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
//