ID A0A0B7NQV0_9FUNG Unreviewed; 1205 AA.
AC A0A0B7NQV0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN Name=PARPA_12180.1 scaffold 44939 {ECO:0000313|EMBL:CEP17880.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP17880.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP17880.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP17880.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
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DR EMBL; LN733737; CEP17880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NQV0; -.
DR STRING; 35722.A0A0B7NQV0; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd12189; LKR_SDH_like; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 933..1147
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 1205 AA; 134755 MW; F8BBA8D64B1F90D8 CRC64;
MIRLKNCKSK ILPRYYTTSN QSSVGIRREN KSRWERRSAL TPSTVKRLIQ ETGTKVYVQP
STKRIFTNED YKKAGAIITE DISKADIILG IKEVPESSLL KDKTYLFFSH THKGNEKNMP
MLQNILDKKI RLIDYELMKD ETGKRLVAFG QFAGNAGMID IFHGMGHRFL GLGYSTPFMY
TSMAHAYPTI AEAKSALHRM GDVITENGTP KDFGPLVYAF TGSGNVAQGA MEIFKEVPHE
FVPAEDLAKL VNDKNPRLGR LYATHLQVKD YIELKDGGGK MIDYEDYLAN PERYQSNFHH
KIAPYTNCVV TGAYWDKNYP RLMTNKQLAD FEKLKKKGLI NKGKMMSLAD IVCDVKGAFE
CLSHSTNVED GFFYYDAIRD IEHKDAEGEG IQIMGIDILP AELPVESSEF FSKALYPYIK
EMVQSSPNTP LDKLPPLLRQ ATIADQGKLT EPHKGLLSSR AATHNNKKTV LLLGSGMVAA
PLVEHLAKRP DVNVVVASNM ADEANALVRN YTNAESAPLD ISDRLELSRL VSKADVVVSL
VPAFLHTQVA NVCIEQRKDM VTASYVSKEM EQLENKAQKA GILIMNEVGL DPGIDHMSAM
KIIDEAHRNG SKIKSFISWC GGLPSPEASN VPLGYKFSWS PRGVLTASGN DAVYWNDAKK
HTISGENLLK EHFPVVQTPY AGFVFEGLAN RNSLGYADIY GLGDLSQMDT MFRGTLRYQG
YSDLLYAFRK LGFLDQERPI AGQCQSWSKY FDFVLSGKSS NLSQDERHQR MVDRLGLPRD
HFMIEKTWSA ISYFLSANDQ EKIHAPNGSA LDLFTILLSR RLKYDKGERD MVAMHHEFGV
QHRSGKKETL TSTLIKYGNQ THTAMADTVG LPTAMAVDLV LDNKIPERGV QRPTKPHVYL
PILDQLEMKG IKFVEKSEPY KFNRLDATGS NSCKMDEMPV INQNRYTVAY GNKNATRQSY
AAIRQAIIHP LYVSSQQRQA QVYATAHTDE IPYDIGLIKL TTPLVPNKFI NRIPLLVNQT
TSMDILETIG MGYTGYQKPQ AEILQFAQCN STNAETLRDN NYNQSIILAT SNAGLCHGDS
GSPLLVKSSS NVDAEYYLGG ILNRILNAYD PDPENGSCPL HESNLTSFIN SFVRPSAHLK
WITSVTKLPL DALMDPMTSA DGTRMFVAPT SSAITDTSFL LRASCFGIDW PIFLLMASLF
TFIYF
//
