ID A0A401RU50_CHIPU Unreviewed; 663 AA.
AC A0A401RU50;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
DE Flags: Fragment;
GN ORFNames=chiPu_0020153 {ECO:0000313|EMBL:GCC21678.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC21678.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC21678.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC21678.1}.
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DR EMBL; BEZZ01002386; GCC21678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RU50; -.
DR STRING; 137246.A0A401RU50; -.
DR OMA; EXIDLEN; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR23167:SF51; [F-ACTIN]-MONOOXYGENASE MICAL3; 1.
DR PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50021; CH; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 515..621
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT NON_TER 663
FT /evidence="ECO:0000313|EMBL:GCC21678.1"
SQ SEQUENCE 663 AA; 75070 MW; 7AFCDE467825BA6B CRC64;
MGDGEKSKIE QSHLLFDNFI QATTCKGTFK GFQELCEILA ITNIDFPNFY PKLKSKLNYW
KAKALFSKLD KRGSHKDYKK NTACANTKCL VIGAGPCGLR MAIELAFLGA KTIIVEKRDT
FSRNNVLHLW PYTIQDLRNL GAKKIYGKFC AGAIDHISIR QLQLVLLKIA LILGIEIHLN
VEFRGLLPPR GQKNPNAGWR AEINPPTSKV SQFEFDAVIG ADGRRNTLEG FRRKEFRGKL
AIAITANFIN RHTREEAQAQ EISGVAFIFN QKFFQDLREA TGVDLENIVY YKDDTHYFVM
TAKKQSLLEK GVILQDFSDT EKLLSRSNMN QEALLNYVKE AANFSTNHQL PHLDFAMNHY
GQPDVAMFDF TCMYASENAS LIREEGGKRL LVALVGDSLL EPFWPMGTGI ARGFLAAFDT
AWMVRNWAQG AAPLKVLAER ESIYRLLPQT TPSNISKNYN LYSIDPVTRY PKVNIHVLDE
NQVRHLYNTG EQKNLPGSET AVIPRSPKFK QTDSLARSHK LLAWCQKQTQ GYKNVNVVDL
TTSWKSGLAL SAIIHRYRPD LIDFDQLNEK DVESNNQMAF DIAEREFGIS PIMTGKEMAA
VGEPDKLSMV MYLSQFYEML KDTAPEEYLL SFHDKSNIVS ATKSPISFLS RLGQTITRKR
GPK
//
