ID B8A371_MAIZE Unreviewed; 557 AA.
AC B8A371;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 22-FEB-2023, entry version 73.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACL54620.1};
RN [1] {ECO:0000313|EMBL:ACL54620.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACL54620.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; BT056013; ACL54620.1; -; mRNA.
DR RefSeq; NP_001146721.1; NM_001153249.1.
DR AlphaFoldDB; B8A371; -.
DR MEROPS; A01.A25; -.
DR GeneID; 100280323; -.
DR KEGG; zma:100280323; -.
DR OrthoDB; 335768at2759; -.
DR ExpressionAtlas; B8A371; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05475; nucellin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033823; Nucellin.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683:SF316; ASPARTYL PROTEASE APCB1; 1.
DR PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..540
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 557 AA; 61731 MW; 238BB3602131B003 CRC64;
MAPPRPPPNP AGEQQPQLHG VVIITLPPAD QPSKGKTVTA FAYTNDPPPP RSPPDPVMGY
PAATEARRRP RRALSTRRVA TAALVLGALA VAAYYCFYSD VAVQFLGMEQ EEEQRNETRS
FLLPLYPKAR QGRALREFGD VKLAARRVDD GGRKARNRME VAKAATARTN STALLPIKGN
VFPDGQYYTS IFIGNPPRPY FLDVDTGSDL TWIQCDAPCT NFAKGPHPLY KPAKEKIVPP
RDLLCQELQG NQNYCETCKQ CDYEIEYADQ SSSMGVLARD DMHMIATNGG REKLDFVFGC
AYDQQGQLLS SPAKTDGILG LSSAAISFPS QLASHGIIAN VFGHCITREQ GGGGYMFLGD
DYVPRWGVTW TSIRSGPDNL YHTQAHHVKY GDQQLRRPEQ AGSTVQVIFD SGSSYTYLPN
EIYENLVAAI KYASPGFVQD TSDRTLPLCW KADFPVRYLE DVKQFFEPLN LHFGKKWLFM
SKTFTISPED YLIISDKGNV CLGLLNGTEI NHGSTIIVGD VSLRGKLVVY DNQRKQIGWA
DSDCTKPQSQ KGFPFFL
//
