ID R4GBG3_ANOCA Unreviewed; 1075 AA.
AC R4GBG3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=TDRD12 {ECO:0000313|Ensembl:ENSACAP00000022641.2};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000022641.2, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000022641.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000022641.2};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000022641.2}
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; R4GBG3; -.
DR STRING; 28377.ENSACAP00000022641; -.
DR Ensembl; ENSACAT00000030058.2; ENSACAP00000022641.2; ENSACAG00000029615.2.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00420000029847; -.
DR HOGENOM; CLU_008124_1_0_1; -.
DR InParanoid; R4GBG3; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000029615; Expressed in kidney and 4 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042078; P:germ-line stem cell division; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd20435; Tudor_TDRD12_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 2.40.50.90; -; 2.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR22655:SF2; ATP-DEPENDENT RNA HELICASE TDRD12-RELATED; 1.
DR PANTHER; PTHR22655; UNCHARACTERIZED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00567; TUDOR; 2.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS50304; TUDOR; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 57..119
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 601..629
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 920..1004
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT ZN_FING 601..629
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 1075 AA; 123238 MW; 67EA30EB66CA1985 CRC64;
MFEVFIIKIE SPDCFWGSIK GGGNFVDNEM AYKKLQFEMN QFYNLTHRGL DEVKPSVLKE
GQVCVVYSQE ENSWCRAIVE SIISCTDNYL AECFLVDYAK NIPVKAEKIC CALESFMRLP
YRAQKFRLYH IKPVTLRVNY YTNNAEIVPA TKWNIAAIRY FQDLLDAASQ VEAKLCAVED
DTFAVYLYVT KRGEKVCVND DLVAKNFASS EKNEERSIIM EEQNQEILGL ESVSVSEISP
AHILSPTSLD IKEPKAVEMC ECGRLSVDNK RDLKMGLKPI LKIWKKFVGP NHVQSYSWPA
IARGYDSVVI CPENDPLIYL LPIITFLQSR NCYLSLPARN GPVALIICTR QRKAELVFEF
VEKYTHCSRP LHPLLLSVGM NKEEIKSVRI PRGCELIVTT PYSLLRLLEC HSLMFLRLCH
LVLDEAEALF SEANDQVFNI LEHYKRSLND EVKEYVPQQI VAIGSRWTKK LEYLTKEFMN
DPYVVITSLE EAAIYGNIQQ VVQVSLECNR ISILLQTLDF TPHNAQKTLI FTSSVEETDN
ICKVSPLAKE QPKAKSILLL TENSAWHTVG VLDYLKRTEA NIPPELHDFT SGVLDAKENC
KSGKPFCRYL KVYGFCKDKK RCPDRHRISL QVDFPKGERN STQPTAGNVT ILPLFIVDAT
NYFGRIVDKT KDQYTALEKE MHQYYKKSSN CISVSLVEKL ALYGVHEKNY IHRVQVLQIA
PKEGKCVFYS IHVKYIDEGR TGQVQNYQLL SLPEHFQVLP PQAVEFIVCR VKPIDNEAEW
NPKVNRYINH KIKGQLHEAK IVHTLNNTIW VDPVVRVTKL PDLKTYINEY NIRSEILATG
FGVDNPEHIC ELQRLFREAE IAFEKKDMPQ QRTDCFTLLQ QTAIGDINPQ KSLNFRQDAC
SLQRPKPGQL CLYCRKHLRI GPRSIKWFEK EDVVVLKIKV QNITNHDCKF FTQRIIGSAE
GKFYLADLEL QENIVEEKSR CVLRGNEVVV SLAKEKKGSW CRLLKQKNPH VSFDFDYLED
DSEESGFPIS VFLHAFVVVA VAVIFPTTPP SGNSCDSISA YILFVGSWIW FDLVP
//
