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Multifunctional fusion protein [Includes: Methionine aminopeptidase (EC 3.4.11.18); Patatin (EC 3.1.1.-)]

 A0A1R3GF21_COCAP        Unreviewed;       726 AA.
A0A1R3GF21;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
20-JUN-2018, entry version 12.
RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU003653, ECO:0000256|RuleBase:RU361262};
Includes:
RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
Includes:
RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
ORFNames=CCACVL1_26346 {ECO:0000313|EMBL:OMO56685.1};
Corchorus capsularis (Jute).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Malvales; Malvaceae; Grewioideae;
Apeibeae; Corchorus.
NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO56685.1, ECO:0000313|Proteomes:UP000188268};
[1] {ECO:0000313|EMBL:OMO56685.1, ECO:0000313|Proteomes:UP000188268}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
TISSUE=Whole seedling {ECO:0000313|EMBL:OMO56685.1};
Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
"Corchorus capsularis genome sequencing.";
Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Lipolytic acyl hydrolase (LAH).
{ECO:0000256|RuleBase:RU361262}.
-!- FUNCTION: Removes the N-terminal methionine from nascent proteins.
The N-terminal methionine is often cleaved when the second residue
in the primary sequence is small and uncharged (Met-Ala-, Cys,
Gly, Pro, Ser, Thr, or Val). {ECO:0000256|RuleBase:RU003653}.
-!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
preferentially methionine, from peptides and arylamides.
{ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Note=Binds 2 divalent metal cations per subunit. Has a high-
affinity and a low affinity metal-binding site. The true nature of
the physiological cofactor is under debate. The enzyme is active
with cobalt, zinc, manganese or divalent iron ions. Most likely,
methionine aminopeptidases function as mononuclear Fe(2+)-
metalloproteases under physiological conditions, and the
catalytically relevant metal-binding site has been assigned to the
histidine-containing high-affinity site. {ECO:0000256|HAMAP-
Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
-!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
motif define the oxyanion hole, and stabilize the oxyanion that
forms during the nucleophilic attack by the catalytic serine
during substrate cleavage. {ECO:0000256|RuleBase:RU361262}.
-!- SIMILARITY: Belongs to the patatin family.
{ECO:0000256|RuleBase:RU361262}.
-!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-
Rule:MF_03174}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03174}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OMO56685.1}.
-----------------------------------------------------------------------
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EMBL; AWWV01014468; OMO56685.1; -; Genomic_DNA.
EnsemblPlants; OMO56685; OMO56685; CCACVL1_26346.
Gramene; OMO56685; OMO56685; CCACVL1_26346.
Proteomes; UP000188268; Unassembled WGS sequence.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
CDD; cd01086; MetAP1; 1.
HAMAP; MF_01974; MetAP_1; 1.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR036005; Creatinase/aminopeptidase-like.
InterPro; IPR000994; Pept_M24.
InterPro; IPR001714; Pept_M24_MAP.
InterPro; IPR002467; Pept_M24A_MAP1.
InterPro; IPR002641; PNPLA_dom.
Pfam; PF01734; Patatin; 1.
Pfam; PF00557; Peptidase_M24; 1.
PRINTS; PR00599; MAPEPTIDASE.
SUPFAM; SSF52151; SSF52151; 1.
SUPFAM; SSF55920; SSF55920; 1.
TIGRFAMs; TIGR00500; met_pdase_I; 1.
PROSITE; PS00680; MAP_1; 1.
PROSITE; PS51635; PNPLA; 1.
3: Inferred from homology;
Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Complete proteome {ECO:0000313|Proteomes:UP000188268};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161,
ECO:0000256|RuleBase:RU361262};
Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU01161,
ECO:0000256|RuleBase:RU361262};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Protease {ECO:0000256|HAMAP-Rule:MF_03174,
ECO:0000256|RuleBase:RU003653};
Reference proteome {ECO:0000313|Proteomes:UP000188268}.
DOMAIN 345 549 PNPLA. {ECO:0000259|PROSITE:PS51635}.
MOTIF 349 354 GXGXXG. {ECO:0000256|PROSITE-
ProRule:PRU01161}.
MOTIF 387 391 GXSXG. {ECO:0000256|PROSITE-
ProRule:PRU01161}.
MOTIF 536 538 DGA/G. {ECO:0000256|PROSITE-
ProRule:PRU01161}.
ACT_SITE 389 389 Nucleophile. {ECO:0000256|PROSITE-
ProRule:PRU01161}.
ACT_SITE 536 536 Proton acceptor. {ECO:0000256|PROSITE-
ProRule:PRU01161}.
BINDING 181 181 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03174}.
BINDING 279 279 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03174}.
SEQUENCE 726 AA; 80625 MW; 310971A855832661 CRC64;
MVGASSFQPR IISSFVGDRL VQSKQPLSQL FGYHPGCKHV SMQLPRRLSG LTNLLFNRRS
DLEEVPNSQR KRLRPGKISP RRPVPNHIQR PPYVKTRMAP GIASGPEVHD LKGIECMRAS
GRLAAQVLNY AGTLVKPGIT TDEIDQAVHQ MIIDNGAYPS PLGYGGFPKS VCTSVNECIC
HGIPDSRPLE DGDIINIDVT VYLNGYHGDT SATFFCGDVD EEARNLVKVT KECLDKAISI
CRPGVEFKKI GKTIHDHADK FRYGVVRQFV GHGIGRVFHA DPVVLHFRNN DGGRMVLNQT
FTIEPMLTIG SINSVMWDDN WTVVTKDGSL LGVLPSSYGQ RITVLSIDGG GIRGIIPATI
LSYLELKLQE LDGENARIAD YFDVIAGTST GGLITAMLTT PDENGRPLYM GKDIAPFYLK
HCPNIFPRSN YRRMIMKIIT LIRPKYNGKY LRKIICKVLG NRRLHETLTR VVIPTFDIKL
LQPTVFSTFE AKIDTSKDAL LSDICISTSS APTYFPAYRF KTKDSEGNDR EFHLVDGGIA
ANNPALLALK PTGTAFPGDQ EGSLGRALNY ENYLIISLGT GTSKMEKKYN AKMAAKWGIL
GWLYREGSSP LVDAFTSAGA DMVDLHMSLI FRSINCEQNY LRIQDDRLSG DASSTDKATQ
KNMKNLVEIG ERLLQKPVSR MNLDSGIFEP FEKEGTNQEA LSRFAKLLSE ERKLRWAEIE
KQLGNN


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