GenomeNet

Database: UniProt
Entry: K5WS50_PHACS
LinkDB: K5WS50_PHACS
Original site: K5WS50_PHACS 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system