ID A0A0M9A2G0_9HYME Unreviewed; 681 AA.
AC A0A0M9A2G0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Tripartite motif-containing protein 2 {ECO:0000313|EMBL:KOX75915.1};
GN ORFNames=WN51_12345 {ECO:0000313|EMBL:KOX75915.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX75915.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX75915.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX75915.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX75915.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ435756; KOX75915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9A2G0; -.
DR STRING; 166423.A0A0M9A2G0; -.
DR OrthoDB; 5387006at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd14961; NHL_TRIM32_like; 1.
DR CDD; cd16579; RING-HC_PML_C-V; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
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; 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:SF8; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01436; NHL; 3.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51125; NHL; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 41..89
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 126..168
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 421..464
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 508..550
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 554..590
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 638..681
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT COILED 225..267
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 681 AA; 75169 MW; 8FEB341142305E10 CRC64;
MEALRLAIQT RLGERMVSMS SMLVETVSIN YEDFNESFLT CGTCLCVYDG GEHTPKLLPC
SHTVCLHCLT RIAASQTRET GAFRCPICRE LITIPRGGVP ALPPSFLVNQ LLDLMSRQRR
EVIPKCSVHI NQELLFCETC DTVFCTVCTG GNHAGTSPGC TEHTIIPFSI AIKRMSEILL
YKANECISKV TLTQAQDSVS TELQRLEASI ERCLSAVDTE FAEIISKIER RRTELQAAVT
AAARDKKHVL EEQHALIEAE KNKVQRECEG LQYQVEVRNI TQRIGSLSDQ LDAATALSEP
KENAFITFEF NHNNALSQLE EALNNLGRVR SSTTLPGLCR ARLKDPAIVK LQAAVIVETV
DYHGHPRNVG GDLITAELTL ADSIHSENQS SSIDTEILSV FERPIKDHPL FFDATEHNEP
IKIYGRRGTG KDEFHQPVAV AVNDDGMIYI LDTGNSRIKV LNCDLEFQRH ITNEGLEGRS
CTGIGISQQG IVVVNWRTRK VTEMSSLGDT IKSFSHNAFQ EPIDIAVDRS YGHILVADNG
QSCVFVFDSD GKILFQVGKR STFKLITSVT VGPNGEIVVA DSRIQVFSAK GDFSEEIYSE
GKGKGTYGGL AVDSEGRILG TRTDKGRSTI QVLKLGGGNI LTEIDSHNSK LRRPSGIAVL
PDNHLVVVDL GNDCIKKYRY W
//
