ID A0A369GTX1_9HYPO Unreviewed; 1584 AA.
AC A0A369GTX1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CP532_2537 {ECO:0000313|EMBL:RDA87234.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA87234.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA87234.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA87234.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000256|ARBA:ARBA00007434}.
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:RDA87234.1}.
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 EMBL; PDHP01000027; RDA87234.1; -; Genomic_DNA.
DR STRING; 2039875.A0A369GTX1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR CDD; cd16449; RING-HC; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF02176; zf-TRAF; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00207}; Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00207};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00207}.
FT DOMAIN 139..180
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 276..322
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 1495..1568
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT ZN_FING 276..322
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1022..1049
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 512..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1584 AA; 178587 MW; EC257382A4BB3428 CRC64;
MSERRPSPAA ARPSPSESSD EGLRMSPAAA RRFARRNLRR TSATPDLVTS LVRPPSPDAF
YVAPGVHARR RPPPRLSSAY SSELIIPMRP SLAASDRRSG PLAPPHPSSL DVPVRHGGAA
VFDMYALSYV ADPDPCLLCP ICHDPLVDPV TTPCDHTFCY RCLRRSIASS PSGTTCPIDR
DPFSWLDCFT AARLLRTQLN ALVVRCPHHT RGCSRELRRE VVERHATSEC RYRDFACPDA
SCTQRVRTKP KDDTCPHAEK SCSLCDAKVD GSEVDAHLLA CPKTKTRCQG CWQLIYRSQL
DAHRTLECDG VEIACPHHDV GCPARALRGD MSTHARMCSF HPDTPSGFII RAQRQLLQSH
DDLQAEMREL RARQAETEGR IDELAAARRG VDPMVHDKHT MQDLDAGFEE VHQNLTQLEA
RQSMWTMNQV MPIREEVTEL RNNINMIRMH VNWLLNRSRE EGRIRAANNT GSSAAIRRDS
SADGGPALPE RRRSSGTDMD LPRLCTMNPD DQPHRPGDEA PDKEKMDQIR ARRVAMLSST
SSSSSSTPKP ADTQKPAAGP SNSGANPFSQ LGVQPGEAQK PQATSGSSSP RKRSAAEDGE
VVQLPRKTSS QQPESDIDYA HRVLTQIFRV TVDPHHMLNP QGQRLVFLAG LNQELNDAGE
PLKLSAANLD QAIIEACSIW PAEKPILDYL LPCWKRALKV VGSARNTTFA RTQVHHEAKR
LCLSNCLFSL TMPVIYGRDD DDKPDHQTLV PYLLRGISAE DGLDFDFIRE SIKRFDDDEA
FPALFNDAMC DISTRLSKMS LGDDYKPYIQ ALLTYTRFPV LVSNLAQHPC FNMAQSAAGI
ERHTILGPFF RISPLQPEAI KSYFPGARSL DKTRIANAQE SLRMVLRAHQ DDLFVIANAF
VRAGPDTRSR TLDWFAHIMN TNHKRRAMQV DPREVASDGF MLNVTSIMDR FCEPFMDNDF
SKVDKIDVKY FRRHPRVEIE DETKINADQA TADAFYEQKE SGDSNFISEA FFLTLAAHHY
GSEALNSQLK TLDREIKYLE KSIKSMEAER PKMANKPQHL RMLEEALKRH TNVLEKTIAL
KYAIEGALLD ERMQSTSLRF MRYVAVWLLR LVTDSDYRPG KESQMINSVL ILVRLPLGTE
TSKAFACLPE YTLQNIVDNF KFVFRWLPTI LPSAVGEEMI ALCITFLRSS ELIKNPYLKS
SLVSLLFSGT WPFMHLKKGV LGDQLIGLPF ANDHLLHALI KFYIECESTG ANTAFYDKFN
IRYEIFQVIK CVWGNDVYKE QLTRESNVNR SFFVQFVNML LNDATYVLDE ALTKFPKMRA
LEREIEDGSL SAEDRQKKEE ELQTLGNQAT SYMQLANETL KMMKLFTQAL SDSFTMPEIV
SRLASMLNYN VETLAGKKAA AELSVSNRDK YHFRPIQLIS DFVDIYLHLG YSAVFVDAVA
ADGRSYKPEV LDRVSKILTS KSQKDTTEMA KWEELKAKFA EAKLRQNQAE IDLGDIPAEF
EDPIMGELMR DPVLLPSKHV VDRSTIMQHL LSDPKDPFTR QPMTIEDAVP QTELRERIEK
WRLDRVAVAQ AKLAGDDGMD TTEG
//