ID A0A0F4GL80_9PEZI Unreviewed; 677 AA.
AC A0A0F4GL80;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Vacuolar segregation protein pep7 {ECO:0000313|EMBL:KJX97988.1};
GN ORFNames=TI39_contig447g00006 {ECO:0000313|EMBL:KJX97988.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97988.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX97988.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97988.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) 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:KJX97988.1}.
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DR EMBL; LAFY01000439; KJX97988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GL80; -.
DR STRING; 1047168.A0A0F4GL80; -.
DR OrthoDB; 1441111at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; 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; 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 SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF140125; Rabenosyn-5 Rab-binding domain-like; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 356..429
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 600..667
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 74977 MW; 98E82AD49AC987BE CRC64;
MASRRSLGGG RVLGSGKGLA PPAPAPAISI PPKQVQATRN TGLLSPSESS VSLNSQASST
PITDHEDLTS RIALDEQGSA QAAAAASSRM VCPICNEEMV TLLQLNRHID DNHANLEVIE
QDEAKTWFKS QMTKAKKFQP LALINQKLRG LEVFESNDEL LQAVTAVTGP PPVAEGRGTP
TAALLAKEEE PPNPDEVVTR THWQRPRVND ACADPMCGRR LGAQNGQINC RHCGKLFCEE
HTMYQMKLSR SAQHEPVRGL WCRVCETCYK SRPGYLDNRG FERDHTDFLK SARRKTVDKK
YLETSRLETR LTRLTQLLAN PPPAEQTTTS MLWSSFAGNK PQIRALEQSV VPWEDDATVA
ACPFCHQPFS QYTMRRHHCR ICGRVVCGDP ATSCSSEIGL DVDLKKAGSG EGKVSVDVRM
CKDCNRTIFS KADFARELST QTPLQRAYQN LISFEHGIRL MLPKFQRILI PLQDPNNPPS
SDQIAEAGKI RKRLTDAFTQ YDVAARRVRD MDTGGSPTQE RLQKAIYLQA TNFLHIHMLP
LKSLPKIMKH ANPSTSSSSR PSTPATPNGH LRPPHLTNGS SSSPLRPDHS RTSSASSAAI
TALEAEEKEL KERLMVLEEQ QFFVKEMIAD AGKRRKYDEV SALTRNAEDL GREVDALRGE
LEGMEGQWRG VYEEGLG
//
