ID A0A3Q3BB23_KRYMA Unreviewed; 1105 AA.
AC A0A3Q3BB23;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000026356.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000026356.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR AlphaFoldDB; A0A3Q3BB23; -.
DR STRING; 37003.ENSKMAP00000026356; -.
DR Ensembl; ENSKMAT00000026695.1; ENSKMAP00000026356.1; ENSKMAG00000019498.1.
DR GeneTree; ENSGT00940000156903; -.
DR Proteomes; UP000264800; Unplaced.
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:SF237; ATP-DEPENDENT DNA_RNA HELICASE DHX36; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 320..490
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 581..751
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 124625 MW; 3A8D26ED9E7602EF CRC64;
MSYGYGGGGG RRGRRGGRGH RDGSRERMDR GGGGGVGSRG HSSFDFDQDR GGGGGGQKDR
PPPHLRGREI GLWYARYGAV RRKQADRRSR AVVQMDEARE EHITKLLNSV QNDQSGPRRV
GRESSTSVSD SWQTAATHSG HCYFDGDLPE EEKYKVEVKS DEEEEDITPG QKKASKRNVS
KAAVKDEAPD NWDEEDQDEE TKEEKPLRRD KDLEFLFQEV VRDNSKDEYL QRDLHSKKSD
SKYKEMLKFR EKLPSYGKKE ASVNFIQLKA NTEHHFYLTL NCFCFVQIII HLLCFRHSSL
PSSSLHSRSS SPHLYPQELV ELINSNRVLV VSGETGCGKT TQVTQFILDD HINRGVGSMC
RVVCTQPRRI SAISVAERVA AERAESVGNG NSCGYQIRLQ SRLPRRQGSI LYCTTGIILQ
WLRSDPLLSS ISHLVLDEIH ERNLQSDVLL IIVKNLLKVR NDLKIILMSA TLNAEKFSKY
FDNCPMIHIP GLTFPVEEYL LEDIVEMTRY CPQSQDRRSS WKKSFWQGRN SRPEKEEKER
EYQESWPCYA RTLQGRYSDS TIQALEMLDG DEKIDLELIL ALIRHIVLNE GEGAILVFLP
GWDNISTLND LLTAQQMFRS DNFVIIPLHS LMPTVNQTQV FKRPPPGVRK IVIATNIAET
SITIDDVVYV IDGGKIKETN FDTNNNISTM TAEWVSLANA KQRKGRAGRV QPGKCYHLYN
GLRASLLDAY QLPEIMRTPL EELCLQIKIL KLGSIGQFLE KALDPPSKKA VALAIKNLTD
LNALDHTENL TALGFHLARL PVEPHIGKLI LFGALLGCLD PVLTIAASLS FKDPFFIPLG
KEKMADMRRR VLSRNSKSDH LTIVNAVTGW EEAKRRGARS EKDYCWDNFL SANTLQMLHN
MKGQFAEHLM HTGFVSSSDP KDPTSNINSG NKEMTSSSDC LVDQTSVLWI STHQISLPLS
RLLSDNEKLI KAVIVAGLYP KVAMIRPSFS KKRPGVKVYT QADGKVCIHP KSVNAEENDF
NYTWLIYHLK MRTSSIFLYD CTEVSPFSLL FFGGDITIQK DEGQETIAVD QWIVFRSPAR
IAHLVKVCEA PAQISCSALL IFTES
//
