ID A0A165WN39_9AGAM Unreviewed; 518 AA.
AC A0A165WN39;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS00028};
GN ORFNames=FIBSPDRAFT_939362 {ECO:0000313|EMBL:KZP07759.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP07759.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP07759.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP07759.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV417741; KZP07759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165WN39; -.
DR STRING; 436010.A0A165WN39; -.
DR OrthoDB; 5483967at2759; -.
DR Proteomes; UP000076532; 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; 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; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 262..284
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 286..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 59212 MW; 6813F1FF3C865CAF CRC64;
MDSIIEQQRQ NHEEIERFER ALYTLLSRHQ PTHESRLLNE HKSAQVLDRI SSRVTALDNI
YAEDDVRQAE INLLSAPQQQ NDLSEFYSRL VKIQEHHSKY PDATPGGFDL ELAALLEEGN
QDDEEQEEED PIALMFSGEE AYGKYVDLYT NHTAYNNLKG IGKRPGYLQY LDILMLASKG
PVHEELSKET RLTKDYESYI KNLHAYLLSF SRRTQPLVDI DAQQREAEAE FETKWEAGDI
PGWEEAKPKT QTSNGEAGGI WCTACQKNYS KQTVYDAHLT SKKHIKATAK QAASDAPPTN
PNGTSTPHAA SVPQQSPANS RLRMAAFFTH LTTSLLVSLA LIINETKSNV ERRFSLTARE
REQELLDQSK PATQPVNSSG QAGEGEEEEE EERIYNPLKL PLGWDGKPIP YWLYKLHGLG
VEYRCEICSD HVYMGRKNFD RHFQESRHAF GMRAMGLPNT KHFHEITRIA DALALAEKLK
QEGRHEIFEN ETMEELEDDE GNVYNRKTYE DLKKQGLI
//
