ID A0A074Y6T0_AURPU Unreviewed; 920 AA.
AC A0A074Y6T0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:KEQ89947.1};
GN ORFNames=M438DRAFT_351293 {ECO:0000313|EMBL:KEQ89947.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89947.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ89947.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89947.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; KL584974; KEQ89947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074Y6T0; -.
DR STRING; 1043002.A0A074Y6T0; -.
DR HOGENOM; CLU_320276_0_0_1; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF00648; Peptidase_C2; 2.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 175..464
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 12..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 404
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 920 AA; 103598 MW; 9388C26376D58260 CRC64;
MDPHAFARAF LNKQTHRPAS SGTTTPDHIT PFPIRLIHER APRRPRSISS IISKPLNDDF
YRFWDRFLAT SPNRALNTSA LARRLEQTLK AASGEENGLH TQESPAASYE QAKRECQTKV
QAIVAECKRL NQRYRDRQFE VELYQHDCIV PLVDDEGNTT AIQPSGVKRV KILKDIFEKP
TFNAEGACGD DVMQGSLGNC WFIAALVSVA AKPGLMQRLC VARDEAVGVY GFVFFRDGIW
IPEIVDDRLF IHVSDGDDLF VGKYVEERQT RSTFNNSNDI TKLRESLQKG GEALYFARCR
DSQDTWLPLI EKAYAKAHGD YGSLHGGWVG EGTEDLTGGV SINLAPSDIM DKARLWEQLM
QVNETYLFAG GAFHYKEAGN FGKHAYAVLQ AVEHKGLRLL KVRNPWGNNK NTDNFDGPFN
HKFEEWSAEL VEQLKFDFKD PGVFWVTLDN FLRYFDSIQR TRLFDETWTL TQQWTSVNVA
AGAVTYLDTS FHITVARPGP IVIVLAQPDV SYFQGLQGRY TYCLHFRVYD AKDPTRYLAR
SMHVSSGNYI NTRSVSVDLD LEAGSYNVLI KISPSRVPYR TAESVIETEA PYRKQKLLQI
GRNFELAHAK GKLREKEQEV RKQKKEQQKR ESRARQSKMR MLRQQVKARE KKRKDRIAQE
KREREKMDLL KRAGVVFAPF PNDDPPVNLT SKPAGGPVSP PPLPPPMKFT GYVGSDMDPN
AELEDDDFAW DSEMDGDVYS SSSEDEKDWF ADDPWNALLV LGLRVYSQAS GVSIKVRDGD
EAYDDFIVVT PPSTSTSDTE MPTKATETKE EKNGKTDDQM ENPKAQTRPE DAKIDGDAEK
QPSVSSEATL VMEATSDTEE KTLRSDFDDK PAHHDASVTI EKPASEGIAS QTPDEEAASA
SKDEQQEAGA GKSISEEKAD
//
