ID A0A2C9KCD0_BIOGL Unreviewed; 1846 AA.
AC A0A2C9KCD0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=106078171 {ECO:0000313|EnsemblMetazoa:BGLB017512-PA};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB017512-PA, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB017512-PA}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB017512-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR RefSeq; XP_013094416.1; XM_013238962.1.
DR EnsemblMetazoa; BGLB017512-RA; BGLB017512-PA; BGLB017512.
DR GeneID; 106078171; -.
DR VEuPathDB; VectorBase:BGLB017512; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000076420; Unassembled WGS sequence.
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; cd16483; RING-H2_UBR3; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 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 118..189
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 118..189
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1846 AA; 209105 MW; B1A80A76191FCE75 CRC64;
MASSGNPNNQ SNVNDSSKKS QSQISLHSSG SASSTNTTVS NSIMTLMKRE KRAVAVYLKE
ESSKSNNTKP LNDHLDTILD PNKPIDDFES IDFCKWIIAG GLTFEDFAKK VREYDSSVMC
GLVWTANFVA YRCRTCGISP CMSICSDCFQ AGNHEGHDFN MFRSQAGGAC DCGDSSVMRP
EGFCPRHGEH RENKSDPEAP AELMAVAKEM VPRLFIRLLY HLREQFLSQV RTSRNSYHLN
INDLEHFLNF MQSLSDMGAA MRRVMAQALI NPSHYAKSTV RSDQVSEGKV DNYTAFKEIL
NGNGLRYPLH FDKYKDKPGM SQKLDYSTII EELVFWVMRY EFPQRLVTFL LGLLPDDLYK
EAFAKAFVKH YSRISVVLSD AQDRSTVANR IVHISVQLFS NENLAVHLTE NHNLLLIIIL
SLASMIQSIK IVSSLEDPDL KSRFHCVVNC EHEIMKDHCY WPVVSDLINV LSHRKIAHVF
LGDSELVNLW LDLLNDMQGM NLNTRELSQH VEYEPDTYYA AFSAELEISA SPMWSLLMHC
QTPDTRHYVL DMIKSATVAL QDWFEAINFK EAMKPNPYQL TFHIPLHRYL ATFIMTAVKY
HDVDLDSILP DEVTLKKIMM HPLQIQVCMA QIYAGMWVRN GIQIKGQAMT YIQCHFCYSM
ADADLYLLQL CATKLDPDSF ITTVLDRFHI LNWMSYSPEP THIGILMEPE QELSMVEGAL
SLFSALMGIH TYLGISEEDL IRKEMASLLC MNDRQHSTLM DLMPERTGVS GLAKELFEPT
LQKLAEYKAP NFEAGGGLQQ GTYVPKAEVW EKDFDPVHVS QRAIYRRDMQ SAMDRYTEYL
RTHKGYKRKT TPWPPFKIED NMHHSYAGIY RLLNCKSMHA FLFTVLHKAL TRDKNLPEAI
LFHAVHLLEL CLHFAPKTFP NRIPGLSLQV QDGQLDKWYG TSDIKANACD IISEVIVPIP
VTEEEIRASG ITADDMDTST LEEMFQLQPS VVSSSTGPIT SAQLGQMPSL AMVSLPALDS
FLPHPPPAST KPATKRFESR GVATAQFVSK KITVKESLIS VLIKLHTKTG GVASYKPKTQ
SPSNVNTILE GGDAQLYIAR FLDRLYTAST AASRVIDETC RALNMTKVKA GPSETEKDSK
RRKAWNRQQK LMAEFASKQK AFMEQAMEEE TEKQEPSSAS ASSEQEESLP SKLYDCVICN
QSTPSTGEKP IGLVVFLQAS SVLGHRQQSN QEHVLSMSDS QVQWHRKTSC GKVNKKKLEI
LQKNFEGKSC EVSVNIGWEG GVVAQTCGHY LHLDCHKSYL DSLRNQNHAE VLAVNKREYW
CPLCRQLSNS VIPMVPDESM TMLVKPLPKD EKEMVADIAE MMIKRRITRD HAMNRAMGTV
MEDLTNITYP NYRAFSATRN PESVLLFICS VARINLEVEL LQMGGKLNDI QPPTKTKNQN
CFLPLVHVLS LHSKVLISTP LYPDLWAHLT GRNFWDEASC VSVYEKQVPM LIKDPLSLFI
QFVLTMSFTI EAEHLDFIIQ MLYNLVYVQA LAYLSCKFSS DERDAWRKKG RQNQSNTLEG
LLSLVISGLS RSSLYEEIDS SHTLPAICQS VWSPQSVEQV IQEYCLPFLR ISALMKLHLF
SIELPSPESG QDEFQLLSRF LNLGLPTPPV TEVASLSTAN VHWVVEEPHV LIRAWCLHIA
EFANNASQDA KSLLTMNPSW QKPSLIKLPN CYYQIFQVFR SAKCNECSRV PKDPALCLVC
GQFLCFREQC CAQNNVHESV GHSIACGAGT SMFLLVNSSL VVVVRGQRAT LWGSVYLDEH
GEEDRDLKRG KPLYLSMARY NLLENQWLSH SFDHSCKRWI WHRDQL
//
