ID A0A165ZYJ0_9AGAM Unreviewed; 673 AA.
AC A0A165ZYJ0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=SWIRM-domain-containing protein {ECO:0000313|EMBL:KZT34768.1};
GN ORFNames=SISSUDRAFT_991406 {ECO:0000313|EMBL:KZT34768.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT34768.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT34768.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT34768.1,
RC ECO:0000313|Proteomes:UP000076798};
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).
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DR EMBL; KV428166; KZT34768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ZYJ0; -.
DR STRING; 1314776.A0A165ZYJ0; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02336; ZZ_RSC8; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR041984; Rsc8/Ssr1/Ssr2_ZZ.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12802:SF41; BRAHMA ASSOCIATED PROTEIN 155 KDA; 1.
DR PANTHER; PTHR12802; SWI/SNF COMPLEX-RELATED; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 92..189
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 283..337
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 342..392
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 345..396
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 552..582
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 73370 MW; 5FFBEBAA6F68DC03 CRC64;
MSSPKRPAPR SSSVSSDPKR QKLSVDPSNV KTETDQDDDA PDVTMDDAVE VEEDEEGSGD
ENDDEDPAAQ EATRIKLEEQ AKKYLAAQTH EVIIPSYSAW FDMSTIHPIE KKSLPEFFNS
RNRSKTPSIY KDYRDFMINT YRLRPSEYLT VTACRRNLAG DVCAIMRVHA FLEQWGLINY
QIDPDTRPSA LGPPFTGHFR LILDTPRGLS SLHPGTKAPA PTVNGLQKHQ QPGQPGQPGQ
PPLPQSTSLE LRSSIYQTTN KASRQLTPAE AAALPSTSST TKTVAYQCDT CGVDCTPERY
HCLKRKNFEL CPSCYLDGRF PSTMFSGDFL KLTSAANGAH ENGSTDPEDW TDQETLLLLE
AIEMYDDDWS AIEEHVGTRS AHACIKKFLE LPIEDPYIEQ EAEGKVGPLR FGRIPWEKAD
NPIMSVVAYL AGVSKDSARK DGEAKEEPKE GVLESKAEES TTDVAPADGD TSMTSNPPET
QPAETSSTSE PNAPPSETTT NGTSKKIGLP TSRAARAAHL ALQSTSRAAN ALSDQTSTQI
RSSLAQIIKL TLTKLDLKMQ HFEELEDALE EERRSLETAK FALVKERMKI RKAFEEMRAN
AMQNGGFGAG GIGGVPGVPG MGGVPGMGGF GEDALLGVTD QGTRVEEVKG DLMMGFEGDL
GPYLDGSTIA QLV
//
