ID A0A409XBL5_PSICY Unreviewed; 686 AA.
AC A0A409XBL5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0008006|Google:ProtNLM};
GN ORFNames=CVT25_005163 {ECO:0000313|EMBL:PPQ88198.1};
OS Psilocybe cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ88198.1, ECO:0000313|Proteomes:UP000283269};
RN [1] {ECO:0000313|EMBL:PPQ88198.1, ECO:0000313|Proteomes:UP000283269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2631 {ECO:0000313|EMBL:PPQ88198.1,
RC ECO:0000313|Proteomes:UP000283269};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
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}.
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:PPQ88198.1}.
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DR EMBL; NHYD01002137; PPQ88198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409XBL5; -.
DR STRING; 93625.A0A409XBL5; -.
DR InParanoid; A0A409XBL5; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000283269; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
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; PF00899; ThiF; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000283269};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 14..471
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 337..408
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 299..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 686 AA; 74725 MW; 0A53351FBC89B12D CRC64;
MSTAKARSAH AKAILGPELH SKLANTSVLL VGAGGIGCEL LKNIVLTGFG KITLLDLDTI
DISNLNRQFL FKKKDVKQSK AMVAAQTASH FNPNVRITPI HDNIKEPQYD VQWFQQFDIV
LNALDNLDAR RHVNKMCMAA QVPLVESGTA GYLGQVQPLL KDETECFDCI PKPTPKTFPV
CTIRSTPSQP IHCIVWSKSY LMGQLFGEDE DAGGELDEAE KQGENEQEIA TLRKEAQAFK
VVRDSLRDSN TTNAAKLVFQ KVFNADIKNL LIMADMWKSR SPPTPLDYDS ILDDTFESGK
VNGTSTPNAV ASGSGTSHST STPNNPTNGH ANGTANASNL KDQRALTLKD NLNLFISSTD
RLADRLRHGE TTISFDKDDE DTLDFVTAAS NLRSYAYGID GKTRWEVKEM AGNIIPAIAT
TNAIISGLIV LQALHLLKKS HGQLRNVHLQ FKPAVPLSAI RLSTPNPQCG VCRDTYAYVP
CDPARTVLRD IVKGIMGDDE RDVSVYEDKR VLSDPDWDDN VDSTLESLNV TRGKFLSIVD
EEGERETISI AIGLLSPNHS VDGPPFILPS SLPIPPPKIK PAPTPATPPR TSQKRPLSVE
NEDGVIDLAP TPKKRRSGPT GSSNGTGSAS KKRKLEDGSS PSKRRRLEED GVVALDGPND
DLGPVDHVQL SSQGQEEAEY ITIDSD
//
