ID A0A9J6F4G9_RHIMP Unreviewed; 1101 AA.
AC A0A9J6F4G9;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=HPB51_017484 {ECO:0000313|EMBL:KAH8041682.1};
OS Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Boophilus.
OX NCBI_TaxID=6941 {ECO:0000313|EMBL:KAH8041682.1, ECO:0000313|Proteomes:UP000821866};
RN [1] {ECO:0000313|EMBL:KAH8041682.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rmic-2018 {ECO:0000313|EMBL:KAH8041682.1};
RX PubMed=32814014;
RG Tick Genome and Microbiome Consortium (TIGMIC);
RA Jia N., Wang J., Shi W., Du L., Sun Y., Zhan W., Jiang J.F., Wang Q.,
RA Zhang B., Ji P., Bell-Sakyi L., Cui X.M., Yuan T.T., Jiang B.G., Yang W.F.,
RA Lam T.T., Chang Q.C., Ding S.J., Wang X.J., Zhu J.G., Ruan X.D., Zhao L.,
RA Wei J.T., Ye R.Z., Que T.C., Du C.H., Zhou Y.H., Cheng J.X., Dai P.F.,
RA Guo W.B., Han X.H., Huang E.J., Li L.F., Wei W., Gao Y.C., Liu J.Z.,
RA Shao H.Z., Wang X., Wang C.C., Yang T.C., Huo Q.B., Li W., Chen H.Y.,
RA Chen S.E., Zhou L.G., Ni X.B., Tian J.H., Sheng Y., Liu T., Pan Y.S.,
RA Xia L.Y., Li J., Zhao F., Cao W.C.;
RT "Large-Scale Comparative Analyses of Tick Genomes Elucidate Their Genetic
RT Diversity and Vector Capacities.";
RL Cell 182:1328-1340(2020).
RN [2] {ECO:0000313|EMBL:KAH8041682.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rmic-2018 {ECO:0000313|EMBL:KAH8041682.1};
RC TISSUE=Larvae {ECO:0000313|EMBL:KAH8041682.1};
RA Jia N., Wang J., Shi W., Du L., Sun Y., Zhan W., Jiang J., Wang Q.,
RA Zhang B., Ji P., Sakyi L.B., Cui X., Yuan T., Jiang B., Yang W.,
RA Lam T.T.-Y., Chang Q., Ding S., Wang X., Zhu J., Ruan X., Zhao L., Wei J.,
RA Que T., Du C., Cheng J., Dai P., Han X., Huang E., Gao Y., Liu J., Shao H.,
RA Ye R., Li L., Wei W., Wang X., Wang C., Huo Q., Li W., Guo W., Chen H.,
RA Chen S., Zhou L., Zhou L., Ni X., Tian J., Zhou Y., Sheng Y., Liu T.,
RA Pan Y., Xia L., Li J., Zhao F., Cao W.;
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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:KAH8041682.1}.
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DR EMBL; JABSTU010000001; KAH8041682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9J6F4G9; -.
DR VEuPathDB; VectorBase:LOC119162276; -.
DR VEuPathDB; VectorBase:LOC119177028; -.
DR VEuPathDB; VectorBase:LOC119180993; -.
DR Proteomes; UP000821866; Chromosome 1.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd11410; bHLH_O_HES; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR017853; GH.
DR InterPro; IPR006047; GH13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003650; Orange_dom.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF07527; Hairy_orange; 1.
DR Pfam; PF00010; HLH; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00511; ORANGE; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF158457; Orange domain-like; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS51054; ORANGE; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000821866}.
FT DOMAIN 880..941
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 959..989
FT /note="Orange"
FT /evidence="ECO:0000259|PROSITE:PS51054"
FT REGION 25..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..242
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..583
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1065
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 122719 MW; C6D5D733BF85C67F CRC64;
MDVESPEPPL ISSTLSVATL RKRFGHPSEA DSEDTLIYST ASDESSDESD SVPVARRKAK
RRLLTTSPSQ SKATPNIQEP PVHTILFAPL NAADSMNRLN RQITSMSLEA LVPGQITDVR
INGRKNESRR YATYCSRRID QVRPFVPKPL QCRKCCKIGH VSAVCTSSAV CSRCSESHNT
EACQAEHRKC GSCQGPHEAS SKQCPNVKKE MHVLRQMARD GSTHREAAAK VRRRRSRHRK
IPRTSSAKAW DTPLPHITHS PPQASTSANT SILRKMQETL TLTRGQRCRA VVIPEKSITI
KFRTSHLTSS TAAELAAIRA ALEFLVGEPQ TGMVSPPSEN AFLLYTTPGG VNVRSWYERY
EPVSYRIASP SGDLQEFADM VRRCKESHVK VFVDVVLNHM TSNIGSGYGY DGTEFNSEAF
AYTGVYSAKD FHSRADCGTA SGLVEDYSNV VQVRNCKFRG RADLNHKLES VRSRITAYLK
QLLSLGVSGF RIDGTDYMWP ADMDIIYRRL SQPDQAKLEL FEAKPAAYRL IETPLDNTPS
DSTSDIPPET PSNTPSEASS DTQPESPSDT SSDAPLDASS DPSVVTAERN TADTETATNV
RKRDTTVEQG GETVSPPHLT SDFDGPFIYH EMSTLNLSWT KEYERIGAVT NATFFKTYAN
ALNRVRERPL KSLRPFVMEA KAAGEAAQVV YVDSHETQRG VDVTDTEGDV VTYRHRKRHV
LATVLMLAQP HGVPRVMSSY DLDRKFETYV PPKTLGPPFD HMFNTKPVLM RENFEWLPIR
NMVSFRNVVA DAAAVNWWDD DADAVAFTRL HRGFVLVNNG PSVVHGLFNT TLPAGYYCDV
LSGSRRDTRT CSGRAVRVRP DGFAELSVDP AAEVPAIALH TQVMKPLMEK RRRARINNCL
SELKRFLMAN DGGTFEKQSS RSQRVEKADI LEMTVKFLRQ RQLQLESDSH DEVERTQRFH
DGYRHCVFEV SRYANAMEPQ LRDTLLTHLQ SRLHHLAAST GGAAIQPAYA DEAVSSTNGD
VPDLQPGRRS PARLHDYGYE AGSVSDVSEE ESSSSDYGDA ASPDAVMFLR SGCQDEPRDY
RLHRDEGLNP DGSNEPMWRP W
//
