ID E3LMK4_CAERE Unreviewed; 1016 AA.
AC E3LMK4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=CRE-CCPP-1 protein {ECO:0000313|EMBL:EFP03091.1};
GN Name=Cre-ccpp-1 {ECO:0000313|EMBL:EFP03091.1};
GN ORFNames=CRE_28464 {ECO:0000313|EMBL:EFP03091.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; DS268411; EFP03091.1; -; Genomic_DNA.
DR RefSeq; XP_003114956.1; XM_003114908.1.
DR AlphaFoldDB; E3LMK4; -.
DR STRING; 31234.E3LMK4; -.
DR MEROPS; M14.A36; -.
DR EnsemblMetazoa; CRE28464.1; CRE28464.1; WBGene00056271.
DR eggNOG; KOG3641; Eukaryota.
DR HOGENOM; CLU_297036_0_0_1; -.
DR InParanoid; E3LMK4; -.
DR OMA; FCGFHKG; -.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0018991; P:egg-laying behavior; IEA:EnsemblMetazoa.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF11; CYTOSOLIC CARBOXYPEPTIDASE 1; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 732..958
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
FT REGION 388..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 116624 MW; D89AF33BF4E999CF CRC64;
MPADAEKISQ TRQTWSHLTV EISNFLAEQP QSRVADTLLQ VYNRVWTEEE KQELIEAFGH
KKRFNLTKSG VKAVLFAFEG DRTQSEIIFL CRLLDLIFSF FSTENDRKKE KYVIKCDAVA
TLCRTTRKRI ILTADATDES TIDQNLDEIL WKLLYSIGLK DSRVSLKVRM GGLITPMCKL
FIRKDNLPEA FIPFFIKISR SPRNGQAIGR HEGFMTRLVA KIKVMDASDQ TSQVLLLDKH
LQLLFFTLKN KRTRTQLLRE NICKYLLEVL RRHLASSSNS RPTRLLSSLF GTFDKSLSAA
HTEVVIGTIA ILRFLSNFKK ARDELKNLQV LDICSRELKE FWSDEWKTGP KARIVDSLSA
LCLRCMSPLP YPLETRRFPV DFPLPTAAPS TPGGHGRVRN SSSINISFDN GRSSDEDGMD
EEDEAFVRDD DDDGKEGVAS DEDDGKDDDE TGGALPKTTR LNQQQLSKYA PFFVENEQGT
LQPTFSMMYQ TNQESWRTTC EKTRHIMPVH HHLPIEMFNT PTRVRERTAK TTNNMKKMII
EELDKPERAT NNQVVYDLDT AAFDGLSAPE LPFPTSGVKL DTSKDLQFDS RFESGNLRMV
MQVSVAPTHY ELFLSPDVNQ FRDHYQWFFF QVSNMRKSVK YTFEIVNCLK ATSLYSQGMQ
PVMYSMMESA NGWRRAGENV CYFRNLYINE HEEKRNVEEQ KKKKYYYSIR FNVTFQNTGD
ICYIAYHYPY TYSFLNSSLT MLRKRKQEGV YCREDVIGHS LAGNPIKMLT ITTPATAAEI
AVREVIVLSA RVHPGETNAS WIMQGILENL LCRQSNEMYR LRETFVFKII PMINPDGVIN
GSHRCSLAGI DLNRVWDRPN EALHPEIVAT KAVIQYLCDV VNKKPFVYVD IHGHSKKWDY
FVYGNNAADS WRADDILDVG PAQIEEEQHL ALPRALEVTC PGRFNASECR FNISRAKESS
ARVNVWRQFG IATSYTLEST FCGFHKGQNS GYQINTSDLK EIGRDLLHSF LEMIKN
//