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Database: UniProt
Entry: A0A010QNM8_9PEZI
LinkDB: A0A010QNM8_9PEZI
Original site: A0A010QNM8_9PEZI 
ID   A0A010QNM8_9PEZI        Unreviewed;      1675 AA.
AC   A0A010QNM8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Endosomal cargo receptor {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CFIO01_09533 {ECO:0000313|EMBL:EXF81712.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF81712.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF81712.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF81712.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC       {ECO:0000256|ARBA:ARBA00007104}.
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:EXF81712.1}.
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DR   EMBL; JARH01000354; EXF81712.1; -; Genomic_DNA.
DR   RefSeq; XP_007594623.1; XM_007594561.1.
DR   STRING; 1445577.A0A010QNM8; -.
DR   KEGG; cfj:CFIO01_09533; -.
DR   eggNOG; KOG1693; Eukaryota.
DR   HOGENOM; CLU_004717_0_0_1; -.
DR   OrthoDB; 1881880at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.40.50.12360; -; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR015720; Emp24-like.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   InterPro; IPR038609; HDA1_su2/3_sf.
DR   PANTHER; PTHR22811:SF50; RE49489P; 1.
DR   PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01105; EMP24_GP25L; 1.
DR   SMART; SM01190; EMP24_GP25L; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1675
FT                   /note="Endosomal cargo receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001456136"
FT   TRANSMEM        180..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..115
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   DOMAIN          281..322
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          232..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1312..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1599..1675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1657..1675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1675 AA;  185890 MW;  EF01B7281900B35D CRC64;
     MRVSAIACGL FACFVSQVAA TALTYKLHAN EKACFYAKTQ KDNEKIAFYF AVQSGGSFDV
     DYTVTGPGNK MILDGAKERQ GDFVFTAQQM GDYEFCFNNE MSTFAEKFVD FEIAVENEVR
     AQLPAKQGAS PEQHSTLEET IFKLSGQLST ISRGQKYFRT RENRNFSTVR STEGRIINFS
     MIQCALIVLM GALQVFIVRF FFQGARKGYT DHTLTREFSQ EQRYLWTRNR IRKLNPPRQR
     ATPKQHTTSI EVDRDSSMLR DSRRSSKHQK KHKEQPKEEW YIIKDILQER RNGSNIEYLV
     DWEDNPETGE RYRPTWAPSK DVTSKAIFDW RRKLDLVYQE DHPGPAGESV LRDVRSVVQQ
     GSPARTPSTR SIDSSQPVQT ANRRRRPQSR QPEDLQDPDS DNDSNPPQQK RYPSEVPSLL
     SSASDVDTDA ASDVAYNNTT TSFFVAIPSK VDRDFSEYIS ISDSQGSTSL GSQPISALED
     EDSQVVITEG LSQRTIPDSQ EYSALDTQDS PFSGRQEAST SNKGDACTER EVPDSQKQSS
     LRTSVSKSTD SQARLLSAPD HRSHFFVRRT PLESPRPASS QDQPVSSGYI PLTQNSPEPS
     QGPGFDLDQA SPFHRHSIAE PAASQPPRRA SREHDSLPSV SDRSIPSHQV DELRAVEQAE
     NSAIGDYPQD SQPTRTPIFH TQPAFDFDTS TSQATSSAKS ASSKSQQHTN NQEWAAEQII
     ACSDSRPSQN TQAAQVVQPL PDISASQSST DEPVVPDTVR RRPRTIRFSG TVASSESPPF
     AFSQAIAAAP SQRDEDDVSE ADSFQTCFER RSLPPHPSSS NKSQDSDQPL SLPPAMDTSG
     DEPLSAIEEL MRIQEAALQG TLGEAGLTSP TTDSAQIRHD GPSMDADLAF SAPMDHPSIQ
     INSQPPLTGD WTMGEPVTSS TDMPGLVGAP VEPTMEPLIH EEHQTASMGD IFPSNLMPPE
     SVEQLPITIS PSDISRSVEP EEASNTLPQP EDHPMDMLPE DQTTAGDQST VTSPDIEEPY
     LSGPPTTVDQ SEYLVTLSFP ANIRPLYRST IKSYRTVIEQ FTKDMQSEED VVDKNTMESI
     GKMLNELRDI CDMPAPLDGA SIDALSAEDL KKHAMGTNSK FFFVGRFLER LQTSHKKILI
     VARDLNVIGY LEAMVGTGEM AYSLKGLHEL ESQDEHSLLV VLVHSEQALV DDLSDFDVVV
     GFDNGILQTD LLDQWGKMNG KKPMLLRLTT TCSIEHLELL LPAEFQGLVR QNALCIAVCQ
     SRKMSYLDER DNQGVMIDHY AVSFANQAIL PDPGFDWDPE LIPSSVLDLY SSSQPESQVE
     EPTRKRKTDG EQLQAVKRLR VSPPPGQEPG DIDAAVRSQL NPQPSQLHIQ TTQQHLNALT
     DKVSELEHQL EEKNTMESNL QKQVTNLSKR VKSYDETTNS IQAAHMASLR ERARFEAERD
     EAKRKEEHAL EKSREWQDKA QAFEEKLKAT SATLEEALVN AGSVATETFK EKTAELEKAL
     AKVAELEKKL ESRDGELSYA RDAYQTANHS NSELSRENRE LKEQVAAMQS SAPGNLAQVL
     NVTANAGQQV KEMQRQIAET KAITKDRERE LARVEKELRA LKNGRRETRQ QSVPRSPRLS
     VMSPRTGRAA GGGGNGGSAS RGTSPTPHES GGGTPVAGLQ FFNNSANNRW PHLRD
//
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