ID U1HPK2_ENDPU Unreviewed; 700 AA.
AC U1HPK2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERF70989.1};
GN ORFNames=EPUS_03268 {ECO:0000313|EMBL:ERF70989.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF70989.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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DR EMBL; KE721267; ERF70989.1; -; Genomic_DNA.
DR RefSeq; XP_007803283.1; XM_007805092.1.
DR AlphaFoldDB; U1HPK2; -.
DR GeneID; 19238314; -.
DR eggNOG; KOG2645; Eukaryota.
DR HOGENOM; CLU_017594_4_0_1; -.
DR OMA; DGHKFGP; -.
DR OrthoDB; 1366859at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd16018; Enpp; 1.
DR Gene3D; 3.30.1360.180; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 4: Predicted;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 78444 MW; 6C9EFD05FB7135E9 CRC64;
MSRSPQDTPL TPATYDNDAT SLTLAHDQSS DSEEERLAEK SRTTLELNEY DASLLRDEDE
RETLLIEKRP LHGIKNVLKN PSGDAGLSLS SREAKSERRK QRRGSTTGRK GDRAEEGKLM
FQMEEGFKDI SSRSSSSDSL HLDQELRGRL KKQPGLFTWR RHLSVSLVIA TLFLVLAFGA
FKASSQFRHA QSVPKLSNGT HLFAPTTILV SLDGFRADFL NRGLTPALNS FIASGVSPRY
MLPSFPSVTF PNHFTLVTGL YPESHGVVGN SFWDPELSEE FFYTDPLRSL QPKWWTAEPL
WVTAENQGVR TAVHMWPGSE AHIPPLEPTY LDKFNKNEAL TTKIERILGL LDLPGDFDNS
EGVSPDRRPQ LIAAYVPNVD SDGHKYGPNS TEIRVTISDV DSMLAILMEG LYDRNLTEIV
NVVVLSDHGM ATTSNTRLVQ LDDLIDLSLV DHIDGWPLRG LRLTNPSRDV PILYEKLLKE
SESSQGFEVY TLDTMPERYH FANNNRIAPL WIMPKTGWAI VERKEFDVTE AQAAGTIYHP
MGIHGYDHEH PLMRAIFVAR GPAFPHAPNS RLPVFQNIEV YNIICDSLGI KPHANNGTLR
LPLSTVGLHD DSDAPELETP HDPPQEAPPF NGIEPGHMER PNQGPALRPG AENDTTETNE
AEEKGDAEMT WWDIMHDRIE KAKEWAKKII EKLKGNSEDG
//