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Database: UniProt
Entry: A0A2I3GQV5_NOMLE
LinkDB: A0A2I3GQV5_NOMLE
Original site: A0A2I3GQV5_NOMLE 
ID   A0A2I3GQV5_NOMLE        Unreviewed;       970 AA.
AC   A0A2I3GQV5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=MORC family CW-type zinc finger 2 {ECO:0000313|Ensembl:ENSNLEP00000033721.1};
GN   Name=MORC2 {ECO:0000313|Ensembl:ENSNLEP00000033721.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000033721.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000033721.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000033721.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; ADFV01177693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01177694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01177695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003258137.1; XM_003258089.3.
DR   RefSeq; XP_012363530.1; XM_012508076.1.
DR   AlphaFoldDB; A0A2I3GQV5; -.
DR   Ensembl; ENSNLET00000056549.1; ENSNLEP00000033721.1; ENSNLEG00000004006.3.
DR   GeneTree; ENSGT00940000153998; -.
DR   OMA; GYLSARW; -.
DR   Proteomes; UP000001073; Chromosome 7b.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.40.100; -; 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:UP000001073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00454}.
FT   DOMAIN          428..482
FT                   /note="CW-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51050"
FT   REGION          468..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..257
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          911..945
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        471..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..578
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   970 AA;  110769 MW;  500E608D6F8EBD6B CRC64;
     MLCFLDDGAG MDPSDAASVI QFGKSAKRTP ESTQIGQYGN GLKSGSMRIG KDFILFTKKE
     DTMTCLFLSR TFHEEEGIDE VIVPLPTWNA RTREPVTDNV EKFAIETELI YKYSPFRTEE
     EVMTQFMKIP GDSGTLVIIF NLKLMDNGEP ELDIISNPRD IQMAETSPEG TKPERRSFRA
     YAAVLYIDPR MRIFIHGHKV QTKRLSCCLY KPRMYKYTSS RFKTRAEQEV KKAEHVARIA
     EEKAREAESK ARTLEVRLGG DLTRDSRVML RQVQNTAITL RREADVKKRI KEAKQRALKE
     PKELNFVFGV NIEHRDLDGM FIYNCSRLIK MYEKVGPQLE GGMACGGVVG VVDVPYLVLE
     PTHNKQDFAD AKEYRHLLRA MGEHLAQYWK DIAIAQRGII KFWDEFGYLS ANWNQPPSSE
     LRYKRRRAME IPTTIQCDLC LKWRTLPFQL SSVEKDYPDT WVCSMNPDPE QDRCEASEQK
     QKVPLGTFRK DMKTQEEKQK QLTEKIRQQQ EKLEALQKTT PIRSQADLKK LPLEVTTRPS
     TEEPVRRPQR PRSPPLPAVI RNAPSRPPSL PTPRPASQPR KAPVISSTPK PPALAAREEA
     STSRLLQPPE APRKPANTLV KTTSRPAPLV QQLSPSLLPN SKSPREIPSP KVIKTPVVKK
     TEPSIKLSPA TPSRKRSVAV SDEEEVEEEA ERRKERCKRG RFVVKEEKKD SNELSDSAGE
     EDSADLKRAQ KDKGLHVEVR VNREWYTGRV TAVEVGKHVV RWKVKFDYVP TDTTPRDRWV
     EKGSEDVRLM KPPSPEHQSL DMQQEGGEEE VVPVAQQAIA VAEPSTSECL RIEPDTTALS
     TNHETIDLLV QILRNCLRYF LPPSFPISKK QLSAMNSDEL ISFPLKEYFK QYEVGLQNLC
     NSYQSRADSR AKASEESLRT SERKLRETEE KLQKLRTNIV ALLQKVQEDI DINTDDELDA
     YIEDLITKGD
//
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