ID A0A1A6A6W0_9TREE Unreviewed; 920 AA.
AC A0A1A6A6W0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=I303_03508 {ECO:0000313|EMBL:OBR85795.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR85795.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR85795.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR85795.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI894030; OBR85795.1; -; Genomic_DNA.
DR RefSeq; XP_018263637.1; XM_018406829.1.
DR AlphaFoldDB; A0A1A6A6W0; -.
DR STRING; 1296121.A0A1A6A6W0; -.
DR GeneID; 28967207; -.
DR VEuPathDB; FungiDB:I303_03508; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000078595; 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:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438,
KW 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:UP000078595};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 26..204
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 284..502
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 581..898
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 197..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 443
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 920 AA; 102244 MW; FF4CB9F8927F4A3D CRC64;
MSNTASGGAS SAPDAEGHRL PTNVYPSLYE LAIKTDLVAS PPTFSGEGII HLDIKEDSSS
IKFHSHKTVT ITHIAISTSD LKTTSNLNLP LSALTLNNEN EVATLDLSSL PGGGLKEGQK
NTKLFVRWEA ELKSAMHGYY RSEGDADENG KKPIYGLTQF EATEARKAFP AWDEPLVKSK
FAISMIAREK NTSLSNMPQI SEKPWKAPSN ASIDNGKTEG KTESNEEGWK ITKYETSPLM
STYLVAFASG GFASLESAHH SKLTGKTVPL KIYATKDQIK QAQFALDIKK WALPVYEEIF
DIPYALPKLD TLVAHDFDAG AMENWGLITG RTTAYLYDPE KSPLSAKKRV AVVQCHELAH
MWFGDIVTMK WWDNLWLNEA FATLMGELVI LDRIWPEWKP RSQFLKSHLQ GALDLDSQRS
SHPIEVDCPD SNQIAQIFDA ISYSKGASVL RMLASVVGEP TFLKGVSIYL KKHIYSNAET
KDLWDGISEA SGLDVAKIMK NWTLKIGYPV IKVEESGDGK IKLTQNRFLS TGDVKPEEDE
TIWYVPLEVA TLGSDGKVSV DHKATLEERS STYDLKGSDS FKLNADTVGV YRVSYEPSRL
VKLGKEASKF TIEDRVGLVS DAANLARAGY AKTSGSLSLI NEIAKGGEDE FLPWSQMNSA
LAKLSGVWWE QSEAVRSAIS KLRIDLLKPQ VERLGFDGSK DEAPEVKELR ELVIGAAAAS
GDEAVLKEIK ERFAPFLASG DDSKIPPDLQ RIIFTYSVEH GGVAEYEKML SVYNKAPNPS
TKVDAMYALT SPKDQGLLDR TFKMLNDGSV KDQDLYIFFF GLTANKYARR RLAEFFVSDF
DVLMKRYPDG YGVNYLVKGA FQSLSSHEDL KMVQDFFKDK DIRKYKSAVA QSCDSIQAAA
DWLQRDSEDV EKWLKENKYL
//
