ID   A0A3B3DW95_ORYME        Unreviewed;       879 AA.
AC   A0A3B3DW95;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=MORC family CW-type zinc finger protein 3-like {ECO:0000313|Ensembl:ENSOMEP00000033620.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000033620.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000033620.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   PaxDb; 30732-ENSOMEP00000033620; -.
DR   Ensembl; ENSOMET00000026889.1; ENSOMEP00000033620.1; ENSOMEG00000019746.1.
DR   Ensembl; ENSOMET00000026929.1; ENSOMEP00000018044.1; ENSOMEG00000019746.1.
DR   GeneTree; ENSGT00940000166590; -.
DR   OMA; CMKWRGI; -.
DR   OrthoDB; 933627at2759; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR045261; MORC_ATPase.
DR   InterPro; IPR041006; Morc_S5.
DR   InterPro; IPR011124; Znf_CW.
DR   PANTHER; PTHR23336:SF22; MORC FAMILY CW-TYPE ZINC FINGER PROTEIN 4; 1.
DR   PANTHER; PTHR23336; ZINC FINGER CW-TYPE COILED-COIL DOMAIN PROTEIN 3; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          415..466
FT                   /note="CW-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51050"
FT   REGION          443..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   879 AA;  98736 MW;  B040D11FAAEE70EA CRC64;
     MARLSEHGIR LSSMNPSFLN SNSTSHTWPF SAVAELIDNA SDPGVSAKQI WIDVVDEDDQ
     RCLTFTDNGS GMTPNKLHKM LSFGFTEKGS GKSSQQAIGV YGNGFKSGSM RLGRDALIFT
     KNGGCQSVGM LSQTYLHNIK AQAVIVPIVP FNQQTKLLVV TEDSTASLAA ILEHSIISSE
     EQIHAHFDSI RSKKGTKILI WNIRRAKDGN TEIDFETDPT DFRLPEISTE EIKKGLSSSG
     SLRHDQNIPD MYYSLRAYLS ILYLKPRTQV ILRGKKIQAK LVSKKLSYIE HDVYKPQFSK
     EKVKVTFGLN SKSKDHYGIM MYHKNRLIKA YEKVGYQLKV SGQRAGIGVI GVIECNFLKP
     AHNKQDFEYT KEYRLTLGAL GLKLNDYWKE VTDKKARERE FKTAEKNDDE NQQSEDEGPA
     WLQCEDCLKW RSIPANYYEV TPESWKCSEN PNPRYRSCSS PEEGEESGDQ LTPSYQKNHK
     KLENRKRQRS FEVCQWQETE SKLLILSRAS SAPERPSSPF SGTSEETASR LGPHSEENTS
     ECPETDTQDL LDQHTDNDAV AQTDTNLQDK YAQTHVGIRD KNEALRAPNI EDQPEDKEND
     TTGDRCIDIS EENKDIFSRK RKPELRSYHG KKKQYLFGEN KFSSRNVDEN LHPRKQPSSQ
     VKTDGSHSEN SGTLQLNPTG TSHTWTHSLQ TTQTVIVPPL SREGHPLQPP EGGDREAKLQ
     RLASMEKEVL RLRGVLGMEV GSTTQGTMTA EDECAEKAAS REVGCQTDPP ECPSVADPSL
     AAVPQGLMVP GQKAESRDQL EQNKARRERA EGQSRMRGSD SESYEDSRLA HQNLHDIRNN
     VVVLLTALLP QLDLNGISLE TADVDNILQQ IIEVNSLKL
//