ID A0A075AV90_ROZAC Unreviewed; 1253 AA.
AC A0A075AV90;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=O9G_001849 {ECO:0000313|EMBL:EPZ34236.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ34236.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ34236.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ34236.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(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|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 EMBL; KE560971; EPZ34236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075AV90; -.
DR STRING; 988480.A0A075AV90; -.
DR EnsemblFungi; EPZ34236; EPZ34236; O9G_001849.
DR HOGENOM; CLU_265577_0_0_1; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030755; 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 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 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 SMART; SM00184; RING; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755};
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|PROSITE-ProRule:PRU00175,
KW ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 821..885
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 727..788
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1253 AA; 146080 MW; C46BA92D3FE5313F CRC64;
MLIGMKGDPE AWKRPIRCKK HGIVVPSSLD EMENNMFKKL PFEENARLSV STVLSYIIEN
IKDVKAREEE VDEGEIAVIL YNDETHSYQQ VIGVLQRAIG VTKEQGQKMA ETVDKRGREI
VIVNSNVDLC RQVAAIISSI GLYVELKNPI KFCRQQICSI LLDWLIKVCK GHPTLCHIVS
QKLVESQETL DVLLLNDIHL WKEMRNGIKE MLINSLLVDA ECRNEMALSF TRCYRELANQ
FFQNIDREPE MSIIFFSVQI FTTPRLALFV SEKGFIFEIL SILKEQFEKC VKDGEFDCDH
EFVQLKRYIH VFLDLRYFLS TDSVKEYARS NSELRNAFLE FFSLFQGIDK FKREEQIHVE
YESDSWVNAF NLSLQLSKIV TLVSEIYRNE ISFEIDFKNE NKNDFMVSKD RISFHLPLQW
VFGASLFHCK AIDKIPANRM KEIMDGPLSL FVLESQVRSG MWVRNGFSLR NQLLNFCGIQ
MREACFDPCF YLIQLGAINL GLDEFYEFVL QRFEINFELN DSNLVFAVED FLQLIIMIFS
ERMWLCEMDI ENEIKRELVH QLMLGPISFS DLIKKVPERL QNHSDFLTIL KSLTTFKFPD
SINENGVYIL KDEFYSLIDP FFIHYSRKDK SNLYENLKSI VIKPPKFRPP ILFENINNLL
FNSIYLNLLI KCFNLCVETS NDSLIDTLVY SWQLLGCSLL ENEDLETKEE VILVYENILS
SRRMEMFSSQ RKRIDSSLEE LKKLKDEHFL KPLLNRVDFD EENVDKRKSK ANLRRKKLME
EMAKVQQSAF SKFEEYLTDE EEEQEENYEI YPSWNLPSGV CIVCQEMTSE NSTNFGFLSF
VQSSRLLGYQ GTFISTCGHS MHLNCYFNYK KNSPSSLEYQ CPLCKTLCNC ILPATPLQSS
FYDDSPISIF ESTDNFDILL GGLENCLSFT ALSTLVEKFT VESNLSLNRI VVLKMLLILV
TLNFKLSQRG NSEDTKRSDE EINSHNLLGI HNELINNASN VQNFVDLVVK MLIKSHPING
KEKFKNDFKI LFNIFNSRIY NEEIKEIEEI EEIKNQNLNL FLNATLLLFN VHFNDEWEIK
AEDLLDNSLH VQSELSPLKL INFKSFNLIN LPERFDLLFK FRDENPCLTC KNIPYDPALC
LFCGRILCSR SYCCNTGGLG EVTTHTEEHG VGIYLLINSC IILVLYRGKA CYLPAPYLDE
HGELDLGLKK GRILFLIEKR YLEIKKMWIQ HRLPNVIASK QKHEDRFINW DFL
//
