ID A0A1A9VV89_GLOAU Unreviewed; 1739 AA.
AC A0A1A9VV89;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT048805-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT048805-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT048805-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|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 7395.A0A1A9VV89; -.
DR EnsemblMetazoa; GAUT048805-RA; GAUT048805-PA; GAUT048805.
DR VEuPathDB; VectorBase:GAUT048805; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000078200; 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; cd19672; UBR-box_UBR1_like; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 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|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 46..117
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 1063..1150
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 46..117
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1439..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1739 AA; 199264 MW; 4D8CA071A7C6F7F8 CRC64;
MYYYMKCMFK ESGAKEGIID VLLEFILGDN PNTVLDKLSS EGATQSVCGK VFKMGEPTYS
CRECGMDSTC VLCVSCFKQS AHRYHKYKMC TSAGGGCCDC GDEEAWKKNP YCEQHLRGKE
NNTKSAIITD AIKERCEIAF VAILSFCVNY LEIESKASLE CLDGEGAGDD HFCTVLYNDE
SHTFDQVIQT LTKIAKCPTK DAGEIVASID REGRAVVKCD GFSECNLLKE AIEKQSVPPN
VPMAPARANQ SLRVSVLHVR AVACQQFALQ LLTWFQEFLV RHSTFRQIFA RVIMDKKAPY
CIRHILEYDV KLWKSARTCW HRLLISGMLM EYDNKMALAQ EFSKNYATIV QDFISDDHDH
SFSIVSLSVQ LFTVPSISHY LIAREGIFHK LLHTFYHRSI EEFVQNKTLQ FSKHVSTASY
FKRASYILYD LRYILSFKPD VWTDELREGF IEGCKALLRV LNAMQGMESI TRQTGQHMDY
EPEWECAFNL HIKLASAITL ILDWCATDRQ VLIKLYQMVM RYLCSNGFIV GDIKTEEKTV
AGHIAKCLMY DVSSSPVSIH LPLSRFFAGV YLHLGSYDLN FDSLTSAKRT PEELMEPILC
TQTMIAQVHA GMWRRNGYSL LHQLYFYRNV RCRTEMLDRD IVGMQIGASL IESNQYLIHL
LNKFRLIDWI QPDYEENATV CASDDDFIRQ LSMIDEFLEL LIVIIGERYM PGVAHVTEDD
RTKKEIIELL CIKAYSHSEL NRSLPDSNND TVLEDVIDSV AVFQKPQKYD AKGVYKLKEE
LYDEYNMYFY HYTKEEKSKS EETQRARRKA KNELVCCPPP KLPKLTDSFI TIANLLQCDV
MMHLINTILE RAIDLKTKGF QENHLQKVLH LIGYGLQEEE SGHYPFLSFY ERSQKYRLLQ
KLEELSHSGR VEAHRDFILW IIRKFKELQS KQASYQAERM QSDDMEVPNQ ANDADANVPL
TTAEQEKLEK EERARLAADR RAKILAQMQN AQKNFMKSHA EMFANANDVA TASTDSLVVS
GGGGLSMEWQ DDSALEGAVA YNSVACLGVE RRLQQPEEEK FNCILCFEEA IVSKDGPTLV
YLAFVQQSKV LKSDRNYPTS LHTSSCGHVM HVNCWQEYYN NEETKESRRP RRSLLISSSA
NTEFQCPYCR CMSNTVLPLT VPLSKYSIPN VIHAGDEMFP IDLWIETMRA FGDKLQSLVD
AEDADMWYYN LPYWLATVKE AHILTDPKLF EIMSQPIKRP EIPESWSYFV QHYVKTLSKN
DEEGLLSMWH SCTYTIQSLE VYLRAVGKPL KDEMSIRHKS CLSGLIRACC LSSANLSQTD
IKNLIKPVND LLNMVLKQQG NSVLEWDCFG EMLLALWMVP NILFAYDHRT TAIVVNGSLM
DFYTLQIFFL ANVVKAVVLF EKPVDGLMDV DEECIELSQK AKENVTAFFN KYNVETRQKA
QQRQKEESKT IAESTPEENN DEGMIEVDGC QAECSLQTLN ALLDYIKTEM REFLRCCCLF
FHFVTDVEFP DFLADNGSDT YDNMCKYLGL STQLESYFDT ESPFATILEM FASHPDITNL
EVVTTKTKRN NQPLRIIPCT RAIPQLVSLP EDYSDLINSI SEFSCPNNER EEMKTPTMCL
ICGEILCGQS YCCQPELHER PVGACTYHAY YCAAEVGLFL RIRDCQIVYL GKNKGCFVQP
PYLDQYGETD MGLRRGNPLR LCTARYSKIH LTWLGHGLHE EIARANEHAS TAGTQWHHM
//
