ID A0A0J9XJS4_GEOCN Unreviewed; 1866 AA.
AC A0A0J9XJS4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=BN980_GECA22s01528g {ECO:0000313|EMBL:CDO57547.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO57547.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO57547.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO57547.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; CCBN010000022; CDO57547.1; -; Genomic_DNA.
DR STRING; 1173061.A0A0J9XJS4; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; cd19672; UBR-box_UBR1_like; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; 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 PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:CDO57547.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 88..161
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 88..161
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1866 AA; 213815 MW; A4F314D607912686 CRC64;
MSHLSLKRFL VEYGYPQQFN LTGADFRTDI SRTLYWHATN KGKYLTKLFK ELDFDENDHS
LEFYKAQDAS CSWKLKSSSS NSGSHEGRPC LRKLEKSEPT YRCINCGFDD TCVLCSRCFD
PEEHKGHQVT VQISMFDGSG ICDCGDPEAW TKPFACKSSK HANGTNENED LPNDFKASIE
ETIKTILDFA ITIFSTEETA LKRNPTPEQV KRFEANGVLD KFTDENDDKE STQIEMYILC
LWNDEVHSFT EVIDLLTTYC GKTEEEAEDI ANMIDNYGKA QIAISEDIDH IVEIQEGVST
GGLSTSIRST RDYLREEISD EIFHWLLDFS ECSLPGVANY VRDTISKLLL ATNWTPGVST
PYRTTLDATC LMNDFTFPEP GKLPLNDVDI EDKVYNPIPQ SDSTSNSDLI YPTVIPSRAN
YLLFFDIRLW KNLRANIRDL FISTLVSESK TKVLFGVQFS TVYPNIIEHF LIAEREPNLS
LVSQLSTQLF TAPSVTLEIT KNGSFPSILL QLVYSFILYR RTGKPPHNSS GWDMLPEDLA
AFQNHGIGSF FYDVNHFLTR LPKKTLLLED KNFLPELSRL LMLFNDAFIE KRALLQHVEY
ERRDWPYLFY FYNFLLSLVD DLFKGFEKEG IDKSKLFDFF TYVAKRYLER TFKDSLEKLD
YIFDAPIFRK IIINHKDDES YIETLFIDRN SASWFHPFEF LFSILFARAG ADKKLLEDSM
IGSYDVFANK RLTKVETQDN CSLMAVFFHN TWKTLSFISQ IDASLWVRNG QVLKLQSSHY
RHQYKNTLYM HDIYWAQVGL ILLHPDDVFI RLMHYWDVMN WPLNFDDDLH AVYMMESFLH
YLIIFLSDRH QLLGLSEEDL KQKHVEREII QTLGFRPTSF EVIAEETSLK SSEELLEPTL
KKIATFKPPI GIHDVGTYVL KPEYMKILDT HYMSFNSSEI EEATKVVKAL NKKTSPEQNF
AEPHLESLTG TPFANIGAFL TTKSFNQFLF KLLYCLQDDF RGSEHYEPIL GYLLRLLLVA
GKNDLQTDFS DKPDYDVSRD SFAAMMCVEI TDFDLSSDFT SFFPESTDKN VANSPVLVLF
HMHQSPLYKD YKGELYGVLT YLFKKAPEFI NNYFTERLGN SFEHYFYTQK TEKSSKSNKS
EKNKARLKQD KALAKILKKQ RLFAENHSVD EDNNDNSDSM DNSVHSHEEI TDWKYPAGEC
ILCRTPCDSS NDYGVIGRFE TTISTAYIGN KLGYLVLDGS DYTTEFDEAE PESGLIPTNL
FPADKRYKTE KGDISFHKRG QLEGSYDENG CLHSKVAFVS CGHILHQKCY DDYAKRQSQS
THLFSTSSSK STMCPLCHFF GDVFTPVLWE TSTRSYENDC NTEETFQYFI VSQCMEITGS
DSECQRRQCH GLATSIVSAL SPKTKLTGVS AMSHLLENVA LPYDFYHRMV GAGQSYKVSK
FKDIDENKLD NFSLVGLLTT SIADVEHSLR GVERKPGELS VLDQIPERVV TNLRLLADHS
RTLVFLAVLN SPESSEFFSN FKEVKQRFDS FGLSSTVGMP SDRLAEGIFL HTGGLGISPK
YLIQNYLIGE ICRALSSYCL ALQKGGSVWE DPNIVQIPIT GEPSQNSLAH LKKLILLFSK
DALKSVVDIP HVTSIVYSLL LRTVTIFLRR TAILIHAIYA KDFNDTSKLN ESDMSKESDK
LCKLLGIDSF DSYLEMMAND VFYGGIAKSW IEGMDIKNQQ LEFPGILKLV KLPERLDEFF
ALPKIKEVLL NAYNIPVVCL FCGDIISIKR NGFSFGFNFN AKSCKDHLKT CQQGTGLFLL
PKENYILVVS HTLMAFIDAP YLDVHGNSKV KDFPMILYKQ RYDYITRTLW LQHTVLDELI
RRGGYI
//
