ID H2B0U0_KAZAF Unreviewed; 902 AA.
AC H2B0U0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=KAFR0J01760 {ECO:0000313|EMBL:CCF60240.1};
GN ORFNames=KAFR_0J01760 {ECO:0000313|EMBL:CCF60240.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF60240.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF60240.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650830; CCF60240.1; -; Genomic_DNA.
DR RefSeq; XP_003959375.1; XM_003959326.1.
DR AlphaFoldDB; H2B0U0; -.
DR STRING; 1071382.H2B0U0; -.
DR GeneID; 13883890; -.
DR KEGG; kaf:KAFR_0J01760; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_3_0_1; -.
DR InParanoid; H2B0U0; -.
DR OrthoDB; 1981312at2759; -.
DR Proteomes; UP000005220; Chromosome 10.
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; 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:UP000005220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 11..205
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 250..482
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 558..872
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 417
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 902 AA; 102349 MW; EB7DE6CAFC5C1BC8 CRC64;
MLLLALDNPG KPVNYKLELD IDPESSDFSG SVDITFHIEK GTIFNEVKLH AGDLSIVSAS
ITNENSTYEA KLDVSYDTTQ QLAIFRNHGG NTLSLTECQI YRLKLGYTGK INDIASPGDK
TVGVFKARHP DNKGYIIATH CQPSFARLIY PCVDEPSVKT TFELSIISSA TMKAVSAASI
DVIEDIGSGK VKTIFRKTPL LTTSLFGFTL GAFDTIKIEI PITQIVEGNE EQQFFPVIMN
SPMNVSLTSF AIETVKTYLP ILVKYFNNFI PYLEKLDFVL LPYLNDMVME NFGMITAHMN
LLLLADDKNV ALKKQMVQII VHELVHQWVG NFISFDSWES LSFNESFATW LSYYLISENE
EDYFTSNDYV YGEIQPAMVH DSGLNSQSIR DSYYSIMKQL DGKGSGTTRE LFNPYSYFKG
VSVLRSLQLT TGESLLQKAL AHLFTTENIP RFHNMSIKPI DIFNEVGAML KSENIANYFS
SWNRLPGLPI LSVTATEDEK TKLVQHRFFS KECGEVNETD FEDVPYHIPL FTLLPDGKND
TKHVLLTDRS LKLDYRILLC NNDAQGYYYV SYESDSLYAG ICQGLQNKTI SSFNLSKIVE
DLSNFIGNLN HQLPIHFTGF FKILNSFISS FESIDEMVKS NYSIPFLKCL AVLETLEVAV
YKSKRTELRD QIHKFGTKMF KSFIINKIDL REVPSDQTTI VSKIIRLTRK NQKTINICEP
IYKSLLKNVS STNKFPVDLL ESVLIVMTTT QVKTVKQWKE HMRLLKDSHS MKAAFFSSLG
YVSTEELVTK LLNFIDSDIK DVNDVTLSLI SLCHYNETRN VNNLIWKWFT SSYKQWANKL
HDAQSFSQIF TIVLSAFIND AKWSSEVAEQ FKDITAVDIT TLLDSWTLEQ QAGATILNQI
AF
//
