ID A0A3Q2DGF5_CYPVA Unreviewed; 1683 AA.
AC A0A3Q2DGF5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000018346.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000018346.1}
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|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR Ensembl; ENSCVAT00000027250.1; ENSCVAP00000018346.1; ENSCVAG00000021775.1.
DR GeneTree; ENSGT00950000183075; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265020; Unplaced.
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; IPR001841; Znf_RING.
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 SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 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:UP000265020};
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|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..48
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 1123..1178
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 1..48
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 975..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1683 AA; 191443 MW; D07E166BECF70826 CRC64;
MSLCAECFNN GDHTGHDFNM FRSQAGGACD CGDSNVMRDS GFCRRHRLRT GENVPSIPRD
LLLMSEMVLP RFILCIIQYL RDGYIEPDTS AERDLQKVLQ QLEPQITFLE ELTKMGGAMR
TVLTKILTNQ QTYKELSMGQ EENLYAKKNY DKYLSALKNS GLVSVEEKIQ GAAADDDQDG
GQFVGQRKRV KLSSSTKDPY IIDSLKHKCF LEELLFWTIK FEFPQKMVTF LLNMLPDQDY
KITFTKTFVQ HYAFIMKTLM KSHESDTMSN RIVHISVQLF SNEELARHMT EECQLLDIMV
TVLLYMMESC LIKSELQDEE NNRHVVVNCS EALLKNNTYW PLVSDFINIL SHQSVAKKFL
EDHSLLVLWM SFVSFFQGMN LNKRELNEHV EFESQTYYAA FAAELEACAQ PMWGLLTHCK
VKETQEYTKT VVRYCLETLQ IWFDAIGFID EPAPNQVTFH LPLHRYYAMF LSRAVKCQGL
DLDSLLPDQE MLMKIMVHPL QIQACLSEIH SNMWVRNGLQ IKGQAMTYVQ SHFCNSMIDP
DIFLLQAGSR LLHFKFKVVD LLTMASQHQN AVLDSEQERP MLEGALTFLV ILTSLRIHLG
MTDDEILRSE MVSQLCMNDR THSALLDLIP ENPNPKSGIV PGSCSFEDVL SAVSDFKAPV
FEPGGSMQQG MYTPKAEVWE KEFDPIMVVL RTVYRRDVQS AMDRYSAFLK QYGIHTGNPW
PPYKERTPLH PSYKGLIRLL HCKTLHIVIF TLLYKIWMDH QNMSEHVLCM VLYLIELGLD
NQVQDCKEDE EPCIEEHCHD SWFPGTNLLS NLHHVINFVR VRVPETAPEV KKETPPSTSA
EASSYGQNLR EAQVFSLVAE RRRKFQEIIN RNNTEASQVV RPKSSSTRWV SPGTPPQLVT
EILEIRESML SLLVKLHQKM SSKQNSLSAS WLEDPDTSRH AHGDGITAIE RILAKAATRS
CQIKRSIQDI CGKVCPPVPP KKNSPSDKKT MDKEERRQRA RERQQKLLAE FASRQKSFME
TAMDVESPEP EAAMDLGSAE VMESEVLYDC VICGQSGPST EDRPTGLVVL LQASSVLGHR
CKNKQPKQLP TSDEEHIYLA DTCGVAHDVR LSLMQQFFKD SSCLQSVSIG WDGGVYVQTC
GHTLHIDCHK SYMESLRNDQ VLQGFSVDKG EFTCPLCRQF ANSVLPCRPG RGTETSGWHT
PTNKATRVLV KEVEDLQEKL GLFPTESNLS KEMELVIKDI KNTTQKKYMD YGKNPGSPDN
DFLFMYSLAR TNLELELVHR GGNLCSGGAS AAAKRSCLNQ LFHVLAMHMR LYSIDSAYNP
WTKLTQIARQ KEERPEVPML FRDVPSLLII FVLTMPQPLR KEHFTCVIKM LYNLQFTQAL
AALSTKLSPE ERQAWVTSGA LKKNTLNAEK SSNALLSHVI NELSKDKSVY KVTSEETTMV
SLYDDCVKLF DEICSWSSVH HLFSCCSQEE EEFSSLAVCL GLLSAAPQPP GAVHSASCLE
WPFNAFDLVT QWCDEVTGLS QMQPEQSLSL LVQDPQWAPP RLLQLPDNYS IIFQYYHRKA
CTACKKVPKD PALCLVCGAF VCLKGGCCKQ QGTCECVLHS QHCGAATGIF LLINASVIII
IRGHRFCLWG SVYLDAHGEE DRDLRRGKPL FLCEERYRVL EQQWVSHTFD HINKRWGPHY
NGL
//
