ID W5MNX4_LEPOC Unreviewed; 1060 AA.
AC W5MNX4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=MORC family CW-type zinc finger 2 {ECO:0000313|Ensembl:ENSLOCP00000010083.1};
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:ENSLOCP00000010083.1, 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:ENSLOCP00000010083.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01005274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01005275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MNX4; -.
DR Ensembl; ENSLOCT00000010095.1; ENSLOCP00000010083.1; ENSLOCG00000008283.1.
DR GeneTree; ENSGT00940000153998; -.
DR HOGENOM; CLU_011516_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG20.
DR Bgee; ENSLOCG00000008283; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16931; HATPase_MORC-like; 1.
DR Gene3D; 3.30.40.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR041006; Morc_S5.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR23337:SF3; CW-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23337; ZINC FINGER CW-TYPE COILED-COIL DOMAIN PROTEIN 1; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF17942; Morc6_S5; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 490..544
FT /note="CW-type"
FT /evidence="ECO:0000259|PROSITE:PS51050"
FT REGION 530..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..319
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1001..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 601..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 119901 MW; A3DA22BB91844508 CRC64;
MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI YTEKKPELRG
GFMLCFLDDG TGMDPSEATH VIQFGKSSKR SPESTQIGQY GNGLKSGSMR IGKDFILFTK
KEDKLTCLFL SRTFHEEEGI DEVIVPLPTW DNKTKQPVTD NPEKFAIETE LIYKYSPFKT
EAQLMEQFGK IEGDSGTLVI IYNLKLMDTR EPELDVETDP RDILMSGTPP EGVKPERRSF
RAYAAVLYID PRMRIFIQGH KVRTKRLSCC LYKPRMYRYT STRFKTRAEQ EVKKADHLAK
IAEEKAREAE SKSLALEVKL GADLTREARV VLRKSQDSAL MLRREAEVKR KIHEAKQRAL
KEPKELCFIF GVNIDQRDLD GMFVYNCSRL IKMYEKVGPQ LEGGMACGGV VGVVDVPYLV
LEPTHNKQDF ADAKEYRHLL KAMGEHLAQY WRDIAIAQKG IVKFWDEFGY LSASWSQPPS
SELRYKRRRA MEIPITIQCD KCLRWRTLPF QMESVDKQYP DNWVCSMNPD STQNRCETPE
QKQNLPVGVM RKEAKTTEDK QKQLSERIRQ QQEKLDALQK TAVVKSQADL KTLPLEVSMK
PAVESSSQAT RSSERVQRPR SPPLPAMIKN APSRPPLVKP PPLSKKPPTP TRTPKPATPP
PPPPPVRRDA RSSAARTPAA RPSARTPAPS KAAASRSARV RTHSTPLVWS ERRCVVLRLK
TKLRTQDDTE STEEEEEEEE EEEKRPSSGK NRLAAAIAPQ VFRAAAEPKR AAASQPSARR
AQSSVVVEHR QAAGSGPSGC SRAWRVALPA ALSPAGKITD SNEEEEEAGV DLKAAKKDRG
LLVEVKVNKE WFTGRVSSVQ AGKQGVLWKV KFDYVPTAIT PRSRWVLKGS DDVRLMRPPT
PESQSPDTLE DAEKEEGAPT RMEPDTTQPT ASREVIESLV VMMRTLLRYF FPPDFQIPKD
DVNTMTAEEL VAFPMKEYFQ QYELGLQTLC NSYQSRADAR ARAVEEKSNS AEARLRETEE
KLQKLRTNIV ALLQKVQEDI DINTDDELDA YIEDLLTKGD
//
