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Database: UniProt
Entry: A0A168PBQ8_ABSGL
LinkDB: A0A168PBQ8_ABSGL
Original site: A0A168PBQ8_ABSGL 
ID   A0A168PBQ8_ABSGL        Unreviewed;       518 AA.
AC   A0A168PBQ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=ABSGL_07869.1 scaffold 9181 {ECO:0000313|EMBL:SAM02106.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM02106.1};
RN   [1] {ECO:0000313|EMBL:SAM02106.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM02106.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT553674; SAM02106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168PBQ8; -.
DR   STRING; 4829.A0A168PBQ8; -.
DR   InParanoid; A0A168PBQ8; -.
DR   OrthoDB; 463769at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF17123; zf-RING_11; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          109..156
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          301..344
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          42..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  57146 MW;  00006A3BB4CBE115 CRC64;
     MGDAMCMLMI PPSTEEHPCP APERANSFRH LTHGAFGLRR FSRSLSGGPS GGSSGDASDP
     HNRQHRRSAT VLSTPSNTLH VRIVPSIENP SRSLIFDIFD RDLAPAVYIK IGRFTDRSPS
     PTRMSFKTKV VSRSHCEIWM ENGKSSSGTF LNHIRICPPN QLSQPHEIKD GDIVQLGVDY
     QGGVEEIYRS VKMRFEVNPT RRQRPLSFNL TAFQHLRQLT APPPASAAIK DAMVNSSSNG
     DSSAAGTAAP TSAVIMDQTR MDPTTLSSEH LTATHNSNNN ISSSNNNNSS PLSSPGELEE
     CCICLYALAP QQGLFVSPCA HTYHFKCIRP LLQSYPGFQC PICRTYSDLD ANLESQPAVF
     KSETPPSATQ QHQQQEQQQQ QQQQQHQQQQ EEQQEEQHSL PTTSTDHMNS ISNTSASQPQ
     PSSLESADDD DMVPLASLPT WEHDDAPLAD DATTSHGIVE KLKLAWFEKR GKKRANRARH
     EELPTSSGIT AHTLSRHSST HLAEIEEEEL AVAPFTTM
//
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