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Database: UniProt
Entry: A0A1X2IT20_9FUNG
LinkDB: A0A1X2IT20_9FUNG
Original site: A0A1X2IT20_9FUNG 
ID   A0A1X2IT20_9FUNG        Unreviewed;      1632 AA.
AC   A0A1X2IT20;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=PXA domain-domain-containing protein {ECO:0000313|EMBL:ORZ21687.1};
GN   ORFNames=BCR42DRAFT_408110 {ECO:0000313|EMBL:ORZ21687.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ21687.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ21687.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ21687.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORZ21687.1}.
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DR   EMBL; MCGE01000005; ORZ21687.1; -; Genomic_DNA.
DR   STRING; 90262.A0A1X2IT20; -.
DR   OrthoDB; 5392990at2759; -.
DR   Proteomes; UP000193560; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00313; PXA; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF140125; Rabenosyn-5 Rab-binding domain-like; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193560};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          116..307
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   DOMAIN          536..678
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          1166..1284
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          339..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1318..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1407..1439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..892
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1632 AA;  183887 MW;  A1F9C49BCA9DDBAE CRC64;
     MMSSLYSSKK LFIILSILCL SLEYYWPYTL YSLVYIIRLG ILSLWGLLVL NLFVLYIYVK
     YFISPTRVGQ DSRNKLDLED FRPFRFTQKH LWSRLEQQRE HENDLTSLPK LCDDNNAAIS
     AAFDELLSYV LRDFIQSWFD NLSPQEHSFP KSVDDIIRSA ALELKRRLTQ VDSLSVLLHR
     LIPRITAHIS EFRASEVALR GRFLERTVTE SDELDLLLAS HYAGGKLHPA LTTAAVTTTK
     PTEVAYLRQL VDRLLPKLLN SEQVACAPVR VIIREIATCA LLQPTMSMLA DPDFWNQTID
     TQLGMALREQ KMVRQLREVL DRHSSDIDIL NELMASDPAN LMNSTATPSS SFSSSKQEQD
     FGGSSTSDNN DNNNNNSNNK QQRRMDPISQ FSSAFLGMDM DDDVAWDDQD FDPEKPKKRQ
     NFGSSRMGRR TFQEFLKMIE EEKNLLDLKR ARNDVVTQLR KKKALILDRD PEEVVDGEKV
     EDLIVYVNRL GVAKKRVDKR IATLSGEHVD FKTSASQFFG VRKQRPKQLP QTSGFTLHDI
     LTNTAGLSYF MEFMDRRGDM VKLQFWLIVE GFRSSDNDGA KRDDRTFLQD VKMVYEMYFA
     STSPHRLAIT DHLDKDLLQS IQHAQQEVMG GADNAAQWGQ AMQEMQDQLY RIQQHVLWQL
     EKEHFPYFKR SDLYFKFLAS SPTPDVPPPG RRSLDDTSLY RRSSSVGQKQ QHHHRPSSHG
     SNFPQHPSSD NSSSTSTHQL SPPQSTVSLG IERSLSARMT TKRTASWIRR DSGQKADSDT
     EISTREKKRP SISVSTVGDG SGLLHQGSEN DASLTTSPSL TTSLNQGTHT RTYSDTVSAG
     GGTSSKFLSF GRVLGSANDW WRATDFGGVS SQQHKAPSIK RSSLQGSVKS TDTEYPDSDE
     ELSRSVTTLY DDQQTTPPYS SSHPLPPPPQ SLIRRNTVDA VEAELQSIID GKENSNEYEK
     EERTLTTTPS SSSTSSSSLS RPNSSSAQGS LHRSPTILLG GTGSDIKSAT ADPVAFAKPV
     PSWTSLGDTQ ALSQVMHHHL LDSGTQNDNQ HTTNDLSLQK SKLISGNDTK NEEEKRDHSI
     KNVHLAPPGD LMLADKVNNL SDKMEKLTQQ EAIVDALIKK AEAKGKVEEL RILIKSKNMF
     RRELEQMQYQ KSQYEFQESE NVLTPDRTKV SITSSTIGSD QHGDFALYVI EIQQVGFDGN
     YASGWIVARR YSEFFGLHQK LKSSYASVKM IDFPSKWPLL KLQKSFVEAR RINLERYLKR
     LLEQPEICHS EALRVFLSQQ NIYVPGPQRP SSSPDAGGLS PFGFFPFIPS SFQGMDLSSP
     SIHPPLPSSS SSSSVTSNSS PTARHLHRSL VLGDESPLGD QRTASDKKTK GFMRHIYNTV
     AAGIDDLFVT PSMLDLITQR LGEQVIGFSN DGDDNDDDDD QRTPPQNDRK SRRGATDDVG
     DMVDETMHTA AAAAAAAASM GSDLKHVDVE GMTRFTEPLC DLFIEMFELK EKNNWLRRQA
     VMIILQQILG GTIERKLRDT VKYLETESMV IFYFRKIMDS LWPGGAKLTF KPARKPDEKL
     QTKEEANRKL STWLPDLLGN MVGRQNARKG ARRLFSVLQN QRLNQHLVYV LLDEIVMALF
     PDIDDPTPLH KV
//
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