ID A0A0V1P1S0_9BILA Unreviewed; 877 AA.
AC A0A0V1P1S0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3A {ECO:0000313|EMBL:KRZ90133.1};
GN Name=Smek1 {ECO:0000313|EMBL:KRZ90133.1};
GN ORFNames=T08_4989 {ECO:0000313|EMBL:KRZ90133.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ90133.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ90133.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ90133.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMEK family.
CC {ECO:0000256|ARBA:ARBA00008809}.
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:KRZ90133.1}.
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DR EMBL; JYDM01000060; KRZ90133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1P1S0; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; P4R3-like_central_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR23318; ATP SYNTHASE GAMMA-RELATED; 1.
DR PANTHER; PTHR23318:SF0; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 REGULATORY SUBUNIT 3; 1.
DR Pfam; PF04802; PP4R3; 1.
DR Pfam; PF00568; WH1; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 17..103
FT /note="WH1"
FT /evidence="ECO:0000259|Pfam:PF00568"
FT DOMAIN 185..375
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 3-like central"
FT /evidence="ECO:0000259|Pfam:PF04802"
FT REGION 112..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 100369 MW; 456DD8283EF84761 CRC64;
MSEPLVDDKC NDKDPSHRVK LYVLNEKRVW DDKGTGHVTC VFNERLQSHT LTVRSEQDGS
ILLESKILNE TAYQKQQETL IVWTEADNSD FALSFQEKQG CDEVWRGICG AQGRDPAQES
SDDTTQDSGS DEDSVENGAL NTVNSPTLQL PPCDLIHLKE INDVIAASFS AVSRRDALAF
AIDGQQYIPK LIKLFHMVED LEDLESLHLL YRIFKNIFFL NKPPLFETLL SEQFLFDVIG
ILEYDPTMQT RRKHREFLWE QAKFKEVVPI NSVPLLSKIH QVYRVQYIYD FIFPAPSIFE
ENVLSTLSSF IFFTRVEIIN MLQEDKTFLA TLFALIKKKE ATVEEFQNVI GLLKEFCSYS
PLLQAVHRES FFRTLMNNGI LDALEFFFQC DDSVVRSMAV DILNLIVDFD APAVRNYCII
ESSATEEKLF LNLVIDLMNR DPDPDLVTTM HAYVVLKNLI DPETMPTATA QQRNDKHEFL
SLFYRCCVPQ IFARFFPSIN GNKLIKDSYR NANLTNVYLE LLTFCIEHHS YHVRSLVLSR
DLVAKILVFL QSRHMFLKLS ALRFFRKIVH HRDDFYNRHI IRHRLFDPVV KCFIANGSKY
NVLNSALIEL FEFIRTENVR ILCLHFVENY MEHFEDVTYV NTFQGLKRRY EQQDSLSMKS
SSHSSSGSLT DSASWRRIRN SRELDEEEQW LNDDDEDEWN SNGGTLNAEQ PRSSVISYPI
GSKSSEGFTV TQPPGANAAS STAYSVDNGS EVNLPPLRSC DDDDDDDGIF FGPVKPKPKP
HKIVIHSSSL AARLNAGENV HKETVAAVRA LVDYNDSDSD EEMDHQHQHD RDQFKGIDSG
SAATAEEAKH DDSVESSSSS EQDLDLNSTP TKKARFQ
//