ID G3THB9_LOXAF Unreviewed; 3042 AA.
AC G3THB9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Snf2 related CREBBP activator protein {ECO:0000313|Ensembl:ENSLAFP00000013943.4};
GN Name=SRCAP {ECO:0000313|Ensembl:ENSLAFP00000013943.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000013943.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000013943.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013943.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000013943.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013943.4};
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; 9785.ENSLAFP00000013943; -.
DR Ensembl; ENSLAFT00000016610.4; ENSLAFP00000013943.4; ENSLAFG00000016601.4.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000157457; -.
DR HOGENOM; CLU_000315_12_2_1; -.
DR InParanoid; G3THB9; -.
DR OMA; FWTFTEA; -.
DR TreeFam; TF106424; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; 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; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
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 PRINTS; PR00929; ATHOOK.
DR SMART; SM00384; AT_hook; 3.
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:UP000007646}.
FT DOMAIN 106..178
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 622..787
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1865..2018
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2035..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2458..2895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2911..3042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..2183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2229..2252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2262..2336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2490..2525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2567..2582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2583..2639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2689..2703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2744..2759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2781..2795
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2798..2815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2836..2866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2867..2892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3042 AA; 325503 MW; AD61F35388C3DD84 CRC64;
MVSDGMTGSN PVSPASSSSP ASSGAGGLSP QHLAQDSSLD GPPGPPDGAT VSLEGLSLPQ
AADLVNKGPK WEKSHAEIAE QAKHEAEIET RIAELRKEGF WSLKRLPKVP EPPRPKGHWD
YLCEEMQWLS ADFAQERRWK RGVARKVVRM VIRHHEEQRQ KEERARREEQ AKLRRIASAM
AKDVRQFWSN VEKVVQFKQQ SRLEEKRKKA LDLHLDFIVG QTEKYSDLLS QSLNQPLASS
KAGSSPCLGS SHTGSAASSP PPPASRLDDE DGDFQPQEEE EDDEETIEVE EQQEGNDAET
QRREIELLRR EGELPLEELL RSLPPQLLGG PSSPSQTPSS HDSDTRDEPE EGGEEEPSQV
LKGKPPPSSV TQRNKQPWHP DEDDEEFTAN EDEAEDEEDT IAAEEQLEGE VDHAMELSEL
