ID A0A2C9V3A4_MANES Unreviewed; 965 AA.
AC A0A2C9V3A4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase M28 domain-containing protein {ECO:0000259|Pfam:PF04389};
GN ORFNames=MANES_10G046500 {ECO:0000313|EMBL:OAY38838.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY38838.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY38838.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY38838.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM004396; OAY38838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9V3A4; -.
DR STRING; 3983.A0A2C9V3A4; -.
DR EnsemblPlants; OAY38838; OAY38838; MANES_10G046500.
DR Gramene; OAY38838; OAY38838; MANES_10G046500.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000091857; Chromosome lg10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF57; 24 KDA VACUOLAR PROTEIN-LIKE; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..358
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 931..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 105614 MW; 76C0F4E8C1D2DD6B CRC64;
MRSNLNYCSS ISKPSTTGSS NIVEDDGLIS GKKRRSGFVL LVLFGVFIYS WAVFRYRFQR
LPSPLTAEQA GESGFSEVEA RKHVQALTQL GPHPVGSDTL DLPWQHVLTA AENIRKTAHR
GVAVQVEHFH AKAGANRLDS GFSKGKTLVY SDLKHVIIRI LPKSTSEAGE NGIASEAAEN
AILVSAHIDT VIAGEGAGDD SSSVAVMLEL ARGISQEAHG FKNGVIFLFN TGEEEGLNGA
HSFITQHPWS KTIRMAIDLE AMGVGGKSGI FQAGPNPFAI ENFALAAKYP SGDIVEQDLF
ATGFSSATDF QVYREVAGLS GLDFAFIDNT AVYHTKNDKL EFLKPGSLQH LGENMLAFLL
QIGPTSHLPK GNTMKEEEKS GQDTAVFFDI LGTYMIVYRQ SFASVLHNLV IAISLIIWNA
SLLLGGYPAA ISFGLSILSV ILMLIFSISF SVLVAFILLL ISSSPVPYVA SPWLLVGLFA
APALIGAMTG QHFGYHLLQI YLSNVYPKKK QLSSVNQADW AKLEAERWLF KAGFILWLVV
LSLGNYYKIG SSYIALFWLV LPAFAYLLVE ATPTPAPSPM PLRLATLLMG LPLPITIAAG
TIIRLAATII GNLIRSDRNP GGSPEWLGSV KLAVFVAVVI CFTMVYVLSY VHLSGAIRTI
ILGTSILFGF SLILVLSGAT PPFTEDTVRT LNVVHIVNTT GSYGNKQHHN SYVSLFSGTP
GKLTKEVKYI GEGFSCGGDK VVDFVNFFAK YSCWSHEDTE GGWDDSDIPT LHVHSDTNGD
ERKTKVSIDT KVSKRWSLAI NTNEVEDFTL KANSKELVPF GNKSSVDGWH IIQFSGGKRS
PRKFKLTLFW AKKPTKSAHS VDEQATEKQQ PLLKLRTDVN RLTPKAERVL RKFPKWCSQF
GKSTSPYNLA FFTSLPVMNH GSRIAWADRQ PGSSKVYVRR KDESAKEASD ASRSAMPSER
RWSSY
//
