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Database: UniProt
Entry: A0A165QKW5_EXIGL
LinkDB: A0A165QKW5_EXIGL
Original site: A0A165QKW5_EXIGL 
ID   A0A165QKW5_EXIGL        Unreviewed;      2797 AA.
AC   A0A165QKW5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=FMP27 GFWDK domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EXIGLDRAFT_635040 {ECO:0000313|EMBL:KZW03765.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03765.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW03765.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03765.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV425882; KZW03765.1; -; Genomic_DNA.
DR   STRING; 1314781.A0A165QKW5; -.
DR   InParanoid; A0A165QKW5; -.
DR   OrthoDB; 607689at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019443; BLTP2/FMP27/Hobbit_C.
DR   InterPro; IPR019441; FMP27/BLTP2/Hobbit_GFWDK_RBG.
DR   InterPro; IPR019409; FMP27_sixth_RBG.
DR   InterPro; IPR019415; FMP27_SW_RBG.
DR   InterPro; IPR019449; FMP27_WPPW_RBG.
DR   InterPro; IPR045167; Hobbit.
DR   PANTHER; PTHR15678; ANTIGEN MLAA-22-RELATED; 1.
DR   PANTHER; PTHR15678:SF6; PROTEIN KIAA0100; 1.
DR   Pfam; PF10293; DUF2405; 1.
DR   Pfam; PF10351; FMP27-BLTP2_C; 1.
DR   Pfam; PF10347; Fmp27_GFWDK; 1.
DR   Pfam; PF10305; Fmp27_SW; 1.
DR   Pfam; PF10359; Fmp27_WPPW; 1.
DR   SMART; SM01214; Fmp27_GFWDK; 1.
DR   SMART; SM01215; Fmp27_SW; 1.
DR   SMART; SM01216; Fmp27_WPPW; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1215..1316
FT                   /note="FMP27 SW motif-containing RBG unit"
FT                   /evidence="ECO:0000259|SMART:SM01215"
FT   DOMAIN          1334..1486
FT                   /note="FMP27/BLTP2/Hobbit GFWDK motif-containing RBG unit"
FT                   /evidence="ECO:0000259|SMART:SM01214"
FT   DOMAIN          1731..2200
FT                   /note="FMP27 WPPW motif-containing RBG unit"
FT                   /evidence="ECO:0000259|SMART:SM01216"
FT   REGION          1535..1555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2523..2603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2713..2797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1540..1555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2527..2543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2544..2562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2563..2588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2589..2603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2713..2736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2740..2757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2797 AA;  311798 MW;  8A7042C18358F61C CRC64;
     MQVWLSYPLY ILGLFAFGPA ADQGALVSWT LQLLRLVLFL LVTRRFIAPF ILAKLSNRIR
     VRSISLRSVR GLYYKQGELV WNVDRIGLAY HRPTKERPRR FAIQVEGLRL NVQHVPGAAH
     NNAATHSTAA IHKRLSSLFI PPPTTPVVAH PNWRSSALTP LRLLAHALDP FARPMLRMLF
     LAGFRILVRC LPALTQVLEF EMDSAVVSFE VLRGAHVRVS GVTVSTQVQF EGLETIRGAA
     ADEAVRGFAF GNFAGWNTRV RASAGRLWDR GWGNTRGAAS VAVKIGEVVG STQPLALDGF
