ID A0A1Y2H045_9FUNG Unreviewed; 823 AA.
AC A0A1Y2H045;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=BCR41DRAFT_346195 {ECO:0000313|EMBL:ORZ27896.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ27896.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ27896.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ27896.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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:ORZ27896.1}.
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DR EMBL; MCFF01000003; ORZ27896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2H045; -.
DR STRING; 64571.A0A1Y2H045; -.
DR InParanoid; A0A1Y2H045; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000193648; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000193648};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 222..255
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 340..373
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 400..433
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 489..823
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 148..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 823 AA; 92788 MW; 40B22E54BDCA464A CRC64;
MASNSLTRRP IRLTVIAADG LYKRDVFRLP DPFAVVTVDG DQTHTTTVMK KTLNPYWNES
FEVMVTNKSV LAVQIFDQKK FKKKDQGFLG TVNIQMGDVF DVNIGGDEML TTELKKSGSN
DVVVQGKLII NISSNTSGQA VANGRLQTPS TAISHNRSSS VISGMSSSAA SSSNQRNSAQ
PASSSSLGTN GHVAGASASI TAAANSATNG GRQLSAYEDQ HGPLPPNWER RIDQLGRTYY
VDHNTRTTTW TRPSLTATTP ERNQELTSQT EMERRQHNNR GLPGERSGGN SPLPTGNSTT
NLAETNSPSQ TIANPSTSTS SSNAAGLAPI SLNSTTAGSG PLPAGWEQRL TPEGRPYYVD
HNTRSTTWVD PRRQQYVRMN DPRSSTTQVA VHQQPVSQLG PLPSGWEMRL TNTARVYFVD
HNTKTTTWDD PRLPSSLDQS VPQYKRDFRR KLIYFRSQPA LRPVPGQCHI KVRRSHIFED
SYHEIMRQSP TDLKKRLMIK FEGEDGLDYG GLSREFFFLL SHEMFNPFYC LFEYSAHDNY
TLQINPHSSI NSEHLNYFKF IGRVVGLAIF HRRLLDAFFI VSFYKMILKK KVTLADLESV
DADVYRNLNW LLDDPSGAET LDTTFTTNDE RFGEIVTIEL KENGQDIVVT EENKREYVDL
MTEWRITRRV EEQFKAFAEG FHQLIPQELV TVFDERELEL LMGGISEIDC DDWKKHTDYR
GYTEQDEVVQ WFWKCVRSWD SEKKARLLQF TTGTSRIPVN GFKDLQGSDG PRRFTIEKAG
EIGQLPKSHT CFNRIDLPPY KSYDVLVNKL TLAVEETVGF GQE
//
