ID A0A1B9G5F6_9TREE Unreviewed; 775 AA.
AC A0A1B9G5F6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alkylbase DNA N-glycosylase {ECO:0000313|EMBL:OCF26232.1};
GN ORFNames=I302_03911 {ECO:0000313|EMBL:OCF26232.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF26232.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF26232.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF26232.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI894020; OCF26232.1; -; Genomic_DNA.
DR RefSeq; XP_019047302.1; XM_019190554.1.
DR AlphaFoldDB; A0A1B9G5F6; -.
DR GeneID; 30208310; -.
DR VEuPathDB; FungiDB:I302_03911; -.
DR OrthoDB; 125113at2759; -.
DR Proteomes; UP000092730; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16536; RING-HC_RNF10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039739; MAG2/RNF10.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 139..181
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 86378 MW; 54D4DE399590E494 CRC64;
MPAVPTPTLN SSARTNPKPD LNMSSDDPST WLNFSLPPRS RAGVPGSGVP GVPRRSRRGE
GWRGGPMSRE KFLNASFKFV LKPTETISYG AHFADPDISL HWPHILQVLV PTFSAFSVAQ
GYVTKRRRRM EEERRGRMCP ICLGKPVAGR MTKCGHIFCF PCILHYIQLS DIPKSARCPI
CGDTIHSSYL KSVKYLDAAA MLKASTGEDD ENEVTPSQSS SSTNTDHTNH EAHGHGIIGV
MDGFEETLEE ARAVDAHLTK GDKSHQIHMR LVQRPQMTTL ALPSSSTWPS DAIPPHTAPW
YFLPDILAYS RFMLSTPEYM LSELSRELSE LKGEWDMLKG DELGREFVKA AKEKVERQMQ
KVRAELVTEL VKRSERAARE AWGEAVGGSR REKERRRERD RIAKEREERQ KTEQDKTDIP
HEFLSGSIPS TPSFDNSANI NIPPNIEVEP NPMPTPTPKK SRRRGGGGHG PNPPPAIPPS
PSYYFYQSSL GANVFLHPLD IRILLAHFKS YSLFPPTISF ATTGYDPGTI NDELRKRCKY
LGHLPIGTEV IFVEADLEPI VSQEVLDQFE QPLKARKMKR KDKLKREDKA KLKWEKSERE
KLPVDLRSTP SAFRTGGAED RDFAIALARS AVEFDPSQNT FQPSSTSSST SMTHQYPIPG
VSPSTSPSNG TGVWGAAQQN QSRATFAHAL HNHTMSSMPV QRRQEIDWEV EAAWEAFENM
STRDRTPLQE GQEEGREVIG ENTIRESEKG GGSRKGKKGK GQKLVLGGGG GARRA
//