ID A8Q4D2_MALGO Unreviewed; 1847 AA.
AC A8Q4D2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=MGL_2526 {ECO:0000313|EMBL:EDP42930.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP42930.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP42930.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP42930.1}.
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DR EMBL; AAYY01000009; EDP42930.1; -; Genomic_DNA.
DR RefSeq; XP_001730144.1; XM_001730092.1.
DR STRING; 425265.A8Q4D2; -.
DR GeneID; 5854451; -.
DR KEGG; mgl:MGL_2526; -.
DR VEuPathDB; FungiDB:MGL_2526; -.
DR InParanoid; A8Q4D2; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008837; 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; cd16482; RING-H2_UBR1-like; 1.
DR CDD; cd19673; UBR-box_UBR3; 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; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; 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:UP000008837};
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 123..197
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 123..197
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1066..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1847 AA; 205060 MW; 236E1E8E2CA5CC0D CRC64;
MDHASAVVEL LPRIASIPIP GNPDTYRVPA ARAREVRQRL CHELLSTVPV TSLFPASIAS
TSADAFALLD QCDWHITMAQ QRAETLQDAH ASAAAAAAAA APSEGVAATA SSQPEYSKNR
RGMACGHVFR KGEPIFRCHE CSFDDTCVQC AMCFRHSIHA REDHDVVFSV ADEGGACCDC
GDEEAWNRDL GCEFHSLRPH NAPEHESGEQ VPRGEQTLDE ILGIVPENVQ QDLGEFVALL
SAFLLETFLH APKQTQLVMG PDVVDSIKRQ PSFENAFPAK GKARQDMSDG AERDPQPPLF
VALLWNDEKH SFNEVSDKIL EVCTTMTPKD ARNFAEAVDR HGRQVVAMSD DVRRLVLMAR
RIGVIYLLVT VQHAFDYYVE EVAGCVLEFL MELASCSLYS ADATSDGRMI KAQITKTLLR
PWLVPEWAEA PAAIRRDLFD PTRLCILDTL LLLDTKMWKG ARLQMRHLLM DLLACREAKR
QIALRFGAVY PKLVEAFILH DREPEHSIYH MTVQLFSVPS IATQLVVERQ FLVVLLYVLQ
ALFANDNETR ITSLVLPAPL PARGQASPDT ALLRQQKCYH IFYDIRYLLG ARDVQLDIVK
HAEMYLGMWL EFFALFHGMA PDKRAVHAHV EFESELWIQV FHINSHLGRI AKLLGEAFAG
ADNARLCEAI GFIGTTILRH MARLSALDPA THPPLAMRPM KLPALEHAPL QDTRSGTEAK
RHDVDVVPFS VSSQPVSFHH PMHWLLAETL KHLHKVQSID ALLPVLNEDD WLRLMEHPVR
VAVKLAQIRC NVWVRNGFVI RSQAYHYRDS MWMRDIMYDQ DLFLQQCGMA FTTPERFLAT
LLDRFELVDF LSGRSAQHNV YDAQQLVFMT EELFLLLTVL LNEVSVMAHW PIEAQVRHEL
IHYLALGPCT YSDLTKQIPE RYTDHGCFDH ELARVAHFRK PDGSADHGLY ELRPAYLADV
QPFFHHYSRN QREQAEQVLA EKRQQGCTLP LYQSSQLHVL ANTPFSGLAH VFTSPVMADM
LFYALSYAIS QPEPPDTLMN VTLHLIAQGI EECGREFVAN ILMPERTSRD ASSETNERAE
SAHEVPVHTP DPISATKGAT EGATEGATAA ASAASSPRTL VALLVQLSQH SQQAAAYKPK
VTYILEKAAV WAPDTAGLVQ HVQKPTEQPT DDDARRKAAR ARQTAILQKF SAQQQSLLAE
LEDELGSDDD DDTEQGYGPC ILCQERLDSG SSFGTLVHVQ HSRLVRTSVP RTSEALSDVL
ATPLNLDRVR AAPHDDIHSS HGSSRDRMRG QYTRTDERGS QLGYPAPAHV TGLVAVSCGH
SMHVSCFHTY LQSTEQRHAF QVARNHPEDL SRFEYVCPLC KSLGNLLLPE PGVSSLGSQA
LWDTSHAIPS SPAQSLGHVQ LSPAPLTEWV RSVNIAILKS TPADSAVLTD HQDMVHGTGC
FVPWLVSGSA QPHNPDLGAG IFGADECHML HRYTSVLQLL SDETAHSRLQ ERHATVLDAL
GSNNTAMYVP ESLVAYTIAQ LDIAQRGMPQ PIAHSLSATQ VRVVQMLLES LGASARLVAH
HVHDAHMLQQ GLYKRLLPQW ASEPAVRSPI ILRHAMGVLV EAAVLVPDQM RHVATLMFYV
NLVQCVFGLA QPMMKPTKPA SPVDSSDLDA ALRIFPHARW LVTSIVSLVG YVRGNMTLGF
DQLSDGELAK ALCSYTLPFL RRAAILMRVV AGEQAVPVVD ADSEYESLLA SLQIIPPTEA
LPVHSQPNAL LTMLVEGWTK HAYVHLAPLF RPLPIQQGPA QSVDSLVLEH PHIYELLPLP
ARPHDPPAAD ASPHVPSLRH VAAHIFPLPA MWRSAVRTVV LLLGSRR
//
