ID A0A1I7SZS4_9PELO Unreviewed; 1228 AA.
AC A0A1I7SZS4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dwarfin sma {ECO:0000313|WBParaSite:Csp11.Scaffold412.g1072.t1};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold412.g1072.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold412.g1072.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361195}.
CC Nucleus {ECO:0000256|RuleBase:RU361195}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family.
CC {ECO:0000256|ARBA:ARBA00005545, ECO:0000256|RuleBase:RU361195}.
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DR AlphaFoldDB; A0A1I7SZS4; -.
DR STRING; 1561998.A0A1I7SZS4; -.
DR WBParaSite; Csp11.Scaffold412.g1072.t1; Csp11.Scaffold412.g1072.t1; Csp11.Scaffold412.g1072.
DR eggNOG; KOG3701; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProt.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; SMAD MH1 domain; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; SMAD; 1.
DR PANTHER; PTHR13703:SF69; SMAD PROTEIN DAF-3; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF56366; SMAD MH1 domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361195};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361195};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU361195};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU361195}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 236..385
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 992..1218
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 137425 MW; 4610D10576BC5DA3 CRC64;
MDNHHNASGY PNGNSNQTPQ YSFATNGQSS SNTGPMHGMK KYSAGLEDIP DIEAYERSLR
IEMPTFSLAM TQVPANIPTH IPPQITPHVQ SQILQLQPLL ELGTHQSHMQ PHLQNHLVQA
FDPPHSQALP QPLTHLSNQS SPPVTDDQSP LMSPVSTSGG KMHRNGIKVE MPPYLDPDSH
DDDPEDGVLY PDPDLFDVKN TVMTEYELDI LKQKKLGIED PRKKMEVPDA SSPPNKIVEF
LMYNRTLKEQ ELSQINAYRT KRNRLSLNHI KNNAEREFDQ KACESLVKKL KDKKHDLQNL
INVVEKKGSD FNGCITIPRT LDGRLQVHGK KGFPHVVYGK LWRFSEMTKN ETRHVDHCKH
AFEMKSDLVC VNPYHYEIVI GTMIVGHRES HDSREMATPH STNGHRYHHQ SSIDDISQGH
RFVQSIQMRP PPHMQPQMPV QIPLQHPQQM PSQHPPQISQ QLQQQMSQHH QQKMSQQNMP
QMAEQHSQEM PQYIPPASMS AQVPPHSASM PPNNASMPPH NVSMPLHNNG SSFDSRYPMQ
YPSHASHFDS PSAPVNSQAS MQYQNQQPQN HYQQQHHLQY PHQHFPQSTS NYHVQQHHFN
MPSQYPYGPP SMEQYNSIRP GTSASFDQHY SPRPPQRNYD YFGYAKMPTK HIFDLDGLYG
SLEMDDFPNS SLIPGPNNVG MGPSNMGSRL SNMEPGSSSM GPGSSSIGPG SSSMGPVSSS
MGPGSSSMGP GSSSTGPGPS NLGPRLSNMG SGPGNIGFGP DFNEPGPSSM GPGSSSMRPG
SSSIRPRPNN MGSGPGNMGF GPDYYEPGPS SMIPGPSSNE PGPSNMRPKP SYNDSGTSNT
FYWPRSMSPI SRYNEPGPSN CPGPSNSFEQ QPQECNFTGE MWTQPEVTVD IATFRRSCKE
YFCHKRFNHN FGTDKEEYHE PESSGKMREF VVSDMLGVTK IKKAIRKGDV YNGDFPADVP
YKDVCKFVLS ITNGKLMMTG EEPESVTGDS LWGVVTYYEH TDTLGCKSIR RGDFHIDGGY
IASSNRFSLG LEDNHQRSHD AFKVRKAIID GIRFSLKKDR SVWIQNNMNY PIFVTSGYLD
EEYGGRKEDK VHKIYGAGKL KVYGHEKVTQ AIRDKLFSRQ MARNHIDGIP TPMGVVYSTR
PTRDVQKEAM RTVDSLCKYC CVKVSLCKGF GAGYPNRPSI IDCPVWLELK VNQAFDYMDD
LQRNLSAEYG DPNIEALQRW GMTNVADD
//
