ID A1DAJ2_NEOFI Unreviewed; 1874 AA.
AC A1DAJ2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
GN ORFNames=NFIA_095020 {ECO:0000313|EMBL:EAW19882.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19882.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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; DS027694; EAW19882.1; -; Genomic_DNA.
DR RefSeq; XP_001261779.1; XM_001261778.1.
DR STRING; 331117.A1DAJ2; -.
DR EnsemblFungi; EAW19882; EAW19882; NFIA_095020.
DR GeneID; 4588688; -.
DR KEGG; nfi:NFIA_095020; -.
DR VEuPathDB; FungiDB:NFIA_095020; -.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_001425_1_0_1; -.
DR OMA; QYYESSY; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 4.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 3.
DR SUPFAM; SSF51126; Pectin lyase-like; 4.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1874
FT /note="pectinesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633939"
FT DOMAIN 410..706
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT DOMAIN 767..1051
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT DOMAIN 1134..1418
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 727..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1874 AA; 195454 MW; 3DCD051B09617C70 CRC64;
MRFWHAWGLT GLASLAVAQN VTVGATVAST SAAATAAASS TASTTTLSSP TSSSVVVVAT
DSSGQFTAIG DAIAYAQKQG IPTVTVKAGT YTQAVTVSAT PSVTIIGETA NENDYAQNQV
TISATSPLVI SVNVLGITFS NINFVNTATG SYGAATIRGS KNAFYQCQFV SAGSLGITAN
LGLGIIANSY IEALDKVIYS YPTLYIYNTT IVPVGSSALL VYNKGYTSGT TLYNSTVVFD
SCSVQQKSGT SNKNVYLAAA NNGGGSVVVF RNTYLAGLIT ATGVHVDTAT QNTLNFYGEY
GTTGAGSYSS NQASRSQYIS LMGASDLIRF SIDQVFAGVY PQFASSSTNW VYSDVLEDIV
NSDVIQSSSS AVAASSAVAT STAVATSTAV VTSSTASATS TAPTPFSTLV VSQNPTAGQY
ANVSQAIAAL PNDGQAYTIY IKAGTYTEQI SITRAGKVTL RGETSFENDY TQNLVTIQFS
YGVLTSAGQN EKTPVIYAKK TDGSGLALYN INFVNTYPQT KNTAALAADF YGSNMAAYGC
SFIGYQDTLL ANKGTQVFSN CYIEGSVDYI WGFSTAYFHQ CYIASNTAGA YIAAQSRSSS
TAAGGYVFDS CYVTYTNTYG TTFGQTYLGR PYSQYSIAVY MNSYLDKHIN SAGWSIWSTS
APQTDHVTFG EYNNSGPGAW SSSRASFATN LTADAASAYT LSSWIGDTAW LDMTGYNYVP
SYSLTGPSTS TNTSTTTPTS TATPSATATA TWGHPTSGTT PPAGALIVSQ GGSVNGSYSN
LTDALAALPN DASTQVIFMY PGTYTEQVPS INRKGPVQII GYQSGNPGET YSTNQVTITF
ARGLSVSPLP TGHSDAETAT LSTASNKIAL YNINIINSDN LDGSQSSYVT LAASIYGSQI
GFYGCSFIGC KDTLLTGSTA GYQYYESCYI EGAIDFIWGY SKAYFKGCTI GAKRAKSAIT
AQSRASSSAV GGYIFDECTF EAAPGATVDL TQSVYLGRPY SAYALVVVKN SYLSDIIQPA
GWKIWSATDP RTDHITFAEF NNSGPGNWEN NAAARQAFGN CTLLTSDTYT LESVMGSTDW
IDLTYWDAVT IPTGTPTTTA TATATPIVSP TPYDGTVPPA GAYIVSKTSI GNVTTYDTIQ
SALNALPTSG KVAPTVFIYP GIYEEQLVLN RSGTTILIGY STSTFDYNSN QVTIQYNAGV
DTQADQSNSD SATVYATGNY IQAININFVN NFGATKNYAS LGFAVKSSKY ASLYGCQVKG
NQDALLINGY LFASNSYIEG NIDMIWGSGA GYFLKSTIAP NKDGINLTAD KRSTNTSAAG
FVFDQCTIVP STGAGTMSDI SLGRPWNSLA RVAYVDSYLD SCVTAAGWEQ WSSSTPNTDG
VVFGEYGNYG PGASTAQRAS FATQLDDSGV SQFQLSSFFA VTSWIDFTHV SGTPFVPGIA
ISTSVPVSSA TPTSSAVVTP STVTTTMTVT DKETVYTTLT STDETSTAKY TVTEDVGTTL
TAAESFKTTT QKTTVTDTVI VTEPTVTITK KVVITSDVGL TATPALSTST STVKQTTTLI
ATATQAPSTV TVKSTLTSSV TTTVTAKAVT TTTTAVSTTT ATTTSTPRTV KVTSTVTVTR
GTGGTTTITA KATTSTVSVT STVSKSKTIT TTIDCIPAAE VKRSVIPRAV AAATVTDYTT
LTTTVKMSTV KLPAPTDIIT VVTTKTIGKT TTIPASTSTI TVLSTVTKGT TSTIPAVTSY
VTQTSISTIG KTTTLKASTT TVTVTSLATK TSTITMVGAT QTVTSLKTTT IESTVSLPRS
TLTVTKSTVS TIHSTVTLAT PTSTVVKTTT YSLKPSMTVT SRATSTKITT VKKTVTQTQT
VTKTSKGAGT CPTN
//
