ID A0A1C7N9U9_9FUNG Unreviewed; 1240 AA.
AC A0A1C7N9U9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DHX38 {ECO:0000313|EMBL:OBZ85830.1};
GN ORFNames=A0J61_06120 {ECO:0000313|EMBL:OBZ85830.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ85830.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ85830.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ85830.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
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}.
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:OBZ85830.1}.
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DR EMBL; LUGH01000354; OBZ85830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7N9U9; -.
DR STRING; 101091.A0A1C7N9U9; -.
DR InParanoid; A0A1C7N9U9; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000093000; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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:OBZ85830.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000093000}.
FT DOMAIN 557..720
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 742..917
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 101..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 141729 MW; C9AF964491B0FFDD CRC64;
MSEDEFIHDI AIDISRALNL TNPNDLIARK VVQFAETNKD FDRFSQVCST FGRFSREFLA
ETYTKINKHR QEKKLAPPNP NAKPVRSDAI KNEVLMLGNN LPGGLITPNK NKSSEADQDR
PIFKVPAVPN KSLLGLDELA RKKRQAEAEK AEREADKKMR LSWDEQEEEQ EEEKQKDDKK
LDEQFSRRHH RPSYRSHRME TPSNPGGVSD SALKRLEEMK RRDRHRSSLH HKVKQPEEPV
TNGSETPRRG GLIKRSQWSS MTPQRGQGSF TPRHTAGNMT PGRHDSGYRM STGANTAAVR
RTWDHMTPSI RSTAYDEVAL EYPEEFTGDD EDRRKWEEEQ AQLDREWYQM EDYGAADDTH
NAFAEYESHD RHREEELTQK QLKKLSARQA QYNRDTDMWE ASRMLSSGVA QRIEVDTDFE
EENENRVHLL VHDIKPPFLD GRMVFTKQLE AVQHVRDPTS DMAIISRKGS RLVREKREQA
ERAKASRFEL AGTTLGNVMG IKEKKEETEG INDDATADSK FASHLKSSEA ASDFARTRTM
REQREFLPAF AVREDLLKVI RDNQVVIIVG ETGSGKTTQL TQYLHEDGYT KYGKVSCTQP
RRVAAMSVAK RVAEEMGCEL GDTVGYTIRF EDQTSEKTLI RYMTDGILLR ESMNSPDLEQ
YSAIVMDEAH ERALNTDVLM GLLKKILARR RDLKLIVTSA TMNAERFSQF FGNAPCFFIP
GRTFPVDVMF SKTSCEDYVD SAVKQTLAIH LSQPAGDILI FMTGQEDIEA TCATLRERLE
QLDDPPPLAI LPIYSQLPAD LQAKIFQRAE NNARKVIVAT NIAETSLTVD GIMYVVDTGY
CKLKVYNPRI GMDALQVTPI SQANASQRSG RAGRTGPGVA YRLYTEDAFR NEMFVNTIPE
IQRTNLASVV LQLKSLGVKN LLEFDFMDPP PQENILNSMY QLWIINAFDN TGDLTDAGRK
MNEFPLDPSL AKMLISAEEQ GCTAEVLTIV SMLSVPSVFY RPKERVEESD AAREKFFVPE
SDHLTLLHVY TQWKINKYRD DWCNKHFIHA KAMRKAREVR SQLMDIMKTI KMPYVSCGTN
WDVIRKCICS AYFHQAARLK GIGEYVNCRS GMKCHLHPTS ALFGAGFTPD YVVYHELVLT
SKEYMQCVTA VDPFWLAEQG PMFFSIRDRD RNYGQKEKRL ANLATESRLN MEMEMKLARE
KEEEEEAKQE RTRINTSRAG RIATPGAREM RTPRRRGLGL
//
