ID A0A0S3RZN1_PHAAN Unreviewed; 1113 AA.
AC A0A0S3RZN1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN Name=Vigan.04G365700 {ECO:0000313|EMBL:BAT86044.1};
GN ORFNames=VIGAN_04365700 {ECO:0000313|EMBL:BAT86044.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT86044.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT86044.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; AP015037; BAT86044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RZN1; -.
DR Proteomes; UP000291084; Chromosome 4.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR025926; PDZ-like_dom.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR46366:SF1; PDZ DOMAIN-CONTAINING PROTEIN C1685.05; 1.
DR PANTHER; PTHR46366; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR Pfam; PF12812; PDZ_1; 2.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 269..333
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 1113 AA; 122465 MW; 5BA08B1E543D963F CRC64;
MGDQEERLGS EGLDSGAVVK TDDLCMEIDP PFQENIATAE DWRKALNRVV PAVVVLRTTA
TRSFDTESAA ASYATGFIVD KSRGIILTNR HVVKPGPVVA EAMFLNREEV PVHPIYRDPV
HDFGFFRYDP GAIQFLNYEE IPLAPEAACV GLEIRVVGND SGEKVSILAG TLARLDRDAP
HYKKDGYNDF NTFYMQAASG TKGGSSGSPV IDWQGRAVAL NAGSKSSSAS AFFLPLERVV
RALRFIQKGS ETYVDKWQAV SIPRGTLQVT FLHKGFDETR RLGLKTETEQ IVRQASPAGE
TGMLVVESVV PGGPGYKHLE PGDVLVRVNG EVITQFLKLE TLVDDSVSKN IELQIERGGT
SKSLTLLVQD LHSITPDYFL EVSGAVIHPL SYQQARNFRF HCGLVYVAEP GYMLFRAGVP
RHAIIKKFAG EEISYLEELI TVISKLSRGA RVPLEYISYM DRHRRKSVLV TVDRHEWYAP
PQIYTRDNST GLWIAKPALQ RDSPFLSSGA KDVENMSRQP ISLTGEHTCE GHVCEGNNQD
FVDGVTNMET NCEDPSECAS HQNASDGVLK KRRVEEDLSA DGSVVADLSQ NGTRETKLEK
SSVTQDDMLM DFQGATAAAA NASVAERVIE PTLVMFEVHV PPSCMLDGVH SQHFFGTGVI
IYHSKDMGLV VVDKNTVAIS ASDVMLSFAA FPVEIPGEVV FLHPVHNYAL ISYDPSALGP
VGGSVVRAAE LLPEPALRRG DSVYLVGLSR SLQATSRKSV VTNPCAALNI GSADSPRYRA
TNMEVIELDT DFGSTFSGVI ADEQGRVQAI WGSFSTQLKF GCSTSEDHQF VRGIPIYAIS
QVLHKIVSGA NGPPLLINGV KRPMPLLRIL EVELYPTLLS KARSFGLSDD WIQALVKKDP
VRRQVLRVKG CLAGSKAENL LEQGDMVLAI NKEPVTCFRD IENACQDLDK SNANDGKLHL
TIFRQGQEVE LLVGTNIRDG NGTARAINWC GCIVQDPHPA VRALGFLPEE GHGVYVARWC
HGSPVHRYGL YALQWIVEIN GKPTPNLDAF VDVTKELEHG EFVRVRTIHL NGKPRVLTLK
QDLHYWPTWE LRFDPNSAMW HRNIIKGLNC STV
//
