ID W5MHJ7_LEPOC Unreviewed; 1419 AA.
AC W5MHJ7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Remodeling and spacing factor 1 {ECO:0000313|Ensembl:ENSLOCP00000007856.1};
GN Name=RSF1 {ECO:0000313|Ensembl:ENSLOCP00000007856.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007856.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007856.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01003066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000007866.1; ENSLOCP00000007856.1; ENSLOCG00000006488.1.
DR GeneTree; ENSGT00530000064411; -.
DR HOGENOM; CLU_002056_2_0_1; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000006488; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0031213; C:RSF complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028938; Rsf1-like.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14296; REMODELING AND SPACING FACTOR 1; 1.
DR PANTHER; PTHR14296:SF3; REMODELING AND SPACING FACTOR 1; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 877..927
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 204..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1147
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 160373 MW; EA26EEA18AD0665A CRC64;
MAASAAAAVE SCPGLCPSFA VVCSFLERYG PLLDLPELTF PQLERALKET STVPPPSVPK
PLVELHLKLM RKIGKSVSAE RWEKYLIKMC QEFNSTWAWE LEKKGYQEMT VECKTGILKY
LCECQFDDNI KFKNVVNEED PDAMRLQPIG RDKDGLMYWF QLDQDHNVRV YVEEQDDQDG
SSWKCIVRSR NDLAETLELL KAQIDPSLLT KPEQQEGSSS TSPGPEDEEN KKEGGEIPPP
GESSDIKADK TDEVSKDQES KSAKETLVPA CSKSVKEEKA PALSEKGEQK SDLNVEVKQV
KQESNESKET TEKNIATLIK EDPKDPKDAQ SSGQNTVASV PEVLVKIELP EEVKEKSPEE
LERALKNDQQ AKIPLKKREL KLTEDFDNGS KIVRNPSITP TKELLKEEGK TDEESKPPVF
CAVEKEGKEL VNGEVQSSGD VNHHQKEKVS LQSEQAKKGE ALPDVSIKKQ ENGLAESSHK
AITSPHKEQE NASEQENAAK TEKVEDAKQV KEEKKETSPK QAEASPSPKA FSHQEESKEE
PMEASEGPVN KPEMTEKPKE PQEGQKDMND ENLDKDSEKS KKDSLVTPME CDISEREEAD
TKKENDTSCA EKAESATVGN AGDEKKQEAS GLEETSVITV TPQEEKSTPT EEAEDNMEKE
KSEKSETQTA GADQQAAVSS DDSKQEVGKK TETLNENEKE AKDEKCNEAS SEIQKGGIRL
KIRIPAHKRK TVIQVEEKRP DCETEVTDGR SLRRSPRICR PTAKVAEIRD KKLEKKQAAA
DEEGEEDNED EEKPAPQRKA KEGSRKTDSE AQTRPTKGRR RHRRTRWTNT RSRWRKAKGS
SEEEEESEED DSDEDYKVEK DKDRHESDSE EEPTPNDDPC KHCGLSNHPE LILLCDSCDS
GYHTACLRPP LMVIPDGEWF CPPCQHKLLC EKLEEQLQNL DVVLKKKERA ERRRERLVYV
GISVENIIPA PEPEVEEGTE EKKKESRKSK TLERRSTRTR KSISYRFDEF DEAIDEAIEE
DIKEAEGGGA GRGKDMANIT GHRGKDISTI LQEEGKENRR PQRAAASRRK KRRRLNDLDS
DSTMEEDESE EEFRVSDSTE EEFVVSDEEA EDSDGDIPSN EDSDLGRRTR RTRQRQTKRQ
SQRIRRRRGR REYSDDDEEE TEEEEEEMGS ETERSSDYSD DDLDLHRRRS RRSKRKPVNY
CETSESEGSR AGGNRDKHKS HRRRLSSSSE GSFLTKDSEE DEEEEEKRQM LKRRKTSEEE
DDDEEDSEEE EERPVRKRLN RIETDEEDEE PKEEAAPEKE LTQEEGQRLG GLKKSNRITS
DDEEDGEALG KEESPMDYNL VELPSTNGQS PGNGLEGFIT KPGPKNSGAP AASSTAANPS
AILAPNGMAG QEVPPQDEDE DDLLGVTDLV DYVCNSEQL
//
