ID A0A397JR67_9GLOM Unreviewed; 564 AA.
AC A0A397JR67;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=PPIase cyclophilin-type domain-containing protein {ECO:0000259|PROSITE:PS50072};
GN ORFNames=Glove_9g107 {ECO:0000313|EMBL:RHZ89882.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ89882.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ89882.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ89882.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC subfamily. {ECO:0000256|ARBA:ARBA00038509}.
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:RHZ89882.1}.
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DR EMBL; PQFF01000007; RHZ89882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397JR67; -.
DR STRING; 1348612.A0A397JR67; -.
DR Proteomes; UP000266861; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01925; cyclophilin_CeCYP16-like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF6; SPLICEOSOME-ASSOCIATED PROTEIN CWC27 HOMOLOG; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000266861}.
FT DOMAIN 18..166
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 290..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 65057 MW; 0802926454008360 CRC64;
MSNIYITEPH TSGKVILHTT AGDINMELFA KETPKACRNF VQLCLEGQYD GTIFHRIVSG
FIIQGGDPTG TGFGGESIYG APFADEFHTR LRFVRRGLVA MANSGKNDNR SQFFITLDRA
DELQNVNTIF GKVVGDTIFN VLKIGELEVD KNERPLYPPK ILSTEVIGNP FDDIIPRITV
AEKIAQKSGS VTKVEEPSKK KLKKNVALLS FGEEVQEDEN DNDSSLKIKS SHDLVENDPR
LSKELAIKES EQKSWFSPTG LEESKLQVRD KVIEKTKVGN SIEVVEREED EESAAFDRKM
KENLRQRQES AKVNASKNNK NNIEEKKLSK MDTMQQEIEQ LKQDIKRMDR PKDHEDDGPK
KKKAKISYVD TERQRFLSSG KAAAARRKKG NEADTLAKLQ SFKTKIMVTE PSVEEPTEGK
DEGELCVLHS VPNCLSCRDT FGQPKEEDTD EGWLTHRLVF VKDYLGKDLM QRRDDPDDYI
VIDPLERKKE AFKQEKEKRA KNNSISEVFT KRDRDRDQHR DSKDRYVYES DRYRNDKGHD
HDRDRNRDRE RDRDRDRDRR DRRH
//
