ID Q7SEJ5_NEUCR Unreviewed; 957 AA.
AC Q7SEJ5;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 2.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=NCU09728 {ECO:0000313|EMBL:EAA35194.2};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA35194.2, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA35194.2, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CM002239; EAA35194.2; -; Genomic_DNA.
DR RefSeq; XP_964430.2; XM_959337.2.
DR AlphaFoldDB; Q7SEJ5; -.
DR STRING; 367110.Q7SEJ5; -.
DR PaxDb; 5141-EFNCRP00000009476; -.
DR EnsemblFungi; EAA35194; EAA35194; NCU09728.
DR GeneID; 3880592; -.
DR KEGG; ncr:NCU09728; -.
DR VEuPathDB; FungiDB:NCU09728; -.
DR HOGENOM; CLU_009988_1_0_1; -.
DR InParanoid; Q7SEJ5; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..957
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004292852"
FT DOMAIN 54..442
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 638..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 104262 MW; 1D6E413476D318E6 CRC64;
MRLPYLSFAV ISTRFLLLSS VPSLVRAGTT ATSPPEPVWV QPSGEWYGID GTWSNFMFAV
GSPAQIVYLT PATALSETWV IGAGGCTSGP GNLPCVDARG GVFDYHISET WQTLGTGAYE
LGMNHTGVQR NGDYGLDTVA FVDTMASSAT SVDGVLIAAV NATEYYQGYI GLGVTQGSIG
SNVTKPLIPQ LVEVNGMIPS HSYGYTAGAY YRDTTTKGTY ASLTFGGYDA LRFVPHDTTF
RLYIGNSTAD SNDRAPTVRL RGLTAQVPSL DKAPGNWTST SQTLVAMNDS ITAMIDSSTP
FLWLPTDICE RIASILDLVW RADLGVYVFA NGGEQYLRYK RMKSIDDLSF TFTVSSYDNS
DNFGYPLNMP GVVNITIPPA AFAQVLRYPW KNIIKFNESS IPYFPLTRST NETNNNQYII
GRVFMQEAYI ITKYDKAAFS IHQALFPDNS ATNHSLQAIE RPPNSPYPEG PPVKKVAKKP
LGVGQTVAIV VSAFAAGSVI GLISFLCCRR GSKVKKNEAR KLEHNSEEVT PIHDEPPQNT
VSRMLSMFVG RRRSRKQSSP KTQAIMTEPV EVGADAHHQV FELPVPPEPI ELDNNDIGHN
DPYLGLDGSR VTSDYEAARQ KLECQLQGSV PTYTRTTEHN ERAAGYPLEK SAQDVTPVHY
RPSEETSSGS SPTYANTDSL SNSLPSPLSP YADWAAGRVF DLPSPITVAS PVRLRNFPTT
TGSDDPAPAH SPVSLHSPYS PHTYLPSPVS PSFDFNGGPE SPTSPTGKPA PLPGSAAIQR
TPIDPIHTQI VCLGPMPENV RLPIPHHLHH HPTVTRIIMP DGLLHPAEQN DQLAGNTDVD
VDGLRRRSDS ITRGSNETLG SNFTMEEESQ LRQVQMAAQR SAAAQEQALP MSPTSHQPPP
PPPPPPPQRR EHEADNTTSL IDKYPRSPRS MERIEAGSEL IHVPQVAAQR YSWEAET
//