AREGELSMEE LLQLYAGAYA SDTSAAGSGS SEEEEEEEEV EPNTSDCEPE EGTEAEEAPQ
ENSSSQSDSA EEQSEDEEDE HSEEEETTVS SESEESESED SEEAQSQSQA DEEEEEDDDF
GVEYLLARDE EQNEADGGSG PPTPGPTTTL GPKKEITDIA AAAESLQPKG YTLATTQVKT
PIPLLLRGQL REYQHIGLDW LVTMYEKKLN GILADEMGLG KTIQTISLLA HLACEKGNWG
PHLIIVPTSV MLNWEMELKR WCPSFKILTY YGAQKERKLK RQGWTKPNAF HVCITSYKLV
LQDHQAFRRK NWRYLILDEA QNIKNFKSQR WQSLLNFNSQ RRLLLTGTPL QNSLMELWSL
MHFLMPHVFQ SHREFKEWFS NPLTGMIEGS QEYNEGLVKR LHKVLRPFLL RRVKVDVEKQ
MPKKYEHVIR CRLSKRQRCL YDDFMAQTTT KETLATGHFM SVINILMQLR KVCNHPNLFD
PRPVTSPFIT PGICFSTASL VLQATDVHPL QRIDMGLFDL IGLEGRVSRY EADTFLPRHR
LSRRVLLEVA TAPDPPPRPK PVKMKVNRML QPVPKQEGRT VVVVNSPRTP LGPVPVRPPS
GPELSAQLTP GSTPPVLPAP LMVSASTTGS PLIPASRPPG PLLLPPLQPN SGPLPQAGEV
VSIGQLASLA QRPVASTGGS KPLTFQIQGN KLTLTGAQVR QLAVGQPRPL QMPPTMVNNT
GVVKIVVRQA PRDGLTPVPP LAPAPRPPSS GLPAVLTPRP TLTPGRLPTP ALGTSRAPIS
TPTLVRPLLK LVHSPSPEVT ASAPGAAPLT ISSPLPVPSS LPGPASSPMP VPNSSPLASP
VSSTVPVPAP VSSSLPISVS TTLPASASAP LTIPISASLP ASASGPALLT TVTPTLAPVV
SAVPGSPSLA PAGASPSASA LTLGLATAPS LSPSQAPGHP LLLAPTSSHV PGLNSTVAPA
CSPVLVPASA LANPFPAAPN PAPAQASLLA PAPSTSQTLA TSLAPMAAPQ TAILAPSPAP
SLAPLPVLAS SQTPVPVLAP SSTPGTPLVS TSSLVPAPTP VLASSSAQTM VSAPVPPPLP
SLASTQTLAL APALASTLSG SSPSQTHSLG TGNPQGAFPA QTLSLTPASS LVPAPAQTLS
LAPGPPLGPT QTLSLAAAPT LAPASPVGLS PAHTLTLAPA SSSASLLAPA SVQTLALSPT
QVPVPTLGPA AASTQAPTSQ PSSLVASTSG SAPFPVTMVS RLPVPKDEPE TLTLRSGPPS
PPSTATSFTG PRPRRQPPPP PRSPFYLDSL EEKRKRQRSE RLERIFQLSE AHGALAPVYG
TEVLDFCTLP QPVASPIGPH APGPNHPTFW TFTEAARRAV LFPQQRLDQL SEIIERFIFV
MPPVEAPAPS LHACHPPPWL APRQAAFQEQ LACELWPRAR PLHRIVCNMR TQFPDLRLIQ
YDCGKLQTLA VLLRQLKAEG HRVLIFTQMT RMLDVLEQFL TYHGHLYLRL DGSTRVEQRQ
ALMERFNADK RIFCFILSTR SGGVGVNLTG ADTVVFYDSD WNPTMDAQAQ DRCHRIGQTR
DVHIYRLISE RTVEENILKK ANQKRMLGDM AIEGGNFTTA YFKQQTIREL FDMPLEEPSN
SSIPSAPEEE EEAVANKQTH ILEQALCRAE DEEDIRAATQ AKAEQVAELA EFNENDGFPA
GEGEEASRPG AEDEEMSRAE QEIAALVEQL TPIERYAMKF LEASLEEVSR EELKQAEEQV
EAARKDLDQA KEEVFRLPQE EEEGPGAGDE ASCGTGGGSH RRSKKIKAPE RPGTRVSERL
RGARAETQGA NHTPVTPTQH TRSTSTPPRS SPARERTPRL APRPRPTPAP AIPVPTPVPI
SSPNPVTILP VHILPPPPPL PPSQIPPSCC SPACTPPPAC TPSPAHTPPP AHTPLLTPSS
PLLLGPSSVP ISPPGTNLPW GPEAELCAQA LASPESLELT GMASSEASPL ALVSPKDLLP
VAAEVLPMSE KNLSLTPPAP SLTLESGSIL NGQEQEVQEP AQGTVLTVLP DGEEVPVCLS
ESNGVELPPS AASDEPLQEP LEAVRNSEEL VEAQTPTSSP EKLQELVTAE VTAPSTSSSA
TSSPEGPSPA RPPRRRTSAD VEIRGQGAGC PGQPPGPKVL RKLPGRLVTV VEEKELVRRR
RQQRGTASTP APVVSETGAS LGSPSTCSTS GQESSPPTSG PCEASPPSTL PTQTQQPFIA
RRRIELGVTG GGSPENGERE LLAITPPAVK RRRGRPPKKN RSPADSGQGV DEIPSSTSKG
KTNGADPVPG AKTLIVAEPV VGPQLIPGPH PLGPQSIHKP EPIILSPVEK RRRGRPPKAR
DLPIPGTISS PGDGNLESRT QPLPLPPPLP SFPPLLACPA TVTNTVTTVT ISTSPPKRKR
GRPPKNPPSP RPSQLPVLDR DSSSVLESCG LGRQQQLQGQ GDSEGSSSDE DGGRPLTRLA
RLRLEAEGMR GRKSEGSMVV AVIQDDLDLV ESGPGGLELT PPVVSLAPKL RSTRLRPGSL
VPPLETEKVP RKRAGAPVGG GPGQAKRGRP QPLSPLGPED SVEESEAEAS GEEEEEDGTP
RRKPGPRRLG GTNQGDQRIL RSSAPPHLAG PTISHRGRKA KT
//
