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Database: UniProt
Entry: V9FTZ4_PHYPR
LinkDB: V9FTZ4_PHYPR
Original site: V9FTZ4_PHYPR 
ID   V9FTZ4_PHYPR            Unreviewed;      1196 AA.
AC   V9FTZ4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=P-type domain-containing protein {ECO:0000259|PROSITE:PS51448};
GN   ORFNames=F443_02626 {ECO:0000313|EMBL:ETI54561.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI54561.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI54561.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI54561.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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:ETI54561.1}.
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DR   EMBL; ANIZ01000465; ETI54561.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9FTZ4; -.
DR   EnsemblProtists; ETI54561; ETI54561; F443_02626.
DR   eggNOG; KOG1065; Eukaryota.
DR   HOGENOM; CLU_000631_11_2_1; -.
DR   OrthoDB; 67479at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd14752; GH31_N; 1.
DR   CDD; cd00111; Trefoil; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR000519; P_trefoil_dom.
DR   InterPro; IPR044913; P_trefoil_dom_sf.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 2.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   Pfam; PF00088; Trefoil; 1.
DR   SMART; SM00018; PD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF57492; Trefoil; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS51448; P_TREFOIL_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00779}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1196
FT                   /note="P-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004775916"
FT   TRANSMEM        1160..1184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          36..84
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
FT   DOMAIN          91..137
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
FT   REGION          510..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1116..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1136..1151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        63..80
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ   SEQUENCE   1196 AA;  131579 MW;  9B901F8529FBFA47 CRC64;
     MMVKLQLLFA SACINFGTGD SNAVDLLSAA LATTAAKCAK EPTQRVDCYP PRANFPDPTE
     ELCLAQGCCW ESLENEGIPC TFAAEEPPSE EKCNNVAKPA RLACRNPRFA SSKVLEDAET
     CESAGCCFDD GDCFQPMSDG YELLTLDETS NGWRGTLALH QGGTGPFGND VPLLELSVVR
     ESSSQLRIRI TDPAFPRYEV PDLPVRRQDR QEDINESDYK VHFTPWPFGV AVTRRDSGEV
     LFNSTPPVER ADKGESFSGL VFENQFLEIS TQLSVSEEDH QPILYGLGER LGPARLRADG
     DLYPMFSRAP NASAPVHSRS GGDNLYGVHP FVLQLEGGQS GNAHGVFMLS SNAMEVLARR
     DALTYRLTGG ILDIFVFSGP TPQNVVDQYT GIVGRPAMPP YWALGYHVGR RGEAKSVEEA
     MKIVTQLRMA GVPMDAYWQD FEYTADNGRA LSLDETKHSH RDMRAFIDDL HFHSQYFVCV
     QVPGITMQST SREIESKSWK RAKHNALTFH TRDTSEDDEG YDHSDDEEGA DGRDASNADD
     NTRDGSGRDI SGEGSGGSDQ SAESDQSEGG EQQWDPIARD EELDIFVKGV NGERYAQKAF
     RSGWAVFVDF FHPQASHFWH EQLAQFHKYV MPFDGLWLDM NEPSSTCDCA LAAEDDICAH
     VCTERHSTRP SNDEGIVEFE QVGVPDGGFI RTNDVNFPFD PYRQPFAPGQ NEPATGGHGN
     LNSATLPMAA LHHFSLHYNL HSLYGHAQAR ATHRALNSIV KKRSVLLSRS TFSGTGRYAG
     HWVGDDAEAS WEQLRLSLSG TLQMNLLGIP LTAASFLPLL RNHAESDDAK QTPVDFDADA
     LNILRSTLLR RYRYLPYMYT LFYEAHRSGS PVVRPLSFEF PDDKNARDVE HQYLLGPALM
     VSPVVHEGAI SAEVYFPDAK WYDAHNGKLA LDPEARDNRR VSLLTPLAKL QVHLRGGYVI
     PTQQSLTTTA LSRRGAFTLL AALDMSQETP SAFGELYVDD GDSLSAVEDR RYSLMNFGVL
     QNSSNSVEFK NSIKFHGYAG PEMQADLSEI RVYGVCGGGF AANSSMDATL LSSGEGSPRE
     VSIKADYFAQ SDMLVLSRLD VPIGQEFHVK VVAQPAATPE GGKRETGVGA NAGKSGSEEE
     AERGAQGGKK PAEKKKKSKF SVTGIVGIVV GCAFLAAIIL VFLLRLRRRR QGYETI
//
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