ID G7DW64_MIXOS Unreviewed; 1418 AA.
AC G7DW64;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 13-SEP-2023, entry version 59.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Mo01524 {ECO:0000313|EMBL:GAA94870.1};
GN ORFNames=E5Q_01524 {ECO:0000313|EMBL:GAA94870.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA94870.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000256|PROSITE-ProRule:PRU01100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA94870.1}.
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DR EMBL; BABT02000047; GAA94870.1; -; Genomic_DNA.
DR RefSeq; XP_014565010.1; XM_014709524.1.
DR STRING; 764103.G7DW64; -.
DR GeneID; 26265664; -.
DR eggNOG; KOG4299; Eukaryota.
DR HOGENOM; CLU_253246_0_0_1; -.
DR InParanoid; G7DW64; -.
DR OrthoDB; 5491843at2759; -.
DR Proteomes; UP000009131; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd15535; PHD1_Rco1; 1.
DR CDD; cd15534; PHD2_PHF12_Rco1; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47636; TRANSCRIPTIONAL REGULATORY PROTEIN RCO1; 1.
DR PANTHER; PTHR47636:SF1; TRANSCRIPTIONAL REGULATORY PROTEIN RCO1; 1.
DR Pfam; PF00628; PHD; 2.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51764; GH26; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU01100};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01100}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1418
FT /note="PHD-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009955571"
FT DOMAIN 61..412
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT DOMAIN 713..762
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 842..896
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 541..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 1418 AA; 151040 MW; 189E96DD8EC34DAB CRC64;
MARQVGRLTC LAACIARAMA APQFTLPPLT PLSIAGDPAS STSISLASLS TATTSAPPTT
TSAVAIPTST GALYEPPGNQ VILGAWVDQA INYSDTPAQV NARLERNFGM FQQTQEIPLV
PYNFTLGAGG QGSELLIAAT NTSAALFLTV YPVNITAVQP VDLEALGYQC QSYIEQGRPT
FIRFAPEMQG PWMPYGVQPT EYIVMWQAMY RAVKAVSPNC ALVWGPNIGS GYPYGVTLGE
IPNVADQRAL DTNNDGVLDS SDDPFTPYYP GDDYTDWHAV SLYYKGPNGG MSYNQAQPGG
FVASLLAGSD PTTGADSGYN FYQTYCANKP NKACMLGESG AAYHVTSDGD ASQLQLQQAW
WQDCLTNATF FDAHPRLKGI MMFEFLKEEY DTGTADLRDY RITNATNILS AFQSDLSSVA
TRYAWASATT ILNACPSSVN LLGVVTTISG TVLTVYETPC ASLPPVTSTA TTSSAAQPSL
TALDPAAAAR MTSSTTSGSF ATFSALGSAP SVQHSNSALF ITASVFLAST LGFNAGSLSD
VGSKDPSLEP VESVVAESAP PATRRPTRSR QRPVSSAASA ASTAETVNPL VAALDAHKER
DPLLTEELAV GFIEMTPSGK LTTSHEDRLP PPPAVKGSVQ SYVQSAVAHK RASMGSGKSH
NDALTLSRTK PTTAIKFSPL KGTRRARRAE GEPKSDDLSS ADTPEPENGI MNNDFCDACK
GKGHFLCCEA CPRSFHFSCL DPPLELSDLP ENSWYCCTCL FSRRKTVVAI PSEAGPFTTL
MTKVAKSNVT EFSLPASIRT FCKDVASREN GDFMDLVEHK PAKKTGVEER DPYKLKSKSG
ASVLCFRCKG AASSPSKPIL SCDFCDQHWH LDCLDPPMAS MPAPTKRWMC PTHPAHVQAK
RKRARNTPVV AISKPGQRNN GDIDIVPGRF SRYFDQEVDY DRMNVNGVRY QVPEDAIILD
FWTKAKDARS FRRVRGNTNQ GALSQLAELQ STFQRQREED SESLSTLSDL SDFVLNNFPT
APHLAAPVSD GGPPSADMDA EPDQASISPI LAQAVLQRVQ SPAEALPTPD NSSESSDETA
GVKVNGQPKS PFDGRRVVGR TIYGATTPNS ITSGSPTRRA QSSKPDSATV SNGKPHPSET
IDRAPSAESA LPAPEDGILG IDNAQDARPQ SNAKKPRHPL KIRLSLKSKG SARASPEFEE
HPVVQDTPVA STSSSTDAVP EGRPRRVTKR TRLSPPAVIQ PPRRKRPSKP RFSKPAASSA
PAPVPMTTDS TPPPMTSLRI DDVLPSSGPH LTAERSPAAA RRSRAGKEPS AGLSTGSNRP
TASQASGSPS GLPANESGSQ GRSQSPIALT DETGVMAPHS GTTMRSATLD DEPHNLGMDS
KAALAQVTGL LQDEDYAMQE DDTLKYLAAP AYVDGATN
//
