ID H2ATL0_KAZAF Unreviewed; 501 AA.
AC H2ATL0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Endonuclease/exonuclease/phosphatase domain-containing protein {ECO:0000259|Pfam:PF03372};
GN Name=KAFR0D00630 {ECO:0000313|EMBL:CCF57710.1};
GN ORFNames=KAFR_0D00630 {ECO:0000313|EMBL:CCF57710.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57710.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF57710.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00006335}.
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DR EMBL; HE650824; CCF57710.1; -; Genomic_DNA.
DR RefSeq; XP_003956845.1; XM_003956796.1.
DR AlphaFoldDB; H2ATL0; -.
DR STRING; 1071382.H2ATL0; -.
DR GeneID; 13885668; -.
DR KEGG; kaf:KAFR_0D00630; -.
DR eggNOG; KOG3873; Eukaryota.
DR HOGENOM; CLU_034001_5_0_1; -.
DR InParanoid; H2ATL0; -.
DR OrthoDB; 50235at2759; -.
DR Proteomes; UP000005220; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0043603; P:amide metabolic process; IEA:UniProt.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR038772; Sph/SMPD2-like.
DR PANTHER; PTHR16320:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G01540); 1.
DR PANTHER; PTHR16320; SPHINGOMYELINASE FAMILY MEMBER; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..345
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
SQ SEQUENCE 501 AA; 56927 MW; 474A1162A262061E CRC64;
MQEKLSYVKL LNTKPGSHHW HMSTISIDDD ISLSLSRKQT HSQYPTIKFL TFNTWGLKFV
SKHRKERLKA IADKLAGIRT GVPLPNLESL RDSPDLNTED TYDVVVLQEI WCKDDWDYLV
YRCKDVFPFY RIFYSGIISG PGLAILSKIP IDSTFLHKFP INGVPSAITR GDWFVGKSIS
VTILKALTED TAPLAILNSH MHAPYALTGE NAYYCHRSCQ AWHFSKIANL YKKAGYAVVI
VGDLNSRPGS LPHTFLTLET GLIDSWEQLN GKQDQGEISK MNPSDQLIFG CTTCDSTLNT
WRSKKRPDEA CRLDYALVDP AKLQTIEAGL RFTERIPNVG SFSDHFAYSC SLRFLPQDIG
LNPVLRNKIY SNSDLNLTRD QLLEKFSTYE ELKLTIASYT KVAKRRKLIR GAYFWIAIYL
LITSITVTSF TSQRAGWSSV FWVIFAIIVS VFGTINGLIS FLFGRSELRA LMEIEHEVTD
AERNLQSVLD MKRTSFILPQ N
//