ID   A0A3Q1H996_9TELE        Unreviewed;      1248 AA.
AC   A0A3Q1H996;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=BRCA1 interacting protein C-terminal helicase 1 {ECO:0000313|Ensembl:ENSAPOP00000025340.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000025340.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000025340.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1H996; -.
DR   Ensembl; ENSAPOT00000006530.1; ENSAPOP00000025340.1; ENSAPOG00000008346.1.
DR   GeneTree; ENSGT00950000182970; -.
DR   Proteomes; UP000257200; Unplaced.
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; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 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; 2.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          11..452
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          118..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1092
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1118
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1175..1201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1248 AA;  139235 MW;  56FE2667CC530A19 CRC64;
     MATSRVEYTI GGVKIHFPCK AYPSQLAMMN SIVRGLNYGQ HCLLESPTGS GKSLALLCSA
     LGWQKAQCVK MQEGRSSVKD KSLSDAPTPC QCVCHSKPSK TVDTAATKPA VVDLTVSPCK
     ETAQPPPPAP KHMSLPEESQ PKEKSIASRL SEKFRASHNC EKDDDFQPDR KRIRTAEIKS
     RKKQRLEQGV VFIDDEPEQE NEPAGPQDWS TETNSQAPCL PSSCSDPEPC SRCPCASAKD
     GVKDKDKDGS KKIPKIFFGT RTHKQITQIT HELKRTVYSH VPMTILSSRD HTCVNQEVAP
     HSNHNERCKD LLDAKDGRSC RYYHGVQKMR DQYTLQHVHG LHDAWDIEEL VTLGKRLRSC
     SYYAARELME SASIIFCPYN YLLDPMIRES MDIDLAGQIL VLDEAHNIED CARESASFTL
     QYNSLLMSRD ELDGMVNSNI RRSSHEPLRD FCYSLINWIQ ESQSLMSERG YESASKVWSG
     KDILSIFHGL GITAGTFSIL KQNLAEVLEK EERVGVVNGR DDMVQVPTIS TATATVLKNL
     FMVLDFLYRD NCRFAEDYRV ALQKTYAWTN QVPPDVPDAQ GFFVRPRHRQ RQSVRVKAEV
     LTLSFWCLNP AVAFSDLSGS VHSIVLTSGT LSPMGSFSSE LGVKFSIQLE ANHVINKSQV
     WVGTVGAGPQ GKKLCATFQH TETYTFQDEV GALLLHVCQV MAKGVLCFLP SYKMLDKLRD
     RWTNTGLWEK LEQQKTVITE PRGGAKGDFD ELLQTYYDAI KYCEGRDGAL LIAVCRGKVS
     EGLDFTDDNA RAVVTIGIPF PNIKDLQVEL KMKYNDQHCS SRGLLPGHRW YEIQAYRALN
     QALGRCIRHR NDWGALILVD DRYRNNPNKY ITGLSKWVRQ LVQHHDTFHN AMQSLAAFSQ
     GQQKVEVASV SAELSPTASS PSPHLVATVE EQSLPKASEL RIPSSCVKPP EPQPDTSPSV
     CHFFSLTQLK GEENKKTEQL KMPHVPPAEP RSRPKTTDQA LFPIFTSSSI STSFKKPIFR
     RRALDNSSQP LETFNHPEDK ENHQISSPPL KTDGVCLEQK AGNNSSEINV ESSCQAPQSS
     TGTAPPCYKS ESASSDDSDD EDQTIFFTPE LFEEEDDEGS PQKEMKTESP SWMVFKTESP
     ALLSEELFGS EQAQGQASAF DGQSAISVSK KSTELSQGQK EEIRGQKQGE EREEVETQNR
     QTGSKLRRLS RSKQKAPCTS TVLQGFFPSK SFGSGICVQL SFPVLSLA
//