ID A0A166JS62_9AGAM Unreviewed; 1033 AA.
AC A0A166JS62;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=PFU-domain-containing protein {ECO:0000313|EMBL:KZP21155.1};
GN ORFNames=FIBSPDRAFT_931789 {ECO:0000313|EMBL:KZP21155.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP21155.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP21155.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP21155.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KV417549; KZP21155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166JS62; -.
DR STRING; 436010.A0A166JS62; -.
DR OrthoDB; 1116432at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.10.20.870; PFU (PLAA family ubiquitin binding), C-terminal domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR015155; PFU.
DR InterPro; IPR038122; PFU_sf.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR013535; PUL_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR19849:SF0; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF09070; PFU; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00855; PGAM; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51394; PFU; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 104..135
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 143..174
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 182..214
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 222..253
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 358..453
FT /note="PFU"
FT /evidence="ECO:0000259|PROSITE:PS51394"
FT DOMAIN 530..816
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
FT ACT_SITE 829
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 903
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 828..835
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 878
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 1033 AA; 111684 MW; 4BAA4F557F8AEC49 CRC64;
MPYKLSATLT AHTSDVRAVV SPTDTLVLSA SRDTTAISWT RDSSSPTFTP GSLLRAGSRY
VNAVAYIPPT ADAPHGYAVT GGQDTVINVF ALDAATKGEP EYSLIGHSEN VCALNVGPDG
TIISGSWDST AKVWKNFKSV YDLKGHERSV WAVLALGGDQ YITGSADKTI KVWQQNKCLH
TLTGHTDAVR GLALMPDIGF VSCSNDSEIR VWTLGGDTVY TLSGHTSFVY SLSVLPDGGI
VSAGEDRSVR VWKDGELTQT IIHPAISVWA VASMPNGDIV SGCSDGLVRV FSESEERWAS
AEDLKEYDQQ VASQALPAQQ VGDVKKTDLP GPEALAVPGK KPGDVKMIKN NEVVEAHQWD
NDTNSWTKIG EVVDAVGSGR KQLYEGKEYD YVFDVDIQDG VPALKLPYNA NENSFTAAQR
FLAKNELPPS YLDQVVQFIE SNTSGVNIGS GNNNDYVDPF TGASRYQSSA NSGSTNQPGG
YMDPYTGASR YTANPAPAAN APASDYMDPY TGASRYSGAP AATVAVSAPP FQPVLTPVPF
KQANVQAMQT KFFQFNDDLR NEISTSTLAM YPEELDLVDE AFAYLTQALG STPTPSGPVL
GVGHLNAIMS ILERWPLAQR FPVIDLSRLV VAFGAAKSAD PETRARFFLA LLTASEWNAT
WSLPLSKTKQ TNILLMLRTI ANVFDEDAPI AEGTWVNEIL DAVGNGPYEA FPKPQRVALG
TVLFNLSCAM ARTPVEKSVR SLYLTILLGV LRAETQDSEA SYRALVALGN TIHTAKTKNQ
LLDASQAAEV RQVASGLPGI FPEDRIKNIA GGIIALLAMA PAVIYIVRHG ETDSNRSGII
QGHLDTDLNS EGLAQAERVA DVLKSIPFDI AFSSDLSRTV KTAEAILQYH PEVRLQKSEA
LRERYMGDLQ GKVFSSEAMS KYSHTMERSE DFAVRASKWW STTLQRLSEL QAHQEQPYNV
LIVSHGGWIQ TLMRTLVNSR KLKVAKGVAI NSCLNVSVTT IETDGNRKGV VVKYGDVSHL
ITKAVASNAD ELT
//
