ID A0A2T3AVP6_AMORE Unreviewed; 367 AA.
AC A0A2T3AVP6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=M430DRAFT_44583 {ECO:0000313|EMBL:PSS12703.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS12703.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS12703.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS12703.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR023577}.
CC -!- SIMILARITY: Belongs to the NOSIP family.
CC {ECO:0000256|ARBA:ARBA00008126, ECO:0000256|PIRNR:PIRNR023577}.
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DR EMBL; KZ679015; PSS12703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AVP6; -.
DR STRING; 857342.A0A2T3AVP6; -.
DR InParanoid; A0A2T3AVP6; -.
DR OrthoDB; 5483933at2759; -.
DR Proteomes; UP000241818; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR016818; NOSIP.
DR InterPro; IPR031790; Znf-NOSIP.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13063; ENOS INTERACTING PROTEIN; 1.
DR PANTHER; PTHR13063:SF10; NITRIC OXIDE SYNTHASE-INTERACTING PROTEIN; 1.
DR Pfam; PF15906; zf-NOSIP; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PIRSF; PIRSF023577; ENOS_interacting; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR023577};
KW Reference proteome {ECO:0000313|Proteomes:UP000241818};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 254..310
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 83..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 40762 MW; 1B77DBDE8AA06645 CRC64;
MSHSKRNTSR AVFTSYERSL AKAAWNSTSA RLSRDSFLPF ASCRLCLIPA RDPVSCSHGD
IFCRECALSN ILAQKKEIKR LEKAREREEK EAEEDRIREE DEARERAVQE FERIQMGLEA
KVGGAGKKIV GREDGKILVE EDVTGSKRGE KRKFELDEDE LLRIAREERT KARKAIDEEK
ASKTTLPSFW IPSITPSSNT NAPLHTISKK AKQSPICPAS PDDNPHPYSL HTLINVVFTE
EEEDATTKTR QRICPSCKKV LSNTSKAMLA KPCGHVLCKS CVTKFMTPSG VHDPHAPEVD
QNAVTCYVCD ADLTDRKPKK DKDAAAAKEG KEKEKVKPGL VEIRCDGTGF AGGGTNKVEK
LGVAFQC
//
