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
//