ID A0A1J1HST2_9DIPT Unreviewed; 1111 AA.
AC A0A1J1HST2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 03-MAY-2023, entry version 24.
DE SubName: Full=CLUMA_CG004749, isoform A {ECO:0000313|EMBL:CRK91061.1};
GN ORFNames=CLUMA_CG004749 {ECO:0000313|EMBL:CRK91061.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK91061.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK91061.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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DR EMBL; CVRI01000020; CRK91061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HST2; -.
DR STRING; 568069.A0A1J1HST2; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:UniProt.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd18493; BACK_BTBD17; 1.
DR CDD; cd18292; BTB_POZ_BTBD17; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR028077; UAE_UbL_dom.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 651..721
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 204..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1111 AA; 125900 MW; 27ECC227B9258B0B CRC64;
MAAEISGIFR QELRELILSS KILVVGAGGI GCEILKNLVM CGFKDIEIID LDTIDVSNLN
RQFLFHKEHV GKSKANVARE TALKFNPNVD IKAYHDSIFN TAYGVSFYQQ FSMVLNALDN
LKARNHVNRM CVNARVPLIE SGTSGYNGQV ELIQRGVTQC YECTAKAAQK TFPGCTIRNT
PSEPIHCIVW AKHLFNQLFG EDNADEDVSP DTADPEASGE AGKDAMVGES NEQGNINRVS
TKQWAQNSDY MPEKLFNKFF FDDVNYLLSM SNLWKTRAPP KPMKFGELDV ISDVNDLSLN
VGVIRDQKIW TVGECQKVFA DSINNLKLQS QQLKEGDHLV WDKDDQDAMD FVTACANVRS
MIFSIPQKSR FDVKSMAGNI IPAIATTNAI TSGFVVLHAF KVLEKNFECC QNVYMRLRAN
PRNQIFVPEK ELLKPNPKCY VCGDKPEVIL KVDTDVVTVK ELRDDILIKG MSMVEPDVML
DGKGIIVISS EEGETECNEG KLLKELSIVD GCILKVDDFF QQYELTITII HKTVGRDDPK
FEIIADQEVL KPTKEETSSK EPQPGPSGLN GGSSNGSKPY ESDDDDVLCV ETVPLQPSAE
KRKHADDDEP SSKRARVENI KTETPLEEVE IGDQQSVLLK VAGLYASHLL SDISLVVGEN
RYPAHRVILS ASSEVFQCML LNPQWQECKE SVINLVEDPQ NCRVFPQFLK YLYTGQVRIS
IETAMPLLSL ADKYNIKDLI VLCRDFMSKS IAIAGIKGYL ISWLQYTLSF NYHQQLTNEL
KNFLRLNIEI VGYSRDFVDI DPNNLVVLLQ QNDLVIKNEA ALFEIVERYL MAKREQIEHE
ESLSDEEKGC HMKSLIEGIC SHIRFPMMTV SELASIPLKA ITSFSKEFFC DRMALGMSFH
AGQPFRLSDC DSHEINLQYT PRLYTCDVFC LEMKVEEIHN VDNYKNFGAC FFSLSEFPYN
SNDSSDENTI QWEIDFFPRG IRYNRAQLIN VYNMPLHHQG KVEVPETILK TVRVRCTCKA
NLIEEQRFKI AVLVSGNQNN ITHTRTLHTR INYFSRENRV INIDNLVNYD ELSTDRSLYL
IGPNHDTVRI HVIITPMQQG LTHDPPNFDF K
//