ID   A0A2I1FU54_9GLOM        Unreviewed;       454 AA.
AC   A0A2I1FU54;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=PHP domain-like protein {ECO:0000313|EMBL:PKY37912.1};
GN   ORFNames=RhiirA4_335793 {ECO:0000313|EMBL:PKY37912.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY37912.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY37912.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY37912.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PKY37912.1}.
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; LLXI01000013; PKY37912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1FU54; -.
DR   VEuPathDB; FungiDB:FUN_025484; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1510348; -.
DR   VEuPathDB; FungiDB:RhiirA1_532326; -.
DR   OrthoDB; 8377at2759; -.
DR   Proteomes; UP000234323; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   NCBIfam; NF038032; CehA_McbA_metalo; 1.
DR   PANTHER; PTHR42924; EXONUCLEASE; 1.
DR   PANTHER; PTHR42924:SF3; POLIIIAC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        71..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..200
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  52762 MW;  266EE420D9BB3298 CRC64;
     MDQEENALLS RPTQNYNTLD SSGIDISPET PLLPTTSSPP QNQRHRLSGG TGPVLSEIKI
     PLKFRLYLRD VLLRFLQFIL ILVFLFTFLT IFKYKAIPDS NDYSDIEFNW RFDPRSYMTP
     IDNDFGEFNV LLDGHSHTKF SDGRMNPEQL LKWAIANGYN AIIVSDHNNI EGALEAQRIA
     REKYNDSITV IPAMEYSSCR LHMQFIGINE TVDVSPDFPS DERLEEIIDH VHKLGGLVSV
     NHIPWSNSTE WGYQVGTLPE HPSREKLRDM GVDGFEVING DTFDWQTYLF VQQNNMLMLT
     GSDVHFPSTG AYAWTVLNVS NITYEGIMTK LRAKRTSFLF DATGTRPSVY PKKNPSYYNL
     LPMTLLADYW TSFYSESKGM YSFQSTFCHQ RKFVMHWESY FWFSLWCLIF FTCYEIGRIL
     FIKGYEYFSI WKLKIGNRGR NENEEERQVD LVDI
//