ID A0A1D1VQV3_RAMVA Unreviewed; 516 AA.
AC A0A1D1VQV3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RvY_14303-1 {ECO:0000313|EMBL:GAV03945.1};
GN Synonyms=RvY_14303.1 {ECO:0000313|EMBL:GAV03945.1};
GN ORFNames=RvY_14303 {ECO:0000313|EMBL:GAV03945.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV03945.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV03945.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV03945.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:GAV03945.1}.
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DR EMBL; BDGG01000010; GAV03945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D1VQV3; -.
DR STRING; 947166.A0A1D1VQV3; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
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; cd20343; BRcat_RBR_HHARI-like; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186922};
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 140..353
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 144..192
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 60026 MW; 872357874A890BA2 CRC64;
MDSDEDVAFD DELDYASERD EEEGDNQHDD QEDHIDVDEE IGGRAPIIHN VSTPKICTPD
SGDYDVLSPD QICTYMNDVV KEVNQVIQQP PTTTRLLLSQ YKWDKEKLIE KYYEDTEKIF
ESCHVMSPVA KMQFGRRNGS SGECDICFMA VRSNDFKGTD CGHRFCTSCW KQYLTNKILN
ENISDKIECP AHGCNILLDD VFVMDMIGNQ PSVKRKYLHG ITNSFVLAHR SIRWCPGTDC
LYAIRVVSPE WMSVICTKCH TTFCFLCAET WHDPVPCTIL KRWKKKCADD SETSNWLVAN
TKECPNCHAT IEKDGGCNHV VCKNLACKGE FCWVCLGQWA AHGSSWFKCN RYSEEESKMA
RSAQEKSRAA LQRYLFYFNR YINHQNSLRL ETKLHNSVRI KMEEMQQHNM SWIEVQFLQK
AVNVLQHCRQ TLMFTYVFAF YLKKNNQQVL FEDNQSDLET ATETLSGYLE RDMTSQESVG
DIKQKVQDKA NYCESRRRVL VEHVHEGYEK DWWEFD
//
