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Database: UniProt
Entry: A0A1R2CN61_9CILI
LinkDB: A0A1R2CN61_9CILI
Original site: A0A1R2CN61_9CILI 
ID   A0A1R2CN61_9CILI        Unreviewed;       448 AA.
AC   A0A1R2CN61;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Methionine aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE            Short=MAP 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE            Short=MetAP 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_03175};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_03175};
GN   ORFNames=SteCoe_7155 {ECO:0000313|EMBL:OMJ90457.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ90457.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ90457.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ90457.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC       nascent proteins. The N-terminal methionine is often cleaved when the
CC       second residue in the primary sequence is small and uncharged (Met-
CC       Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000256|HAMAP-
CC       Rule:MF_03175, ECO:0000256|RuleBase:RU003653}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000294, ECO:0000256|HAMAP-
CC         Rule:MF_03175, ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC       and a low affinity metal-binding site. The true nature of the
CC       physiological cofactor is under debate. The enzyme is active with
CC       cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC       aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC       physiological conditions, and the catalytically relevant metal-binding
CC       site has been assigned to the histidine-containing high-affinity site.
CC       {ECO:0000256|HAMAP-Rule:MF_03175};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase eukaryotic type 2 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03175}.
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:OMJ90457.1}.
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DR   EMBL; MPUH01000102; OMJ90457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CN61; -.
DR   OrthoDB; 5473250at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01088; MetAP2; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_03175; MetAP_2_euk; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002468; Pept_M24A_MAP2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00501; met_pdase_II; 1.
DR   PANTHER; PTHR45777; METHIONINE AMINOPEPTIDASE 2; 1.
DR   PANTHER; PTHR45777:SF2; METHIONINE AMINOPEPTIDASE 2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW   Rule:MF_03175}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03175};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03175,
KW   ECO:0000256|RuleBase:RU003653};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT   DOMAIN          136..335
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         230
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         230
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         299
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         332
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         429
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         429
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
SQ   SEQUENCE   448 AA;  50602 MW;  CF9011205A63436A CRC64;
     METEELKSEP LVEKPIAEET KDTSQAKKKK KKRNKKKKPA EPSIAQPTNS IPNPPVKSSQ
     MSPSFFNKFQ DNSHLRRVKN WNEDPTYKQT NPPSVPLSQQ FAQGNFPHGE EVNYTSRITS
     QEHRERERIS NYDYDAMRKA AECHRQIRRW AQGVLKPGVE LHDFVEELEN YSRTLLEADG
     IEGGVGFPTG VSLNFCAAHY TPNPGDKVYL TEDDLCKLDF GTHIGGRIID CAFTVAFNPK
     FDNLIQASQE ATNTGLREAG IDARFSEIGA AIQEAMESFE VELDGKVYKV KSIRNLNGHL
     IGPYHIHAGK SVPITKNNDP GRMEEGEVYA IETFGSTGKG VVHDDMECSH HMIDFDMFQK
     PVPIRDPKAR ALLKHIEKKY GTLPWSRRQL TRDGEIKHLM PLKSLINSGI VVPYPPLCDV
     RGSFVSQMEH TVLLRPTCKE IISRGDDF
//
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