ID F8P0N0_SERL9 Unreviewed; 673 AA.
AC F8P0N0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0000256|PIRNR:PIRNR039133};
GN ORFNames=SERLADRAFT_416361 {ECO:0000313|EMBL:EGO22714.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO22714.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO22714.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718, ECO:0000256|PIRNR:PIRNR039133}.
CC -!- SUBUNIT: Heterodimer. {ECO:0000256|PIRNR:PIRNR039133}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|PIRNR:PIRNR039133}.
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DR EMBL; GL945436; EGO22714.1; -; Genomic_DNA.
DR RefSeq; XP_007319954.1; XM_007319892.1.
DR AlphaFoldDB; F8P0N0; -.
DR GeneID; 18813468; -.
DR KEGG; sla:SERLADRAFT_416361; -.
DR HOGENOM; CLU_013325_7_3_1; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008064; Unassembled WGS sequence.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniRule.
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; IPR030661; Uba2.
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 PIRSF; PIRSF039133; SUMO_E1B; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039133};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR039133,
KW ECO:0000256|PIRSR:PIRSR039133-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039133};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR039133};
KW Zinc {ECO:0000256|PIRNR:PIRNR039133, ECO:0000256|PIRSR:PIRSR039133-3}.
FT DOMAIN 21..485
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 195..423
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 309..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1,
FT ECO:0000256|PROSITE-ProRule:PRU10132"
FT BINDING 40..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 72..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 133..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
SQ SEQUENCE 673 AA; 73488 MW; 2913AB7F3AE1F179 CRC64;
MNSPGPVNSP KNSSRYSHAR AILGPELSKR LPETRVLLVG AGGIGCELLK NIVLTGFGHI
TLLDLDTIDL SNLNRQFLFR KKDIKQSKAL VAAQTAGAFN PNVHINPIHG NIKEPQFDIE
WFQQFDVVLN ALDNLDARRH VNKMCMAAQV PLVESGTAGY LGQVQPLLKD RSECFDCIPK
PTPTSFPVCT IRSTPSQPIH CIVWAKSYLL PQLFGEDENA GTELDDAEKQ GENAQEIATL
RREAQAFKAV RTALRSESTA ADASRMAFQK VFNSDVLNLL SMADMWRSRV PPQPLDFDAI
KEGQFKLKHQ ASNTANPPAN GKSIPRKNGS AKGKHEPTNG NNVEPSGSQN GAGLKDQRAL
SLQDNLALFV SSTNRLAARL QTGKEDTISF DKDDDDTLDF VTAAANLRSA AYGIERKTRW
EVKEMAGNII PAIATTNAII SGLIVLQALH LLRKSYSALK NVHLQFKPTV PLSTINMCPP
NPKCGICRDT YAKVLCDPFK VTLGEFVDGI LGDGEGEGQG TGKREVSVYE DKRVLSDPDW
DDNNARTLES LNVTRGKFLT IVDEEGEWGT ISVALGVLPA DYPTSGPAFI LPSPLPKPPR
QVRPSTPPPP APSLKRSAPD DDDVSEIEPS SKRLKTNGDV TSPNKKRKLD EDGLILLDSA
NDKMLDEDVI EID
//
