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Database: UniProt
Entry: A0A369GTX1_9HYPO
LinkDB: A0A369GTX1_9HYPO
Original site: A0A369GTX1_9HYPO 
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}.
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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
//
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