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Database: UniProt
Entry: A0A1S2ZIB3_ERIEU
LinkDB: A0A1S2ZIB3_ERIEU
Original site: A0A1S2ZIB3_ERIEU 
ID   A0A1S2ZIB3_ERIEU        Unreviewed;       931 AA.
AC   A0A1S2ZIB3;
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 3 isoform X1 {ECO:0000313|RefSeq:XP_007519789.1};
GN   Name=MORC3 {ECO:0000313|RefSeq:XP_007519789.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007519789.1};
RN   [1] {ECO:0000313|RefSeq:XP_007519789.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_007519789.1; XM_007519727.2.
DR   AlphaFoldDB; A0A1S2ZIB3; -.
DR   STRING; 9365.ENSEEUP00000013432; -.
DR   CTD; 23515; -.
DR   eggNOG; KOG1845; Eukaryota.
DR   InParanoid; A0A1S2ZIB3; -.
DR   OrthoDB; 933627at2759; -.
DR   Proteomes; UP000079721; 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   CDD; cd00890; Prefoldin; 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:SF17; MORC FAMILY CW-TYPE ZINC FINGER PROTEIN 3; 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, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00454}.
FT   DOMAIN          404..454
FT                   /note="CW-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51050"
FT   REGION          493..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          687..728
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          814..855
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        526..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   931 AA;  104345 MW;  5FF4FDB8AA51BD26 CRC64;
     MAAQPPSGIR LSALCPKFLH TNSTSHTWPF SAVAELIDNA YDPDVNAKQI WIDKTVINKH
     ICLTFTDNGN GMTSDKLHKM LSFGFSDKVT MNGHVPVGLY GNGFKSGSMR LGKDAMVFTR
     NGESMSVGFL SQTYLEGINA EHVVVPIVSF NKHRQMINLA ESKASLAAIL EHSLFSTEQK
     LLAELDAIMG KKGTRIIIWN LRSYKNATEF DFDKDKYDIR IPEDLDEATG KRGYKKQERV
     DQIAPESDYS LRAYCSILYL KPRMQIVLRG QKVKTQLVSK SLAYIERDVY RPKFLTKTVR
     ITFGFNCRNK DHYGIMMYHR NRLIKAYEKV GCQLRANNMG VGVVGIIECN FLKPTHNKQD
     FDYTNEYRLT IAALGEKLND YWNEMKVKKN SEYPMNLPVE DIQKRPDQTW VQCDSCLKWR
     KLPDGIDQLP EKWYCSNNPD PQFRNCEVPE EPEDEDLVHP TYEKTYKKKD KERFRIRQLE
     ALPRINPELF RIPPLMSPSF SPGKDSVPRG HTPEAVGTYA TRLLNSHRGS PQAEPESSSL
     KRRLSPRSSN LNAKTRRLSN QALENSARRD DDDVIILEES STPKPAVDPE AGVKLEAGPE
     GQGGARAEPG LQAASAGPSS GCGQGTAATQ TELPGLAVKK EEASEDEMDS RNGDAALPPP
     CVEAQGQPRE TPETCGAPAG DPAGCQLSKV RQELLLATQE KESYRSQCQV LAAQVKDWQQ
     RVAELNDRCV KKETCHQATE TEAAFLLESM NGEAGSPGRA AAQYQQALEE LERLRKQCGA
     LQLLKTECGH CSRGEDRSEV DEMVVQLDDV FRQLDRCTVE RDQYKSEIEL LEVEKSQIRS
     QCEELKNEIE RLKSANQPTT GPVVSTSSSI EEAVNYASGE SLKLRSLRVN VGQLLAMIVP
     DLDLQQVNYD VDVVDEILGQ VVEQMSEISS T
//
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