ID A0A1J9R6G3_9EURO Unreviewed; 875 AA.
AC A0A1J9R6G3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACJ73_05431 {ECO:0000313|EMBL:OJD23221.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD23221.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD23221.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD23221.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJD23221.1}.
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DR EMBL; LGTZ01000848; OJD23221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9R6G3; -.
DR STRING; 1658174.A0A1J9R6G3; -.
DR VEuPathDB; FungiDB:ACJ73_05431; -.
DR OrthoDB; 1752784at2759; -.
DR Proteomes; UP000242791; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07199; Pat17_PNPLA8_PNPLA9_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000242791};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 327..373
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 392..604
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 875 AA; 97998 MW; 178594700F622840 CRC64;
MAHYGNFAGP IIVEVASGSG MVQIYKRTTF LSSPPIPEFL QTAIQRAARR RTHQAAPRHA
TAMRAYQSSG LTPHDVGGLE AVQSLLMKWA TIGSASTLPD TIRPRIIVVT GKDNDSITQA
LLNEEFFLLD IANDALFHSA FADISISRHP PGELFPDARY LDLHADIARE LHLARSARKI
HQVLFSATHM NAFYEDGLRH VTANMFTPFD FIHASRRLNP VSGSLVPHLS TVLNQGVNKR
MPYEDLVSYT ASAILMDAYP PLMHGIAYEQ VLGNCALADL MCQNVDHQLE RLFEFMSMKG
DSSSHIHRYN LNQRRKHLAL LRLNSVCLVC VIRCAEYRLP CGHALCDSCV ERFGEGCAGA
ESEYVVTTCP LCNTPTALKV RVKPSTFAAR LFSIDGGGLL GIIPAELLVF MQKRLLCNLQ
LRNLIDYFIG TSSGGDISLD IGICQNGAEK CSERFQQLAK GFFGGQQRGC VSKLRRLAKI
WTADGMYDSR ALEHVFRQHY GATLRMFDTP RTMIAGWRVA VTSTSVADGT PFLFTNYNGE
TPLRNDCVYG CLRTMVDDEP FVWQAARATS AAPVLFPSID IPSVGSFQDG GMKQRHNNPI
RSGLSEVRRL WPRTPKPHVV ISLGTGTVSR ALKTSDSRNI LLDGWLPRIY RSYMSSFDGE
ETWNELQGEL DDQTSKNYFR LNYSFTGARP SIVDISAMEN ISRSIQKNPP AADKMEEALL
TLLASSLFFE LDSIPEFQNG FFRCVGTIRC YGPTRPIIRS LLALRPAHHE FYKDDINLGL
YLSEDDICVE FQRYCQPVRF SVRHLQEKIT MTLRSDGTAL LLNGFPNATQ WYIDEQGLDG
VFGASNHGAP FRIQCDTCER RLNGKEKKRK YMYTR
//