     VESPLEIRPS NAVRKGTFLA IRCPVDLRAA LRFDPRRVKV DRHSLDMSVD VAGIEVMADV
     LQALVDLVEE AQRAGPGQEY FSTGRSFSPP TSPLLGAWKE MNSRGSPNVP VLPGKKKPSG
     LKRLAPFLKN VRIGLQSVTT TFRTPETAYL YRLSLDSFTV QARLSTPTSN RLHQRWLGST
     NSQDCGEGVV FDVTTDLRTL ALERSEGPGV SDMWTPLVAV TRIDCRTLIT DVVFGVKSRN
     RIFAGDPNSA FVVCELIVDN VSVTERIDAV NESLAQAELA APRPTTKRTA LPSQDMPRIR
     VDLLVRNVDL VLLRRADNVT DVELAVHTRT ERFEFHAETM FVPDCASKSF SASAPVLSEP
     SPLSKLRFNG TAILHPVFTR MTIQGLPEHL IEVAQEPFIS LDKVEVFVSG DAYALPTEDV
     AVVNTASVMA DISCVSDALS IELWNPHRVD ALAKLVSSIN VSKQPKTMTT AKAPLDILPS
     GVNARASVGE ILIIVTGPDL NPDCPLELSR GLAVKSSASL SYCFMQPSHS ERTRSQRLRT
     GSNRQRLGLQ EDLLVQAVAK ANAQTSPDDL VALVHMIVWQ TSCRVAVATE VAADHENAAN
     TFRLPHSPNG PAVVSAPMIV GRIALQRKHQ RALFDSQRHA DTCDAQVILS RLAATYNLLN
     VYCALLAADT LRKLVPKRSA TTSKPPSQLQ VSLRLSIEVF DMFFGLARGQ RVFFRVESIS
     VEKFAKVLRA RFHALKAFVP SVTHPEDATS AVQWDELGQL KALSASVTET DARERDIAVA
     ADSLCIRVAS GFKISDLILD IGVAVKAVKH LYAMVALGTF LDHPPPEAEG AKVVPNIQIR
     VETVVLEVED LVLDRKLNLI WQAGSLAQPV RLEREAAFDA KCAAILREGS PNPLVNLGSK
     GRYNFSAKHT VSIADARDRL NMLHSLSWAR RFNQSRTEQI RFEEQAARRV RTVSSSSESV
     WPIQRRHQDF STPLIRLQIA GLDLKLSQPS FELSALPDVL HDLGNGMPRD MQYTLLIPLH
     LEASFKHGTV QLRDYPLPLL YVPQHPAEPV AAFEFSTDLI IAEEIGPAFS TKWVQCPVVP
     ADSGIPGAHP LLFAVPKTAM PVKTYARPTV RVLTTETTHI SWGVSYLPVM QEVLRFVDTL
     TTPPDDNANP VGFWDKLRLV MHWQVRASFT GPVRFVLKGS RDPHSIIGAG AGFGLSWQGG
     TEVTVGYTDE AQELVQVTSD TMQLIIPDLQ RFTTRDPRRA AGTGDTNSQS ASRSGTQKVC
     AKFTNGVRMG LGFVFERTCA PKCADCPEDP FYRKCRLFDF KPHYRVQTRA SSASDGRDSF
     EGFRSDFIHM SFSLTTPTMP TPGRHGGHNN IYLSPLAFQH FWHWWDLFDN SMSLRIRQGK
     LFPDNVKETK KFGRFIATIK YRFYIEKLFI THIYQHDTRE AWTKGETPFI GVKAFMQSFH
     ADLHQSTQEI SLRRAGKDAV VSKHKKFNAV EVVIAGLELR AMAAVFAEPH KQLITLKRAS
     DESLRPWDDM EPHDVRSRWV DLDDFVELMW SAADRKPRIY LSHLASCPRF MFSKQAACRE
     PWVPQSTIHG VAESSAVSKF GTEHSHLCFL GKEPSAKQTQ MDLASQRLQH LLGERFQLSA
     AKSATDSPTS LSSVERVVDS PTDSVLTPEQ SLDKKIELLQ EYIEQLNLDS PDATGQVYYV
     AADSVDSSAW AEFGNVYHVH SPNIFVNNSN RNLLLTYYQA SRKRRGFEYH MATRAVKFLH
     DLAVEDSTRG DGEGAKGPWT AVGGAQAAVD VFRNLLIAEK TSTEDHSRDV HEPFSPEDPL
     RGWSDGVALS KSHYCVLFKP QFVLQSQKID DACVVVTASD ISLQNFLVID IQNQDDPVTG
     HIMNRNHAAV NGLQVFSPTT ALQPLEARKR LSHNVPLEVL VDYRCECNDF DRLVPQTEAV
     FHYDKFNRNR PRASASTDVP SHIAHQMDLV VVNMPRFSVA AKCKNFEAIS SVVTDLILFS
     DPAHKSRVER LETFIFSYDF TDLDGAADLV AKLQARIRQL QVIERGYVAR TDILDATERL
     DLLSIHAQIF VLAEELNLVF DAIAMAQDQN SDLHEDQQSA LKLVVSSKEI SWHMLDDRAS
     LLAKLEVLGV VFSWLSKQDG STSNDLVLKD ARALHSSPTA LWPEILIMHD QPANHPMVKA
     KQFAHAVWSV LPPVGGIPIY QNFQLDLHPI RLQIEAEIGR KLLEYVWPAR RARNGTQLLL
     VDDGLEEPST NDSSTTTLDR QKARQDTLSV HGLRERGLTR PRSHNNLRVQ ARPTLHRFKS
     STALNDMNDG SKSDDDRRPV KRATRVDQEI DAAAMRARST QQKTFFRVHI PRIHVLLSAR
     SDDFFCNEAQ LYTNEININN KTTSFEDMVT QYMPAVPNWK GWVRLVWSQD VIPVLPVAKE
     LFAKTKWGSK AAASQKNLLR SGTTMTSPTP VRQGSKHFWN RNRKNSEEAD HSSRPRSRSR
     PRTDKHRHDS SPAPHPRHDN IIISVQEPSP SVDRSFP
//
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