ID A0A1S3JS14_LINUN Unreviewed; 1114 AA.
AC A0A1S3JS14;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Ubiquitin conjugation factor E4 B {ECO:0000313|RefSeq:XP_013412896.1};
GN Name=LOC106175438 {ECO:0000313|RefSeq:XP_013412896.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013412896.1};
RN [1] {ECO:0000313|RefSeq:XP_013412896.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013412896.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_013412896.1; XM_013557442.1.
DR AlphaFoldDB; A0A1S3JS14; -.
DR STRING; 7574.A0A1S3JS14; -.
DR EnsemblMetazoa; XM_013557442.1; XP_013412896.1; LOC106175438.
DR GeneID; 106175438; -.
DR KEGG; lak:106175438; -.
DR InParanoid; A0A1S3JS14; -.
DR OrthoDB; 1554at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
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; cd16658; RING-Ubox_UBE4B; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 1041..1114
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 127795 MW; DA140833BAD60E0D CRC64;
MSELTPDEMR RRRLARLGAS PASSPGGGSV SPQTPASLGA SPSLRTQAAS STQPSPSETP
MSVDQSASET SNMETDDSSC EKSAQSQVDV DSGIETNMEV DDEPRAETKR KRDISVSEAS
EEQTIAAICR LFIVSWKERS EETLYLPDLA ESCSGSENGY EDYQDLISQI LMEVLTVMSQ
QSKNPMLSLK PPKLAGSPSK YGASPGAGAM LLHERPTRDF PRLKFQPEDS KEVEMLKYLL
DCFDRCLNEE RLSSKRSRVP PLSTAIEETR TQCVNMAALV LQGVLTHPRS PARPSLLLPF
LLNHNLPAGF LEMLVKQTSG CQRSFKQVFA PILQGLYNTI KRLSFDEDDY RQPILVLRQL
CDIQTFGKQK PVCSLIIQLD NWLPAGMTEA EGMELQKLAF LGPFFALSVF AEDNTQVVEK
LFANKEMPPD SIRLVHQRLR SEMDFARNEL FEIVHTFLRN VDTRDSCLNF ITAVIQRNLK
RAQIQADERL LCGEGLMLNF LTVLQKLSRP IKLEKVDPFY LFSPNARVNI SEEARLKCTT
QDSTQWIEEL NKDTSHIWQD AKFPTECYFL TLHSHHLSIL PITRKYQRRL RAMRDLTRMI
EELENHEPQW KHLPTVASRN RELLKRWKSQ ERRLQRGKMC ADAAVFQESL LVGTLQFFET
LVQYLLRLVC PSYPRISLPL PQEVPMLFAA LPEYYVEDLA DFFLFVIQYT PHILETSLTH
IKDLADFLIV FISSSHYIKN PYLVAKLIEV MFVLNPNVQP RTEKTSDMVL NNSLALDNLS
PALMKFYTDV ESTGASSEFY DKFSIRYHIS IIFKTLWENP AHKGKLIEEA NSGKQFVRFV
NMLMNDTTFL LDESLDTLKS IHEAQELMEN KAEWGKLSRE QQQSKQRQLA QDERQCRSYL
TLGSETVEMF YYLTRQIQMP FLVPELADRL AAMLNFNLQQ LCGPKCKELK VKNPDKYGWE
PKKLLDRLTS IYLHLNNCDA FAQAIANDER SYRKELFDDA VARLKKACIK THTEIAQFQQ
LQSKVEKLLV EKHKEETDFG DIPDDFRDPL MDTLMTDPVI LPSGTVMDRP IIQRHLLNSS
TDPFNRQHLT EEMLIPATDL KKRIEQWKRE KTKK
//