ID A8NN69_COPC7 Unreviewed; 666 AA.
AC A8NN69;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Uba2 {ECO:0000313|EMBL:EAU86701.1};
GN ORFNames=CC1G_06462 {ECO:0000313|EMBL:EAU86701.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU86701.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU86701.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU86701.1}.
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DR EMBL; AACS02000012; EAU86701.1; -; Genomic_DNA.
DR RefSeq; XP_001835059.1; XM_001835007.2.
DR AlphaFoldDB; A8NN69; -.
DR STRING; 240176.A8NN69; -.
DR GeneID; 6011585; -.
DR KEGG; cci:CC1G_06462; -.
DR VEuPathDB; FungiDB:CC1G_06462; -.
DR eggNOG; KOG2013; Eukaryota.
DR InParanoid; A8NN69; -.
DR OMA; RFDIKQM; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000001861; 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:UP000001861};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 14..469
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 330..407
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 299..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..646
FT /note="Basic and acidic 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 666 AA; 72988 MW; 089C05644AA7CB5F CRC64;
MSTAKGRSTH AKAILGPELY AQLENTHVLL VGAGGIGCEL LKNIVLTGFG KITLLDLDTI
DLSNLNRQFL FRKKDVKQSK AMIAAQTAAP FNPNVKLHPI HDNIKEPQYD IPWFQQFDIV
LNALDNLDAR RHVNRMCLAA GVPLVESGTA GYLGQVQPML KDRTECFDCI PKPTPKTFPV
CTIRSTPSQP IHCIVWSKSY LMGQLFGEDE DAGGELDEAE KQGENAQEIA ALRKEATAFK
AVRDALRSSK SDDVAKTVFK KVFDSDIRNL LSMADMWKSR TPPTPLDYDG ILSGEFTAKK
PNAPAPPVAN GNAVASSSKS SDTAAPANGQ TNGKSTSGLK DQRSLSLKDN LELFIDSTKR
LAHRLQNGED TISFDKDDDD TLDFVTAASN LRSTAYGIDT KTRWEVKEMA GNIIPAIATT
NAIVSGLIVL QALHLLRKTY DRMRNVHIQF KPEVPLSTIT LSPPNPQCGV CRDTYGLLLC
DPSRAKLGEV VKGLLGDDDR EVSVFEDKRM LSDPDWDDNF DRTLESLNVT RGKFLAIVDE
DGELSTLSIG LAPLPPNHPV DAPPFILPSP LPKPSRKPKP RAPTPETPHK ANGKRTLPVE
NDDGIIDLAP TPKKPKFSVA SNLPLKRKAE DEPSPSKKRK LEEDGLVVLD GADDKIEEQD
YIVIDD
//
