ID A0A5A7VHS8_CUCME Unreviewed; 906 AA.
AC A0A5A7VHS8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=folate gamma-glutamyl hydrolase {ECO:0000256|PROSITE-ProRule:PRU00607};
DE EC=3.4.19.9 {ECO:0000256|PROSITE-ProRule:PRU00607};
GN ORFNames=E5676_scaffold384G00920 {ECO:0000313|EMBL:TYK27907.1},
GN E6C27_scaffold271G00990 {ECO:0000313|EMBL:KAA0066760.1};
OS Cucumis melo var. makuwa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=1194695 {ECO:0000313|EMBL:KAA0066760.1, ECO:0000313|Proteomes:UP000321393};
RN [1] {ECO:0000313|EMBL:KAA0066760.1, ECO:0000313|Proteomes:UP000321947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chang Bougi {ECO:0000313|Proteomes:UP000321947};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAA0066760.1};
RA Kwon S.-Y.;
RT "Draft genome sequences of two oriental melons (Cucumis melo L. var
RT makuwa).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate;
CC Xref=Rhea:RHEA:56784, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:141005;
CC EC=3.4.19.9; Evidence={ECO:0000256|PROSITE-ProRule:PRU00607};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family.
CC {ECO:0000256|ARBA:ARBA00011083}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0066760.1}.
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DR EMBL; SSTE01000806; KAA0066760.1; -; Genomic_DNA.
DR EMBL; SSTD01002424; TYK27907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A7VHS8; -.
DR STRING; 1194695.A0A5A7VHS8; -.
DR Proteomes; UP000321393; Unassembled WGS sequence.
DR Proteomes; UP000321947; Unassembled WGS sequence.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.1030.20; DNA polymerase delta, p66 (Cdc27) subunit, wHTH domain; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR015527; Pept_C26_g-glut_hydrolase.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR019038; POLD3.
DR InterPro; IPR041913; POLD3_sf.
DR PANTHER; PTHR17598; DNA POLYMERASE DELTA SUBUNIT 3; 1.
DR PANTHER; PTHR17598:SF13; DNA POLYMERASE DELTA SUBUNIT 3; 1.
DR Pfam; PF09507; CDC27; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51275; PEPTIDASE_C26_GGH; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00607}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000321393};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT REGION 551..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 906 AA; 100349 MW; B1C91DB63534DF03 CRC64;
MFKKVVGFKP TISEHPFSPA SVSLFKYTWV FFLIIISLKF SLVHAVHPYP NIILPSQSVL
DSSPSCTAMD PTLNYRPVIG ILSHPGDGAS GRLSNATNAS YIAASYVKFV ESAGARVIPL
IYNEPLEVIF EKLSLVNGVL FTGGWAKKGL YYLVAEKIFK KMLERNDAGD RFPLYGVCLG
FEILSMIISK NRNILEPFNA SYMASTLQFV DNVNIQGTVF QRFPHYLLEK LSTDCIVFQN
HLYGISPERF AHNEELSRFF QILTTSSDKD NKVYVSSVQA WDYPVTAFQW HPEKNAFEWG
YSVIPHTEHA IEVTQHVANY LVSEARKSSN RPPAQKVIEN LIYNYSPTFG GKAGVSSGGG
KIVDILLSIS RFVFPFSFSV SLPISTQMAE IETLGILQDI ESLVADKLQV VSYKWLSRSY
LISSDTAKRL LKEFVEKHES GLQVVYALSG WLKKDPPSYH IRLVSGSKLP EAKQDFDGTC
SIQVYSVQAS IPKDPAALWN AEFVQAEELF KQPFTVDNCL RDNRFCGISN SYVKRNIDEI
PASIAASIPK SAVDTESSKK MTSYQNTTVP QPEKSEMQKV STNVGLQSST VVKEVKSEGN
HTDHQASKPI AVKEKVASLP ANKKKAQGDK TCSSTGGLAN LWGRVPIKSK LGDDHADVNR
ATAANPSVSS AEAQICAHEA LQIENSDDDD QDVNIKRSSN ESGRKRRVVF DFSDDEEFED
AVSLASPENP KEQSCLDLKQ HTELPKEKAH LNNDEQLNGK LKIKEEKTSE LEQSSVEEKQ
RNCSTEKNEV CAHENDSIKG EKPVDATPAS PKRRKVLRTR IDERGREVNE VVWEGEEQKQ
KKDDVSSAKI SDQKAVETTT NRPPAAKKSP ALGNGGANPA VKAGAKKTGN AAGPKQGNIL
SFFKRV
//
