ID   V5FA79_BYSSN            Unreviewed;      1076 AA.
AC   V5FA79;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Ubiquitin conjugation factor E4 {ECO:0000313|EMBL:GAD93224.1};
GN   ORFNames=PVAR5_1831 {ECO:0000313|EMBL:GAD93224.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD93224.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD93224.1}.
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DR   EMBL; BAUL01000051; GAD93224.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FA79; -.
DR   eggNOG; KOG2042; Eukaryota.
DR   HOGENOM; CLU_003224_0_1_1; -.
DR   InParanoid; V5FA79; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000018001; 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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16657; RING-Ubox_UBE4A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT   DOMAIN          984..1058
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          521..548
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1076 AA;  122788 MW;  53FFEB03DF40B0EC CRC64;
     MSDTLSDADK IRNKRLAKLA SQASPSQSSS QAAGASEQPS TPSEGPSTPQ EQQPPRQQIN
     VNSAPPSLSP SPRPDTQQSE GKRIKITPAP GVSTVPERPQ STSIPPKRQA PKPEETLEVF
     EDRTLSAIFK VSLKEDRQHD IHGQKLNYLP GVRAELEEQG RDLRMDVSVL DQALLEAASN
     IGRQKPLDYL LPCWKRVSRL YKGFKKSRDD DPKFDVIREA RRLCMSYCIF AITMPEMFGL
     DSPDQSPLKP YLLLDPEEDR GIDMDFLVEA VRRFPEDESI KPAFISAVEA LSQDLAVKTI
     NDDYKPYVMA LRNLVRHAAI ASAITESSIF NETQDPPTFE TKTLLGPWFR LSPLHGSVTT
     SYFSSPKTRD QGYILTAQRS LRMTQQMLNS DLLDVVNHLI RASKDAREKV LDWFATAVNI
     NHKRRAMQVD PKTVSSDGFM FNITTCLDHL CEPFMDAGFT KIDRIDADYL HRKPRVNMRD
     ETKINADQHA SDEFYSKSVE GTNNFITEVF FLTVAAHHYG SESLTSKLDQ LEKDLRHMEA
     TITKFELERH KWIHNPVQLR TFEEALKKYK DKFDLGLSFK YSLQGILFDD QWQARSMLFM
     RYVAVWLLRL ASGVDFPKKQ IKLPLPEQQP EVWKCLPEYF LDDIVSNFKF IMWAMPQIIT
     STEGDELVML CVTFLESSAY VKNPYLKAGL VSILFRGTWP RPGGARGVLV DLLNSMPFAN
     EYLLHALMKF YIEAEFTGTH TQFFDKFNIR YEIFQIIECI WPNTLYRTKL SNQAQQNLDF
     FVRFVNLLLN DVTFVLDESF GAFMTIHDTQ VLLNQSGSTM DPAQRQQKEE QLAAAQRNAK
     SYMQLTNMTV AMLKLFTDAL ADSFTMPEIV QRLADMLDYN LDAMVGPKSS NLRVDNLQEY
     GFSPRTLLSE IVDVYLNLMN KENFIYAVAR DGRSYKPGNF EKAAEILRKW SLKSPEELKR
     WEILQKKVQA AKKEDEQAEE DLGEVPDEFL DPLIYTLMED PVILPGSKVS IDRATIRSHL
     LSDPHDPFNR MPLKIEDVTP DTELKAKIEA FKAERKSAAK NRQMAQGAES MDTSSG
//