ID C9SLI4_VERA1 Unreviewed; 280 AA.
AC C9SLI4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Phosphoglycerate mutase family protein {ECO:0000313|EMBL:EEY19552.1};
GN ORFNames=VDBG_05661 {ECO:0000313|EMBL:EEY19552.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; DS985219; EEY19552.1; -; Genomic_DNA.
DR RefSeq; XP_003004548.1; XM_003004502.1.
DR AlphaFoldDB; C9SLI4; -.
DR STRING; 526221.C9SLI4; -.
DR GeneID; 9531539; -.
DR KEGG; val:VDBG_05661; -.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_0_0_1; -.
DR OMA; DFNRHEH; -.
DR OrthoDB; 9136at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT REGION 191..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 94
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 280 AA; 30227 MW; 18CBF72593C16F79 CRC64;
MGKVNIFLIR HGESVDNVAG LYAGSRDSPL TAHGVLQARR LASHMATGAP PATHIFTSNL
KRAVHTAATV REAQPPPLAG MPAVDVVQLL DLREKDFGAD EGKKYGQRDH VRATDAETHD
AMHTRASRFV DSQLAPIVAA LADKPACVMI VAHGLILASL LRVLRSNAWF ASSSEPGDSH
ASWSNTGYTQ LVVEPSHPPS SQPRQDAGEP PCRPSNHGPR WPDLRLSIVV FNNTTHLAGL
KKTRGGIGSA EFDQRQKTLT SFFAAAPPPK KRKAEDQLEK
//
