ID A0A139H867_9PEZI Unreviewed; 1591 AA.
AC A0A139H867;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=AC578_4296 {ECO:0000313|EMBL:KXS98601.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS98601.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS98601.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS98601.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:KXS98601.1}.
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DR EMBL; LFZN01000110; KXS98601.1; -; Genomic_DNA.
DR STRING; 321146.A0A139H867; -.
DR OrthoDB; 2342218at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR003689; ZIP.
DR PANTHER; PTHR11040:SF60; FAMILY ZINC TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04010)-RELATED; 1.
DR PANTHER; PTHR11040; ZINC/IRON TRANSPORTER; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF02535; Zip; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW Signal {ECO:0000256|SAM:SignalP};
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|SAM:SignalP"
FT CHAIN 18..1591
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007806531"
FT TRANSMEM 598..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 963..988
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1459..1481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1028..1427
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 758..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1591 AA; 173006 MW; 910F7F93BA801D9F CRC64;
MLAHTLISLG FLGSCFAQSS HSNPQSGSAG QITFTNSRRL LFDTNGNQID AYGSKVNYFN
GSYYLYGNSF STKGVAYGIK SYSSVDLENW QYNGFLFDPA AGNAAVCLAD GGCGRPHIVY
NGKQYVLWAN AGPNGYLVAT SSSPSGPFTF SQNRAAIDPQ FSALQPADFT TTVLNNTGYL
VFSALNFRDP RAGSIWPPIF QTLHTTELTS DLTNTTLKSY PVQSSTFDLI DQAAESPDLF
YRQGWYYISA SNTCGYCNGS IGLLYRSRSI QGPWTRQILA GYSCNGQVEG VLPLTNPDTN
QTTYVWHSTS VPGGPRTGFG GHIFQPLIFN SDGSVQDLDC SDNAEFPVTF TKGSATIASS
SASDGSPATA AYFPICDSDS FDLFQTWRAA KSGTIKSVSV NIAGAKVQTI PLALTVFKFS
SYSDLLAPEY KWTAMGTKSV NASDLSYVFD SAKVDVTSNA TVEAGDYLGL AIAGQDFTPY
CHLEYANDDA SHVLYQRGAG QNSWRDLQGK TGPVYERKGK GVKFFARQRS GRRLRDVGAH
RQSRQAAAVG TRWCALVTIM TRDERHDLLV LQAELQRRQA AGERPACGSD NKNREYNFGL
HLVALFLILI LSTLACSFPL IVRRFPRLPV PNHALFVSRH FGTGVLIATA FVHLFPTAYT
NLLDPCLPPF WTDVYPAMPG FIAMVSVMVV VGIEMFFAAK GAGHSHHVDF EQLRTRETDG
LDTRPALGRK SQSFNRFQQL PLGNAEHGDI ALAEQRSPYL DAPPTPTSSS ESPALNKPLP
RTPSPGRQDE DEDDDLHLDE LDPAAEDTQP LTRGNHSDDN EDLVMAPNGH ANGHARPMRH
NRKVSWADQA PEHSNTPHQT TPLEQRLVIQ CLMLEAGILF HSLFVGLALS VSTGSSFVVL
LIAISFHQTF EGLALGSRIA SIGSLSTASY KPWLMSLMYG ITTPIGQAIG LGVQGLYDPQ
SQFGLLMVGI MNAISSGLLL YAGLVQLLAE DFLSDASYVE LRGKRRLQAC GAVVAGAMLM
ALHILGRDVA ELAGPNISAG KRVMVCEGTS DRRFDAYNLP GRAMMVNGVH FMFKLAHQAS
QLLHLLPGSS VQAGNAIWAI AQESCTEENP ELWDCEEQRG EVFSANESST WSTSQVSNGS
YYNLNPVIES MLGLNANASY GLDTVTLGTA NGVLPALPNQ LVARIASNDF WVGVIGLSPL
RLNTTGFDDP VRTLMDTLSE PEERKIPSTT WAYTAGAFYK DAPIFGSLTL GGYDSMRFDP
NNSVSVPFSI NPSQDLQINL QSITYNGTTT QSSSYLLTDT ITAYVNSMIN YIWLPPEVCD
VFESAFGLEY DAATEFYLMN DTTHANLLAE NPTFTFTLGG ANSNETATIV LPYAAFDLNV
SYPHVNGSQW YFPIKRAQYI SQYTLGRVFW QEAYVIADYD RRNFTVAQAL FPSNSTPELV
RILPPGASDS DGGGLSGGAI AGIVMAVLAV VASVLVAFCL LRRKKRRRQA QEAGAMTTEI
KHVPAAPAAP GEIDGQQIHE KSADGVPFNK KDSELNKAHT WDTTDAPASE LSTGQTPQSL
YLETNWPRQF SELPAELPPV VEMEAGRRNG T
//