ID A0A015JNH8_RHIIW Unreviewed; 860 AA.
AC A0A015JNH8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Dap2p {ECO:0000313|EMBL:EXX56514.1};
GN ORFNames=RirG_215530 {ECO:0000313|EMBL:EXX56514.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX56514.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX56514.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 197198w {ECO:0000313|EMBL:EXX56514.1}, and DAOM197198w
RC {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004576}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family.
CC {ECO:0000256|ARBA:ARBA00006150}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXX56514.1}.
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DR EMBL; JEMT01027688; EXX56514.1; -; Genomic_DNA.
DR EMBL; JEMT01027688; EXX56515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015JNH8; -.
DR STRING; 1432141.A0A015JNH8; -.
DR MEROPS; S09.006; -.
DR HOGENOM; CLU_006105_0_0_1; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000022910; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000022910};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..567
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 661..853
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 98999 MW; 7534C6499D67C7F4 CRC64;
MSFMKYISLP SKETEHDPRL SSVNETGDPL DSPNSDNGFG HKNSEEEQET MLNKERGEDD
TVLDMEENID SMEYGKQDKI DRSILPCLCI AGIFVFAWVA SAIIYGFYRT GHMSGTGSLA
SRIQFDDLYN GSFIPEYQKL EWIKTDDDVD GAFIYRDHDD SIIVKYVADD KKKILVNGKD
IVDPNGKHLH YNDFVVSPDS EYVLLTTNRT KQWRFSHFSN YWIFNITSRS TFPLTNPIDK
DHQAVIAHAQ WSPVGHTVAF IKDNDMYVSV NLVDERRLTF DGSAVIFNGM PDWIYEEEVL
KTDNAIWWSN GGKRIGYLRL NESEVPEYEF PIYLTHFNAT PYPKEVVMRY PKPGYPNPIA
TFHVYDLETP LASQFGAITF EDDFSDDERI ITEVMWAGDD TVLVRVMNRV QDISRIVLVN
VNTRKGKTVR EEDADKMDGG WYEINRSMFY VKKSGSLEQD GYVDIVVNNG YDHLALFSPV
DSNTPKFLTS GEWEVDGRIQ AVDYERELIY YISTEKSSIE RHLYSVDFNG KNRTALTDIN
NEGFYSVSFS PGAQYYNLNY EGPDIPWQKV LKIGDPSKFN KNNNNKFFFY FSSIRLYGVI
ILTYVFCQLV LNVVEIRPPG MDESGKTKYP VLFNVYGGPN SQLVQTRFKI DWHVFLASSE
RLKYITVIVD TRGTGFKGRK FRCGVRKHIG DFESKDVVNA GRYWSKLPYV DSNKMAVWGW
SYGGFLTTKV IELDSRVFQV GMAVAPVTDW RYYDSIYTER YMKTPAQNPN GYEHSAITNM
TGFDNAKFLL VHGTGDDNVH FQNTANLIDR LTLASVHNYR VQFYTDSNHN IDLHNANREL
YYLLTEYLWQ SFGTGGKNEN
//
