ID   A0A452GH00_9SAUR        Unreviewed;       885 AA.
AC   A0A452GH00;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51193};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000000861.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000000861.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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; A0A452GH00; -.
DR   Ensembl; ENSGAGT00000000978.1; ENSGAGP00000000861.1; ENSGAGG00000000211.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT   DOMAIN          8..433
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          77..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  100193 MW;  569DA345F672CB32 CRC64;
     RSAAVGKGRV NFPFPYTPYS IQEDFMANLY DVLEAGKVGI FESPTGTGKS LSLICGALSW
     LRDFEEKKKQ EEARLLADEH SGQDKQQQPT SCSAEASNCQ GSAGELVWIT EFMQKKEEQA
     MVDRLKEEQI RRKKREDRLE KIRHNVQLKY ASKRKRLEDD ETQRLLQLSK EILSTELGSD
     VLEQLDHEEE ELILAEYESD EEKKGRQTAL LEFLQSSFSF SSQIYYCSRT HSQLAQFVHE
     VQKSPFGEEI RLVSLGSRQN LCVNEEVRHL GAVQLINDRC VEMQKNKHEE SEGKKRRVSR
     AVCPFYSYEQ MQFLRDEVLV KVKDIEQLVA LGKETKACPY YGSRYAIPAA QLVVLPYQML
     LHESTRCASG IKLKDQVVII DEAHNLIDTI TCIYSAEVRG SQLCCAHSQL LQYMERYRKR
     LKAKNLMYIK QILYLLERFV SILGGNVNQN PNAQSISQAG TELKSINDFL FQSQIDNINL
     FKLFGFVERY GATSVVKINK EKQKMAGLQN FLLTLHQGPD KGEFRCRVED GQPKMASPLM
     QIEGFLSALT SANQDGRVIL NRQGTVAKSS LKFLLLNPAV HFAKVLKECR AAIVAGGTMQ
     PVSDFREQLL SCAIGADRVV EFSCGHVIPP DNILPIILCS GPSNQQLEFT YQKRDLPHMM
     DEMGRILGNL CNVVPGGVVC FFPSYEYEKQ VYTHWEGTGL LTRLATKKKI FQEPKKANQV
     EQVLAEYTKC IKRCSQVGGH VTGALLFSVV GGKMSEGINF SDDLGRCVVM VGMPYPNIKS
     PELQEKMAYL DKTMPRTAGQ PPSKMLIENL CMKAVNQSIG RAIRHQKDFA SILLVDHRYA
     RPSVFNKLPQ WIKERTEIKY TFGLAFAALR KVSQKPPEGD GRALC
//