ID G3NIY9_GASAC Unreviewed; 2225 AA.
AC G3NIY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Snf2-related CREBBP activator protein {ECO:0000313|Ensembl:ENSGACP00000005299.1};
GN Name=SRCAP {ECO:0000313|Ensembl:ENSGACP00000005299.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000005299.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000005299.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000005299.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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DR STRING; 69293.ENSGACP00000005299; -.
DR Ensembl; ENSGACT00000005314.1; ENSGACP00000005299.1; ENSGACG00000004035.1.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000157457; -.
DR InParanoid; G3NIY9; -.
DR OMA; VCWCSKS; -.
DR TreeFam; TF106424; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000004035; Expressed in head kidney and 10 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
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; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 128..200
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 587..752
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1845..1995
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 29..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2129..2225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2207..2225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2225 AA; 247439 MW; 2ED2374D1EC0A5CB CRC64;
CASSSSALAP HSPGYEVSQW IADRINENAS PVSPATFPSY PGPSPSSDWS SQRRDKSSPL
RGPHGKFVSP ISVGGYSSCS SSPDQAATPQ RPRGERHTGM AELAKHEADI EHRTQSLKRE
GFWSTKRLTR LTEPPRPKVH WDYLCEEMQW LSADFAQERR WKRGVARKVV RMVMRHHEDL
RQKEEKAKRD EHSKIRRVAS SIAKEVRAFW SSVEKVVQYK QQSRLEEKRK KALDLQLDFI
VGQTEKYSDL LSQSLAPAET EPEHVSPTPQ KSAPSAADED AAGASDLSDE SYYRDFEPPC
EEEDDEETIE VEEQQEGNDA ESHRREIELL KEEGLLPLDQ LLSTLKLPQV PTGYSLYSLS
PKYFNTNVNN GNEAGSDEEC SDVTSSSVEE DGEFTANEED AQDEEDTIAA QEKVEGQVDH
AEELDDLARE GDMSVEELLE KYKGAYASDF EAPSASGSKD SSDSEVSGDE EEETDEDESD
AETNSSSSGY LYLSLNNFTY LSDSQGDSGA EDDSGDEGME VLLKEGDNSP PSSSSRPKKE
ISHIAATAES LQPKGYTLAT TKVKTPIPFL LHGTLREYQH IGLDWLVTMY EKKLNGILAD
EMGLGKTIQT IALLAHLACE KGNWGPHLII VPTSVMLNWE MELKRWCPGF KILTYFGSQK
ERKLKRQGWT KPNAFHVCIT SYKLVLQDHQ AFRRKSWRYL ILDEAQNIKN FKSQRWQSLL
NFNSHRRLLL TGTPLQNSLM ELWSLMHFLM PHVFQSHREF KEWFSNPLTG MIEGSQEYNE
GLVKRLHKVL RPFLLRRIKI DVEKQMPKKY EHVVRCRLSK RQRFLYDDFM AQASTRETLA
SGHFMSVINI LMQLRKVCNH PNLFDPRPIQ SPFITKPIVF HTASLVQDAL EVSPLKRAQR
CDLSMFDLVG LESRVSRYQA DVFLPRHKVR RQLIQEILES PDPPPRPRPV RMKVNSRMFQ
PPPKSENRPV LLMNKPTCSV PPAAQNPKPP PVPEVSAAPQ TAPQTAPQPA PQTAPVVQQG
NWSWPRLPRP ARVSLTLMEI YCFSLIKIFP PPQVVCTVTT AAAPRPSMHP TAQIAVRSGA
PRPVLTVRPP AASCAAGIPV HPGPNPGSVL PQRVLLSPDM QARLPSTSAG EVVSIAQLAS
LAGRPVSSCQ GSKPVTFQLQ GNKLTLSGAQ IHQVPGASPR PVQGNVMHLV SSGVQHHLIS
QPAQVAVQGN TPSTVPPTNR LALNASAPPL SYCSSGSASK LNLFPYPQLL QRNISNSLGF
SPRVTLIQLQ TKILIYPLRS LVSQLCFHVS SVPPSIMSSP GVVKIVVRQA AGKDGGPVPT
LAVAPSPRVA SLTSLHPHTN TTPVRTAAPL QIAQRTPGPA TATAHYTIAP PGNPGPTPSQ
PHPPRPVLKV VQPPPSSAER PGERERGRFA CVTRRTVSQQ CSRGPHVLRR TGSLLVSQES
QALTERNYFT PPQSSLSQII LKRSFLSPAQ LWSRWPARLL HPSPQRLCGK AAVKRRSPQS
RGRVPALRPS LPPGECPGSL PALRSTRGLC SCSLPRLLTS RPPPFLFSTE VARGRTQAAA
RQPPGLHHSS QREPLRGQTR IRPGGFRLPD IPPRATTCAG PPAPSEGVGS LGPQQRSALA
VGEQIQLHVP ESCCERGHPQ RGGPAGAAQR RRGQVDILEL SFLSGWVLLL DENSTVTVLR
GHKSLKEMLL YFFDNLAVYI CVLQVKIKIT LPLTFVWLFV FLKEGLVTRD VFMSRKNNLM
FLFSTASGWY KPSSFWDTER AVFYLSLTIV SFRFTFAIPP VEAPQISIHC CHPPPSLSHK
QAVFSSQLST QVTPLTRSLH RIQCYMRTQF PDLRLIQYDC GKLQTLHTLL RKLKTGGHRV
LIFTQMTRML DVLEQFLNYH GHIYLRLDGS TRVEMRQSLM ERFNADRRIF CFILSTRSGG
VGVNLTGADT VVFYDSDWNP TMDAQAQDRC HRIGQTRDVH IYRLISERTV EENILKKANQ
KRMLGDMAIE GGNFTTAFFK QFLSKPIREL FDMSEGEKRE AAVELSVTPA EEEETVNKQS
TTILEQALCR AEDEEDIVAA SQAKAEQVAE LAEFNENIPL DDGGEQEEVE ELSKAEQEIA
ALVEQLTPIE RYAMNFLETS LEDVCKEELK QAEEQVEAAR KGLDQAKEEG LKLHASSDED
NDDFLSPPAS VEPSQPARRG RKPKDKAVSS TRTSGRLRGA SPEAEPEPTR PTAPTPPTTA
TPTAP
//
