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Database: UniProt
Entry: A0A093C575_9AVES
LinkDB: A0A093C575_9AVES
Original site: A0A093C575_9AVES 
ID   A0A093C575_9AVES        Unreviewed;       755 AA.
AC   A0A093C575;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
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};
DE   Flags: Fragment;
GN   ORFNames=N339_03543 {ECO:0000313|EMBL:KFV08194.1};
OS   Pterocles gutturalis (yellow-throated sandgrouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX   NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV08194.1, ECO:0000313|Proteomes:UP000053149};
RN   [1] {ECO:0000313|EMBL:KFV08194.1, ECO:0000313|Proteomes:UP000053149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV08194.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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=2.3.2.27; 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   EMBL; KL234835; KFV08194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093C575; -.
DR   Proteomes; UP000053149; 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:UP000053149};
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          34..75
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          124..165
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          331..432
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   REPEAT          484..527
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          531..574
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          575..616
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          620..663
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          669..710
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          711..754
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          441..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV08194.1"
FT   NON_TER         755
FT                   /evidence="ECO:0000313|EMBL:KFV08194.1"
SQ   SEQUENCE   755 AA;  82675 MW;  0885877DC4845C9E CRC64;
     KGTGPICQWS RMASEGSNIP SPVVRQIDKQ FLICSICLDR YKNPKVLPCL HTFCERCLQN
     YIPAHSLTLS CPVCRQTSIL PEKGVSALQN NFFITNLMDV LQRTPDSSIE ESSILETVTA
     VAAGKPLSCP NHDGNVMEFY CQSCETAMCQ ECTEGEHAEH PTVPLKDVVE QHKASLQVQL
     DAVNKRLPEI DSALHFISEI IHQLTNQKAS IVDDIHSTFD ELQKTLNVRK SVLLMELEVN
     YGLKHKVLQT QLDTLLEGQE SIKSCSNFTA QALNHGTETE VLLVKKQMSD KLNELAERDF
     PLQPRENDQL DFIVETEGLK KSIHNLGTIL TTNAVASETV ATGEGLRQTV IGQPMSVTIT
     TKDKDGELCK SGNAYLTAEL STPDGSVADG EILDNKNGTY EFLYTVQKEG DFTLSLRLYD
     QHIKGSPFKL KVVRSADVSP TTEGVKRRVK SPGSGHVKQK AVKRPASMYS TGKRKENPIE
     DDLIFRVGTK GRNKGEFTNL QGVAASTNGK ILIADSNNQC VQIFSNDGQF KTRFGIRGRS
     PGQLQRPTGV AVHPSGDIII ADYDNKWVSI FSSDGKFKAK IGSGKLMGPK GVSVDRNGHI
     IVVDNKACCV FIFQPNGKIV TRFGSRGNGD KQFAGPHFAA VNSNNEIIVT DFHNHSVKVF
     NQEGEFILKF GSNGEGNGQF NAPTGVAVDS NGNIIVADWG NSRIQVFDGS GSFLSYINTS
     ADPLYGPQGL ALTSDGHVVV ADSGNHCFKV YRYLQ
//
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