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Database: UniProt
Entry: A0A3B3WKT1_9TELE
LinkDB: A0A3B3WKT1_9TELE
Original site: A0A3B3WKT1_9TELE 
ID   A0A3B3WKT1_9TELE        Unreviewed;       742 AA.
AC   A0A3B3WKT1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Tripartite motif-containing protein 2 {ECO:0000256|ARBA:ARBA00039484};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=E3 ubiquitin-protein ligase TRIM2 {ECO:0000256|ARBA:ARBA00041590};
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM2 {ECO:0000256|ARBA:ARBA00043214};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000003259.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000003259.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
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DR   RefSeq; XP_014832820.1; XM_014977334.1.
DR   AlphaFoldDB; A0A3B3WKT1; -.
DR   STRING; 48701.ENSPMEP00000003259; -.
DR   Ensembl; ENSPMET00000011155.1; ENSPMEP00000003259.1; ENSPMEG00000004389.1.
DR   GeneID; 106910648; -.
DR   KEGG; pmei:106910648; -.
DR   CTD; 100003782; -.
DR   OrthoDB; 5387006at2759; -.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd14960; NHL_TRIM2_like; 1.
DR   CDD; cd16767; RING-HC_TRIM2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR001298; Filamin/ABP280_rpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR   PANTHER; PTHR24104:SF50; TRIPARTITE MOTIF-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF17170; DUF5128; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF01436; NHL; 4.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS51125; NHL; 6.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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:PRU00024}.
FT   DOMAIN          23..64
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          113..154
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          320..421
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   REPEAT          471..514
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          518..561
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          562..603
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          607..650
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          654..697
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          698..741
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   COILED          183..210
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   742 AA;  81120 MW;  16BACC4711BCEE56 CRC64;
     MATESSTIPS PVVCQIDKQF LICSICLDRY QNPKVLPCLH TFCERCLQNY IPAHSLTLSC
     PVCRQTSILP ERGVAALQNN FFITNLMDVL QHRPDTCRQE ATTLSNITTV ATGRLLSCPN
     HGGSVMEFYC PPCETAMCQE CTSGEHREHP TVPLKDVVEH HKASLQDQLN AVKKRLPEID
     SALLLLSEIL QQLTNQKSSI EDEIHTTFDE LQKTLNVRKS VLLMELEVNY ALKQKVLQAQ
     LDTLLQGQEG INSSCNFTEQ ALSHGTEAEV LLVKKQMGER LVELANQELP LQPGENSQLD
     FLMETDGLKK SIHNLGTVVT TNAVASETVV TGEGLRHCVV GVPTAVTITT KDKDGELCKM
     GNAVIAADIS SPDGSKVDGE ILDNQNGTYE YLFTAPKEGF LTLSLRLYNQ HIRGSPFKIK
     ATIHSSPNTD GIKKTLKSPG SGHVKQKAIK RPASMYSTGR RKENPIEDDL IFRIGTKGRN
     KGEFTNLQGV AASSQGKVLI ADSNNQCVQI FSNDGQFRSR FGIRGRTPGQ MQRPTGVAVH
     PSGDIIIADY DNKWVSIFSN EGKFKNKVGS GKLMGPKGVA VDRNGHVIVV DNKACCVFIF
     QVNGKLVTKF GNRGNGDKQF AGPHFAAVNN NNEIVVTDFH NHSVKVFNTE GEFLLKFGSN
     GEGNGQFNAP TGVAVDINGN IIVADWGNSR IQVFDASGSF LSYINTSADP LYGPQGLALT
     SDGHVVVADS GNHCFKVYRY LQ
//
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