ID A0A139H225_9PEZI Unreviewed; 710 AA.
AC A0A139H225;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cutinase {ECO:0000256|ARBA:ARBA00013095, ECO:0000256|RuleBase:RU361263};
DE EC=3.1.1.74 {ECO:0000256|ARBA:ARBA00013095, ECO:0000256|RuleBase:RU361263};
GN ORFNames=AC578_3231 {ECO:0000313|EMBL:KXS96462.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS96462.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS96462.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS96462.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants. Degrades cutin, a macromolecule that
CC forms the structure of the plant cuticle.
CC {ECO:0000256|RuleBase:RU361263}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000256|ARBA:ARBA00034045,
CC ECO:0000256|RuleBase:RU361263};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361263}.
CC -!- SIMILARITY: Belongs to the cutinase family.
CC {ECO:0000256|ARBA:ARBA00007534, ECO:0000256|RuleBase:RU361263}.
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:KXS96462.1}.
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DR EMBL; LFZN01000174; KXS96462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139H225; -.
DR STRING; 321146.A0A139H225; -.
DR OrthoDB; 1112460at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR InterPro; IPR043580; CUTINASE_1.
DR InterPro; IPR043579; CUTINASE_2.
DR InterPro; IPR011150; Cutinase_monf.
DR InterPro; IPR003689; ZIP.
DR PANTHER; PTHR48250:SF3; CUTINASE 1-RELATED; 1.
DR PANTHER; PTHR48250; CUTINASE 2-RELATED; 1.
DR Pfam; PF01083; Cutinase; 1.
DR Pfam; PF02535; Zip; 1.
DR PRINTS; PR00129; CUTINASE.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00155; CUTINASE_1; 1.
DR PROSITE; PS00931; CUTINASE_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR611150-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361263};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW Secreted {ECO:0000256|RuleBase:RU361263};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487,
KW ECO:0000256|RuleBase:RU361263}; Signal {ECO:0000256|RuleBase:RU361263};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361263"
FT CHAIN 18..710
FT /note="Cutinase"
FT /evidence="ECO:0000256|RuleBase:RU361263"
FT /id="PRO_5007747341"
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 445..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR611150-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR611150-1"
FT ACT_SITE 283
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611150-1"
FT DISULFID 122..201
FT /evidence="ECO:0000256|PIRSR:PIRSR611150-2"
FT DISULFID 266..273
FT /evidence="ECO:0000256|PIRSR:PIRSR611150-2"
SQ SEQUENCE 710 AA; 74752 MW; 594EAEC7A1C217AD CRC64;
MLFSNFFLVA MASLALAKPV EKNPEAAGRA ASILGAVLMP RYSCAATCGS SADCQVDGLY
GMDAAMSRWR GVHCTRMFFT PVLIGLLAAS AYAFPADNVD EVAKSLEARQ SVNSDELESG
ACLQVTFIFA RASTESGNMG ATVGPQTCSA LKRRLGSSNV ACQGIGAPYY ATLGDNALPR
GTSDAAIAEA SRLFKLANTQ CPDTIVVTGG YSQGTAVIAA SLSDLSQQAP DVAGQVAGAI
LYGYTRNQQN GGRIPNYPTE RTKVFCAAGD LVCKGTLIVL APHFSYGVDV DEAAEFLAQR
VQAAVPSNEI TADSPNSIDN MGTCGTGTRH ENYNLPLHVG ALFIILGVSA GACALPLMAL
KVPQLHIPPK ALFVFRHFGT GVLIATAFVH LFPTAFVSLT DPCLAPFFNE QYPALAGAIS
LAAVFIITIA EMIFSPGRSL CSGPEASGLH DLDSKDAQTE RTSRQAANAD SLVEEDITPA
QATPQFGRTR SGRSHSVMKT APASLTGQAQ DSHLELDGLP DHTGSIAESR MSEESLGSTA
AKEAEQQRKK LTMQCMLLEC GILFHSVFIG MALAVAVGSE QVILLIAIAF HQTFEGLALG
SRIAAVGWNP RALQPWLMAL AYGCTTPLGQ ALGIATRNLY SPDSETGLTV VGTMNAISAG
LLTYTSLVDL LSEDFLSDHS WKTMRGNKRI IAMSLVFLGA FCMSLIGAWA
//
