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Database: UniProt
Entry: A1CMP5_ASPCL
LinkDB: A1CMP5_ASPCL
Original site: A1CMP5_ASPCL 
ID   A1CMP5_ASPCL            Unreviewed;       238 AA.
AC   A1CMP5;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAW08832.1};
GN   ORFNames=ACLA_097730 {ECO:0000313|EMBL:EAW08832.1};
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:EAW08832.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW08832.1, 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).
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DR   EMBL; DS027058; EAW08832.1; -; Genomic_DNA.
DR   RefSeq; XP_001270258.1; XM_001270257.1.
DR   AlphaFoldDB; A1CMP5; -.
DR   EnsemblFungi; EAW08832; EAW08832; ACLA_097730.
DR   GeneID; 4702241; -.
DR   KEGG; act:ACLA_097730; -.
DR   VEuPathDB; FungiDB:ACLA_097730; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_1165599_0_0_1; -.
DR   OrthoDB; 2404758at2759; -.
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   CDD; cd07061; HP_HAP_like; 1.
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; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   238 AA;  26874 MW;  2B470A5A37506C76 CRC64;
     MSQADSFWAI TLSLLAAIIG ALFYSCGSEF TVCSTDHSCT SQSPYYPSWN TWFHPSSSQN
     SKNAFAQKEW DLLYHLGGYR PWIEKIDGHP ELQGLDPPEG CSIDQVHMMS RHIALLDRIQ
     NANVVMNGSL SFLNNWTYFT DQPSKDFDQL TRTGPYAGTL EAFMTGVRFL TRYMHLLQPG
     QRTRIWASDS ERVIDTAKYF ASGFFGQNWE KDGKAVVEVI PETLERALPA LKANGLII
//
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