UniProt: A0A195FM35

Database: UniProt
Entry: A0A195FM35_9HYME

LinkDB:  A0A195FM35_9HYME 
Original site:  A0A195FM35_9HYME

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (16)   

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ID   A0A195FM35_9HYME        Unreviewed;      1961 AA.
AC   A0A195FM35;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   ORFNames=ALC56_04538 {ECO:0000313|EMBL:KYN41386.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN41386.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN41386.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN41386.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN41386.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KQ981490; KYN41386.1; -; Genomic_DNA.
DR   RefSeq; XP_018339499.1; XM_018483997.1.
DR   STRING; 34720.A0A195FM35; -.
DR   GeneID; 108746908; -.
DR   OrthoDB; 51389at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000078541; 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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044046; E3_ligase_UBR-like_C.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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   Reference proteome {ECO:0000313|Proteomes:UP000078541};
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          88..159
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         88..159
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          1146..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1961 AA;  222085 MW;  D414D658ABB43993 CRC64;
     MASTSSSDVQ VLMGKGKCGA AAYISLATGR DTGTNRNPPY LNELLDVLLN PSKPIDDWET
     IDWCKWLMAG GRTPDEFANT VRTYDNATTC GLVWTPNFVA YRCRTCGISP CMSLCTECFK
     KGNHYRHDFN MFLSQAGGAC DCGDTSVMKE TGFCDRHGPN ATVNKSVAPS DLMSVAEAMM
     PRIILRLIQH LRENSQKSAI HEADAYLTML LDLNNMGALM RHVMTSALTN PQKYRGLMDP
     SVLTGQSEYD SYCQDSNKMY QHAVKSLPNP EPPDEYKECV SLQEHLEHTT FLEELMFWTV
     AYEFPQKLVC LLLNMLPDPD YKEALTRAFV LHYSRISMML ERSMDPDTLS NRVVHVSVQL
     FSNEKLALRM VDQLKLLHVM VISLKYMMSK ILIQNTLHDP DKNFHYVVDC GRQVMKEHCY
     WPLVSDLNNV LSHKPVAVKF MSDNTLLEMW FDFLSMFQGM NVNQRELSQH VEFEPNTYYA
     AFSAELEASA YPMWALVSHL RGPESATLSR RVLTFCLTAL QDWLDAVNYT DPNVSDSLQV
     SFHLPLHRYL AVFMCQAIRQ QGATLRELLP PTDMLHLLMM HPLRVQVAFY EILNGLWVRN
     GLQIKGQAMT YIQCNFCNSM VDADLYLLQI CATKLMPDVF LKTVIEKFHV VEWMSLCLYH
     APQNEYLEGE HDTPMLESCL TFLATLVNVR TNLGLSDPEM SRLEMVTLLC MSDKTHSQLM
     ELMPERCGTT QNRDFESVLA DVAQYRAPNL EASGNMQQGM YGPKGRVWEE LFDPLHVLLR
     AVHRRDFQIS MDRFTEYVKQ SGKLKNNATL WPPFRQPAPV SSDYDDPRIV LRSRVFHAMI
     LIILYKAVNG RNISEHVMAL AIYLLEMAVI TAEPPDKFGS PLCQYTGGSF HVIKDMDLAG
     WYESDSLSEN LRTTIPQVIL VQESEHSSSD SEFEWEMIHG EMSEVATSLM LNDGADDGAE
     EVSLELLGFS VDTVRDDNGV SNASASLPAL LPSVESAASL PALPSTSVEY GVAIVPEDGI
     VAIPARSNSE DDLTIPLQRA LPPSEEESMA IHLAIESPPS PNNEIGGQPA LPPVPQRPAV
     LAGNEIVTAQ PINYRATEIV PSTSNSYKHF KRRELQGGPM QPQSVKVGES IISLLLKLHS
     QLSGVPDSYN PEQSAMSDNE VSSSSSSSSS ISSSSSSSSF ISLLPSESRI GDGPFFISQL
     LRKIADLDPI CKQTIIETRN KLWPRMQECE EDEQREKENR EREERRKRAK ERQQKLMAEF
     ANKQKQFMEK AMETEDADAS GMDWDQEENE TKLTSKKEYD CVICNQTTSS SEDKPMGLVV
     LVQATSIIGH ERQQSNRLVL PTSDEDPPIP KGETRGAHFD RRMDEMNRLF DTLSWLLSVN
     IGWEGGVHVQ TCGHHLHLDC LKSYLESLRS QQRQQSLAVE RGEYLCPLCR QLANSVLPLS
     PQLGECSAVV RSRHASTATI LADLNTFLKE IQRNPVSSNL SVAMGKAMED MTSCTYLKYK
     QKNCKPSHQS LFLFVTSVAR TNFEIELVQR GGSLCVAPPT TIPLMPKRDC IVALLHVLAM
     HARVLTTWPV HHVWQQLSGI SLMEESTSSL ALTPHERQVP LLLRDPTAML IQFILLLPLH
     LDQTYFSGVV KVLYNLLYYQ VMLQVSCNFS REERNMILKK RCSCATTPSE TILAEIIEYF
     SESGLYPGTD DNKPSTSTSP TYARVKSHCI EQQVQSLCLP FLRVAALLRY HLYEQPLPLI
     RTQQSEFVRL VYYLELVTEG MSWDSFDSTV ALNWQEPEAG VSVPLFWCDQ LIAFLANWRG
     HQPARNLIME QHISWHVPKL VSLPREYEKI FTYYHERQCS MCHSVPPEIS ICLLCGTIVC
     LKQNCCRQMN VFEATQHSID CGGGTGIYLV VTSTYIIVIR GRRACLWGSL YLDDFEEEDR
     DLKRGKPLYL SQDRYQLLEQ QWLAHRFDHT KRTWVWHRDA L
//

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