ID W9R9Z1_9ROSA Unreviewed; 1102 AA.
AC W9R9Z1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Putative zinc protease pqqL {ECO:0000313|EMBL:EXB64100.1};
GN ORFNames=L484_013111 {ECO:0000313|EMBL:EXB64100.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB64100.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; KE344494; EXB64100.1; -; Genomic_DNA.
DR RefSeq; XP_010096429.1; XM_010098127.1.
DR AlphaFoldDB; W9R9Z1; -.
DR STRING; 981085.W9R9Z1; -.
DR MEROPS; M16.004; -.
DR eggNOG; KOG0959; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF33; STROMAL PROCESSING PEPTIDASE, CHLOROPLASTIC; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EXB64100.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 192..323
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 338..407
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 856..1005
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 124043 MW; 98FBE05C50D9C89D CRC64;
MNKLKGKANP DDYYYSSDNS DYNSGNSTSS NNTSGNYTSG KTPAPAATTP AAATTPAATT
PAATTPITIA TTAARSRRRC CVLLLRSHSH PHLSVSHGSP CRRLSPQSSP LARPPLALLW
FLGFLSAALS LTVKEALAGG RRSVDLLSPP RARTSASAKL RRGLAFVSPL SICIKLGRLP
IADCFSTCSF EAHLEVHVGP VHEEDDEQGL AHMTEHVLLD CDSFFQLPGP DSGKAAYTSF
NQTVYHITSQ TILEHFNEDL PDEDLVPYVL NYLNEIAFKP KIRASYLEKQ RDIVLSELQM
GDAIDHRIEL QLYQHMHSEN KLSKRCNILG LEEQIKKWNV AQIKKFHNRW YFPGNATLYI
VGDINDVSKT IDAIQAAFGK SNKRSSAMLK NRRPDHPIRP LLTIYHNWSL PKCNIDDQRP
PVQIFQHNLI HNFSFHICSK IPLNKLKTYG DLRNFVMKQI YLSILDFRIN AKYESSNSSS
RIMELNHWDF GQFGCACTSL AMASEPRDWE TTIKMAFHEV RRLKELGINY EELTIHKDAI
VKDNTILRRV LDNTSSHDAV KFIMYNDTLG HTTMEQREAD ESLAAVATTI TLEEVNSIGA
QLLEFVSDFG KPSAPVPTTI MACAPSTCEV NGELIKFTIN RSEIEFAMKQ GLEEVVHAEP
EIEIPTELIS SSELQELWLE RQPTFIPPIS SKPNVMKLHD KGTDTTQLRL SNGISVNYKI
SKNEGEEGVI RVIIDGGRAR ESSDLKGAIV VGVQTLFEGG CVGNFTKEQS TEEFISVELS
FTTRENGMQA AFQLLHMLLE QSVWLEDAFD RARQLHFSKF QSNLKSLEQS TTRKMMLDML
GGDERFVKPT QISLQNLTLQ SVKDAVLNQF RGNNMEVSIV GDFCEEDIDS FIIHYLGTVK
ATRNFKIEVP QYNPIKYGAS TSHMQSQSQV YLKDTKERSY ACVAGLTPNM WGFTIDGKHY
LKSKFIEGPS LHNKLRGHPL FFGITMEYLT YILDSIIGAN INASSLSYEA TFNTRLFDKL
NLGWYMISIT STPSKDFSMV RRVMLSRHED EIKSNAYWLN LLCHMQPSSL PRKDISCFKD
LASLYEVVNM EDIFFCIRSV KS
//