ID H2ZUK3_LATCH Unreviewed; 1724 AA.
AC H2ZUK3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=UBR1 {ECO:0000313|Ensembl:ENSLACP00000001074.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000001074.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000001074.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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 ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; AFYH01246087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01246096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000001074; -.
DR Ensembl; ENSLACT00000001084.1; ENSLACP00000001074.1; ENSLACG00000000962.1.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_001801_2_0_1; -.
DR InParanoid; H2ZUK3; -.
DR OMA; TWMKLLA; -.
DR TreeFam; TF323875; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000000962; Expressed in chordate pharynx and 6 other cell types or tissues.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16685; RING-H2_UBR1; 1.
DR CDD; cd19678; UBR-box_UBR1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR047507; UBR-box_UBR1.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF27; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 70..141
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 70..141
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 828..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1724 AA; 197751 MW; CFF244029DE99A9E CRC64;
WQDCPDLKYE VYRHLAQYVP KIYCTRAEAK PVEEEELVQG ALLRPLEWYL FGEDPQVGLE
KLIQSSGSSE LCGKVFKGGE TTYSCRDCAI DPTCVLCMDC FQNSIHKNHR YKMNSSSGGG
FCDCGDVEAW KNGPACKKHD PGAAGDASQQ HPLVFQAEDV AERARKLFTV LLQYMVDMMV
WEEEKELPSD LQLGEKPDTY YCVLFNDEHH SYDQVIYTLQ RALACDQREA QVHTTSIDKE
GRRAVKMGTV QICQEAKEVI CRQSENISLQ PLHAEVLHST VMAHQSFAYR ACTWLIQILS
YAGRFRQVFC EVALEQDPNS EQPCLVSRLM KWDAKLYKVE SSTRKDNFSQ QTMYDLELPD
LKFACNFAKH YKQLQKDFIE DDHERNICVT ALSVQMFTVP TLSRHLIEEQ NIVKIIIETV
MEMLSEHLGA NGKFHFQSHN SDKFFRIQVI FYDLKYILTS KPPVWTDRLK VQFLEGFKSF
LKMLACMQGM EEVKRQFGQH IEVEPEWEAA FTIQIHLKHI LTMFQDWCAS NEEVLLKAYR
ECHNAVMQCS RKAFTRETRP LSMCGHTFTS RAYRVSTDPV TVHLPLSRML AGLHVQLSRT
GAIARLHEYV PAEELQVEVL VEYPLRCLVL LAQVSAEMWR RNGLSLVSQV YFYQDVKCRE
EMFDKDINML QIGLSLVDPN SFLMLILQRF ELFDILNKPM LTKDKVSDRK KNDLIKQFNR
LTEEMLLLII TIVGERYVPG ISHVSKEDVI MREVIHLLCI QPMAHSGLTK SLPENESNET
GLEKVIHQVA TFKKPGVSGH GVYELKKECL KEFNLYFYHY SKSQHTKAED AQKKRKKQEN
SDEALPPPVP PDFCPAFANI VNLLNCDVLM YILRTILHRA VETKSRLWTE AMIQMVLHLI
AYGLLEEKSQ LEKSPEEEVK FDFYHKATRL GSTSTNVQSI MMLLEKIRTV PQLEAQKDMV
NWTLQMFDTV KCLREKSFPP QASSSEVPKP EETVQEKEKA ERKRKAEAAK LHRQKIMAQM
SAMQKNFIET HKLLYESGTE GQDQEETKAE EESIQMAVDD SRVALGPKRG SCVVEKEVLI
CILCQEEQEV KADKTAMVLT ACIQRSTTLT QQKGKVFPNP ENFDPLFMNS DLAWGTHTGS
CGHVMHAACW QKYFEAVQNM TRHRLHAELI FDLENGEYLC PLCKSLCNTV IPLIPMQAQK
INRWVHTSDL SNLKHWLQIV LARVKGLETG IAKAPTFQLS EENEIRNVIE YPFSSLFPCS
TTYSDSIQEM LVLFATAAYR VGLKVAPNEA DPRVPVMVWS TCAFTIQSIE NLLEDEDKPL
FGSLQNRQNS GLQALVQFAA AHRMKASQQT IQNHLTRLLT VLLPNLNVEH SPSILDVDMF
HVLVSLVLSF PSLYWEEAVD LQPSFLSSSY NDLYLFHLVT MAHIVQIILT ADKDPAPVED
PEESEETYSA AALYRDLLLR TNSCLRDDVP GWYLRDCVRR GLTPYLRCAA LFFHYLLGVT
PPDDLHNGSS EGQFGALCSY LSLPTNVFLL FQEYRETVDP LLHRWCTDPS VQSFLNGERT
AIRYPRKRNK LMQLPEDYSC LLNQASHFKC PRSADDERKH PVLCMFCGVM LCSQNTCCQE
TVDGEEVGSC TAHTISCGAG IGMFLRVRHI KTAMRLVSAC FLSTPYRVGH GACIANLRRG
NPLHLCQERY RKLYLLWQQH CIMEEVARIQ EVNPTIFDFE WQQL
//
