ID A0A182TBU6_9DIPT Unreviewed; 733 AA.
AC A0A182TBU6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Anopheles maculatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; Anopheles maculatus group.
OX NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM023696-PA, ECO:0000313|Proteomes:UP000075901};
RN [1] {ECO:0000313|Proteomes:UP000075901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles maculatus species B.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMAM023696-PA}
RP IDENTIFICATION.
RC STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM023696-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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
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DR AlphaFoldDB; A0A182TBU6; -.
DR EnsemblMetazoa; AMAM023696-RA; AMAM023696-PA; AMAM023696.
DR VEuPathDB; VectorBase:AMAM023696; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000075901; 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 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; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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 SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU366018};
KW Transferase {ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 54..135
FT /note="Adaptor protein ClpS core"
FT /evidence="ECO:0000259|Pfam:PF02617"
SQ SEQUENCE 733 AA; 85462 MW; 8A8BDCF3577D3243 CRC64;
CISDDKAQDE QQQEPLSDDK KTRCGIVFRA ILDYCMQTLQ MHGSGNFPEW EDDENTHCTI
LYNDETHTFE QVIQTLTSIV KCEHKTAIEY VTSIDREGRA VVKCASFEVC KKLKEDIENK
AMRSSLASRT IPLKVTVMHR NEVACQHLAM QMLAWFQEFL TKHSSFRRIF TDTITVPQET
YNLKFILSND HNLWKSARTS WHRLLISGML MDYDNKKLLA ITFTKLYASL MQDFIRDDHY
HSFSIVSLSV QLFTVPTIAH YLIEKESAFF KLLHTYFSEA IDKYVKNRQL VFIKNTSSMN
TFKRASYILI DLKYLLSFKP DKWTNELRTG FVHGLQQLIR LLKYMQGMDA ATRQVGQHLE
YEQEWETAFT LHLKLSHLIT LVLEWCATDR IVLGKVFRMV MSSLSDTKFI AQESETVVRT
VGEHSASCLT YDVLSRPVSV HLPLTRFLAG LYTVFERHDF TFDTFTPNTA DYPTPEQIIE
PVLCARTMMS QVHAGMWRRN GYALINQLFF YRNVKCRYEM LDRDIVILQI GASLIEANKY
IVHVLNKYKL IEWLDKDVQE RPRSAEASGG DDDYIRQVGV LVEEFLELLI VVIGERYVPG
VGNVTESDRI KKEIVQQLCI KPHSHSELSR ALNEDNCSEI MFESVIDDVA VFEKPNDAEK
RGMYILKQEY YSWYNLYFYH YSKEDKSKSE ERQRNQKKEK NELVCCPPPA LPKLTQLFKY
DRVAIVPQKG QLS
//