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Database: UniProt
Entry: S8C261_DACHA
LinkDB: S8C261_DACHA
Original site: S8C261_DACHA 
ID   S8C261_DACHA            Unreviewed;       878 AA.
AC   S8C261;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-SEP-2023, entry version 47.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H072_4394 {ECO:0000313|EMBL:EPS41707.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS41707.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS41707.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS41707.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS41707.1}.
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DR   EMBL; AQGS01000224; EPS41707.1; -; Genomic_DNA.
DR   RefSeq; XP_011110294.1; XM_011111992.1.
DR   AlphaFoldDB; S8C261; -.
DR   STRING; 1284197.S8C261; -.
DR   eggNOG; KOG0801; Eukaryota.
DR   eggNOG; KOG1729; Eukaryota.
DR   HOGENOM; CLU_340635_0_0_1; -.
DR   OMA; FGHQATA; -.
DR   OrthoDB; 38671at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15737; FYVE2_Vac1p_like; 1.
DR   CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23164; EARLY ENDOSOME ANTIGEN 1; 1.
DR   PANTHER; PTHR23164:SF30; LD23155P; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          380..472
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          832..874
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..599
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  93432 MW;  CB1ED6CE256AEC1A CRC64;
     MAMTESSSQQ LLVLDPSSEG PSLAGPASSS SSSPSPALLI DDLKRTKLDA PSSSSAAASS
     SRVHVSVKDS GPTPPSSPSQ HIGTAAAAAA AAALAGDATD NVASDAAPPD TEHEHHHHDN
     IIVNSSSSSS SSVDQPGADL LPAGALAAAS SSPRLIHQQP TPPSTLPEDA AFPQAATDHH
     NLIVPPSSVE DSSSVSSSSQ NPVTEPYLVE REEDPLPQPI SGTRSASPAA SPRSSSSSLP
     STLNDDEDDD NGVPTLDANE AAFLLEADAM ESNLGNNNNL GTTANSDSPA PIARPTALPR
     IPSSSSQHST LADLPTLQIP QHSPPVPFQP HQTGSQYSFP YASTLDSRIS SSTTTTATTS
     RPERDLRTPL SPEVPPWQPD SEVSNCPICT TTFSFFYRKH HCRKCGRVVC APCSPHRIVI
     PRSFVVYPPN SIDPDLSSQA YVDSAGNRRS SFGGGDAGVE VRICNQCLAG DYPSSSSSSN
     QRRQSIQSPP GGAGRFWQDF GPPTGVNANN YVPPQNVAFG GNHGAPRRRT VSSGNNFSQA
     HGGQGYPGAM YHHHYGQAHS LGRNQHGAFP GQPHPPYHSH PVQQQLPPLQ HPTPSYPLPQ
     PGHHNFSFVP AQFYPSPQPP QHHHQHQGHQ RSVSSSSHPY SQYSPINQPI SGHLDTSQRP
     VPAFSMPDTS RPNLPIAGHF MHGNTLRELQ THSAPPQPRL KETDYCPICQ NVLPPPNPVT
     RDETAREAHI QQCIDNTISG NSSSVARRRS TSGAPSSHAS LANTTMSSQP SASHQSTSIP
     TPNHQPQPSD SVRRSRASSR PTGGRMFVYT ATAKDTLPSG SDAKADDQKA ECVICFEEFE
     EGDSIARLEC FCRYHKKCIT DWFNRRGDGQ CPVHAMNE
//
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