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Database: UniProt
Entry: A0A319E9D0_ASPSB
LinkDB: A0A319E9D0_ASPSB
Original site: A0A319E9D0_ASPSB 
ID   A0A319E9D0_ASPSB        Unreviewed;       675 AA.
AC   A0A319E9D0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=FYVE-domain-containing protein {ECO:0000313|EMBL:PYI06040.1};
GN   ORFNames=BO78DRAFT_344583 {ECO:0000313|EMBL:PYI06040.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI06040.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI06040.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI06040.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ826353; PYI06040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319E9D0; -.
DR   STRING; 1448318.A0A319E9D0; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd15761; FYVE1_Vac1p_like; 1.
DR   CDD; cd15737; FYVE2_Vac1p_like; 1.
DR   Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   InterPro; IPR021565; Rbsn_Rab-bd.
DR   InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13510; FYVE-FINGER-CONTAINING RAB5 EFFECTOR PROTEIN RABENOSYN-5-RELATED; 1.
DR   PANTHER; PTHR13510:SF44; RABENOSYN-5; 1.
DR   Pfam; PF01363; FYVE; 2.
DR   Pfam; PF11464; Rbsn; 1.
DR   SMART; SM00064; FYVE; 2.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF140125; Rabenosyn-5 Rab-binding domain-like; 1.
DR   PROSITE; PS50178; ZF_FYVE; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          205..261
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          344..422
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          594..621
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        19..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  74822 MW;  5A987C19DD678883 CRC64;
     MPRRTLGGGR VLGPANARSP SALTPSPQPS NPRLLTLSPS ASSVSLNSQA SASQISSEAQ
     DLTSRISLEN VSASIPAAPA AAGAQLACPI CSEEMVTLLQ LNRHLDDVHQ NLEDDRQDEV
     KDWFKTQMDK AKRFQPLAVL NQKLKGLDVF ESNENIQPFA GPSRPSAPAS THPLEPARGP
     DPDDVITRDH WQARTLYDVC LEPSCGKRLN ATNGCVNCRK CGKLFCEDHT MYQMKLSRSA
     QHEPVRGLWC RVCETCYKSR EGYNDHNGLV RDRMDEFKAM RKQTVDKALL EVSRLEKRLT
     RLTQLLASLP MEQIQSSANK LWSISWQGDQ RKALEQTIVS WQDDTSVSRC PFCQQDFTSY
     SFRRHHCRTC GRVVCGDPAT GCSTEVPLSI SPLAKTSAEK SVRAGVINVD IRLCKECRST
     LFDRRDFEAD IMGRPPAVRA YDNLTQFERG IRLLLPKFQK TLGALQDPRR PPSSAQISEA
     SKVRKRLTDS FAQYDVAARR IRDMQTDSPT QQRLQKAIYQ QASNFLHLHM LPLKSLPKVL
     KHASSNGRPP SSTSSPTSPS PSNGSPGGHR RQGPALASIK YGSIAASGSN SSLASDASSA
     ISALEAEEKS LRERLIVLEE QKFFVSEMIA DANRRRKFDE VSSLAMNIED LTREIDRVNG
     MLDGLDFEGV YTGTH
//
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