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Database: UniProt
Entry: A0A316W827_9BASI
LinkDB: A0A316W827_9BASI
Original site: A0A316W827_9BASI 
ID   A0A316W827_9BASI        Unreviewed;      1572 AA.
AC   A0A316W827;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN   ORFNames=IE81DRAFT_319838 {ECO:0000313|EMBL:PWN45982.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN45982.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN45982.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN45982.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KZ819353; PWN45982.1; -; Genomic_DNA.
DR   STRING; 1522189.A0A316W827; -.
DR   InParanoid; A0A316W827; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000245783; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   PANTHER; PTHR19241:SF298; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR   PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14510; ABC_trans_N; 1.
DR   Pfam; PF06422; PDR_CDR; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        572..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        604..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        648..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        713..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        817..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1256..1278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1290..1308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1328..1354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1366..1392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1398..1419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1520..1542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          211..461
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          922..1161
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1572 AA;  171934 MW;  B58FC6D8B022DF62 CRC64;
     MSHNAPIAQQ SNVAAEQVTG EVQPAAEAPK AAPAAIPNFQ GGADAAPMSS AGTWGESQRG
     KPVDPARARE DFELARLASR QRSTTSRDPS FAGGGTIAQI ISGSSRRAKN AEKAIEEGSG
     TDDEKADAKA HLATSDEDFD LGAWIQSRFA QQQRQGVNSK KPLGLSWRDV SISAPGAGGG
     GIFVKTVPQS IINTATNDPL GILAKLVPGF GKLLSKASGL QQSPLLHPTS GVLRSGEMVL
     VIGRPGSGCT TFLKALTSSS DANVSQGGSI SYSGLSPAEI NKRYRGEVVF SGEDDIHFST
     ITVGQTLKFA LRNKVPTKKA RLEGESRDDF IETIVTLLLK MFNMSHVRDT IVGDAAVRGV
     SGGERKRVTL SEALITRASV IAFDNATRGL DASTALEYAR SLRIITDLAE RTTIATLYQV
     SESIFDLFDR VAVVDEGRVI YYGPRNQTRS YFEGLGYYTP ERQTTSDFCT ALVDPDQVQF
     KEGFETRAPR TAEDRERAWL QSDLYKALLN ETQEYESATA DADHAQQLGT VTANEKNTGV
     KPSSPYTVSF WQQTKACMWR QLLIQWSTRE DMYLKLFTIV TINLVIGALF FGQSRDSTGV
     FTRGGVLLFA TLLNGWLQLE VAFSAVAGRP MLARHRTFAF HRPAAVSLAR AIIDIPFLAV
     QCLLTTIILY WIANLRADAG AFFYFFLVVF LCAYNLTALY RAIASLVPGF NEAIRFSVMA
     LNVIIMTIGY VIRRPQMNWT IFLNYISGIP YAFEALLVNE LVGPIPCNPS QIVPFNEPRD
     VTYQTCAITG ASPGSLDTPS EDYLSTTFRY QSRTRGYNWA VVLAFTILYL IITLVAVEKL
     DWTAGGGGVT IWARTKEAKR RLAGATTEPA RKDDPEAAPV KPSRSNSGEA SDETRANSPE
     QTTGDANVQK KALDKWNDKA IFTWKDINLT LGNGRKLLHE VDGWVRPGQM TALLGQSGAG
     KTTLMTALSQ RGAAGHLTGE MLVDGKPIDK AFSKGTGLVL QADMHLATQT VREAIEFSAL
     LRQPAEIPRA DKLAHAQEVI ETLELESLAD ALIGMPGAGL SIEKRKRVTI GVELAAKPDL
     LLFLDEPTSG LDSAGAAAIV RLLRRLASEG QAILCTIHQP SALLFESFDN VLLLKPGGEV
     TFFGQAGNVA GKGSERIRRY FESQGAPECH PAQNVAEYIL EVVGGSLGRG VDWGKKWRES
     DDSKAVRTEI DNIIGERSQR PNKVASRDLR EYSAHTYEQI RVLVHRQLRD TWRDSAFTYG
     LLFSHLLVGL LSGGIFYGLN TSPVDLQNRI FVVFLILLNV PAVVNAIISK FFELRVLFEA
     RESPSKIYAW YSLIAAFLIA LTPVALVCAV IYFVPGFFLP YGKQPTYVAG FFFLNTLTVV
     YFFILFALIL VGSCPSPVIA AELVPFLLPI LAICNGVIVP RASMPQPFRS FVYYVNPISY
     YVQAQVSTIM HPLQVVCERE DLAIFNPPPG QDCSAYAGAW AQTAGGYLSN PEATAECGFC
     QYREGSQFAM TLNADYSFRW QAWGILLGFT FFNLFAVFFG YWWMNVKGYG IGVAASKSVA
     ARAWRSVRKS KK
//
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