi 517342213 483 LILDEPNSNLDAEGEAALErALLQAKAGgtTVIIVTH 519
Cdd:PRK11147 462 LILDEPTNDLDVETLELLE-ELLDSYQG--TVLLVSH 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
348-519 |
4.89e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 348 LKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgadypTWDRK-----QlggyigYLAQD----VQLLPGSIAEN 418
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELKisykpQ------YIKPDydgtVEDLLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 419 IarfdagvsDANI--TEAASRAQAHALitglkqgyqttMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:PRK13409 428 L--------GSSYykSEIIKPLQLERL-----------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180
....*....|....*....|....
gi 517342213 497 EAALERALLQ-AKAGGTTVIIVTH 519
Cdd:PRK13409 489 RLAVAKAIRRiAEEREATALVVDH 512
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
320-488 |
5.74e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNL-FWAPTHAradtSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVA--EPTGGTIALDGAD-------- 388
Cdd:NF040905 258 FEVKNWtVYHPLHP----ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEvdvstvsd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 389 -------YPTWDRKQLGgyigylaqdvQLLPGSIAENIarfdagvSDANITEAASRAqahaLI-----TGLKQGYQTTM- 455
Cdd:NF040905 334 aidaglaYVTEDRKGYG----------LNLIDDIKRNI-------TLANLGKVSRRG----VIdeneeIKVAEEYRKKMn 392
|
170 180 190
....*....|....*....|....*....|....*....
gi 517342213 456 ------EAAGGSLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:NF040905 393 iktpsvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
344-538 |
6.86e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 344 VSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYP---------------TWDRKQLGgyigylaqdv 408
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairagimlcPEDRKAEG---------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 409 qLLPG-SIAENI---ARFDAGVSDANITEAASRAQAHALITGLK---QGYQTTMeaagGSLSGGTRQRIGLARAFFGNPK 481
Cdd:PRK11288 342 -IIPVhSVADNInisARRHHLRAGCLINNRWEAENADRFIRSLNiktPSREQLI----MNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 482 LLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAV 538
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
320-536 |
7.03e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 320 LTVKNLFWAPTHAraDTSAAIIKDVSFDLKPGHVLAILGPSGSGKS----SLARLL-AGVAEPTGGTIALDG-----ADY 389
Cdd:PRK15134 6 LAIENLSVAFRQQ--QTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGesllhASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 390 PTWdRKQLGGYIGYLAQD--VQLLPGSIAEN----IARFDAGVSdaniTEAAsRAQAHALI--TGLKQGYQTtMEAAGGS 461
Cdd:PRK15134 84 QTL-RGVRGNKIAMIFQEpmVSLNPLHTLEKqlyeVLSLHRGMR----REAA-RGEILNCLdrVGIRQAAKR-LTDYPHQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 462 LSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAG-GTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
347-519 |
1.17e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 347 DLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADyptwdrkqlggyIGYLAQDVqllpgsiaeniarfdagv 426
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT------------PVYKPQYI------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 427 sdaniteaasraqahalitglkqgyqttmeaaggSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQ 506
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170
....*....|....
