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Database: UniProt
Entry: A0A395RJ17_FUSSP
LinkDB: A0A395RJ17_FUSSP
Original site: A0A395RJ17_FUSSP 
ID   A0A395RJ17_FUSSP        Unreviewed;       514 AA.
AC   A0A395RJ17;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Matrin-type domain-containing protein {ECO:0000259|PROSITE:PS50171};
GN   ORFNames=FSPOR_10847 {ECO:0000313|EMBL:RGP60107.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP60107.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP60107.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP60107.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SF3A3 family.
CC       {ECO:0000256|ARBA:ARBA00008776}.
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:RGP60107.1}.
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DR   EMBL; PXOF01000197; RGP60107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395RJ17; -.
DR   STRING; 5514.A0A395RJ17; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR031774; SF3A3_dom.
DR   InterPro; IPR024598; SF3a60/Prp9_C.
DR   InterPro; IPR021966; SF3a60_bindingd.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12786:SF2; SPLICING FACTOR 3A SUBUNIT 3; 1.
DR   PANTHER; PTHR12786; SPLICING FACTOR SF3A-RELATED; 1.
DR   Pfam; PF16837; SF3A3; 1.
DR   Pfam; PF12108; SF3a60_bindingd; 1.
DR   Pfam; PF11931; SF3a60_Prp9_C; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          419..450
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50171"
FT   REGION          111..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..387
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  59661 MW;  3E5FFC81AB3321D0 CRC64;
     MLVLEEQRYI HEDLERLEQG IADRIRDEPR HVSRFNSLTI RLLTFQIRDR LNRDHEISQL
     LDQIQVQSSN LLGIYKDENG VRAQEIQQIG TGDPFAEFYK QLKDVRDHHE RYPHEQAENS
     EQRYKVKRSD GEPMPSIVDS LFSGEEAYGR FFDLTTSHEA YLNLPNVRRL TYLQYLETFD
     NFSPAHGGVT RTGKLTDQYF KYVGQLADYL ESFMRRTRPL ENVDKVLASF DGEFETAWEK
     DEIQGWEKDA SSTNGTAKET STADAVWCDD CQKEFKNENV YKNHLTGRKH IKAAEQRKQQ
     DSAPTDDAGN GTSATRLKER AVAEREHRVK RLASAMSTER SDTRVNVERK QGMTERERAQ
     ELENYFNSED APQEPQEEGE GDDEDGEERI YNPLKLPLAW DGKPIPFWLY RLHGLGVEFP
     CEICGNFVYM GRRAFDKHFN EARHIYGLKC LGITNTTLFR DITGIAEALQ LWEKIQKEKK
     RTTVDEGSVV QMEDGEGNVM PEKVYYDLQK QGLL
//
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