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
//