ID A0A2V5IFJ2_9EURO Unreviewed; 238 AA.
AC A0A2V5IFJ2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Matrin-type domain-containing protein {ECO:0000259|PROSITE:PS50171};
GN ORFNames=BP00DRAFT_483988 {ECO:0000313|EMBL:PYI35468.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI35468.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI35468.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI35468.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SF3A2 family.
CC {ECO:0000256|ARBA:ARBA00008995}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ825469; PYI35468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IFJ2; -.
DR Proteomes; UP000248817; 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: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 InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
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; PF16835; SF3A2; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM01050; CactinC_cactus; 1.
DR SMART; SM00451; ZnF_U1; 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 Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 54..84
FT /note="Matrin-type"
FT /evidence="ECO:0000259|PROSITE:PS50171"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 27363 MW; 026F2813DAB0EBFF CRC64;
MDYQNRAGSK FGGGGVASHS ATNADRRERL RKLALETIDL DKDPYFFKNH VGSFECRLCL
TVHQNDGSYL AHTQGRKHQT NLARRAAREQ REGKHQDPAA LPGALGVQVK KQTIKIGRPG
YKITKIRDPL TRQLGMLFQL QYQEITPGVT PRVRFMSAFE QKVEEPPDKS FQYLVVAAEP
YQSCAFKLQA REIDRREGRY WTWFDEDSKE FWVQIMFKTE REERFSGVPG LAPLEPNA
//
