ID I0Z285_COCSC Unreviewed; 890 AA.
AC I0Z285;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:EIE24754.1};
DE Flags: Fragment;
GN ORFNames=COCSUDRAFT_14361 {ECO:0000313|EMBL:EIE24754.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE24754.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE24754.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE24754.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:EIE24754.1}.
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DR EMBL; AGSI01000005; EIE24754.1; -; Genomic_DNA.
DR RefSeq; XP_005649298.1; XM_005649241.1.
DR AlphaFoldDB; I0Z285; -.
DR STRING; 574566.I0Z285; -.
DR MEROPS; M01.005; -.
DR GeneID; 17042755; -.
DR KEGG; csl:COCSUDRAFT_14361; -.
DR eggNOG; KOG1046; Eukaryota.
DR OrthoDB; 745at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EIE24754.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 74..177
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 216..428
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 435..555
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 561..889
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIE24754.1"
SQ SEQUENCE 890 AA; 98442 MW; 1C7FC94B596140E4 CRC64;
QDYRPTPYLI KHVHLDFNLN EDSTRVTSRL SMLPNYGSAA APPSLELDGR KDIKLVAVKV
AGKELQPSEY EIAEKKLTLS KLPKGEFEVE IEENTSLEGL YKSGGNFCTQ CEAEGFRGIS
YFLDRPDVMA KYTTRIEADA KSYPVLLSNG NLLEQGSLEG GRHFAVWEDP FVKPCYLFAL
VAGDLAVRED TYQTMSGRTV TLRIYTRAKD IDRVAWAIES LKRAMKWDED TFGLEYDLDL
FNIVAVDDFN MGAMENKSLN IFNSRLVIAS PATSTDMDYS RVEGVVGHEY FHNWTGNRVT
CRDWFQLTLK EGLTVFRDQE FSADLNSRPV KRIEDVSRLR TAQFVEDAGS MAHPIRPDSY
IKMDNFYTLT VYEKGAEIVR LYQTLLGKDG FRSGMDLYFK RHDGQAVTCD DFRNAMADAN
GQDLSAFAAW YAQAGTPHVK IAASYNAANR TYTVKASQNT PPSPGQSDKG PVPIPVAVGL
LGQDGTELPL TLKVCTTSYL FCFALENRST CSGEPETTKV LLLTEKEQEF VFTEVSENPV
PSLLRDFSAP VKLEVEGQTE DELVFLLAHD KDSFCRWEAG QRLLRGLLSS LYSAGSASKE
SLSAAGGVPE KVVAAIGAVL SDAGLDGAFV AAAISLPAAA ELIGTIPNID PVLLHNVRQY
VAWELAARLR PELEAAIKRN ESAPGASYTP GDSAQRAIKN KALSYLSTLK DPSVTADLLQ
RTRSATNMTD QISALACLVD SESQERETAL AEFYEQWKDD GLVMLKWIAL QAGSNLEGNL
KNVEKLVTHP AFSITNPNAC YSLFLAFLRS PVNFHAADGS GYNFIADSIL KVDKINRQVA
SRMVSSSAFT AWKDYDVERQ HMMKEQLAKI NAENGLSENV FEIVSKSLEG
//