gi 517342213 507 -AKAGGTTVIIVTH 519
Cdd:cd03222 117 lSEEGKKTALVVEH 130
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
322-548 |
1.45e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.59 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 322 VKNLFWAPTHARADTSaaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYI 401
Cdd:PRK13545 24 LKDLFFRSKDGEYHYA---LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 402 GYLaqdvqllpgsiaENIAR--FDAGVSDANITEAASRAQAHALITglKQGYQTTMeaaggSLSGGTRQRIGLARAFFGN 479
Cdd:PRK13545 101 TGI------------ENIELkgLMMGLTKEKIKEIIPEIIEFADIG--KFIYQPVK-----TYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 480 PKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEIL 548
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVV 231
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
334-543 |
2.36e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 334 ADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGvaEPTGGTIALDG--ADYPtwdRKQ--LGGYIGYLAQD-- 407
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIriSGFP---KKQetFARISGYCEQNdi 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 408 ----VQLLPGSIAENIARFDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGgsLSGGTRQRIGLARAFFGNPKLL 483
Cdd:PLN03140 964 hspqVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517342213 484 ILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVL--KCDKALVL-RNGAVDAFGP 543
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIfeAFDELLLMkRGGQVIYSGP 1104
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
330-519 |
3.51e-08 |
|
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: 56.95 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 330 THARADTSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPT--WDRKQLGGYIGYLAQD 407
Cdd:TIGR01257 1944 TKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTniSDVHQNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 408 VQLLPGSiaENI---ARFdAGVSDANITEAASRAqahalITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:TIGR01257 2024 DDLLTGR--EHLylyARL-RGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190
....*....|....*....|....*....|....*
gi 517342213 485 LDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTH 519
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
339-549 |
4.17e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 339 AIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAG----VAEPTG----GTIALDGADYPTWDRKQLGGYIGYLAQDVQ- 409
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 410 LLPGSIAE--NIARFD----AGVSDANITEAASRAQAHALITGLKQGYQTTmeaaggsLSGGTRQRIGLARAF------- 476
Cdd:PRK13547 95 AFAFSAREivLLGRYPharrAGALTHRDGEIAWQALALAGATALVGRDVTT-------LSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517342213 477 --FGNPKLLILDEPNSNLD-AEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNGAVDAFGPASEILQ 549
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
431-519 |
9.05e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 431 ITEAASRAQAHALITGLKqgYQTTMEA-AGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKa 509
Cdd:PLN03073 315 IDAYTAEARAASILAGLS--FTPEMQVkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP- 391
|
90
....*....|
gi 517342213 510 ggTTVIIVTH 519
Cdd:PLN03073 392 --KTFIVVSH 399
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
348-523 |
1.04e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 348 LKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGtialDGADYPTWDR-------KQLGGYIGYLA----------QDVQL 410
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLG----DYDEEPSWDEvlkrfrgTELQDYFKKLAngeikvahkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LPgsiaeniARFDAGVSDAnITEAASRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNS 490
Cdd:COG1245 172 IP-------KVFKGTVREL-LEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|...
gi 517342213 491 NLDAEGEAALERALLQAKAGGTTVIIVTHRPAI 523
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-523 |
1.07e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 349 KPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIaldgADYPTWDR-------KQLGGYIGYL----------AQDVQLL 411
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF----DDPPDWDEildefrgSELQNYFTKLlegdvkvivkPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 412 P----GSIAENIARFDagvsdaniteaaSRAQAHALITGLkqGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:cd03236 100 PkavkGKVGELLKKKD------------ERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 517342213 488 PNSNLDAEGE---AALERALLQAkagGTTVIIVTHRPAI 523
Cdd:cd03236 166 PSSYLDIKQRlnaARLIRELAED---DNYVLVVEHDLAV 201
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
343-522 |
1.20e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKqlggYIGYLAQDVQL-LPGSIAENIaR 421
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP----YCTYIGHNLGLkLEMTVFENL-K 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 422 FDAGVSDaniteaaSRAQAHALITGLKqgYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALE 501
Cdd:PRK13541 93 FWSEIYN-------SAETLYAAIHYFK--LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170 180
....*....|....*....|.
gi 517342213 502 RALLQAKAGGTTVIIVTHRPA 522
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSHLES 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
341-536 |
1.56e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGADYPTWDRKQLGGYIGYLAQDVQLlpgsiaenia 420
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHL---------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 421 rFDAGVSDANitEAASRAQAHALITGLKQGYQTTMEaaGG-----SLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAE 495
Cdd:PRK10522 409 -FDQLLGPEG--KPANPALVEKWLERLKMAHKLELE--DGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 496 GEAALERALL-QAKAGGTTVIIVTHRPAIVLKCDKALVLRNG 536
Cdd:PRK10522 484 FRREFYQVLLpLLQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
335-550 |
2.35e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.99 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 335 DTSAAIIK---DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEP----TGGTIALDGADY----PTWDRKQLGGYIGY 403
Cdd:COG4170 14 DTPQGRVKavdRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklsPRERRKIIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 404 LAQDVQ--LLPGS-----IAENI----------ARFdagvsdaniteAASRAQAHALI--TGLKQgYQTTMEAAGGSLSG 464
Cdd:COG4170 94 IFQEPSscLDPSAkigdqLIEAIpswtfkgkwwQRF-----------KWRKKRAIELLhrVGIKD-HKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 465 GTRQRIGLARAFFGNPKLLILDEPNSNLDAEGEAALERALLQ-AKAGGTTVIIVTHR-PAIVLKCDKALVLRNG-AVDAf 541
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlNQLQGTSILLISHDlESISQWADTITVLYCGqTVES- 240
|
....*....
