ID G3AFR1_SPAPN Unreviewed; 858 AA.
AC G3AFR1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=SPAPADRAFT_48101 {ECO:0000313|EMBL:EGW35050.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW35050.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; GL996499; EGW35050.1; -; Genomic_DNA.
DR RefSeq; XP_007372462.1; XM_007372400.1.
DR AlphaFoldDB; G3AFR1; -.
DR STRING; 619300.G3AFR1; -.
DR GeneID; 18871177; -.
DR KEGG; spaa:SPAPADRAFT_48101; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; G3AFR1; -.
DR OMA; YYSYDWL; -.
DR OrthoDB; 2045396at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..336
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 443..547
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 97927 MW; 72CD5F8629157B36 CRC64;
MTYATEDTGS SHNQDSEFTP LLTSSKGSNS SSHGGLDEGL DLSSSQETSG EVNMKPHEYL
VSPPPTGSEI YSRQQQQQQE QDEEDDDDDD DDNVSRILKI AKRPSFIWIC TLGVVAFIIF
QLTFLPRTSL GRDYRRWHGI HLTKSDVKRL FLQMAGIGNS HNSLTTEEYI DSWLTNFTSI
NSKSTVNMIA DDNLELVSFV ETNFKQFGFK TESFSYDAPH SLTRPVSSTL RLLDKNGQVA
YSPVVGEPNF KTPAFYAFGT NASIVANFVF INEGTIHDYN LLEKHSIDVH NKIVIIKSNL
CNKNITIAEK VAIAKQRGAS GVINYYDFSA SNNVENESSL AHAISRASIF QQFRLPSIPV
SKKIIKPILD TLSADPQPDF SHWDYPPVGS TPMKVELNTT FAAAPLHPAK LTTVVASLKG
IMNDADVIIG ARRDSYTCNN PLSGHAILLE IMRNYQRLVA KGWKPLRNIK FVSWDGSNTD
LIGSHKFTDD VNVYNPKRSI VAYINIDGDA VMGSKLAVDA NPMLHSLLRN TAKFIPIPKE
ATSYKTLKND DDDEDDEGYT TLHRYWMKQD NATINSVMGL PISQTESIIF QQHLGTPSIN
IKFENDAKRD SSVYVPNSNF YSKDWLIKRE IDDDLLLHGS MIRFIGLLAI SLSEHEVVSY
KTHSYFKSIE GYFNELLEDK RNTLGFWHSE PVSNYVIAKS SIYQDLGIDN VKFGDLIRQF
KHLMNETVYQ SGIFDEWNNH VEDMLMQDYP WYLYYKKLQH FAQFKVTNYK LSHLERDLKL
QDKDYQYLNK DKSYYDSVIY GTKKFDPAEV TQEYFNDKLK TSTFTHLYSA IEVRDFEMTV
KWLVLIYEKF KNLRYKMT
//
