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Database: UniProt
Entry: A0A1F5LC87_9EURO
LinkDB: A0A1F5LC87_9EURO
Original site: A0A1F5LC87_9EURO 
ID   A0A1F5LC87_9EURO        Unreviewed;       667 AA.
AC   A0A1F5LC87;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0000259|PROSITE:PS50178};
GN   ORFNames=PENARI_c016G12077 {ECO:0000313|EMBL:OGE50697.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE50697.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE50697.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE50697.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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:OGE50697.1}.
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DR   EMBL; LXJU01000016; OGE50697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LC87; -.
DR   STRING; 1835702.A0A1F5LC87; -.
DR   OrthoDB; 1441111at2759; -.
DR   Proteomes; UP000177622; 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; 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; 1.
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   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:UP000177622};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          197..253
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          336..411
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  74668 MW;  84267053A5C27F9E CRC64;
     MSRRTLGGGR VLGNPSALAS VPSPQPKPRV LSPTASSVSL SSQTSASQFS SETQDLTSRI
     SIENGDTSIS AAPAAPGAQL SCPICNEEMM TLLQLNRHLD DIHQNLEDDR QDEVKDWFKV
     QMEKARKFQP LAVLNQKLKG LDVFESNENQ NAPLVSRPLA THAGSSEPPR PLDPEDLITK
     DHWQASCIYD ECLEPSCGKR LNATNGCVNC RSCGKLFCEE HTMYQMKLSR AAHHEPVRGI
     WARVCETCYK SREGYNDHNG VTRDQTDAFK SIRKQTVDRD FLEISRLEKR LTRLTQLLAS
     LPPDQIHPSA TKLWSLAWQS DQRKELEQTI VSWQDDASVS RCPFCQQDFS GYTFRRHHCR
     TCGRVVCGDQ NTECSSEVGL SIAPSSSEKT NTDKLINIDV RLCKDCKATL FDRRDFKADT
     MRKPSEIRAY ENLIQFERGI RLHLPRFQKL LTSLQDPRRP PSSAQIADAS KVRKRLIDSF
     AQYDVAARRI RDMPTNSPTQ QRLQKAIYQQ ASNFLHLHML PLKTLPKILK HATPASDRIP
     SRTSSPSTPV NSSTSNIRPS ESALASIKYN SVAASGSNSS LVSETSSAVS ALEAEEKSLR
     DRLIVLEEQK FFVSEMIADA NRRRKFDEVS SLAVNVEDLS REIDRVNGML AGLDFEGVYT
     ANLQPST
//
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