gi 517342213 542 GPASEILQR 550
Cdd:COG4170 241 GPTEQILKS 249
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
341-528 |
2.54e-07 |
|
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: 51.87 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLARllagvaeptgGTIALDGadyptwDRKQLGGYIGYLAQ--------DVQLLP 412
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAF----------DTIYAEG------QRRYVESLSAYARQflgqmdkpDVDSIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 413 G-----SIAENIARFDAGVSDANITE-----------AASRAQAHALItGLKQGYqTTMEAAGGSLSGGTRQRIGLAR-- 474
Cdd:cd03270 75 GlspaiAIDQKTTSRNPRSTVGTVTEiydylrllfarVGIRERLGFLV-DVGLGY-LTLSRSAPTLSGGEAQRIRLATqi 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 475 --AFFGnpKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCD 528
Cdd:cd03270 153 gsGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAAD 206
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
350-519 |
2.66e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 350 PGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGadypTWDrkqlggyIGYLAQDVQLLPGSIAENIA-------RF 422
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQ-------LAWVNQETPALPQPALEYVIdgdreyrQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 423 DAGVSDAN-----------------ITEAASRAQAHALITGLkqGY-QTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLI 484
Cdd:PRK10636 95 EAQLHDANerndghaiatihgkldaIDAWTIRSRAASLLHGL--GFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 517342213 485 LDEPNSNLDAEGEAALERALlqaKAGGTTVIIVTH 519
Cdd:PRK10636 173 LDEPTNHLDLDAVIWLEKWL---KSYQGTLILISH 204
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
16-281 |
2.66e-07 |
|
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: 52.48 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 16 IFFSILINLFLLVPSIYM---MQVY-DRVLpSASIPTLVYLSLIALG-ALIFLATLDAVRAVYCQR----VALSLDKHF- 85
Cdd:cd18569 4 LLFVVLAGLLLVIPGLVIpvfSRIFiDDIL-VGGLPDWLRPLLLGMAlTALLQGLLTWLQQYYLLRletkLALSSSSRFf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 86 ----------------GEdafiasISSPKAAMGDIQPL--RDLATtrsfvaskglaNLIDLPFAPIFAVILYCIHPVLCL 147
Cdd:cd18569 83 whvlrlpveffsqryaGD------IASRVQSNDRVANLlsGQLAT-----------TVLNLVMAVFYALLMLQYDVPLTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 148 VTVAGAAVMILM--VVASHYATRS-----AAGKAQEAAVAAnllaqafTRNRETVQGMGMIGHVTERWGRRFADAANLQD 220
Cdd:cd18569 146 IGIAIALLNLLVlrLVSRKRVDLNrrllqDSGKLTGTTMSG-------LQMIETLKASGAESDFFSRWAGYQAKVLNAQQ 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517342213 221 GASAINAIFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVA 281
Cdd:cd18569 219 ELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVG 279
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
340-541 |
3.02e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 340 IIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTI--------------ALDGAD------------YPTWD 393
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDlssnpllymmrcFPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 394 RKQLGGYIGYLAqdvqlLPGSIAeniarfdagvsdaniteaasraqahalitgLKQGYqttmeaaggSLSGGTRQRIGLA 473
Cdd:PLN03073 604 EQKLRAHLGSFG-----VTGNLA------------------------------LQPMY---------TLSGGQKSRVAFA 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517342213 474 RAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKAGgttVIIVTHRPAIVL-KCDKALVLRNGAVDAF 541
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVSHDEHLISgSVDELWVVSEGKVTPF 705
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
343-529 |
3.18e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDlkPGHVLAILGPSGSGKSSLARLLagvaeptggtialdgadyptwdrkqlgGYIGYLAQDVQLLPGSIAeniarf 422
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAI---------------------------GLALGGAQSATRRRSGVK------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 423 dagvsdANITEAASRAQAHALITGLkqgyqttmeaaggslSGGTRQRIGLARAF----FGNPKLLILDEPNSNLDAEGEA 498
Cdd:cd03227 60 ------AGCIVAAVSAELIFTRLQL---------------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|.
