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Database: UniProt
Entry: A0A151I8Q0_9HYME
LinkDB: A0A151I8Q0_9HYME
Original site: A0A151I8Q0_9HYME 
ID   A0A151I8Q0_9HYME        Unreviewed;       791 AA.
AC   A0A151I8Q0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 32.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=ALC62_14345 {ECO:0000313|EMBL:KYM95015.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM95015.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYM95015.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYM95015.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM95015.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KQ978339; KYM95015.1; -; Genomic_DNA.
DR   RefSeq; XP_018404133.1; XM_018548631.1.
DR   AlphaFoldDB; A0A151I8Q0; -.
DR   STRING; 456900.A0A151I8Q0; -.
DR   GeneID; 108780815; -.
DR   OrthoDB; 2943236at2759; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd20338; BRcat_RBR_RNF19; 1.
DR   CDD; cd20355; Rcat_RBR_RNF19; 1.
DR   CDD; cd16629; RING-HC_RBR_RNF19; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR11685:SF427; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
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   TRANSMEM        336..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..326
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          111..159
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          39..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  85528 MW;  7CB56994D875F46D CRC64;
     MFKENENGVG GCNGAPPRPR RLFPRFSLRR LLHSSPLIGR RIARTPSASN RNAKAKDHAN
     SRATDVEKGE ARVSNGSSHF QFHNIDLQRA PSKGSVLSSA GKSNENGLMD CPLCLAELPV
     EFFPIIQSCH HRSCYDCFQQ YLKMEISESR VNIACPECSE PLHPNDIRMI LNDQTQLEKY
     EDFMVRRVLA IEPDARWCPA PDCSFAVIAS GCASCPKLRC ERPGCDSYFC YHCKARWHPN
     QTCDAARAQR SQYYERSSSL SFSQTDSQHR DDIKPCPRCQ VLIVKMDDGS CNHMTCAVCG
     AEFCWLCMKE ISDLHYLSPS GCTFWGKKPW SRKKKILWQL GTLVGAPIGI GLVASIAFPA
     MIIGIPVWVG QKLYTRYEKA NKHKRNAFIA GGVTASVLVS PVLAGLAVGI GVPILLFYVY
     GVVPVSLCRS GGCGVSTSGT GVRFEFDDEN ELMGALGVRN GGDAASIDVA SHRGGNPSIG
     EASLSLGSGS QLEKLGREND RESASNVALA GTSLAGSIAS SVLPGGQRLE VQADVTSTQR
     FSLCSETASA ATSLSEKSVN ASIALDDGAA STRALAGSVL NFKMDGSSIS GGRSTEGEQA
     ASSANDGHMD SAGQATSLSS LEEVAPGLAK RIRRKLTFDR QCSDSSSWTM CGEDGGSERV
     RFDDHVSVIE ADQERIVGKL EGCVVNNRSA GGRKRNKDSE IEMEVQKTSK NSNGELNAES
     PVDDTSRERV NVATLKNVFF HASAVSTDRE KRLSVIEEPM PIVPHISGNQ IFTPLHNECQ
     SPTSTDKSLQ C
//
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