ID Q22CM6_TETTS Unreviewed; 494 AA.
AC Q22CM6;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 24-JAN-2024, entry version 96.
DE SubName: Full=Ubiquitin-conjugating enzyme {ECO:0000313|EMBL:EAR83026.2};
GN ORFNames=TTHERM_01027520 {ECO:0000313|EMBL:EAR83026.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR83026.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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DR EMBL; GG662566; EAR83026.2; -; Genomic_DNA.
DR RefSeq; XP_001030689.2; XM_001030689.3.
DR AlphaFoldDB; Q22CM6; -.
DR STRING; 312017.Q22CM6; -.
DR EnsemblProtists; EAR83026; EAR83026; TTHERM_01027520.
DR GeneID; 7840258; -.
DR KEGG; tet:TTHERM_01027520; -.
DR eggNOG; KOG0895; Eukaryota.
DR HOGENOM; CLU_532671_0_0_1; -.
DR InParanoid; Q22CM6; -.
DR OrthoDB; 276854at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR CDD; cd05467; CBM20; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR46116; (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR PANTHER; PTHR46116:SF12; UBIQUITIN-CONJUGATING ENZYME PROTEIN 17-RELATED; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 1..108
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT DOMAIN 233..400
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 144..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 57357 MW; 2ADBA0CA1C30C436 CRC64;
MINIRFEAKV HTSFGQKVLL VGNHPQLGDW QPANGLQLST YEGLYPIWRS EQQLRIPEGF
DLEFKIIVIN NNQQLDHWEN LPQNRTYTPS LCKESVLLRM HESSLWIEEF YDGPVDKIHE
NSLQNYTRIM APMKIRSSRI LNPVIANQPT KKQEEKQVRK AEENSLNSES ITIESNGNKP
NEKDGETKKL SHPLKENLQQ TENQQETEQT NTIKYFYKQI ASKSESVLVS THVKVQRLKN
ELKQLAKSLP IQSSNSIFLV YDEQRLDVMR ALIFGSEDTP YAHGAYFFDI FIPDDYPQNP
PKVSIVSTKD NSIRFNPNLY ADGLVCISLL GTWEGDQSEN WDPTNSNIYQ ILISIQSLIM
NEDVYFNEPY YQEWKGSEQG DKCNRAYSNI VKYYNIQHAI GDMIENPPYE FQQVIYTHFL
LKREAIKATA QAWIEQAKKG EECLYDELIE DHNQQISSKF SSEKDAYLHS LQEEVERVNK
LLDSLDERLV LISS
//