GenomeNet

Database: UniProt
Entry: A0A151MSB9_ALLMI
LinkDB: A0A151MSB9_ALLMI
Original site: A0A151MSB9_ALLMI 
ID   A0A151MSB9_ALLMI        Unreviewed;      2146 AA.
AC   A0A151MSB9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=Y1Q_0021242 {ECO:0000313|EMBL:KYO27319.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO27319.1};
RN   [1] {ECO:0000313|EMBL:KYO27319.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO27319.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO27319.1}.
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   EMBL; AKHW03005226; KYO27319.1; -; Genomic_DNA.
DR   STRING; 8496.A0A151MSB9; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   Proteomes; UP000050525; 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: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; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
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:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   Pfam; PF07533; BRK; 2.
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; SSF160481; BRK domain-like; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
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   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:UP000050525};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          232..295
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          315..381
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          414..588
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          728..884
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1003..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1571..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1747..1780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2073..2146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1581..1606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1607..1633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1634..1655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1660..1679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2085..2125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2146 AA;  245260 MW;  302AACB870FE0C00 CRC64;
     MHPWHSSVSN QHVQGRNRVT LQGQPPSSKK TDGSGAYTKL QNTQVRAMSE KKQKKKVESE
     SKQEKANRII SEAIAKAKER GERNIPRVMS PENFPSVSAE GKEEKKGRKI KSKPKDKESK
     KPRTGSSSKI KEKTKIGKLI ITLGKKQKRK NESSDELSDA KQTPQRSFKD EDLQKRRSNR
     QVKRKKYAEE GEGKQSEEEA KVSVKIKKNS APLPAEQPLQ LFVENPSEED AAIVDKILSS
     RIVKKEVSAG VTVEAEEFFV KYKNYSYLHC EWATEQQLLK DKRIQQKIKR FKLRQAQRAH
     FFADMEEEPF NPDYVEVDRV LEVSFCEDKD TGEPVVYYLV KWCSLPYEDS TWELKEDVDQ
     AKIEEFEQLQ ASRPDSRRLD RPPPNSWKKI EHSREYKNGN QLREYQLEGL NWLLFNWYNR
     RNCILADEMG LGKTIQSITF LYEILLTGIR GPFLIIAPLS TITNWEREFR TWTDINVVVY
     HGSMVSRQMI QQYEMYFRDS QGRIIRGTYR FQAIITTFEM ILGGCPELNA IEWRCVIIDE
     AHRLKNKNCK LLEGLKLMNL EHKVLLTGTP LQNTVEELFS LLHFLEPLRF PAESTFMQEF
     GDLKTEEQVQ KLQAILKPMM LRRLKEDVEK KLAPKEETII EVELTNIQKK YYRAILEKNF
     AFLSKGAGQA NVPNLVNTMM ELRKCCNHPY LIKGAEEKIL GEFRETHSPT APDFHLQAMI
     HSAGKLVLID KLLPKMKAGG HKVLIFSQMV RCLDILEDYL IHKRYLYERI DGRVRGNLRQ
     AAIDRFSKPD SDRFVFLLCT RAGGLGINLT AADTCIIFDS DWNPQNDLQA QARCHRIGQN
     KAVKVYRLIT RNSYEREMFD RASLKLGLDK AVLQSMSGRE NSVGGIQQLS KKEIEDLLRR
     GAYGAIMDEE DEGSKFCEED IDQILQRRTK TITIESEGRG STFAKASFVA SGNRTDISLD
     DPNFWQKWAK KAEIDIEAIS GRNSLVIDTP RIRKQTRPFS ATKDELAELS EPESEGDEKP
     KLRRPCDRSS GYGRTECFRV EKNLLVYGWG RWREILSHGR FKRQLNEQDV EIICRALLAY
     CLVHYRGDEK IKSFIWDLIT PTEDGQTREL QNHLGLSAPV PRGRKGKKVK TQASTFDIHK
     AEWLRKYNPE HLLQDEGYKK HIKHHCNKVL LRVRMLYYLK QEVIGNDFQK VFDGADASEI
     DIWVPEPDHS EVPAEWWDAD ADKSLLIGVF KHGYEKYNTI RADPALCFLE RVGKPDEKAV
     AAEQRANDYI DGDVEDPEYK PAPAMFKDDM EDDVSSPGDL VIADGDGQMM EGDKIYWPTQ
     SALTTRLRRL ITAYQRTNKN RQTQQIQPAF PVQASMMQPS YEEAALNPKM AAKIERQQRW
     TRREEADFYR VVSTFGVVFD PDRGRFDWTK FRAMARLHKK TDESLEKYLY AFMSMCRRVC
     RLPSKEELVD PGIFIQPITE ERASRTLYRI ELLRKVREQA LRHPQLFERL KLCQPNPDLP
     VWWECGTHDR DLLIGAAKHG VSRTDYHILR DPELSFMSAQ RNYSQNKVAL SRTSTPLLHQ
     YQMALSASPL ASQARLPDAK GNALEDTKAK NENVKEEPHS SEEESMSTEE IQTGMKSESL
     SPKNGTPSQT TNHKPKSDSD EEAQKRAEGT PHMKAYDEES VASLSTTQDE TQDSFQLNNG
     TQNSTYLLQG GYMLAASYWP KDRVMINRLD SICQTVLKGK WPSARRSYDN NTVASFYTTK
     LLDSPGAAAD YSEPSAPTPP SAGVKEERDQ SPQMSKVKKH VREKEFTVKI NDEGGLKLTF
     QKQGLSQKRP FESEEGTLGQ QQYLARLREL QNASETSLVN FPKSLPESGT SSQLTASANG
     VIADSQPVVK KRRGRRKNVE GVDILFINRN KQPNHVSPGI NTSQIAPGIN PTFTFAQSQS
     LLDEESPVPV INLKDGTRLA GDDAPKRKDL EKWLKEHPGY VEDLGAFIPR MQLHDGRPKQ
     KRHRCRNPNK LDVNSLTGEE RVQLINRRNA RKVGGAFAPP LKDLCRFLKE NPEYGVAPEW
     GEVVKQSGFL PEGMLLTPGL NLHIPALSQS NIFDVQNSEN NDTGSVKPTE EKEENSRIRD
     QEDKGGTEPS SHNENSTDEG SEKADASSGS DSTSSSSEDS DSSDED
//
DBGET integrated database retrieval system