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Database: UniProt
Entry: A0A1S3JWM3_LINUN
LinkDB: A0A1S3JWM3_LINUN
Original site: A0A1S3JWM3_LINUN 
ID   A0A1S3JWM3_LINUN        Unreviewed;       926 AA.
AC   A0A1S3JWM3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC106176552 {ECO:0000313|RefSeq:XP_013414439.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013414439.1};
RN   [1] {ECO:0000313|RefSeq:XP_013414439.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013414439.1};
RG   RefSeq;
RL   Submitted (SEP-2023) 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}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358}.
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DR   RefSeq; XP_013414439.1; XM_013558985.1.
DR   AlphaFoldDB; A0A1S3JWM3; -.
DR   STRING; 7574.A0A1S3JWM3; -.
DR   EnsemblMetazoa; g3815.t1; g3815.t1; g3815.
DR   EnsemblMetazoa; XM_013558985.1; XP_013414439.1; LOC106176552.
DR   GeneID; 106176552; -.
DR   KEGG; lak:106176552; -.
DR   InParanoid; A0A1S3JWM3; -.
DR   OMA; CNVPVNE; -.
DR   OrthoDB; 5481936at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd15525; PHD_UHRF1_2; 1.
DR   CDD; cd20388; Tudor_UHRF_rpt2; 1.
DR   CDD; cd01797; Ubl_UHRF; 1.
DR   Gene3D; 2.30.30.1150; -; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 2.30.280.10; SRA-YDG; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036987; SRA-YDG_sf.
DR   InterPro; IPR003105; SRA_YDG.
DR   InterPro; IPR021991; TTD_dom.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   InterPro; IPR045134; UHRF1/2-like.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR   PANTHER; PTHR14140:SF45; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF12148; TTD; 2.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 2.
DR   SMART; SM00466; SRA; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS51015; YDG; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00358}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
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:PRU00175}.
FT   DOMAIN          1..78
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          473..524
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          577..740
FT                   /note="YDG"
FT                   /evidence="ECO:0000259|PROSITE:PS51015"
FT   DOMAIN          857..896
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          81..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   926 AA;  104226 MW;  9510E7C6DCB8253F CRC64;
     MWIQVRSMDG KTCHRIDGLS KLTKIEDLRS KLVDPFDAPA ERQRLFYRGK QLEDGHTLFD
     YDVHLNDIVQ LMVRMAAPPC EKEVTKDTEE VNSEDDSNSS NKENEPENMQ TSEPSTSQHT
     TSSTDSGFED MHSTYKVGDI IDARDNTMGA WFEGKIVKIT RYVDEDSSDN ESVKSVEKNN
     NMKEENPTIS PTNEEKEQSE DLKVDETLVK NEATAEVTGN NNNIEETMEV DDPQDKEITC
     DNVTDPNPLG MSTSDQHQTS EKDQEDNTSN NVKDTNDAGN SDPEEGALTS VQGEYQKEQN
     GSLSIGNSNT SESSKDLISK VELEKIPDDD FIYHVQYEGY EEEEDIAKVR SSSIRPRARN
     TISLKDIQVN DRVMVNFNYD EPKARGYWYD AIITGKRDTR TIKELYATVF LGADLMALED
     CKILFIDEVF AIEKPGSQIN TSDPGSAAAT PTKRQNKPEC DHCLDNPRRK CKHCACHGCG
     GKNDPDKQIM CDECDMAFHL ACLDPPLEAV PDVEEWYCPL CKNDESEVVK AGEKLKQSKK
     KSKMASANST AQRDWGRGMA CVGRSKICNI VPPNHFGPIP GIEVGTTWKF RVQVSEAGVH
     RPHVAGIHGR DVEGAYSIVL SGGYEDDEDN GDTFYYTGSG GRDLSGNKRT AEQSCDQTLT
     RTNRALAKNC NAPLNDKQGG EASDWKAGKP VRVVRNCKGR KHSKYAPEEG NRYDGLYKVV
     KYWPEKGKSG FIVWRYLFRR DDPTPAPWTK AGKKRIEELG LTIQYPQGYL ESQREKEQQN
     AEAENKKGKG KRKREESESP KSTPEKKQKV AAYKFDPEVA NLVKEDVENK KLWKEAKEHA
     KEGVQKFLAK VEELFLCICC QEIAYKPVTT KCHHNVCKSC LSRSFKAEVY SCPMCRTELG
     KEYSMAVNKT LSKILNALFP GYENGR
//
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