ID A0A3B4C092_PYGNA Unreviewed; 1348 AA.
AC A0A3B4C092;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000004069.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000004069.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSPNAT00000007633.1; ENSPNAP00000004069.1; ENSPNAG00000010700.1.
DR GeneTree; ENSGT00940000158780; -.
DR Proteomes; UP000261440; Unplaced.
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; 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; IPR022735; bMERB_dom.
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; PS51848; BMERB; 1.
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 Coiled coil {ECO:0000256|SAM:Coils}; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 516..619
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 746..808
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1284..1348
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 662..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1294..1321
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 662..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1348 AA; 151460 MW; 97F2E01E5F54B2D6 CRC64;
MGEMEDERNS QASQLFENFV QASTCKGTLQ AFGVLCRQLE LDPADHQGFY SSLKAAVTSW
KAKALWTKLD KRASHKEYKK GQACTDTRCL IIGSGPCGLR TAIEMALLGA KVVVIEKRDT
FSRNNVLHLW PFTIHDLRNL GAKKFYGKFC AGAIDHISIR QLQLILLKVS LIVGVEVHVN
VEFLSLLEPS EEQGSDGLGW RAEIRPAGHP ISDYEFDVLI GADGRRSTLD GFRRKEFRGK
LAIAITANFV NRNTTAEAKV EEISGVAFIF NQKFFLELKE ETGIDLENIV YYKDNTHYFV
MTAKKQSLLD KGVIIHDYIE TERLLHSDNV NQEALLSYAR EAADFGTNYQ LPSLDYAINH
YGQPDVAMFD FTCMYASENA ALIREKSSRQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TAWMVQGWAQ GKEPLEILSE RESIYRLLPQ TTAENIMKNF EQYTIDPATR YPNLNSSCVR
PHQVRHLYIN GEQSSCSVER GGPTRRSVNI TRRESEVRPS RLLLWCQKQT QGYRGVDVTD
LTTSWKSGLA LCALIHRQRP DLIDFDSLNE ADCARNNQLA FEVAERAFGI QPLITGKEMA
AVQEPDKLVM VLYLSKFYEM FRNSSLPAPG VAREKDENSE DYSSKSANSV YNLMNISVPR
KRVPKDDKKL EDNDPNKKRR KGSNYAEELS SQGALTAGEG LEQKENKVRS MATQLLAKFE
ENAPSCALRR QANVRREFAP GVGGSDICHF CKKRVYVMER LSAEGYFFHR ECFRCDVCNT
TLRLGGHVFD CDQNKFYCKL HFSQRKASHR HRKKEIHGGG VSSVDGSDGY SATGSLRSQP
SDTLGVRSST ARQYGRVQNG PLDPSVVTES PSEERLSNPP ELISTRVTDS SVQDAPTESE
PLGPNSPQLK VERSFTKGGI TTRNNWKKKF RAKLIWIKTP DRSRVAGGDD ALIEEDGDSD
FEEIHVPDPP AKPASETADP HCPLQDKEEQ PAPVEIPHYR THGISASPKP STSSTEPQTV
APDKQNALIP KKKLSLSSSE KEKLLDWDLM TPEKFSEAAE ATDRSEKEVQ SSPENQTKPQ
KAPDHSPPLS GFQLWASALR KSFSSSGNNT KVIRRNRPPR ARPLSEGSFS LSSVFGASTQ
IHEEDEERAR SRGDMDGSQP CSKSRSEITA MLEEVTLSTK PPGGSKDDMA SLPPRKLNFF
SSLRVKRTEG VGRSRTDSQT KDIWAILSKF RNKASTQEQQ QQQKQEEDNS SSEEGPESTT
RRSDPDDSER QRRNQEKMLL QQSKREQLKR LHRAQVIQRQ LEEVEEKQRV LEEKGVTLEK
VLRGEQGKQH LSFCLPFLRS PSVAQTIQ
//
