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Database: UniProt
Entry: A0A8B8DIT7_CRAVI
LinkDB: A0A8B8DIT7_CRAVI
Original site: A0A8B8DIT7_CRAVI 
ID   A0A8B8DIT7_CRAVI        Unreviewed;      1671 AA.
AC   A0A8B8DIT7;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   18-JUN-2025, entry version 19.
DE   SubName: Full=LOW QUALITY PROTEIN: ATP-dependent RNA helicase DEAH12, chloroplastic-like {ECO:0000313|RefSeq:XP_022327509.1};
GN   Name=LOC111126885 {ECO:0000313|RefSeq:XP_022327509.1};
OS   Crassostrea virginica (Eastern oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=6565 {ECO:0000313|Proteomes:UP000694844, ECO:0000313|RefSeq:XP_022327509.1};
RN   [1] {ECO:0000313|RefSeq:XP_022327509.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole sample {ECO:0000313|RefSeq:XP_022327509.1};
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
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DR   RefSeq; XP_022327509.1; XM_022471801.1.
DR   GeneID; 111126885; -.
DR   KEGG; cvn:111126885; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000694844; Chromosome 3.
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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20335; BRcat_RBR; 1.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR056245; KH_DEAH11/12.
DR   InterPro; IPR056247; KH_DEAH11/12_2nd.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF81; ATP-DEPENDENT RNA HELICASE DEAH11, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF24471; KH_DEAH11; 1.
DR   Pfam; PF24641; KH_DEAH11_2nd; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694844};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          227..390
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          420..596
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1456..1671
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1671 AA;  190073 MW;  6C9A7A96FE5D7AAD CRC64;
     MEREHTDEET NQKDSDGNRQ STEGFPLVDE PENDLDETDT LEKAIVETEE KQSELLERKE
     NSSRNIPKSR RGIQRETLEL KKDKSDKNQK QSFQDRPQEG SVSKEEYKID IKTLQHIQTE
     AEESLRSHQE KKSDTERKIS ALSSKDDKST QKHKEAEKEA LTAKLEELNQ QQGEFQMCLS
     KIINDVELRI GKSIDQEEFN ALMNRFEVES TRLRQALPIY AKRSQIMDTI LQSQVSIILG
     ETGSGKSTQI TQYILESSLS SAGKXVCTQP XKVAAVSLAE RVASELNSKV GELVGYQVGM
     KSMLSKNTKV LYMTDHMLLN ECLKDPLLKD FSCVVIDEAH ERSVYTDLLL GMIKKCLSQR
     RDLRVVVTSA TIDPDVFVKY FGGPELCPVL KVSGRMFPVE IDWLNVSAGT EVVDDYETKA
     IETAADIHRT EPPGDILIFL TSQIEIEQCR GKLHALLQMK KDFLILPLHG KLQADEQNLV
     FQVTPEGKRK IVLATNVAET SVTIPGIKYV VDTGAVKELS YDSSKKVSSL RVVKVTQSSA
     NQRKGRAGRT GPGKCYRLYS QKDYEIMCPT SIPEIQKIHL SHAILKLLQL NVDPLDFDFV
     EAPERISMDN AFQHLSGLGA IKKGKITPLG KWIAKLPFEP NLGVFVHDSI DSNVGVEGII
     IAASCTVSGS LFYRSGTKEQ KEIADKLKVQ FCHKRGDLFT NLCVFKEWYK VDEKRKGKWC
     IDNSINGKAL RIIRDSAKEI MHTLKKDLDI RIEFKFSESV DMERVLQKLL FKSFQNNLCH
     FLGHEKAGYH FIDKNQQVIL HPSSALQSLA SFPEWVIVEN ILQTSMDYAL NVTAVADEDI
     LDALDNRSLK FDFKDVTERK VTQVVTEYVG IQGHKEFVGP RFCKVRAMQE QLLKQHKDAV
     FVIDADRDKG EISIFAPIRD KNIYLQTLKS ALDPIREKIR SETAEHPVIP EIQSVRIVIG
     AGGQIQDVLY HDEFKNVFIF GENPGSNDRI KEWFGQYGSI SSFIPKSQKS RNPKYIGQIT
     YENSESARKA VNATEKGQCD YTASPPKVKA KSDGGDLLRA RLTWCRRKSR GFGFVEILDE
     NKIDMIILSC SSKKVNAGGK YMKIKRKQNE RQDEKKNELY VSGLGESVNE DVLRECFLNN
     FDVSEEDIGK VAIVREKKDT RPEMLQSLKS QLEDAFSNNI ERDMFSVSVM EPKPADFTYQ
     ASITCKDPEK GLEVCSSMQH NLFIEGHSVS ITPEMNTRLS VLTPVYQRIE KEIERYCEKI
     RNETRGRRAT VRRLKNEKYV IDISTDSIES LVDTRNEIQR MLEGEKVNVD RIPDLPHLFT
     RDGQEKVRRV MQKTNTTILL DHRNISVSIH GKTEERVLAL EKIKRYVEKL SSSKVRLYDL
     KGESKPPGLM KAVILKHGKD LQGLKDLSAL TAIELDLRNH RIKMLGSDDA VAKAVEEIDE
     MATQVPGKCS ISITSNEPEC AICLCVIPET EMYRLESCGH PYCKDCVKLN LESTMQRREF
     PLKCCHDVCQ MLWAWKDFIY MTNIGFCSLQ NIIDSSISSH VRENKDKVKY CITPDCPMVY
     KVTENGGRIV CDKCKTGMCS SCHVEYHDGL LCYQYKLSKG NVNYNNECWI QEWMRQDPIN
     RKQCPRCFTG IEKNGGCQHM TCQACTIHIC WTCMETFNSG TECYEHMGTK H
//
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