ID H2AVZ5_KAZAF Unreviewed; 638 AA.
AC H2AVZ5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 03-MAY-2023, entry version 60.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=KAFR0E03940 {ECO:0000313|EMBL:CCF58545.1};
GN ORFNames=KAFR_0E03940 {ECO:0000313|EMBL:CCF58545.1};
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:CCF58545.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58545.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; HE650825; CCF58545.1; -; Genomic_DNA.
DR RefSeq; XP_003957680.1; XM_003957631.1.
DR AlphaFoldDB; H2AVZ5; -.
DR STRING; 1071382.H2AVZ5; -.
DR GeneID; 13883361; -.
DR KEGG; kaf:KAFR_0E03940; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; H2AVZ5; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000005220; Chromosome 5.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..638
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003558982"
FT DOMAIN 69..410
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 482..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 340..374
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 638 AA; 66064 MW; E95E9DDC997C5550 CRC64;
MKASLVSVSS VALFSSLKAA AAEAPGFVGV QFSKRYGKSI SDSSLAKGNL VKRSSGTDEV
ELINESVFYA IDMEIGTPKQ SVTVLVDTGS SDFWVPSSTN PYCESKSATS TIASSDLIDC
TTYGTFSVSD SSSFVYNNTD FQTQYADGSS ATGFWGHDVV DFGGQELSDI SIAVADQTDS
SFGVLGIGLT GLESTYSGSA AASSSTGRYQ YDNFPIRLVQ ENVIQANAYS LYLDPATGSS
GTILFGGVDH NKYSGDLNTI PLINTLEANG YTSPIKLQVT LNGLGVSDGS STSTVTTTQI
PALLDSGTTL TYLPTAMFDL LAEQIGATYS STSNGYVLSC ANVDEDSMIV YDFGGFQIQT
PLAGSLYQLS DDQCELAIGS TSSSYATLGD LFLTHAYVVY DLDNKEISMA QINYNATTED
IEIISDSVPG ATKAAGYYNT WTTSESITAG GNIFTLTNGV AKAIETAVPD VSYQTSSTTT
VSSYNDASVT TSPTSSTTTV TSSSETPSSD TTSSSTSSTT TVTLSSSAYS SPISSVTTVT
LSSDASSSFF TSDVVTKVNV TSSQNSSSVP TVLASATLSS IAPSSSLTSD IVTKVSSTSS
QTSSSSIATV LASANGAAQF GASHLLAPLF IFISSIIF
//