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Database: UniProt
Entry: A0A0P7B7H9_9HYPO
LinkDB: A0A0P7B7H9_9HYPO
Original site: A0A0P7B7H9_9HYPO 
ID   A0A0P7B7H9_9HYPO        Unreviewed;      1639 AA.
AC   A0A0P7B7H9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Ubiquitin conjugation factor E4 {ECO:0000313|EMBL:KPM36318.1};
GN   ORFNames=AK830_g10249 {ECO:0000313|EMBL:KPM36318.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM36318.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM36318.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM36318.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) 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:KPM36318.1}.
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DR   EMBL; LKCW01000208; KPM36318.1; -; Genomic_DNA.
DR   STRING; 78410.A0A0P7B7H9; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000050424; 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   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   SUPFAM; SSF49599; TRAF domain-like; 1.
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:UP000050424};
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          185..226
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          323..368
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          1551..1624
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   ZN_FING         323..368
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..433
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        9..23
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1639 AA;  184974 MW;  8E917ECDA8BA485E CRC64;
     MPTDQPADEP ADVLPPPETQ PSPPASTVAT TTDPATIATT AAATAARAGH TPLTLLITSD
     SESGETEPYH LTPAAIRRLA RRNLRRTSPT PDLVTSLVRP PSPDTLYVGT RAVQNTLRVP
     PDGASPGTSQ PAGLLIPNAN SERRSGPLLP PHLSSLNIPK RYGGECIFDL YSLTYVQDPD
     VNLLCPICHD PLVDPVTTPC DHTFCYRCLR QSIYTSPSGT ACPVDREPLV WSNCFSAARL
     VRTQLNNLVV KCPYHGRGCK EELRREVVEA HATTECRFKD FTCPGTDCDK RLRSKPADHT
     CPHREIRCSY CQAEIEAPDR DFHMLSCAMS KTRCETCWRL VRRRQMDSHQ ELECEGVVIV
     CQYQEFGCPI RSTRGMMASH TVTCAFHPDT PSGIIIRHQR ELIQSYSDLG QQIQQLNSRQ
     DETNRRINEV TVAVARRGGG DSTGGDSRTI QDLDAGFEEV HQNLTHLEAR QSMWTMNQVM
     PIREEVTELR NNINMIRMHV NWLLNRSREE GRIRAANNSG SSTMRQDSPG NGGSMLPERR
     RSTSQETNLP LGWHPSSRKS SGPVPQIRAR RLAKLGTSTP KSEETKTSEP ESSTPSRAST
     PKPQTTPAAE SSRPKINITS AAGSGPNPFA KLGVKDNGKS EPSSSTGSFR PSRKRLASEI
     DDAVSADRPP QRTNNAQPES DDDYANRILS HIFRISVDPH HMTDSHGHRL VFLPGLNEEL
     NGSGDSLKLS VNSLDQAIME ALGAWPQNKP LMQYLLPCWK RAVKAAATTK LTEGPRFEAH
     EEAKRLCMSS CLFALTMPDL YGREPNPKHD TLMPYILQGV QSEDGLCFDF IREAIKRFDE
     DEAFPGIFSN AMVQISGKLS SLSMDDDYKP YMQALMTYTR FPPLIVNLAK HPCFKMAQSP
     SGIERHTILG PFFRISPLQS EVIQSYFPGA RTLDKARIRN AQDALRMVIR THQDDLFAIA
     NAFIRAGPDT RSRTLDWFAY IMNKNHKRRA LQVDHREVAS NGFMINVTAI LDRFCEPFMD
     NDFSKIDKID DDYFRKNPRV DIKDETKLNA DQAYSDEYYS KTLPGEPNFI SEAFFLTLAA
     HHYGSEACNS QLKNIDRDIK YLEKHVKAME AERPRVANVP HQLRHLEETL TRHTAVLEKT
     MGMKYAIEGV LLDERMQSTS LRFMRYVAVW LLRLATRSKY APGLESKEIK LPLPEEKLDT
     FSCLPEYALQ NIVDNFKFIF RFLANILPSA VGDEMIALCI TFLRSTDYIK NPYLKSSLVS
     LLFSATWPFM HLKRGVLGDQ LISSKFANEH LLHALMKFYI ECESTGADSA FYDKFNIRYE
     IFQVIKCVWV NDHYKRQLTQ ESRVNKQFFV QFVNMLLNDS IYVLDEALSK FPKIRLLEKE
     LENPSLSAED RQKKEEEHQT MAGQATSFMQ LANETLEMMK LFTDAMSEAF TMPEIVTRLA
     GMLNYNLETL AGKKAAAELS VANKDKYHFR PIQLISDIVD IYLNLGNSPV FIDAVAADGR
     SYKPEVLDRV SRILTSRHQK DAADIARWDK LKVKFIDAKL IIDQAELDLG EIPTEFEDPI
     MGDLMKDPVL LPSRQVVDRS TIVQHLLGDP KDPFTRQPMS IDDAIPQTEL KEKIDKWREE
     RMQAAKDKLK EAIMDTTEG
//
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