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Database: UniProt
Entry: A0A0P7BG07_9HYPO
LinkDB: A0A0P7BG07_9HYPO
Original site: A0A0P7BG07_9HYPO 
ID   A0A0P7BG07_9HYPO        Unreviewed;       688 AA.
AC   A0A0P7BG07;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Matrin-type domain-containing protein {ECO:0000259|PROSITE:PS50171};
GN   ORFNames=AK830_g7064 {ECO:0000313|EMBL:KPM39486.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM39486.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM39486.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM39486.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SF3A2 family.
CC       {ECO:0000256|ARBA:ARBA00008995}.
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:KPM39486.1}.
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DR   EMBL; LKCW01000106; KPM39486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7BG07; -.
DR   STRING; 78410.A0A0P7BG07; -.
DR   OrthoDB; 5475496at2759; -.
DR   Proteomes; UP000050424; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.2690; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR031781; SF3A2_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23205; SPLICING FACTOR 3A SUBUNIT 2; 1.
DR   PANTHER; PTHR23205:SF0; SPLICING FACTOR 3A SUBUNIT 2; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF16835; SF3A2; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM01050; CactinC_cactus; 1.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          505..535
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50171"
FT   REGION          419..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  74997 MW;  00EB1782FE99496F CRC64;
     MSQDLTQRLQ AELDAAVARY AQRNPRSRAL HDEAVKSMPG GNTRTVLYTD FTAEFTAALY
     GHSHPVLLSA IRDVLQNTGL NVGATTAQEQ VFARELCSRF HIEHVRFANS GTEANLHALA
     AARAFTKKRK VVAFGGGYHG AVLGFAGGKP GANNVDLGDW VVARYNDLES AHSAISGEGV
     AAVVVEGMQG SGGGITGSPE FLSGVQEAAN KASAGVLVIL DEVMTSRFTP GGLAELRGLT
     PDLKTFGKYL GGGLAFGAFG GRADIMAAFD PRLPGSLSHS GTFNNNTLVT HAGYAGLTKV
     YTPEVATRFT KRGDELRESL NEVTRGTRVC FTGMGTIMGV HFPNDGTRDF QRGGEVEEND
     ALRALFWFDM LEEGFWVVRR GFIALVLETP ESELESYDLA SVIDIASVNS STSLVASSSR
     TKLLNHPPSA AQTTARKATR NPPALSHPLE AMDFQNRAGS KFGGGGVASQ SATNADRRER
     LRKLALETID LDKDPYFFKN HVGSFECRLC LTVHQNDGSY LAHTQGKKHQ TNLARRAARE
     QKEGKQAVDP ATGLPIGVSG TGFAARRNVV KIGRPGYKIT KIRDPVTRQQ GLLFQLQYPD
     ATPETAPKWQ VMNAFTQHIE EPDKNFQYLL VAAEPYETVG FKIPARELDK REDRQFCFWD
     PDAKEYWIQV MFMTEREERF NAAPGTAR
//
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