ID A0A195D3R1_9HYME Unreviewed; 1132 AA.
AC A0A195D3R1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=ALC62_01734 {ECO:0000313|EMBL:KYN07532.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN07532.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN07532.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN07532.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN07532.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; KQ976885; KYN07532.1; -; Genomic_DNA.
DR RefSeq; XP_018405264.1; XM_018549762.1.
DR AlphaFoldDB; A0A195D3R1; -.
DR STRING; 456900.A0A195D3R1; -.
DR GeneID; 108781703; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KYN07532.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000078542}.
FT DOMAIN 448..611
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 625..808
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 129181 MW; B5B7B94043777EF0 CRC64;
MSDDLSLYRL EGSGTNEGGG LIIRKKTSDH TFKKPSMLGL DKLAEQKRRA QSQDPTSSKS
NKSEGKDRRY RSYEEETPTH TGGVNSEAQQ RLESRLKRQR LSADDRNSRN LYRSRERDRD
RRRDRDRESR GRDSSIRQTP LRFKDEPQTP KFRTKDPTSK SNWDDDEDEE PKRSSWDHPT
PNLYTNRDGR DSIRSEFTPS YKYNSWNKDF KSSGVTPIID GEEKEMWEEE QQRLDREWYA
LDDGENNAFA NVSEEYTRKK EMELEARRQK RLSAQQRQIN KDNELWERNR MLTSGVVSSL
DHDDDPDDEG EARVHLLVHN VVPPFLDGRI VFTKQPEPVV PVRDPTSDMA LVARKGSALV
KAYREQKERR RAQKKHWELA GTHIGNIMGV HDRRKDDKEH AGQETDFKAG QKYARHIGSG
EVTGEAKYKS IQHQRRSLPV FAVRQELLNV IRENSVVVIV GETGSGKTTQ LTQYLHEDGY
SRYGIIGCTQ PRRVAAMSVA KRVSDEMATA LGDKVGYAIR FEDCTSKDTV IKYMTDGILL
RESLREGDLD RYSVIIMDEA HERSLSTDVL FGLLREVVAR RHDLKLIVTS ATMDCSKFSA
FFGNAATFEI PGRTFPVEVM HAKNPVEDYV DAAVKQVLQI HLQPKSGDVL VFMPGQEDIE
VTCEALKERL AEIESAPLLS ILPIYSQLPS DLQAKIFQRS EGGLRKCVVA TNIAETSLTV
DGIVFVVDSG YCKLKVYNPR IGMDALQVYP VSRANADQRQ GRAGRTGPGQ CFRLYTRRQY
MDELLLTGVP EIQRTNLANT VLLLKSLGVQ DLLAFHFMDP PPQDNILNSL YQLWILGALD
HTGRLTPLGR QMAEFPLDPP QCQMLIVASQ LGCTADILII VSMLSVPSIF YRPKGREEDS
DSAREKFQVP ESDHLTYLNV YNQWKANGYS SSWCNDHFIH AKAMRKVREV RSQLEEILKQ
QKMDVVSCGT DWDIVRKCIC SAYFHQAARL KGIGEYVNCR TGMPCHLHPT SALFGMGFTP
DYVVYHELVM TAKEYMQCVT AVDGHWLAEL GPMFFSVKET GRSGRAKRRQ AMQHLHEMEH
QMKEAEEEMK ARAQEQLERE QASVRKKEIL TPGIREPGTP APYRNTPGRL GL
//
