PFF1_COLGM
ID PFF1_COLGM Reviewed; 1034 AA.
AC E3Q4R4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Vacuolar membrane protease {ECO:0000250|UniProtKB:P38244};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-related family protease 1 {ECO:0000250|UniProtKB:P38244};
GN ORFNames=GLRG_01223;
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212;
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000250|UniProtKB:P38244}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P38244};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG697333; EFQ26079.1; -; Genomic_DNA.
DR RefSeq; XP_008090099.1; XM_008091908.1.
DR AlphaFoldDB; E3Q4R4; -.
DR SMR; E3Q4R4; -.
DR STRING; 645133.E3Q4R4; -.
DR EnsemblFungi; EFQ26079; EFQ26079; GLRG_01223.
DR GeneID; 24406588; -.
DR VEuPathDB; FungiDB:GLRG_01223; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..1034
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411714"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..418
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 419..439
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 471..491
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..497
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 498..518
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 537..557
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..567
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 568..588
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 704..724
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..736
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 737..757
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 763..783
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..1034
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 623..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 344
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1034 AA; 114272 MW; 286172921971D497 CRC64;
MAVKNPFGFT TGPVTFWLIV VYAAFLIPLV WIHESVPAVP SSSKNPYPQL NVTEAWHDLT
HITRKYHPYN SRANDEVGAY FMKRIEEILV RNKVEYTKEK DAGGVIWPQE AYDAPAPAKR
DVQRRDSKGP AVTIFDDTIS NTTYLGTSGS FNQAGAYGTY FEGTNKLVYI RGTLDEDGEW
WNGKRDPRKI GQGGVLVNAH YDSVSSGYGA TDDGMGCVSI LQILNHYTSP GHQPMRGIVL
LLNNGEEDGL YGAKVYHYSP LYYFTTSFVN LEGAGAGGRA ILFRTTDLEV TKGYEGAPHP
FGSVVAADGF KLGAIRSETD YKVWTESYGQ RGLDIAFYRP RARYHTNQDD TRHASQESLW
HMLSNSLAAV DNLQHTTGYF SGSRNDGDKK KVASGSGTDG VWFDMFGTGF AILELRGLFA
WTLTLLIVSP LVLALVTYIL SRKDKYYFFS RKVTADEDDE PVSVGGWKGF FRFPFALVLS
ASITVLSAFL IRRVNPHIIY SSPYAVWAMT LSLFFLVFWT IAKGASVVRP SALQRGYAHI
WLFVISWVIL VAVTAAADRF KIASGYPFAF FHSAVFVSAL ISLCDLFALP SKQEFARNAH
NDQQTRDNIS EVPNSDALIS SRHSHVEDDV AEEPTETTPL RSGENGNGNN GTIRTTFATT
YRRSLSAIMR TPDEEENKET EQQPYDHEQQ WSANLPSWTW FFQLLLLAPI TITVFLQIAL
FIVSAIHSAA ADGNDPILVY AAIAAFSIII LLPATPFIHR ASFYLPLFLL LVFFVTLIYN
LVAFPFSAEN RLKVRFQQTL DLDANTSVIS ITGLEKYTRK MIAELPSGAG QPVNCTPGYG
LTSDCRYNGA AVMPNLPQFT HALPANVSKG RYANLVTVNI SRSDSSSKLE FGIDAAESKV
CNLAFDTPVS FNVRGSAGID PIFSRPTEQG VRMLTLWRRD ASIPWVVDVE PIKTKAVPAG
VLAKSSDSDA GAVHEDLRVR KSAELSGTIA CQWSDANVLG TIPAFDEALQ FSPDWIAVTK
ASVGLVEGRK KFRA
