ID K5WS50_PHACS Unreviewed; 689 AA.
AC K5WS50;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0000256|PIRNR:PIRNR039133};
GN ORFNames=PHACADRAFT_175614 {ECO:0000313|EMBL:EKM53222.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM53222.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM53222.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM53222.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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; JH930474; EKM53222.1; -; Genomic_DNA.
DR RefSeq; XP_007397915.1; XM_007397853.1.
DR AlphaFoldDB; K5WS50; -.
DR STRING; 650164.K5WS50; -.
DR GeneID; 18909725; -.
DR KEGG; pco:PHACADRAFT_175614; -.
DR HOGENOM; CLU_013325_7_3_1; -.
DR InParanoid; K5WS50; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008370; 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; 2.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000008370};
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 9..486
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 184..271
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 363..423
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 600..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1,
FT ECO:0000256|PROSITE-ProRule:PRU10132"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 61..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 122..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 166
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 689 AA; 74611 MW; 044986F73B9B9EAD CRC64;
MSGRSRHTSA ILGPELAARL PEVKVLLVGA GGIGCEVLKN IVLAGFGNIT LLDLDTIDLS
NLNRQFLFRK KDVKQSKAMV AAKTASAFNP NVRIHPIHGN IKEPQFDISW FRGFDLVLNA
LDNLDARRHV NKMCMAADVP LMESGTAGYL GQVQPIVKDK SECFDCVPKP TPKTFPVCTI
RSTPSQPIHC IVWAKSYLIP QLFGEEEDSG EELDEAEKQG ENAQEIATLR KEAQAFKKVR
NALQQSDVGS DDAARLVFSK VFHDDINNLL SMADMWRTRA KPTPLDFNGI KNGTFCIAHK
RTGGALQVNG GSSKQPADGA LVNGDTAGGS AATERMLDGT PSASGLKAGW GSAGLKDQRA
LTLQDNLGLF VSSTNRLAAR IRNGEETISF DKDDGDTLDF VTAAANLRAA AYGIHGKSRW
EVKEMAGNII PAIATTNAII AGLVVLQALH LLRKTYNKLR NVHVQFRPSL PLSTINLSAP
NPKCGVCRDT YAEVLCDPSQ VTLRQVVEGI LGDGDGDGED GGTGPRDVSV YEAQRVLSDP
DWDDNLDRDL EGMGVTRGKF LSIVDEDGEY ATIQVAIGQL PPNHPIDGNT LMLPYPLPRP
PRIVKPTETP GLKRAAPDDE EEDDIIVDVP PAKRMRTNPT DTANTLPASV TVPVTPSKKR
KLDEDGILLL ESKDEVVEDD DAVEVIELD
//