ID S7NT04_MYOBR Unreviewed; 1726 AA.
AC S7NT04;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=D623_10015380 {ECO:0000313|EMBL:EPQ19955.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ19955.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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}.
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DR EMBL; KE164760; EPQ19955.1; -; Genomic_DNA.
DR eggNOG; KOG1140; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000052978; 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; cd16686; RING-H2_UBR2; 1.
DR CDD; cd19679; UBR-box_UBR2; 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 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; IPR047508; UBR-box_UBR2.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF28; E3 UBIQUITIN-PROTEIN LIGASE UBR2; 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; SSF46785; Winged helix' DNA-binding domain; 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:UP000052978};
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|RuleBase:RU366018}.
FT DOMAIN 35..106
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 35..106
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 975..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1726 AA; 197147 MW; A70F4246B12EC092 CRC64;
MLAQLVLLGP MEWYICGEDP AFGFPKLEQA NKPSHLCGRV FKVGEPTYSC RDCAVDPTCV
LCMECFLGSI HRDHRYRMTT SGGGGFCDCG DTEAWKEGPY CEKHKLNTSE IEEEEDPLIH
LPEDVITRTY NIFATMFHYA VEILTWEKES ELPADLEMVE KTDTYYCMLF NDEVHTYEQV
IYTLQKAVNC TQKEAIGFAT TVDRDGRRSV RYGDFAYCEQ AKSVIVRNTS RQTKPLKVQV
MHSSIVAHQN FGLKLLSWLG SVIGYSDGLR RILCQVGLQE GPDGENSSLV DRLMLNDSKL
WKGARSVYHQ LFMSSLLMDL KYKKLFAVRF AKNYQQLQRD FMEDDHERAV SVTALSVQFF
TAPTLNYERL QSDYVTDDHD REFSVADLSV QIFTVPSLAR MLITEENLLT IIIKTFMDHL
RHRDAQGRFQ FERYTALQAF KFRRVQSLIL DLKYVLISKP TEWSDDLRQK FLEGFDAFLE
LLKCMQGMDP VTRQVGQHIE MEPEWEAAFT LQMKLTHVIS MMQDWCALDE KVLIEAYKKC
LAVLMQCHGG FTDGEQPVTL SICGHSVETI RYCVSQEKVS IHLPISRLLA GLHVLLSKSE
VAYKFPELLP LSELSPPMLI EHPLRCLVLC AQVHAGMWRR NGFSLVNQIY YYHNVKCRRE
MFDKDIIMLQ TGVSMMDPNH FLMIMLSRFE LYQIFSTPDY GKRLSSEITH KDVVQQNNTL
IEEMLYLIIM LVGERFSPGV GQVNATDEIK REIIHQLSIK PMAHSELVKS LPEDENKETG
MESVIEAVAH FKKPGLTGRG MYELKPECAK EFNLYFYHFS RAEQSKAEEA QRKLKRQNRE
DTALPPPVLP PFCPLFASLV NILQSDVMLY IIRTILHWAV EHNGYAWSES MLQRVLHLIG
MALQEEKQHL ENVMEEHVVT FTFAQKISKP GEAPNNSPSI LAMLETLQNA PYLEVHKDMI
RWILKTFNAI KKMRESSSAS SVAETEGTIT EESSRDKDKA ERKRKAEIAR LRREKVMAQM
SEMQRNFIDE NKDLFQQTVA EEASNSAVLD NSPMVSDTTL TALGPEQTQV PKQRQFVTCI
LCQEEQEVKV ESKAMVLAAF VQRSTVLSKN RNKVIQDPEK YDPLFMHPDL SCGTHTGSCG
HVMHAHCWQR YFDSVQAKEQ RRQQRLRLHT SYDVENGEFL CPLCECLSNT VIPLLLPPRN
IFNNRLNFSD QPNLTQWIRT ISQQIKALQI LRKEESIPNI ASSKNSENMD ELQLPEGFRP
DFHPKNPYSD SIKEMLTTFG TATYKVGLKV HPNEEDPRVP IMCWGSCAYT IQSIERILSD
EDKPLFGPLP CRLDDCLRSL TRFAAAHWTV ALLSVVQGHF CKLFASLVPN DNYGDLPCIL
DIDMFHLLVG LVLAFPALQC QDFSGISLGT GDLHIFHLVT MAHIIQILLT SCTEENGMDQ
ETPAGEEELA VLALYKTLRQ CTGSALKEIP SGWHLWRSVR AGIMPFLKCS ALFFHYLNGV
PSPPEIQVSG TSHFEHLCNY LSLPNNLICL FQENSEITKL LVESWCQHIE VKRYLEGERD
AISYPRESNK LIDLPEDYSS LINQASNFSC PKSGGDKSRT PTLCLVCGTL LCSHSYCCQT
ELEGEDVGAC TAHTYSCGSG VGIFLRVREC QVLYLAGKTK GCFYSPPYLD DYGETDQGLR
RGNPLHLCKE RFKKIQKLWH QHSITEEIGH AQEANQTLVG IDWQHL
//
