ID A0A2Y9QH07_TRIMA Unreviewed; 2312 AA.
AC A0A2Y9QH07;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=LOC101352430 {ECO:0000313|RefSeq:XP_023580758.1,
GN ECO:0000313|RefSeq:XP_023580759.1, ECO:0000313|RefSeq:XP_023580760.1,
GN ECO:0000313|RefSeq:XP_023580761.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023580761.1};
RN [1] {ECO:0000313|RefSeq:XP_023580758.1, ECO:0000313|RefSeq:XP_023580759.1}
RP IDENTIFICATION.
RG RefSeq;
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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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 RefSeq; XP_023580758.1; XM_023724990.1.
DR RefSeq; XP_023580759.1; XM_023724991.1.
DR RefSeq; XP_023580760.1; XM_023724992.1.
DR RefSeq; XP_023580761.1; XM_023724993.1.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR PANTHER; PTHR46850:SF3; DNA HELICASE; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 2.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 445..511
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 544..718
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 858..1009
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1930..1958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2164..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2211..2312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2225..2241
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2246..2260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2266..2284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2312 AA; 263334 MW; 7C6411114C1E9097 CRC64;
MKGESKRITL VLQQPQSGGP QGHRHVVLGS LPGKIVLQGN QLAALTQAKN AQGQPAKVVT
IQLQVQQPQQ KIQIVPQPPS SQPQPQQPPS TQPVTLSSVQ QAQLMGPGQS PGQRLSVPLK
VVLQPQAGSS QGASSGLSVV KVLSASEVAA LSSPASSAPH TGGKTGMEEN RRLEHQKKQE
KANRIVAEAI ARARARGEQN IPRVLNEDEL PSVRPEEEGE KKRRKKSSGE RLKEEKPKKS
KTSGTSKTKG KSKLNTITPV VGKKRKRNTS SDNSDVEVMP AQSPREDEES SIQKRRSNRQ
VKRKKYTEDL DIKITDDEEE EEVDVTGPIK LEPILPEPVQ EPDGETLPSM QFFVENPSEE
DAAIVDKVLS MRVVKKELPS GQYTEAEEFF VKYKNYSYLH CEWATISQLE KDKRIHQKLK
RFKTKMAQMR HFFHEDEEPF NPDYVEVDRI LDESHSIDKD NGEPVIYYLV KWCSLPYEDS
TWELKEDVDE GKIREFKRIQ SRHPELKRVN RPQASAWKKL ELSHEYKNRN QLREYQLEGV
NWLLFNWYNR QNCILADEMG LGKTIQSIAF LQEVYNVGIH GPFLVIAPLS TITNWEREFN
TWTEMNTIVY HGSLASRQMI QQYEMYCKDS RGRLIPGAYK FDALITTFEM ILSDCPELRE
IEWRCVIIDE AHRLKNRNCK LLDSLKHMDL EHKVLLTGTP LQNTVEELFS LLHFLEPSQF
PSESEFLKDF GDLKTEEQVQ KLQAILKPMM LRRLKEDVEK NLAPKQETII EVELTNIQKK
YYRAILEKNF SFLSKGAGHT NMPNLLNTMM ELRKCCNHPY LINGAEEKIL TEFREACHII
PHDFHLQAMV RSAGKLVLID KLLPKLKAGG HKVLIFSQMV RCLDILEDYL IQRRYLYERI
DGRVRGNLRQ AAIDRFSKPD SDRFVFLLCT RAGGLGINLT AADTCIIFDS DWNPQNDLQA
QARCHRIGQS KAVKVYRLIT RNSYEREMFD KASLKLGLDK AVLQSMSGRD GNITGIQQFS
KKEIEDLLRK GAYAAIMEED DEGSKFCEED IDQILLRRTT TITIESEGKG STFAKASFVA
SENRTDISLD DPNFWQKWAK KADLDMDLLN SKNNLVIDTP RVRKQTRHFS TLKDDDLVEF
SDLESEDDER PRSRRHDRHH AYGRTDCFRV EKHLLVYGWG RWRDILSHGR FKRRMTERDV
ETICRAILVY CLLHYRGDEN IKGFIWDLIS PAENGKTKEL QNHSVFDVSP SPGLSIPVPR
GRKGKKVKSQ STFDIHKADW IRKYNPDTLF QDESYKKHLK HQCNKVLLRV RMLYYLRQEV
IGDQAEKVLG GAIASEIDIW FPVVDQLEVP TAWWDSEADK SLLIGVFKHG YEKYNTMRAD
PALCFLEKAG RPDDKAIAAE HRVLDNFSDI VEGVDFDKDC EDPEYKPLQG PPKDQDDEGD
PLMMMDEEIS VIDGDEAQVT QQPGHLFWPP GSALTARLRR LVTAYQRSYK REQMKIEAAE
RGDRRRRRCE AAFKLKEIAR REKQQRWTRR EQTDFYRVVS TFGVEYDPDT MQFHWDRFRT
FARLDKKTDE SLTKYFHGFV AMCRQVCRLP PAAGDEPPDP NLFIEPITEE RASRTLYRIE
LLRRLREQVL CHPLLEDRLS LCQPPGPELP KWWEPVRHDG ELLRGAARHG VSQTDCNIMQ
DPDFSFLAAR MNYMQNYQTG APAPSLSRCS TPLLHQQYTS RTASPLPLRP DVPVEKPPEE
TAAQIPSLES LTLKLEHEVV ARSRPTPQDY EMRVNSSDTA PLVSRSVPPV KLEDEDDSDS
ELDLSKLSPS SSSSSSSSSS SSTDESEDEK EEKLTADRSH SKLYDEESLL SLTMSQDGFP
NEEGEQMTPE LLMLQERQRA SEWPKDRVLI NRIDLVCQAV LSGKWPSSRR NQEMVTGGIL
GLGNHLLDSP SLTPGEYGDS PVPTPRSSSA ASMAEEEASA VSTAAAQFTK LRRGVDEKEF
TVQIKDEEGG LKLTFQKHKL MANGVMGDGH PLFHKKKGNR KKLVELEVEC MEEPNHLDVD
LETRIPVINK VDGTLLVGED APRRAELEMW LQGHPEFAVD PRFLAYMEDR RKQKWQRCKK
NNKAEFNCLG VEPVQTANSR NGKKGHHAET VFNRVLPGPV APESSKKRSR RMQPDLSKMM
ALMQGGGPGS LSLHNTFQHS SSGLQSVSSL GHSSATSASL PFMPFVMGGA ASSPHVDSST
MLHHHHPHPH PHHHHHHHPG LRATGYPSSP ATTTSGTALR LPPLQPEEDD EDEDEDDDDD
LSQGYDSSER DFSLIDDPMM PANSDSSEDA DD
//
