ID L5K5S8_PTEAL Unreviewed; 937 AA.
AC L5K5S8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=RNA-binding region-containing protein 3 {ECO:0000256|ARBA:ARBA00020364};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=PAL_GLEAN10017322 {ECO:0000313|EMBL:ELK05838.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK05838.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; KB031037; ELK05838.1; -; Genomic_DNA.
DR AlphaFoldDB; L5K5S8; -.
DR STRING; 9402.L5K5S8; -.
DR eggNOG; KOG4206; Eukaryota.
DR InParanoid; L5K5S8; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd12239; RRM2_RBM40_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 6.10.250.610; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045164; RBM41/RNPC3.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR16105:SF6; RNA-BINDING REGION-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR16105; UNCHARACTERIZED; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 404..482
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 105685 MW; D110638EDD83D5EC CRC64;
MAAPEQPLPM SRGCQSSISL SPPRGDRTLL VRHLPAELTA EEKEDLLKYF GAQSVRVLSD
KGRLALTRLH QLKLLGHTLV VEFAKEQDQV HSPCPSSGTE KKKRSDDPVE DDKEKKELGC
LTIENGIAPN HGLTFPLNSC LKYMYPPPSS TILANIVNAL ASVPKFYVQV LHLMNKMNLP
TPFGPITARP PMYEDYMPLH APLPPASPQP PEEPPLPDED EELSSKESEY ESSDDEDRQR
MTKLMELANL QPKRPKTIKQ RRVRKKQKIK DMLNTPSSVS HSSLHPVLLP SDVFDQPQPV
GNKKIEFHIS TDMPAAFKKD LEKEQNFEEQ NCDLPATEID ASSIGFGKIF PKPNLNIAEE
SKEDSDEMPS ECISRRELEK GRISREEMET LSVFRSYEPG EPNCRIYVKN LAKHVQEKDL
KFIFGRYVDF SSETERIMFD IRLMKEGRMK GQAFVGLPNE KAAAKALKEA NGYVLFGKPM
VVISPPNENV VINNPSRPWW ERYQPISYKL CTRSGNEDEF KDMVTRCNNV GVHIYVDAVI
NHMCGNAVAA GTSSTCGSYF NPGNRDFPAV PFSGWDFNDG KCKTGSGDIE NYNDPYQVRD
CRLVGLLDLT LEKDYVRSKI AEYLNHLIDI GVAGFRIDAA KHMWPGDMKA ILDKLHNLNT
TWFPEGSKPF IYQEVIDLGS EPIKSSEYFE NGRVTEFKYG AKLGTVLRKW NGEKMAYLKN
WGEGWGFMPS DRALVFVDNH DNQRGHGAGG ASILTFWDSR LYKMGVGFML AHPYGFTRVM
SSFRWPRYFE NGKDVNDWIG PPNNNGVIKE VTINADTTCG NDWVCEHRWR QIRNMVMFRN
VVDGQPFTNW WDNGSNQVAF GRGNRGFIVF NNDDWPLSLT LQTGLPTGTY CDVISGDKIG
DNCTGIKIYV SGDGNAHFSI SNSAEDPFVA IHAESKL
//
