ID C4Y6M7_CLAL4 Unreviewed; 939 AA.
AC C4Y6M7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=CLUG_03811 {ECO:0000313|EMBL:EEQ39683.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ39683.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ39683.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ39683.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; CH408079; EEQ39683.1; -; Genomic_DNA.
DR RefSeq; XP_002616570.1; XM_002616524.1.
DR AlphaFoldDB; C4Y6M7; -.
DR GeneID; 8496688; -.
DR KEGG; clu:CLUG_03811; -.
DR VEuPathDB; FungiDB:CLUG_03811; -.
DR HOGENOM; CLU_003705_3_0_1; -.
DR InParanoid; C4Y6M7; -.
DR OMA; DMAMENF; -.
DR OrthoDB; 1981312at2759; -.
DR Proteomes; UP000007703; 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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF287; PROTEIN TMA108; 1.
DR Pfam; PF11838; ERAP1_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:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 19..218
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 255..489
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 567..917
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 423
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 939 AA; 106884 MW; 985CCFD5FBC9E595 CRC64;
MSSEAGIASS LVLVNAFLPK SYDLKVSVDH SKPNFSGSVV IPLTKNDQCV EDSSTFSMIL
HAHKLVVMKA TLQMSDVGSI PLKIVTLRDR MMISLSTSEV VMSQITEKAS PTVTISFMGC
INSIKTFNDD TYGVFKTNYS DSIEGKSDNF VIATHCQPFG CRTIFPVIDE LVIKVPIKLT
ITTKSSFKAV SNALLERTTI VDMTENSVFE FKPTPPISPS IFGFVIGDLE CVECLDSSIP
IRAFVTKGDG PLINYALKVA EALLPKFVDT LGVQYPLEKF DIVTLPFLSD GVMENWGMVT
IFRNSVLMDA NNADDSGKFQ VRQLIAHQLT HQWIGNLVTL DDWKYMWLIE AFATWVGNYL
LSLAKIENSD FADYEIDRVI SMESFMDKDC LLQNRIPSLH EHMMKLRLNK DSRTNSIFER
DAYEKGMILV NMIASLFKFE RNEESFKGFF SALKNVLEGC KHQTIKPFEL WQQLNSYLSV
DLLTFVQTWT QYEGYPLVKV KISGDKIKFE QNRFFFNDDV NNVGLENPPF HVPLSLKILT
ETKEVKLVNL ILSDRSMEVD IVPSSLISVN ANKSFYYRTV YDPKFVPIVL KNVASNMLPS
LDLFGIINDY GKILGQPEPS IDAELFGSNQ LMTLLNICDA LACEEWEDDF NVLRCALDYL
EVVNTTFVHF SRYIEFKRWL DKFSLKLFNK LGGWDLVLDS GNEYDVSEYQ VRNMVLQLAS
ASKESQSVCK KIFKSFFNSG VSNKFIPKEL FTSMFNVTMM NANMNEYKQI LNLVKNSNVS
YLKHSNGSIQ DLQTAAVSSL SFTTKPELLS KTLHFVNNNI DSKLIEFALI GFKYHYETVI
KDIIWGWYKV NYDQWVKRSL RKGSDWSKQI GVTVGNITRL VLGEVMQYKH EDAEKFVAQK
SKELPPHQLS ERWEAVEEEN AERRAIASYY EDVVAQFSM
//
