ID W5M0N9_LEPOC Unreviewed; 1142 AA.
AC W5M0N9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Zinc finger, RAN-binding domain containing 3 {ECO:0000313|Ensembl:ENSLOCP00000001946.1};
GN Name=ZRANB3 {ECO:0000313|Ensembl:ENSLOCP00000001946.1};
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:ENSLOCP00000001946.1, 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:ENSLOCP00000001946.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01011639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01011640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M0N9; -.
DR STRING; 7918.ENSLOCP00000001946; -.
DR Ensembl; ENSLOCT00000001951.1; ENSLOCP00000001946.1; ENSLOCG00000001673.1.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000158559; -.
DR HOGENOM; CLU_004251_0_0_1; -.
DR InParanoid; W5M0N9; -.
DR OMA; WRKVVLH; -.
DR Proteomes; UP000018468; Linkage group LG12.
DR Bgee; ENSLOCG00000001673; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004520; F:DNA endonuclease activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:2000674; P:regulation of type B pancreatic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR CDD; cd18010; DEXHc_HARP_SMARCAL1; 1.
DR CDD; cd00085; HNHc; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.30.50; -; 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 Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002711; HNH.
DR InterPro; IPR003615; HNH_nuc.
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 InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR45766:SF7; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3; 1.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01844; HNH; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00507; HNHc; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 40..202
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 325..485
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 632..661
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 535..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 127092 MW; 9E9E550FA3B5B860 CRC64;
RAMAEAGQEQ LCSGELDSRL ATLPDRLRGR LLPFQREGVT FALSRRGRCM IADEMGLGKT
IQAISVALLY KQEWPLLVVV PSSMRYPWVE EMEKWIPELN PDDINLVESK TDVGRIPTSL
VTVLGYGLLT SDAKLLLGAL EAQSFRVVIV DESHYLKSRT AARTKILVPL IQKASRAVLL
TGTPALGRPE ELFMQIDALY PRRFGTWSDY AAKYCNAHFR FFGNRRQWDC RGASSLGELH
QRLSEVMIRR LKDEVLTQLP PKIRQRIPFD LPKEGSKEAC ASFEEWEKLM RTLDAGTAGT
DNPFVEVMGL VTRMYKQTAI AKAGAVKDYI KMMLENEKLK FLVFAHHLAM LQACTEAVIE
AKARYIRIDG SVPSSERIHL VHQFQSDPDT RVAVLSIQAA GQGLTFTAAT HVVFAELYWD
PGHIKQAEDR AHRIGQSCCV HVHYLIAKGT FDTVMWGMLN RKEGVTGSTL NGKKEHLKAE
LGDREKWEFL SFASAWTPGD SFQGDAPGSQ DEVFFSHFEK DKQRDIRTFF LEKKRRRSDE
EPLAEAAAAE GPAEEEEESP AGVARKEAAV LPRPSGQPHA KRPRGSSRAV GHPTRGAGRR
SWAGGASTPL SCPRPPRLSD GDRPASGEAP SSGGEWRCSG CTFANSPLLP YCEMCEAPRP
PHARGGEDPP PPQFISAMKR YVSCVCVCVS PLPGPSQEPL SELQGAEERR SDTEGRADPP
PHRQHACRTE SGRREEEQGA GSSGKTALSH KGGNRNPWGI APTQRVEWAG GPPVMCSSSD
FRLTETECGS ADSTIPVQEG LKFCASRNTD RIYLYSKDGV PLNCNFIPLD IKLENWEDLP
EMFQHPENRQ QVLRFVRAWS ALTAMKQRAI RRSGRVFLDP RAALDDIAGG QRRHSSTKRY
LTKEDVAQAS LRKVLKDGGF VRVIARENPF LPKSKTNQVH QTCLAVTEEL KAGFLDSLPG
PETGCCHVVR RERSEAPGVP LAEKLLCLKA GGEQDSRFCS QDCQEDFLVR SSQAHMRARV
LATERGVCQQ CGLGAQELYQ RVRDAPPARR KEILESSGLA QLPLRQLNEI IRDPAEGQFW
QVDHIRPVYG GGGQCSLDNL QTLCTLCHRK RTAQQAKERS QMKRSMAASK LASDITRFFI
KK
//
