ID A0A091PGT0_LEPDC Unreviewed; 1110 AA.
AC A0A091PGT0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
DE Flags: Fragment;
GN ORFNames=N330_05126 {ECO:0000313|EMBL:KFQ06566.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ06566.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ06566.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ06566.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-
CC (R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-
CC COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044,
CC ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.225; Evidence={ECO:0000256|ARBA:ARBA00001591};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR EMBL; KK672963; KFQ06566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PGT0; -.
DR PhylomeDB; A0A091PGT0; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; 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 CDD; cd21250; CH_MICAL2; 1.
DR CDD; cd09439; LIM_Mical; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 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 InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF39; [F-ACTIN]-MONOOXYGENASE MICAL2; 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 Pfam; PF00412; LIM; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 519..625
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 987..1049
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 893..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ06566.1"
FT NON_TER 1110
FT /evidence="ECO:0000313|EMBL:KFQ06566.1"
SQ SEQUENCE 1110 AA; 125699 MW; FD26B35920641D11 CRC64;
SQNMGENDDE KYSQAGQIFE NFVQASTCKG TIQAFNILTR QLELDPLDNR NFYTKLKSRV
TTWKAKALWN KLDKRASHKE YKRGKSCMNT KCLIIGGGPC GLRTAIELAF LGAKVVVVEK
RDTFSRNNVL HLWPFTIHDL RGLGAKKFYG KFCAGSIDHI SIRQLQLILF KVALMLGVEI
HVNLEFVKVL EPPEDQENQK IGWRAEFLPV DHPLSEYEFD VIIGADGRRN TLEGFRRKEF
RGKLAIAITA NFINRNTTAE AKVEEISGVA FIFNQKFFQD LKEETGIDLE NIVYYKDSTH
YFVMTAKKQS LLDKGVIIND YIDTELLLCG ENVNQSNLLS YAREAADFAT NYQLPSLDYA
INHYGQPDVA MFDFTSMYAS ENAALVRERH RHQLLVALVG DSLLEPFWPM GTGCARGFLA
AFDTAWMVRS WAQGKPPLEI LAERESIYRL LPQTTPENIN KNFDQYTIDP GTRYPNLNSS
CVRPHQVRQL YVTNELQQCP LERVSSIRRS VNLSRHESDV RPNKLLTWCQ KQTEGYRNVN
VTDLTTSWKS GLALCAIIHR FRPDLIDFDA LNEEDVVKNN QLAFDVAEQE FGIPPVTTGK
EVGSAGEPDK LSMVMYLSKF YELFRGAPLR AVDAGDKQNG ENNDLCSAKS SNFIFNNYIN
LTLPRKRVPK VEGKMEENET NKRRRKGLFG VFEEVGVQWC QGTNTGKEQS DVREGTNQNK
VKSMATQLLA KFEENAPNTI FRKQVEKDVK TCISYVGMIY FGAWTQASEM QKQIFFTSSV
SQFQVVARSE HEVREPKQSL NGSDHMARRA KTVQKTDTQP NLSETSENLA SACSAAFVLS
GVLERLQHLE EKMKQKRAQT IANREFHKKN IKEKAAHLAS MFGYMEFPKN KLPTKGLSHS
QPPTPSCPPT HDSAAVSSPS SVGSASPAVP SRQMTVGKVS HAIGAVAEVL VNLYVNDHRP
KPQLPPLELV RPNPQQNKFP QSIGGSDICY FCKKRVYVME RLSAEGHFFH RECFKCEICS
TTLRLGIYAF DVEEGKFYCK PHFTHCKIST KHRKRRATLQ IQGKVRMEAW KKEEPKPTET
TTESALSTAS SPEDRSPVQF IIPVLHPLTG
//
