ID A0A091DWH6_FUKDA Unreviewed; 1075 AA.
AC A0A091DWH6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 1 {ECO:0000313|EMBL:KFO36489.1};
GN ORFNames=H920_02116 {ECO:0000313|EMBL:KFO36489.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO36489.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO36489.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO36489.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC {ECO:0000256|ARBA:ARBA00006180}.
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DR EMBL; KN121407; KFO36489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DWH6; -.
DR STRING; 885580.ENSFDAP00000005191; -.
DR eggNOG; KOG2073; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634:SF13; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 REGULATORY SUBUNIT 1; 1.
DR PANTHER; PTHR12634; SIT4 YEAST -ASSOCIATING PROTEIN-RELATED; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT REGION 27..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..913
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1066
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 117289 MW; C15E2A470A9A97C6 CRC64;
MGPNNGPEMK NINLEVSSGT HFLIQFLQGA STRRREEATK WENHSEPHGL NDDEVQENPA
SDAARGGLVK QPATVTRMAG GGLRSPQAAR RRREETEWKQ SSRASPGESP EGVLGLEPKA
ERSGGCGSGS ATRETPDQEA PRASEPSGWD AEGRSTCALV GLGFIRGETV GNNGLRRSEA
GGFWGAGTGA QAHCAEARPE KLRTRKRPGL RNRAAGTLRA VAPAHWSGAM FWKFDLHTSS
HLDTLLERED LSLPELLDEE DVLQECKVVN RKLLDFLLQP PHLQAMVAWV TQEPPASGEE
RLRYKYPSVA CEILTSDVPQ INDALGADES LLNRLYGFLQ SSDSLNPLLA SFFSKVMGIL
INRKTDQLVS FLRKKDDFVD LLLRHIGTSA IMDLLLRLLT CVERPQLRQD VFTWLNEEKI
VQRLIEQIHP SKDDNQHSNA SQSLCDIIRL SREQMMQGQD SPEPDQLLAT LEKQETIEQL
LSNMLEGELS QSVLISGIQV LLTLLEPRRP RSESVTMNNF FSSMDGQLEL LAQGALDSAV
SSMGALHALR PRLGHFHQLL LEPLQLEPLQ MTWGSLAPPL GNTRLHVVKL LASALSANDA
ALTQELLVLD VPNTMLDLFF HYVFNNFLHT QVEVCVSAML SLGPPPSSGS ETLGLNPVLK
HLLQHCRLVE RILTSWEEND RVQSGGGPRK GYMGHLTRVA NALVQNAEQG PNAEQLGQLL
KELPGEQLER WEAFVSGPLA ETNKRNTVDL VNTHHLHSSS DDEDDRLKEF SFPEEAVLQQ
AFMDFQMQRM TSAFIDHFGF NDEEFGEQEE SVNAPFDKTA NITFSLNADD ENPSANLLEI
CYKDRIQQFD DDEEEEDEEG QGSGESDGEY GAWQGSPLSR AARSGQLPGA RSSGSTDSED
EDEEEEEEEE GGGDPMPPGP QPPGPSWTAT FSPVPVDNLS GPSDSGVEEL LPPAPDPATP
QLRSQDPVPT SAPQIAADGS EVAEPSAPCQ ALVSVEALQA ALRGMRSAPS SSDSAPRDPS
TSVPAFGAQH PPQTKEGEKS PEPLGLPPSQ SAQAHEPPPM PNGSAPVAPL SPGSQ
//