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Database: UniProt
Entry: A0A1X2IY55_9FUNG
LinkDB: A0A1X2IY55_9FUNG
Original site: A0A1X2IY55_9FUNG 
ID   A0A1X2IY55_9FUNG        Unreviewed;       353 AA.
AC   A0A1X2IY55;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=HAD-like domain-containing protein {ECO:0000313|EMBL:ORZ24220.1};
GN   ORFNames=BCR42DRAFT_387062 {ECO:0000313|EMBL:ORZ24220.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ24220.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ24220.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ24220.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORZ24220.1}.
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DR   EMBL; MCGE01000002; ORZ24220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2IY55; -.
DR   STRING; 90262.A0A1X2IY55; -.
DR   OrthoDB; 5473812at2759; -.
DR   Proteomes; UP000193560; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT   DOMAIN          174..332
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          31..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  39963 MW;  2840B7374B6468BA CRC64;
     MGWSTSKSSK RRRTAGRKFL SILTCCSLSG KSHQDTNKCQ PTPQGTIHRT SSTHVTPSQT
     ITYSTTSIAS KEVNNYSNIA TDSKAKDYNK DEKDQITDHG TNEYQTDDLS NQLDTDTASK
     HSHHSLVPAQ NDNTDHMKRD DCYRRSSYDD VHETTTPSLE SEQDLWLLAP ISEQDKGRKC
     LVLDLDETLV HSSFKVTPQA DFVVPVEIDG SYHNVFVLKR PGVDAFMKRM GELYEIVIFT
     ASLSKYADPV LDTFDIHRTV QHRLFRESCF HYKGTYVKDL SQLGRQLNQV IILDNSPASY
     IFHTANACPV SSWYNDPHDS ELLDLIPFLE DLAFVDDITD VLDNTIPGPF SHF
//
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