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Database: UniProt
Entry: T1IMQ6_STRMM
LinkDB: T1IMQ6_STRMM
Original site: T1IMQ6_STRMM 
ID   T1IMQ6_STRMM            Unreviewed;       619 AA.
AC   T1IMQ6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR002269-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR002269-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) 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}.
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DR   EMBL; JH431092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1IMQ6; -.
DR   STRING; 126957.T1IMQ6; -.
DR   EnsemblMetazoa; SMAR002269-RA; SMAR002269-PA; SMAR002269.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG4582; Eukaryota.
DR   HOGENOM; CLU_007287_2_1_1; -.
DR   OMA; NIRINMM; -.
DR   OrthoDB; 45541at2759; -.
DR   PhylomeDB; T1IMQ6; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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:UniProtKB-UniPathway.
DR   CDD; cd02339; ZZ_Mind_bomb; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR042056; MIB1/2_ZZ.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR037252; Mib_Herc2_sf.
DR   InterPro; IPR040847; SH3_15.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR24202:SF53; E3 UBIQUITIN-PROTEIN LIGASE MIB1-RELATED; 1.
DR   PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF06701; MIB_HERC2; 2.
DR   Pfam; PF18346; SH3_15; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS51416; MIB_HERC2; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          15..83
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   DOMAIN          89..141
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          152..230
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   REPEAT          473..505
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          506..538
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          539..571
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          572..604
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   619 AA;  67191 MW;  EDD36BF45FE66970 CRC64;
     MPEMEPTGNG PTNRAARVTM EGVGARVLRG PDWKWGKQDG GEGHVGTVRN FESPEEVVVV
     WDNGTAANYR CSGAYDLRIL DSAPTGIKHE GTMCDTCRQQ PIFGIRWKCA ECTNYDLCSI
     CYHGDKHHLR HRFYRITTPG SERVLLEPRR KSKKIAIRGI FPGARVVRGV DWQWEDQDGG
     NGRRGKVTEI QDWSAASPRS AAYVIWDNGA KNLYRVGFEG MADLKVVNDA KGGTVYRDHL
     PLLGEQGPGR SGPHGLAIGD QVNVDLDLEI VQSLQHGHGG WTDGMFECLG TTGTVVGIDE
     DHDIVVSYPS GNRWTFNPAV LTKVNTTPPP SASGGEGATG QQFAVGDLVQ ICSDPERIKI
     LQRGHGEWAE AMTPTLGKIG RVQQIYHDND LKVEVCGTSW TYNPSAVTKV ASDGTVPGTS
     SGERLSALLK KLFENHVSGD VNEELVKAAA NGDAQKSEEI LKRPEAEVNG VFAGHTALQA
     ASQNGHLEVI KALLRQKADV EIEDKDGDRA VHHAAFGDEP GVMESLARSG ADLNARNKRR
     QTALHIAVNK GHVGVVKTLL ELGCHPSLQD SEGDTPLHDA ISKKRDDMLT LLLDQNADIT
     LTNNNGFNAL HHAALRGNP
//
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