gi 517342213 499 ALERALLQAKAGGTTVIIVTHRPAIVLKCDK 529
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLPELAELADK 149
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
12-270 |
4.15e-07 |
|
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: 51.87 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 12 WVEVIFFSILINLFLLVPSIYMMQVYDRVLPSASIPT--LVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGEDA 89
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 90 FIASISSPKAA-------------MGDIQPLRDLATTRSFVASKGLANLIDLpfapiFAVILYcIHPVLCLVTVAgaaVM 156
Cdd:pfam00664 81 FKKILRQPMSFfdtnsvgellsrlTNDTSKIRDGLGEKLGLLFQSLATIVGG-----IIVMFY-YGWKLTLVLLA---VL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 157 ILMVVASHYATRSAAGKAQEAAVAANLLAQAFT---RNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSS 233
Cdd:pfam00664 152 PLYILVSAVFAKILRKLSRKEQKAVAKASSVAEeslSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 517342213 234 RTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISG 270
Cdd:pfam00664 232 QFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
341-561 |
4.23e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSLArLLAGVAEPTGGTIALDgadYPTW--DRKQLGGYIGY--------------- 403
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWR---F*TWcaNRRALRRTIG*hrpvr*grresfsgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 404 --LAQDVQLLPGSIAENIARFDAGVSDANITEAASRAQAhalitglkqgyqttmeaaggSLSGGTRQRIGLARAFFGNPK 481
Cdd:NF000106 105 enLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA--------------------KYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 482 LLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKAL-VLRNGAVDAFGPASEILQRLSGA--KPRP 558
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELtVIDRGRVIADGKVDELKTKVGGRtlQIRP 244
|
...
gi 517342213 559 VNA 561
Cdd:NF000106 245 AHA 247
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
348-523 |
6.72e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 348 LKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGtialDGADYPTWDR-------KQLGGYIGYLA----------QDVQL 410
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLG----DYEEEPSWDEvlkrfrgTELQNYFKKLYngeikvvhkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 LP----GSIAENIARFD-AGVSDanitEAASRaqahaliTGLKQgyqtTMEAAGGSLSGGTRQRIGLARAFFGNPKLLIL 485
Cdd:PRK13409 172 IPkvfkGKVRELLKKVDeRGKLD----EVVER-------LGLEN----ILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517342213 486 DEPNSNLDAEgeaalER----ALLQAKAGGTTVIIVTHRPAI 523
Cdd:PRK13409 237 DEPTSYLDIR-----QRlnvaRLIRELAEGKYVLVVEHDLAV 273
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
343-536 |
8.49e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG--ADYPTwDRKQLGGYIGYLAQDV-QLLPGSIAENI 419
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALENGISMVHQELnLVLQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ArfdagvsdaniteaASRAQAHALITGLKQGYQTTM------------EAAGGSLSGGTRQRIGLARAFFGNPKLLILDE 487
Cdd:PRK10982 95 W--------------LGRYPTKGMFVDQDKMYRDTKaifdeldididpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517342213 488 PNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLK-CDKALVLRNG 536
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
345-550 |
9.74e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 345 SFDLKPGHVLAILGPSGSGKSSLARLLAGvaeptgGTIALDGADYPTWDR------KQLGGYIGYLAQD--VQLLpgSIA 416
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG------ELPLLSGERQSQFSHitrlsfEQLQKLVSDEWQRnnTDML--SPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 417 ENiarfDAGVSDANITEAASRAQAHALITGLKQGYQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEPNSNLDAEG 496
Cdd:PRK10938 95 ED----DTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 497 EAALERALLQAKAGGTTVIIVTHR----PAIVlkcDKALVLRNGAVDAFGPASEILQR 550
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNRfdeiPDFV---QFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
