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Database: UniProt
Entry: A0A1S3EZS6_DIPOR
LinkDB: A0A1S3EZS6_DIPOR
Original site: A0A1S3EZS6_DIPOR 
ID   A0A1S3EZS6_DIPOR        Unreviewed;      1038 AA.
AC   A0A1S3EZS6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=MORC family CW-type zinc finger protein 2 {ECO:0000313|RefSeq:XP_012869896.1};
GN   Name=Morc2 {ECO:0000313|RefSeq:XP_012869896.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012869896.1};
RN   [1] {ECO:0000313|RefSeq:XP_012869896.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012869896.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_012869896.1; XM_013014442.1.
DR   AlphaFoldDB; A0A1S3EZS6; -.
DR   STRING; 10020.ENSDORP00000001048; -.
DR   GeneID; 105984306; -.
DR   KEGG; dord:105984306; -.
DR   CTD; 22880; -.
DR   InParanoid; A0A1S3EZS6; -.
DR   OrthoDB; 933627at2759; -.
DR   Proteomes; UP000081671; Unplaced.
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:SF7; ATPASE MORC2; 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:UP000081671};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00454}.
FT   DOMAIN          490..544
FT                   /note="CW-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51050"
FT   REGION          530..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          285..319
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          979..1013
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        533..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..719
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..802
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  118238 MW;  4D3CABC3F8A0DD4E CRC64;
     MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI YAERREDLRG
     GFMLCFLDDG AGMDPSDAAS VIQFGKSAKR TPESTQIGQY GNGLKSGSMR IGKDFILFTK
     KEDTMTCLFL SRTFHEEEGI DEVIVPLPTW NSRTREPVTD NVEKFAIETE LIYKYSPFRT
     EEEVMTQFMK IPGNSGTLVI IFNLKLMDNG EPELDIVSNP KDIQMAETSP EGTKPERRSF
     RAYAAVLYID PRMRIFIHGH KVQTKRLSCC LYNPRMYKYT SSRFKTRAEQ EVKKAEHVAR
     IAEEKAREAE SKARTLEVRL GGDLTRDSRV MLRQVQNTAI TLRREADVKK RIKEAKQRAL
     KEPKELNFVF GVNIEHRDLD GMFIYNCSRL IKMYEKVGPQ LEGGMACGGV VGVVDVPYLV
     LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY WKDIAIAQRG IIKFWDDFGY LSANWNQPPS
     SELRFKRRRA MEIPTTIQCD LCLKWRTLPY QMSSVEKDYP DTWVCSMNPD PEQDRCEASE
     QKQKVPLGTL KKDTKTQEEK QKQLTEKIRQ QQEKLEALQK TTPIRSQADL KKLPLEVTTR
     PSTEEPARRS QRPRSPPLPA VIKNAPSRPP SLQTARLTNQ SRKAPVISSS PKPPVLTARA
     EASTSRLLNS ADPPRKPLSV PIKAASRPAP VVQPSPSSLL PNAKNPREIP PPKAIKNPVV
     KKPEPPVRLS AANRKRSLVI SDEEDTEEEA EKRKERCKRG KFAVKEEKKE SNEVTGDASL
     QQSDSAGEED QAELKNAQKD KGLHVEVRVN KEWYTGRVTA VELGKNVVRW KVKFDYVPTD
     TTPRDRWVEK GSEDVRLMKP PSPEYQSPDT QQECGEEEEA VLVQQPVALV EPSTSDCARI
     EPDTTAPNTS HETIDLLVQI LRNCLRYFLP PSFPISKKEL SVMNSHELIS FPLKEYFKQY
     EAGLQNLCNS YQSRADSRAK ASEENLRTSE RKLRETEEKL QKLRTNIVAL LQKVQEDIDI
     NTDDELDAYI EDLITKGD
//
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