ID M3CD59_SPHMS Unreviewed; 938 AA.
AC M3CD59;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Zn-dependent exopeptidase {ECO:0000313|EMBL:EMF11001.1};
GN ORFNames=SEPMUDRAFT_150045 {ECO:0000313|EMBL:EMF11001.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11001.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF11001.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF11001.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KB456266; EMF11001.1; -; Genomic_DNA.
DR RefSeq; XP_016759122.1; XM_016905932.1.
DR AlphaFoldDB; M3CD59; -.
DR STRING; 692275.M3CD59; -.
DR GeneID; 27903069; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_1_0_1; -.
DR OMA; YPRKDGR; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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:SF71; CARBOXYPEPTIDASE TRE2, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10650)-RELATED; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..404
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 535..722
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 797..928
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 105718 MW; 4700CDCD7BAD44FC CRC64;
MDMNDDEDDD KYVRYAHVPI PSYEDAIQRP NSSQNHGQAE QEREGLLDQH GRTRSYQPPT
AESPRSSEDS DLRLPEVDGD DNDERRRVEE LDYLDPSTAD PDSRRAGLYH RSRIRSKFSQ
HLSNLGATLS SLRLPSFRSL YTPVQSELEQ NNNNNNNEND HENENSSEPP RRWAWLYRPL
PSLPVQYRMG AATAARLCGL MSIAILIYVL FILDVFPNSG RYIGTRFDPE SVRSYVQENV
DAARIEEYLY HITGYDHVAG TEGDLYMAEW MKGKWEEEGH LDSVALRSYY VYLNYPKQDG
RSVSIVAPEN KKWKAKLEEE RADPVKQQTW AWHGHSKNGL VEGHLIYANG GNREDFAWLR
DQGVTLNGSI ALMRYYSTQG DRALKIKAAE DAGCIGALIY SDPTEDGSVR GPVWPEGPWR
SEDSLQRGGV SLMSWIAGDP LTPGYASTKD AKVHDKENNP GLVGIPSLPL SWRDAKVLLE
SLSGHGVQVP KEWVGGDKSF TKEWYSGASP DKSSDTPIVN LKNHNDENDK QQIWNLHGLI
EGLEQPEKKI LIGNHRDSWC FGSVDPGSGS AVMMEMVRIF GALRKLGWRP LRSIEFISWD
AEEYNLVGST EYVEDNMEAL REDAVAYLNI DVGVYGPDPV FRAAGSPVWE RPLLHILDRV
NTPSGSATLR QIWDDRKSKL EGLGAGSDYV AFQDMAGTSS IDFGFEGPEY GYPYHSCYET
FDWMKRFGDP DFGWHRTLGQ LWALLILEIA DRPIVPFDLR SYADALDGPY LDTLQNYATS
QLQKLGQSTP SDNKTEIDIS SLKEAAQHLK SVASHFHKFE DLWTTNVLGT GGLETSSYAI
RRLAYNDALS TFETDLLDIP SSPLDTDQHG VPGREQFKHI VFGPQAWSGY DEAYFPAVRD
ALDVGDWALA QKQVDKAADI LERAIKRLEG KGRKLMLK
//