358-519 |
1.10e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 358 GPSGSGKSSLARLLAGVAEPTGGTIALDgadyptwdrkqLGGYIGYLAQD------------VQLLPGSIAENIARFDAG 425
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNERLGKLRQDqfafeeftvldtVIMGHTELWEVKQERDRI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 426 VSDANITE--------------------AASRAQAHALITG--LKQGYQTTMEAAGGslsggTRQRIGLARAFFGNPKLL 483
Cdd:PRK15064 103 YALPEMSEedgmkvadlevkfaemdgytAEARAGELLLGVGipEEQHYGLMSEVAPG-----WKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 517342213 484 ILDEPNSNLDAEGEAALERALLQAKAggtTVIIVTH 519
Cdd:PRK15064 178 LLDEPTNNLDINTIRWLEDVLNERNS---TMIIISH 210
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
460-519 |
1.60e-06 |
|
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: 49.14 E-value: 1.60e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 460 GSLSGGTRQ------RIGLARAFFGNPKLLILDEPNSNLDAEG-EAALERAL-LQAKAGGTTVIIVTH 519
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIeERKSQKNFQLIVITH 181
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
103-280 |
3.60e-06 |
|
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: 49.02 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 103 DIQPLRDLATTrsfvaskGLANLID--LPFAPIfAVILYCIHPVLCLVTVAGAAVMILMVVASHYATRSAAGKAQE--AA 178
Cdd:cd18546 105 DIDALSELLQT-------GLVQLVVslLTLVGI-AVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRAREriAA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 179 VAANL--------LAQAFTRNRETVQGMGmigHVTERWGRrfadaANLQdgASAINAIFAGSSRTLRMVLQLAILGTGAV 250
Cdd:cd18546 177 VNADLqetlagirVVQAFRRERRNAERFA---ELSDDYRD-----ARLR--AQRLVAIYFPGVELLGNLATAAVLLVGAW 246
|
170 180 190
....*....|....*....|....*....|
gi 517342213 251 LVLQGQMTAGMIFASSTISGRALQPIDQLV 280
Cdd:cd18546 247 RVAAGTLTVGVLVAFLLYLRRFFAPIQQLS 276
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
275-387 |
3.83e-06 |
|
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: 49.80 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 275 PIDQLVAGWRQIVDARKAWKRLGSVIASGKGHRADRLILPEPE-----GRLTVKNLFWAPTHARADTSAAIiKDVSFDLK 349
Cdd:COG4615 278 PLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPapadfQTLELRGVTYRYPGEDGDEGFTL-GPIDLTIR 356
|
90 100 110
....*....|....*....|....*....|....*...
gi 517342213 350 PGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDGA 387
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
343-493 |
6.04e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 343 DVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIAL-----DGADYPTwdRKQlggyIGYLAQDVQL---LpgS 414
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT--RRR----VGYMSQAFSLygeL--T 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 415 IAENI---AR-FDagvsdanITEAASRAQAHALIT--GLkqgyQTTMEAAGGSLSGGTRQRIGLARAFFGNPKLLILDEP 488
Cdd:NF033858 356 VRQNLelhARlFH-------LPAAEIAARVAEMLErfDL----ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
....*
gi 517342213 489 NSNLD 493
Cdd:NF033858 425 TSGVD 429
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
346-516 |
7.12e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 346 FDLKPGHVLAILGPSGSGKSSLARLLAGvaeptggTIALDGA---------------DYPtwdRKQLGGYIGYLAQDVQl 410
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNG-------EVLLDDGriiyeqdlivarlqqDPP---RNVEGTVYDFVAEGIE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 411 lpgSIAENIARFDA-------GVSDANITEAAsRAQA---HALITGLKQGYQTTMEAAG-------GSLSGGTRQRIGLA 473
Cdd:PRK11147 93 ---EQAEYLKRYHDishlvetDPSEKNLNELA-KLQEqldHHNLWQLENRINEVLAQLGldpdaalSSLSGGWLRKAALG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517342213 474 RAFFGNPKLLILDEPNSNLDAEGEAALERALLQAKagGTTVII 516
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFI 209
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
16-283 |
1.36e-05 |
|
