ID A0A0B2VZF4_TOXCA Unreviewed; 621 AA.
AC A0A0B2VZF4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=RNA-binding protein 28 {ECO:0000313|EMBL:KHN87038.1};
GN Name=Rbm28 {ECO:0000313|EMBL:KHN87038.1};
GN ORFNames=Tcan_11197 {ECO:0000313|EMBL:KHN87038.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN87038.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN87038.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN87038.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926}.
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:KHN87038.1}.
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DR EMBL; JPKZ01000486; KHN87038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2VZF4; -.
DR STRING; 6265.A0A0B2VZF4; -.
DR OMA; TSSKCAN; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd12415; RRM3_RBM28_like; 1.
DR CDD; cd12416; RRM4_RBM28_like; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR48039; RNA-BINDING MOTIF PROTEIN 14B; 1.
DR PANTHER; PTHR48039:SF5; RNA-BINDING PROTEIN 28; 1.
DR Pfam; PF00255; GSHPx; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS50102; RRM; 3.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 78..143
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 210..291
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 360..452
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 32..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 70054 MW; FC09380DD7314D41 CRC64;
MAPAASHSVM SGRIDISFES VLSIFRMTSS GHGQHQVFPE SDIEEADKPR GSGDKDAVRD
AENFNRRKYF QDAKRKGWRL IMRNLAFSTK KEDLQVLCSK FGPFTEIVLP PCKDPRYPQS
CAGFAFIQFK NREAAKNAIH SLNMSQKVWE EESGVSETAG DEGEEQEESG SDENDRDEKE
HDEASTNNGS SRKKGSGHKT RSNQAVEQGR VVFVRNMSYE TTDEMLKESL EKFGEIELAI
ICRYAESGHS KGSGFVYFES RHQADACLDA ITTDPGIMID SRRIYAHRAL PRNDAAAIEK
ENLKRKPKDK RNLHLLRVGV VRPGTVAARG MSEMDAKKRA KLALAAKAKL RNLHMFVSPT
RLVLHNLPMS LTDNSLKSLC FLAAGNPDAR ITECRIWRDR EKSNVKGIGR SRGFGFVAFS
EHSDALAALR KLNNNPETFS DERRPIVEFS IENLSALRFR ESRVTKSKEK LAKGTEEKGM
SEKTRREVEE TKREMAAGGQ KPLPSHVGPK IRHRDLIKKS LPKRGKDQEP GCELDIKEFV
TKKYSFKPDL YSKIEVNGEL AHPLYKFLKE EQGGTLTNAI KWNFTKFLVD KNGHVVKRYS
PQTQPKDMVK DIETVLSGSK L
//
