ID G8YCJ6_PICSO Unreviewed; 977 AA.
AC G8YCJ6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Piso0_002414 protein {ECO:0000313|EMBL:CCE82677.1};
GN Name=Piso0_002414 {ECO:0000313|EMBL:CCE82677.1};
GN ORFNames=GNLVRS01_PISO0J11471g {ECO:0000313|EMBL:CCE82677.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE82677.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; FO082050; CCE82677.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YCJ6; -.
DR STRING; 559304.G8YCJ6; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; G8YCJ6; -.
DR Proteomes; UP000005222; Chromosome J.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase 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; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR PANTHER; PTHR10404:SF46; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 70; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 200..272
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 385..573
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 857..968
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 271..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..829
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 110614 MW; 67103BB132D9F09F CRC64;
MTDQFLDEKK GWSDEPVLPL HEEHNEEEYG RFKISKKFIV KVLLCMGFYF FLISPAAFKV
PSWAKGLKGV VSDYSYYGKA QQEKSLDVFF KALETNFASN WSKKYTAEPH LAGTNFGLAE
WTKEKFEEYG LKSTIDQYEV LLSYPHEQDL RLLDTNTGEQ LYRAPLKEDE IEEDETTKGE
GLVPTFLGYA ANGNVTSSFV YVNYGTKDDF AYLQKLGVDV TGKIVIARYG AIFRGLKVKF
AQENGAAGVL LYSDPGDDHG ITPAKGFGQY PDGPARQESS VQRGSAQFLG GIGSSPGDPT
TPGYASKPGV DRQDPHANIG KIPALPISYR EVKPILDKLN GHGTKVSLNN WKGELDGFEY
WTGPNEDVQL NLYNNQIYNI STLTNVYGEF EGERKDEAII IGNHRDAWIK GGAGDPNSGS
AVLLEIARAL GELKANGFKF KRTIILQSFD GEEYGLLGST EFGEYASKRL QHNVAAYLNL
DSAVVGKQLD LSASPLLNDV LRSAASKLAY PEPGVGTLYD HFVKEGDDKI GILGSGSDYT
VFLEHLGIPS ADIGFRGGKG DPVYQYHSNY DSYYWMANFA DKGFVYHNLM AKYLGLVTLE
LSQKEVLPFG LNKYAKALKE YFNNAAASVP EEWLNEKVHH KDLRKFYNHD FDDETFVRES
SNGHYASPFL PRMGCHRSAM IHHLKDEKPK KLHFGDIHKS QKKNSDQVGH FEATSKAHHT
GYNDEEQDVE TIEDGNRASQ ERHEEKTKIK VEKIKPGCHS FDTKKMNKFG KKQAIKKPDV
QIYHEKDSEV TQSEHTPSGD TDYHKSSHGK SFHVKDEHHK AKKGHHKDKF HPPHPIEMER
KHGNETLRML LEKTAYDLDS LFNATLDFDA KSEYLQSQYD DDNISWWQRI KLHFQIKKHN
KIAQYFERGF LHKKGLHERP WFKHIVYASG RFTGYQGQTL PGLNEALEDK DFGRFVKWLG
IVSRAFKRSF YPISSTN
//