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: 47.04 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 16 IFFSILINLFLLVPSIYMMQVYDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQRVALSLDKHFGEDAF--IAS 93
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYdhLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 94 ISSP---KAAMGD-IQplR---DLATTRSFVASkGLANLIDLPFapIFAVILYC---IHPVLCLVTVAgaAVMILMVVAS 163
Cdd:cd18542 85 LSFSfhdKARTGDlMS--RctsDVDTIRRFLAF-GLVELVRAVL--LFIGALIImfsINWKLTLISLA--IIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 164 HYAT--RSAAGKAQEAAVAANLLAQ----------AFTRNRetvqgmgmigHVTERWGRRFADAANLQDGASAINAIFAG 231
Cdd:cd18542 158 VFFKkvRPAFEEIREQEGELNTVLQenltgvrvvkAFARED----------YEIEKFDKENEEYRDLNIKLAKLLAKYWP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 517342213 232 SSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLvaGW 283
Cdd:cd18542 228 LMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQL--GR 277
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
341-528 |
1.63e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLKPGHVLAILGPSGSGKSSL---------ARLLAGVAEPTGGTIALDGADYPTW----DRKQLG--------G 399
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypalARRLHLKKEQPGNHDRIEGLEHIDKviviDQSPIGrtprsnpaT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 400 YIG-----------------YLAQ--DVQLLPGSIAEniarfdagVSDANITEA----ASRAQAHALITGLKQ---GYQT 453
Cdd:cd03271 91 YTGvfdeirelfcevckgkrYNREtlEVRYKGKSIAD--------VLDMTVEEAleffENIPKIARKLQTLCDvglGYIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 454 TMEAAGgSLSGGTRQRIGLARAFF---GNPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCD 528
Cdd:cd03271 163 LGQPAT-TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCAD 239
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
16-264 |
2.82e-05 |
|
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: 46.40 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 16 IFFSILINLFLlvPSIYMMQVyDRVLPSASIPTLVYLSLIALGALIFLATLDAVRAVYCQ----RVALSL---------- 81
Cdd:cd18557 5 LLISSAAQLLL--PYLIGRLI-DTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNiageRIVARLrrdlfssllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 82 ------DKH-FGEdaFIASISSpkaamgDIQPLRDLATTrsfvaskGLANLIDLPFAPIFAVILYCIH-PVLCLVTVAga 153
Cdd:cd18557 82 qeiaffDKHkTGE--LTSRLSS------DTSVLQSAVTD-------NLSQLLRNILQVIGGLIILFILsWKLTLVLLL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 154 AVMILMVVASHYA--TRSAAGKAQEAAVAANLLAQ-AFTrNRETVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFA 230
Cdd:cd18557 145 VIPLLLIASKIYGryIRKLSKEVQDALAKAGQVAEeSLS-NIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQ 223
|
250 260 270
....*....|....*....|....*....|....
gi 517342213 231 GSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFA 264
Cdd:cd18557 224 GITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTS 257
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
454-566 |
6.28e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 454 TMEAAGGSLSGGTRQRIGLAR----AFFGnpKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDK 529
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATqigsGLTG--VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADY 558
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 517342213 530 ALVLRNGA------VDAFGPASEIL--------QRLSGAKPRPVNANRVSV 566
Cdd:TIGR00630 559 VIDIGPGAgehggeVVASGTPEEILanpdsltgQYLSGRKKIEVPAERRPG 609
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
341-523 |
7.29e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 341 IKDVSFDLkPGHVL-AILGPSGSGKSSLArllagvaeptggtialdgadyptwdrkQLGGYIGYLAQDVQLLPGSIAENI 419
Cdd:cd03238 11 LQNLDVSI-PLNVLvVVTGVSGSGKSTLV---------------------------NEGLYASGKARLISFLPKFSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 420 ARFDagvsdaniteaasraQAHALI-TGLkqGYqTTMEAAGGSLSGGTRQRIGLARAFFGNPK--LLILDEPNSNLDAEG 496
Cdd:cd03238 63 IFID---------------QLQFLIdVGL--GY-LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180
....*....|....*....|....*..
