ID A3M0M1_PICST Unreviewed; 800 AA.
AC A3M0M1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Membrane protein involved in vacuolar protein sorting {ECO:0000313|EMBL:ABN68551.2};
DE EC=3.4.17.21 {ECO:0000313|EMBL:ABN68551.2};
GN Name=VPS70 {ECO:0000313|EMBL:ABN68551.2};
GN ORFNames=PICST_33956 {ECO:0000313|EMBL:ABN68551.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68551.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68551.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; CP000502; ABN68551.2; -; Genomic_DNA.
DR RefSeq; XP_001386580.2; XM_001386543.1.
DR AlphaFoldDB; A3M0M1; -.
DR STRING; 322104.A3M0M1; -.
DR GeneID; 4840855; -.
DR KEGG; pic:PICST_33956; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; A3M0M1; -.
DR OMA; LWNVIGT; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ABN68551.2};
KW Hydrolase {ECO:0000313|EMBL:ABN68551.2};
KW Protease {ECO:0000313|EMBL:ABN68551.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 165..241
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 355..544
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 680..794
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 800 AA; 90468 MW; AB9BE88DB5CDCCDF CRC64;
MSDEKGFYTP IEVAPSRKQS WLKRFAAGAI GAAASLYLLS SAASYLSTEI SETEAKKIIL
DALETNLAGN WSKIYTAEPH LAGTNFGLVQ FTRDKFEEYG LDASIDTYEI YVSYPNDHDL
NLLDAKTEEI LYKAPLKEDV LKEDETTHGN DTVPTFLAYA ANGNVTGQYV YANYGTKKDF
EQLQEWGVDV KGKIVIVRYG AIFRGLKVKF AQENGAIGVL IYSDPGDDHG ITEKNGYKQY
PHGPARQESS VQRGSVQFLG GVGATPGDPT TPGYASKPGV ERKDPHASIG KIPALPISYR
EVKPILEKLN GEGHHAKEDS WIGELEGFKY YTGPSKNYTL NLYNDQIYNI STLYNVYGEI
PGEKRDEVII IGNHRDAWIK GGAGDPNSGS ATIVEVARAL GELKKAGYKF KRTIVFQSYD
GEEYGLLGST EQGEYFADKY KRTVVAYLNL DASTTGSHLK LGASPLLNNI LREAAKELEY
PAKGVGSLYD HFVQETGDNI KNLGSGSDYT VFLEHLGIPS VDLGFGQGKG DPIYHYHSNY
DSFYWISEFA DKGFVYHNLA AKYLSLIVFG LGERELINFK LTDYSKDLIK YYNETIKAVP
KKWFHQEISQ ETWDKYLNHD IADIEFISKA TSRTYLPRRW FPFPELLNVR DCKMKGHLMY
DSKHHKNATL EDLLLKTLED INTLQNSTVS FDLKTFDLQS QHENKDDLNF WQRFKLHFQI
KGHNKLLQYF ERNFLYHKGL YERPWFKHIV FASGRFTGYE GQTFPGLKEA LEDGDFERFV
DWLGIVSKAI RRINAEIAVK
//
