ID A0A0V1MG50_9BILA Unreviewed; 982 AA.
AC A0A0V1MG50;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ubiquitin-conjugating enzyme E2 K {ECO:0000313|EMBL:KRZ70820.1};
GN Name=ubc-21 {ECO:0000313|EMBL:KRZ70820.1};
GN ORFNames=T10_4524 {ECO:0000313|EMBL:KRZ70820.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ70820.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ70820.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ70820.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:KRZ70820.1}.
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DR EMBL; JYDO01000107; KRZ70820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MG50; -.
DR STRING; 268474.A0A0V1MG50; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd16666; RING-H2_RNF43-like; 1.
DR CDD; cd14313; UBA_II_E2_UBE2K_like; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00179; UQ_con; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 363..403
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 787..936
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT DOMAIN 942..982
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 544..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 875
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 982 AA; 108520 MW; BAA1419489BB6AD9 CRC64;
MQNNRKLCGV VCSLRILTNQ SSQPVHFKKL EKQFSFYANI KKSTIVIRRK QRERIKAMLP
LLHGIIAWRR RPGCTLLVLL LLIMLLGCGQ VCPVLINDDG QSESVMVTGD ARIELFFNDG
SATLSGNYSV YGKRRSVVGR IFQLHPLRAC KRNSIGLDSG LVGQIAVVIM DGVIQPFIAG
CVSPYNQALF AFDSGAKAVI LDMQNCRLNE WPAVDIPVIT TNGFQAEMLK ALLAKVPNQD
LSEVSVSIGP TTPLTVEYES ATTSTTTTTF KDMFPAIFDK GVFPALILLL FLVAAILLGG
VRSRVKLRDT LPADTSVRKL AEAALARMEL RKFRKPKKIS DECSVEAGLL NGSKLSLNSV
DGCAICLESY KDGQILRVIA CGHEFHKKCV DPWLLLNRTC PLCMYNVILE RHVSPEPESG
SSPSRAAPLL VENINIAAAL ASSANNSIQD HNTTNSNTIT TTTTTTTINN TTNNNNTSTR
DNINIIVQNQ QMCSGEIRGE IPNQINKSGD MPNVQTLNEL PSPSKRYRQA IEMEKQQMMR
IASIPNTSNN NNNNSSSSSS SSKARPSMYC GHAMHTNLPK RTMKLYPDIE VVMFAHSGGG
GRYPSGDNSV GCTERIYKRK HRRCAADGKT TQKRSTHRGR VSSRSGGNRA APFAKYAPLH
QQHKLRINPL LPDCISEGYL SDISAVTEIA IDHPAEEEAK PMGMTNYHHH HHHHQQQRLI
TLSRDQATAS TLCCDTAPQN CGNQQQLVQE TQQQQQQQQQ QEHLTPILYH TDYIILKGVL
TPEMANISLK RITREFKDVT SSPDLEQSGI RVSFANDSHH VLRGEIRGPP DSPYEGGVYE
LDIQIPETYP FTPPKVKFLT RIWHPNISSA TGAICLDVLK DQAASLTLRT VLLSIQALLG
APEPRDPQDA VVAKQMMEAP SVYAETARFW ASIYAGSANA IPEDMNKKVQ KIVDMGMSKD
DAITALSHSR WDVSQAIEYL FS
//