gi 517342213 497 EAALERALLQAKAGGTTVIIVTHRPAI 523
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDV 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
461-533 |
1.59e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517342213 461 SLSGGTRQRIGLARAFFG---NPKLLILDEPNSNLDAEGEAALERALLQAKAGGTTVIIVTHRPAIVLKCDKALVL 533
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
109-260 |
1.83e-04 |
|
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: 43.58 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 109 DLATTRSFVASkGLANLIDLPFAPIFA-VILYCIHPVLCLVTVAGAAVMILMVVASHYATRSAAGKAQEA-AVAANLLAQ 186
Cdd:cd18551 102 DTTLLRELITS-GLPQLVTGVLTVVGAvVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDAlGELSAALER 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517342213 187 AFTRNReTVQGMGMIGHVTERWGRRFADAANLQDGASAINAIFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAG 260
Cdd:cd18551 181 ALSAIR-TVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVG 253
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
101-279 |
2.50e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 43.27 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 101 MGDIQPLRDLATTrsfVASKGLANLIDLPFapiFAVILYCIHPVLCLVTVAGAAVMILmvVASHYA--TRSAAGKAQ--E 176
Cdd:cd18564 118 TGDVGAIQDLLVS---GVLPLLTNLLTLVG---MLGVMFWLDWQLALIALAVAPLLLL--AARRFSrrIKEASREQRrrE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 177 AAVAAnLLAQAFTrNRETVQGMGMIGHVTERWGRrfADAANLQDG--ASAINAIFAGSSRTLRMVLQLAILGTGAVLVLQ 254
Cdd:cd18564 190 GALAS-VAQESLS-AIRVVQAFGREEHEERRFAR--ENRKSLRAGlrAARLQALLSPVVDVLVAVGTALVLWFGAWLVLA 265
|
170 180
....*....|....*....|....*
gi 517342213 255 GQMTAGMIFASSTISGRALQPIDQL 279
Cdd:cd18564 266 GRLTPGDLLVFLAYLKNLYKPVRDL 290
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
136-281 |
2.82e-04 |
|
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: 43.21 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 136 VILYCIHPVLCLVTvagAAVMILMVVASHYATR-----SAAGKAQEAAVAANL--------LAQAFTrNRETvqgmgmig 202
Cdd:cd18549 135 IILLTINVPLTLIV---FALLPLMIIFTIYFNKkmkkaFRRVREKIGEINAQLedslsgirVVKAFA-NEEY-------- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 203 hvtERwgRRFADAANLQDGASAIN----AIFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQ 278
Cdd:cd18549 203 ---EI--EKFDEGNDRFLESKKKAykamAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRR 277
|
...
gi 517342213 279 LVA 281
Cdd:cd18549 278 LVN 280
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
136-264 |
5.34e-04 |
|
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: 42.09 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 136 VILYCIHPVLCLVTVAGAAVMILMVVASHYATRSAAGKAQEAavaanlLAQAFTRNRETVQGMGMI------GHVTERWG 209
Cdd:cd18576 129 VLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDE------LAEANTIVEETLQGIRVVkaftreDYEIERYR 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 210 RRFADAANLQDGASAINAIFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMIFA 264
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVA 257
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
109-279 |
8.18e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 41.70 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 109 DLATTRSFVAsKGLANLIDLPFAPIFAVILYCIHPVLCLVTVAGAAVMILMVVASHYATRSAAGKAQEAAvaanllAQAF 188
Cdd:cd18543 105 DLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQA------GDLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 189 TRNRETVQGMGMI-GHVTERW-GRRFADAA-NLQD---GASAINAIFAGSSRTLRMVLQLAILGTGAVLVLQGQMTAGMI 262
Cdd:cd18543 178 TVVEESVTGIRVVkAFGRERReLDRFEAAArRLRAtrlRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTL 257
|
170
....*....|....*..
gi 517342213 263 FASSTISGRALQPIDQL 279
Cdd:cd18543 258 VAFSAYLTMLVWPVRML 274
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
329-386 |
1.62e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 1.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 517342213 329 PTHARADTSAaiIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPTGGTIALDG 386
Cdd:PRK13546 30 PKHKNKTFFA--LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
242-296 |
2.23e-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: 40.50 E-value: 2.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 517342213 242 LAILGTGAVLVLQGQMTAGMIFASSTISGRALQPIDQLVAGWRQIVDARKAWKRL 296
Cdd:cd18571 240 ILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
353-372 |
2.85e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 38.62 E-value: 2.85e-03
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
353-372 |
4.66e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 38.85 E-value: 4.66e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
462-524 |
5.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517342213 462 LSGGTR-Q-----RIGLARAFFGNPKLLILDEPNSNLDAE-GEAALEraLLQAKAGGTTVIIVTHRPAIV 524
Cdd:COG4717 559 LSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDErLRAALE--LLAELAKGRQVIYFTCHEELV 626
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
336-378 |
6.94e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 6.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 517342213 336 TSAAIIKDVSFDLKPGHVLAILGPSGSGKSSLARLLAGVAEPT 378
Cdd:PLN03140 176 TKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPS 218
|
|
| |
