ID A0A151PB21_ALLMI Unreviewed; 744 AA.
AC A0A151PB21;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
GN Name=TRIM2 {ECO:0000313|EMBL:KYO46306.1};
GN ORFNames=Y1Q_0021829 {ECO:0000313|EMBL:KYO46306.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO46306.1};
RN [1] {ECO:0000313|EMBL:KYO46306.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO46306.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
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:KYO46306.1}.
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DR EMBL; AKHW03000533; KYO46306.1; -; Genomic_DNA.
DR RefSeq; XP_006264581.1; XM_006264519.3.
DR RefSeq; XP_014449340.1; XM_014593854.2.
DR RefSeq; XP_019337020.1; XM_019481475.1.
DR RefSeq; XP_019337021.1; XM_019481476.1.
DR RefSeq; XP_019337022.1; XM_019481477.1.
DR RefSeq; XP_019337023.1; XM_019481478.1.
DR RefSeq; XP_019337024.1; XM_019481479.1.
DR RefSeq; XP_019337025.1; XM_019481480.1.
DR AlphaFoldDB; A0A151PB21; -.
DR STRING; 8496.A0A151PB21; -.
DR GeneID; 102565512; -.
DR KEGG; amj:102565512; -.
DR CTD; 23321; -.
DR eggNOG; KOG2177; Eukaryota.
DR OrthoDB; 5387006at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19824; Bbox2_TRIM2_C-VII; 1.
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; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
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 473..516
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 520..563
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 564..605
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 609..652
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 658..699
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 700..743
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 430..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 81501 MW; 569C1961640EAAAC CRC64;
MASEGSNIPS PVVRQIDKQF LICSICLDRY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
PVCRQTSILP EKGVSALQNN FFITNLMDVL QRTPENSIEE SSILETVTAV AAGKPLSCPN
HDGNVMEFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AVNKRLPEID
SALQFISEII HQLTNQKASI VEDIHSTFDE LQKTLNVRKS VLLMELEVNY GLKHKVLQTQ
LDTLLEGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSDK LNELADRDFP LHPRENDQLD
FIVETDGLKK SIHNLGTILT TNAVASETVA TGEGLRQTVI GQPMSVTITT KDKDGELCKS
GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIKGSPFKLK
VVRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVGTKG
RNKGEFTNLQ GVAASTNGKI LIADSNNQCV QIFSNDGQFK SRFGIRGRSP GQLQRPTGVA
VHPSGDIIIA DYDNKWVSIF SSDGKFKAKI GSGKLMGPKG VSVDRNGHII VVDNKACCVF
IFQPNGKIVT RFGSRGNGDK QFAGPHFAAV NSNNEIIVTD FHNHSVKVFN QEGEFILKFG
SNGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
LTSDGHVVVA DSGNHCFKVY RYLQ
//
