ID A1CBA2_ASPCL Unreviewed; 584 AA.
AC A1CBA2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Histidine acid phosphatase, putative {ECO:0000313|EMBL:EAW13020.1};
GN ORFNames=ACLA_014570 {ECO:0000313|EMBL:EAW13020.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13020.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW13020.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; DS027049; EAW13020.1; -; Genomic_DNA.
DR RefSeq; XP_001274446.1; XM_001274445.1.
DR AlphaFoldDB; A1CBA2; -.
DR STRING; 344612.A1CBA2; -.
DR EnsemblFungi; EAW13020; EAW13020; ACLA_014570.
DR GeneID; 4706126; -.
DR KEGG; act:ACLA_014570; -.
DR VEuPathDB; FungiDB:ACLA_014570; -.
DR eggNOG; ENOG502SM2K; Eukaryota.
DR HOGENOM; CLU_023111_0_1_1; -.
DR OMA; STQEWCL; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF127; -; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..584
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633008"
FT TRANSMEM 449..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 535..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64045 MW; F8E5E877AE543B30 CRC64;
MLISAKQYLA LAAALQMSAG ASAQNLKEQV WSIFAYNLHG DSIPIALPRP RALTPYGAND
MYSAGGAFRN RYVAVHNDEG NASTRIPSLS PYLLESEEVS ILSSTDQPAV ASAQAFMQGL
YPPLKKTYNG NYFDPSFQLA NGSMSTAPMN GYQYAQVLTL SPADPRSILL DGQAECTLHQ
VADSEYQFSL EVEDMNQKSE AFYGRLHSQA LRGIFDLSSA KYSNANSISE FLQYQLLHNK
TLLHHLNRED IELARWYADH YVYATNGHTS SPGVIGSNKI RTIAGRTLAS YVLEAFDRNI
EYRGVNDKMT FLFGASEPAV ALASLMQVAS SNQEMFYPRP NLGASLVFEL YSLESEAYPT
YPEPSQLYVR FLLRNGTDSA AEFQSYPLFG HGPSNDAIPY SDFRAQMKKF SLGSIKQWCI
ECSSSAVFCS GVVDQVKKTP ASNKGLNPAV AGVIGAVITV VTLALIAIVV FLVFGMRMKR
VHRSGLGGFK GSNKMASDSD VTFKNTTRED VKTAEDSHNG ISGVSGAVVR GHERTGSWEM
RDQQEGALAT STGGQETVSP FENDHDDIWR RHSILEPVKA LEHV
//
