ID A0A067TM42_GALM3 Unreviewed; 1155 AA.
AC A0A067TM42;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GALMADRAFT_91633 {ECO:0000313|EMBL:KDR80944.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR80944.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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DR EMBL; KL142371; KDR80944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067TM42; -.
DR STRING; 685588.A0A067TM42; -.
DR HOGENOM; CLU_004235_0_0_1; -.
DR OrthoDB; 1789161at2759; -.
DR Proteomes; UP000027222; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd20335; BRcat_RBR; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF00642; zf-CCCH; 2.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000027222};
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, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 18..45
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 92..119
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 821..1033
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 825..866
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 18..45
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 92..119
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 129983 MW; AEA08ABCF8E4C63A CRC64;
MSAEGQSMGS PPSNQRSATR QRPCNNWKQG YCRFGVNCKF QHDSANQPVP RGGSRRNSNQ
QSGPDRPEST INQPSGSGST NAVTGNRKTN RPNHAVTCRD WKAGNCPRGD NCRFRHEDEP
THTKIQPSES SSAGLVGSKN NSDDAHQKNR TRTLEGRAER DGPEQGERMP HPARTEAEKW
ENGEMIAREQ ADREAREKER QTGEALRMEA ERQARVARLA RERAELEVEE MRRQAQEQAR
RTEEASRLEA ERLRKLAAEK VARQARAEAL RQERARKAEE ERKRKEAEKL AREKAEAEAR
VRRQVQMQAQ REREAGAIEQ YIVLDSSLVT CCAGLNIRHV VTGFDLCKIT IKNLPKDAKR
AEIADLFLHQ GVESSEFFIF QVKPDASGSV LEAVILANAE HGQTIALGLQ GIEFRNRVLS
FSVSDNASGN AMDTPTRNSP FLLVSWRAPS ETLIATYSSM EEAQEKARKL NQAIWRGRQI
SAVMNDRPQG VAALRHFVPS SVKIMGLPPG VPVDADLVEF TGTWNLKMLK SISFDLPFSF
HTIRQHLTNS PGVRMGTYET LGSGEQASGE AKVKVLFDEW EAAKEAYASI GQIRLGPNSP
RFRAWLPPKP LLYTIKITRQ QYEAQKKQWD ALSEKKPGSD AHVQPRIGER GDVFIQVLGQ
DKKAAGSLKV RVESMVSGEK LDASYWHSSF GSQDGRAFFN RLYGEKKVFV RNDFKTRSLR
VYGEPEAVLD VRDMIKHEVE RLAGRDITRT LDQSCIGFFV REGLGKLTEL LGEGNVSLNL
SSRPCKITVK GGEEAIHHLH RLMDESRGGS FLGAALPGRV ERELCPICTD DVSNPEQLGC
GHTYCAGCLK HFLTSAADTK TFPLVCMGND ATCNVPISIP FIRRFLPAPI FQSLVEAAFL
SYLDQHPQEL KYCTTPDCKQ MYRHREEPTV LQCPSCFSTI CAACDEEAHD GMTCQERRLH
KNPAEQERLN EQLAAANGYK KCPQCKVWIE KTEGCNHMSC KCGAHICWRC MGIFDRATIY
QHMQTAHGNI YDEVPAGVNV GNAANNVFLA GQVDELARIE RERERTRQPV MANQPGLAPR
RFAAYGGQMG QYGQQEEERR RQAEAARRVN ERWRLEAEQA AAARRRQADE QTRQLLQERQ
PPRQEEERRG WCVVM
//
