ID B6QIT7_TALMQ Unreviewed; 1049 AA.
AC B6QIT7;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=GH16 domain-containing protein {ECO:0000259|Pfam:PF00722};
GN ORFNames=PMAA_098720 {ECO:0000313|EMBL:EEA23282.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA23282.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
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; DS995902; EEA23282.1; -; Genomic_DNA.
DR RefSeq; XP_002149449.1; XM_002149413.1.
DR AlphaFoldDB; B6QIT7; -.
DR VEuPathDB; FungiDB:PMAA_098720; -.
DR HOGENOM; CLU_297715_0_0_1; -.
DR OrthoDB; 1949878at2759; -.
DR PhylomeDB; B6QIT7; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00413; Glyco_hydrolase_16; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR PANTHER; PTHR38121; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR38121:SF2; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1049
FT /note="GH16 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002848267"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..260
FT /note="GH16"
FT /evidence="ECO:0000259|Pfam:PF00722"
FT REGION 373..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 118175 MW; D529FAD85C9FE391 CRC64;
MFPSAWRGLL FAFLVVLKTA QGATITTNVE DCGCGFYDEN ADLYFTDSTI VYFNESSSIP
SDFVVEEFEH RYDRGWNNMY RMGAAVDNVQ ITRDVTAKNL TSLELSCHPP EKEHLVVGSS
IRTSRQDIFF GSFRTTLRPA RQWSLGSVIS MNLVHNQTES WQIDVMNTDN RNQSWVDMLM
RGQFANTWLG RNFTNLTAEG LNPWMYTEYR VDWTRDSINY YIGDVLRTSY NTSVNSSIPS
TPAPLKFQHW STGNKYTSQG PPISTNLANI GYTRLFFNSS TWNETTRTAY DQRCSTQKAC
NMNDLSLRGS SHFEPESLDP WKQYQPPYRI RWAPLIIDIV FAAVFLVLTG KTLWRRFTWH
KLMIFLGVHE RDPPKPRSFD APPPSTASMD RDSQTNRDSA DTGSNSPVSH NNEHPNIHRN
ESFNTLPPYK GSQTPLPQYQ SPAVSRRPSL SNMAGNSFAY PVSINGTIQV ESSRVTSRAA
SRAPSLHTGS IVDYSTTPGQ EVQATGVTKV EDNSEKNKEV IKTEAVPVAK DEQTKPGEAG
KDGKPAAGAA AASAKPPRVD YLAGFISISA LLVTVNHFGL TYFGAVIMPG NSPHYQSETI
ARKTFATYFL DPLWIGPFLM ISTRFLSSNY IRTGKLDNMA QKIVARPFRL LTPVASIAFL
EYFLMDAGAL NWLEYLPSVT WSDWPFTAIT LNPGTFISEI IQLAFLIPNA APMITTNYST
GVLWTIPVQL QGAWQTLLGL IMIRQIKTPW KRFSFYFFCT IMHWYALSWG SYYYVGILLA
DLDLTYKYKQ KWLYPRPWLY WPVLILMACT AIGAFSIDLV TQHNGINYAQ IEYGWHPDPK
TGNSLAQENS APYPDYFIPR LNAFLATITM QGVVEISPTL QKMLSVKVLQ WLFPHIFSIY
LIHGFVMWSV GSWAMISMFS HGYPYWLCTL VTAIVCYGTL FAVLPILTPP IEALGKGFTQ
RLWQFASSEP VERKPTTYPF GEEFLTTRDQ LENSSKPGSL NGVSPSPAPS SSGGVTVVNE
KDVSGKGKEV DLTVRELKNG RIMEHVNEF
//