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Database: UniProt
Entry: A0A182TBU6_9DIPT
LinkDB: A0A182TBU6_9DIPT
Original site: A0A182TBU6_9DIPT 
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
//
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