ID G4UYG0_NEUT9 Unreviewed; 469 AA.
AC G4UYG0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=PAP2-domain-containing protein {ECO:0000313|EMBL:EGZ69069.1};
GN ORFNames=NEUTE2DRAFT_93841 {ECO:0000313|EMBL:EGZ69069.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ69069.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ69069.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GL891258; EGZ69069.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UYG0; -.
DR STRING; 510952.G4UYG0; -.
DR eggNOG; ENOG502QPQM; Eukaryota.
DR HOGENOM; CLU_030747_0_1_1; -.
DR OMA; WSIYDAQ; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR31310; -; 1.
DR PANTHER; PTHR31310:SF11; INOSITOL PHOSPHORYLCERAMIDE SYNTHASE CATALYTIC SUBUNIT AUR1; 1.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..345
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 469 AA; 52711 MW; 3337CD76CFD9CA9D CRC64;
MQDFEPILAP AKPKQKKLPF GWPPALKLST LNPVPQRRRL RRKSTASQDN VAALKTSFDV
WESIKTLQTR KWKIYDIQHV VCLGFILFSL FILPSAPIIK TAVLLALGGL LLMPITQQFF
LPSLPIWTYL LYFFASRFIA PEYRPHIWVK VLPALENVLY GANLSNILSA HSHPVLDLLA
WFPYGIGHFA LPAICSAILF LFAAPGSTPV FARAFGYMCM LAVTIQLIFP CTPPWYEKAH
GLEPAHYGME GSPAGLARID KLFGVDMYTT SFTTAPLPFG AFPSLHGANA VLEALFMQYY
FPKFKYFFIF YVGWIWWATM YLNHHYAVDL VGGGLMAAIA YYISRVRWLP RPQLEKRTRW
EYEYVEFGDR PKTYDEEYGS ASAYGLGLLE RRTASDSDEW TLGSSSSLDS LSRGDTVCGS
SSSTPDILSP TTPNDDFKHV VLGLTPQGDI WNGGRLARES ELSDVVVLS
//
