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Database: UniProt
Entry: A0A098VWD4_9MICR
LinkDB: A0A098VWD4_9MICR
Original site: A0A098VWD4_9MICR 
ID   A0A098VWD4_9MICR        Unreviewed;       556 AA.
AC   A0A098VWD4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative chromatin remodeling complex subunit protein {ECO:0000313|EMBL:KGG52071.1};
GN   ORFNames=DI09_215p30 {ECO:0000313|EMBL:KGG52071.1};
OS   Mitosporidium daphniae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX   NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG52071.1, ECO:0000313|Proteomes:UP000029725};
RN   [1] {ECO:0000313|EMBL:KGG52071.1, ECO:0000313|Proteomes:UP000029725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UGP3 {ECO:0000313|EMBL:KGG52071.1,
RC   ECO:0000313|Proteomes:UP000029725};
RC   TISSUE=Spores {ECO:0000313|EMBL:KGG52071.1};
RA   Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA   Ebert D.;
RT   "A new species of microsporidia sheds light on the evolution of extreme
RT   parasitism.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|RuleBase:RU000487}.
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:KGG52071.1}.
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DR   EMBL; JMKJ01000128; KGG52071.1; -; Genomic_DNA.
DR   RefSeq; XP_013238507.1; XM_013383053.1.
DR   AlphaFoldDB; A0A098VWD4; -.
DR   GeneID; 25259045; -.
DR   VEuPathDB; MicrosporidiaDB:DI09_215p30; -.
DR   HOGENOM; CLU_490084_0_0_1; -.
DR   OrthoDB; 196861at2759; -.
DR   Proteomes; UP000029725; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF16; ACTIN-RELATED PROTEIN 5; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029725}.
FT   REGION          206..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  64529 MW;  54754D647B5593CE CRC64;
     MLRLMQLKYP YFPTKMSLSH AEASVRNFCY VSEHYTSELR SFRDSASFLN DKDCVIQYPI
     PESSYSSVPD EDQSKLLEER KKAFSEKMKL HSEKRKQEKI VALKSDLVGL REMQATRAEY
     ETEDDYLEML KDYGYSSISD LEQVILDFET RLDKLVYGKD SSQKETVKYD YSILEIPDAD
     LSEEKIKEKR KLRLLKAGFD ARERARLEKE DEDRAKEKEE LKENMRREAD PEKWIAEKRA
     LRSQLKSKLK QLKQERDGLS DRKSSSSIRR IKSLSTLVNG RPSSSDFNDE NASLKKKRKA
     GQDTRKDKSP MDDDPMFGDN ESDWSIYREL NKAPGTSDDS FEDLERLENE IDRIDELLSH
     HDPNFWNLEQ EEKKASFIDH FTYGIEEASE REGDSNDTQN RLSSLPYQLH INIERIRVPE
     ILFQPSIIGL GSMGIVETLN ETFAHISKEH DITKREEVFL TGGNVAFPGF PKRLFNGLRS
     MRPSSSILNI LSPQFKEPSL DDISASNTLF NSPWRGAAKW ASKSHGSVDS WISRAEYEEE
     GIERCISRFR SAFFIH
//
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