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Database: UniProt
Entry: T2M3P7_HYDVU
LinkDB: T2M3P7_HYDVU
Original site: T2M3P7_HYDVU 
ID   T2M3P7_HYDVU            Unreviewed;       270 AA.
AC   T2M3P7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=STUB1 {ECO:0000313|EMBL:CDG66582.1};
GN   Synonyms=LOC100210298 {ECO:0000313|RefSeq:XP_002169066.2};
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG66582.1};
RN   [1] {ECO:0000313|EMBL:CDG66582.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole animals {ECO:0000313|EMBL:CDG66582.1};
RX   PubMed=24065732; DOI=10.1093/gbe/evt142;
RA   Wenger Y., Galliot B.;
RT   "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT   bilaterian, euteleostome, and hominidae ancestors.";
RL   Genome Biol. Evol. 5:1949-1968(2013).
RN   [2] {ECO:0000313|RefSeq:XP_002169066.2}
RP   IDENTIFICATION.
RC   STRAIN=105 {ECO:0000313|RefSeq:XP_002169066.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR   EMBL; HAAD01000350; CDG66582.1; -; mRNA.
DR   RefSeq; XP_002169066.2; XM_002169030.3.
DR   EnsemblMetazoa; XM_002169030.3; XP_002169066.2; LOC100210298.
DR   EnsemblMetazoa; XM_002169030.4; XP_002169066.2; LOC100210298.
DR   GeneID; 100210298; -.
DR   KEGG; hmg:100210298; -.
DR   OMA; WAGVEHD; -.
DR   OrthoDB; 313431at2759; -.
DR   Proteomes; UP000694840; Unplaced.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd16654; RING-Ubox_CHIP; 1.
DR   Gene3D; 6.10.140.2020; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045202; CHIP_RING-Ubox.
DR   InterPro; IPR041312; CHIP_TPR_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46803; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   PANTHER; PTHR46803:SF2; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   Pfam; PF12895; ANAPC3; 1.
DR   Pfam; PF18391; CHIP_TPR_N; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00028; TPR; 3.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS51698; U_BOX; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome {ECO:0000313|Proteomes:UP000694840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   REPEAT          37..70
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          71..104
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          193..267
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
SQ   SEQUENCE   270 AA;  31228 MW;  1671F868F679FE4C CRC64;
     MSALDLKEQG NRLFAARSYD DAIGCYTKAI IKDPSAGSYY TNRALCYLKL KKWKLAIADS
     QHAIDIDPKN VKAHFFIGQA YMENNSFDEA ITNFQIAYDL AKEQKLNFGD DIASSLRAAK
     KKRWSLLEEK RIQEEIELQS YLQRLILEEK ERKLQTVVEG SENASLIEAD TKKRLLELNS
     LFAQVDERRQ KRDVPDQLCG KISFEIMKDP VITPSGITYD RKDIEEHLQR VGHFDPVTRA
     PLNVNQLIPN LAMKEVVEEF LEKNEWAEYY
//
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