ID A0A2H3DHZ2_ARMGA Unreviewed; 960 AA.
AC A0A2H3DHZ2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARMGADRAFT_125859 {ECO:0000313|EMBL:PBK93454.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK93454.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KZ293656; PBK93454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3DHZ2; -.
DR STRING; 47427.A0A2H3DHZ2; -.
DR InParanoid; A0A2H3DHZ2; -.
DR OMA; NIPHDAR; -.
DR OrthoDB; 49069at2759; -.
DR Proteomes; UP000217790; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd16449; RING-HC; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
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; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 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:UP000217790};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 692..903
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 696..744
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 108047 MW; 0BABC5C25462AA2F CRC64;
MQIFSSSENE PVDGENQTPK DENRASSANV PLPNHAWMNT RGEGYQFVHG ANSHLNQEDH
VKLAKEKAED KAENERLRQE EVQRKMDEET RIHQEEEQRR MNEEQFTADA HWSRTRQYIV
FGTIDSGSEA GPSRQPQENN VMIAEAKAQE LREENERLYQ EEVRRKRDER HRQEETRIRQ
EEEQRRIDEE QRTADAHRAH QCTVFGSIVT FSSGLAIQNI IAGFDCCRIR VKNIPHDARP
HEVEDLFLQQ GLDVSEFHVV SVDSTSNGTK QADIVTNATV AQILAAGLEG MEFRDERLEF
EICTFNLPGG MGALAPEDEN VLTISCRGPS TTYSVAYPDM ATCHLKVAEL NGHICSGRKV
KVEINQTLFG HVVPAYRRNA IRISNLPYDA SLAMVCDFAK PGYLHVQLLT SSNFDIDAAC
LQLQWQINKA AGSEVQSFDV TSRGDTEAGI VSVRVRFETW ECAKKVEDAL ANRCYPFVGN
SMFRSNLPQQ QLYTIIIPSQ QYRAQASLWT DLEASIKDPK ACDLFIRQEP GGDFRVQISG
AVKAAIGAPK VRIENLASGE KFDQWHEHLA LPSAALMKKI KDAGAFMRSD FRKHSVKLYG
TSVAITQAKA ILKEEIDHLM SMQSSVQLER RSVGYFLRTG LTAMKEVFGE NCVALDIRSA
RITIRGGEEI RLHLKNHIAE SLKAVIVQIA PGNHTCPVCY DEASSPFQLV CQHVYCTACI
RHFLTSAAET GIFPLACMGN NATCGTLISI PVLQKFLPQN SFNHLLETAF TSYVDKQHQV
FGYCKTPDCT QIYRKSESPF PLLCPSCFSE ICSSCGEDSH VGKSCEEARI FNNTAEQERL
SEAWIMQQSG IKKCPTCSRL LEKTAGCNHM QCPCGSHICW RCMSVFPAAD IYRHMNAEHG
GYYTADPTPD ANLNNNVPDP FQGADYREQA RLLHELEVRR QQGRELPVQP QERGSYCVVM
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