ID A5DZ31_LODEL Unreviewed; 800 AA.
AC A5DZ31;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK44439.1};
GN ORFNames=LELG_02618 {ECO:0000313|EMBL:EDK44439.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK44439.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK44439.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; CH981526; EDK44439.1; -; Genomic_DNA.
DR RefSeq; XP_001526060.1; XM_001526010.1.
DR AlphaFoldDB; A5DZ31; -.
DR STRING; 379508.A5DZ31; -.
DR GeneID; 5233061; -.
DR KEGG; lel:LELG_02618; -.
DR VEuPathDB; FungiDB:LELG_02618; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; A5DZ31; -.
DR OMA; RNGMIAR; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 177..253
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 364..552
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 679..795
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89922 MW; 99BDE415E2AD6625 CRC64;
MKAKKEMEME KDTKTKPNRH LQQVSQERIA NAHGGPLKLL LIGGLLYLFY RLFAISTPPS
IGNLALVEPA QIVLDALELN YARNWSQKYT AEAHLAGTNY PLVEWTEQKF LEYGFDTTID
SYEILASYPK DHSLSLLDKH EQIVYTAPLK EDSIDEDPTT HNNTVPTFLG YAANGNVTAQ
YVYANYGTKS DFEALKEHNV DVTGKIVVVR YGKIFRGLKV KFAQDRGAIG VLIYSDPGDD
FGITPKNGYK QYPHGPARQE SSVQRGSVQF LGGEGSAPGD PTTPGYASKP GVERKDPHTS
IGKIPVLPIS YREVKPILQK LNGKGAKVKG FEGELDGFEY TTGPSEYSLN LYSDQDFKYA
TMWNVYGEIK GEKADEVIIL GNHRDAWIKG GAGDPNSGSA TLLEVARALG TLKAKGHKFK
RTIVLHSYDG EEYGLLGSTE QGEYFAKKYQ REVVAYLNLD VSVSGKNLGL GSSPVLNNLL
LDVAKELEYP EGGSLYDHYV KVHGSDAIKS LGSGSDYTVY LEHLGIPSVD LGFGGGKKDP
IYHYHSNYDS FHWMEKFGDK NFVYHNLAAK YLALLALRLS EKEVIQFRLE SYASSLIDYF
EKTSQRVPAE WLNKTTAFSD YRGSHLLDED TFIRDVTQSQ YTCPMRKNQQ MRLTHGLNCF
EAKKTATLGQ RLDQTLHLLH GFQKSAQAFD EKSLHLQDQA DNYLNLSLPG KIWLHLKIRK
HNRSLKYFER NFLHHEGLDT RPWFKHILFA SGRFTGYAGQ DLPGLNEAIE DGDLGRLSKW
IGILDRTVHR VSHHLHQRVI
//
