ID A0A3B4TGM0_SERDU Unreviewed; 1438 AA.
AC A0A3B4TGM0;
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 Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000005326.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000005326.1}
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; ENSSDUT00000005428.1; ENSSDUP00000005326.1; ENSSDUG00000003944.1.
DR GeneTree; ENSGT00940000158780; -.
DR OrthoDB; 5399346at2759; -.
DR Proteomes; UP000261420; 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; PF12130; bMERB_dom; 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; SM01203; DUF3585; 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 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 740..802
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1259..1411
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 624..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1438 AA; 162430 MW; AA5FF82D01F46DAC CRC64;
MGETEDERTA QASQLFENFV QASTCKGTLQ AFSILCRQLE LDPLDYSNFY SSLKAAISTW
KVKALWTKLD KRAQHKVYSQ NKACEGTRCL IIGGGPCGLR TAIELALLGC KVVVIEKRDT
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLMLLKVS LILGVEIHVN
VEFVKLLEPP AEQSEDSPGW RAEVRPSSHP VSDFDFDVVI GADGRKNTLD GFSRKEFRGK
LAIAITANFV NRNTTAEAKV EEISGVAFIF NQKFFLELKE ETGIDLENIV YYKDNTHYFV
MTAKKQSLLD KGVIINDYIE TERLLSLDNV NQEALLSYAR EAADFGTNYQ LPSLDYAINH
YGQPDVAMFD FTSMYASENA ALLREKHGHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TAWMVKGWTQ GRTPLEILAE RESLYRLLPQ TTTENISKNF EQYAIDPATR YPNLNSSCVR
PHQVRHLYID GQQGSCNLER GGPTGRSVNL SRKESEVRPG RLLTWCQKQT QGYRGVDITN
LTSSWRNGLA LCALIHRQRP EFIDYESLNE EDVAGNNQLA FDVAEREFSI QPVTTGKEMA
AEAEPDKLLM VLYLSKFYEA FRNSPVNNGT READENSEDY PSKTNHKLNL PPPRKRNPRD
DKTVEDDSIN KRPRKGNHYL TELSCHSALP AGEDGELREN KVRSMATQLL AKFEENSSTA
KTRSKSVVRK DFSSGLGGSD ICHFCTKRVY VMERLSAEGY FFHRECFRCD VCNCTLRLGG
HTFDSHEAKF YCKMHYAQRQ SSTHLGRFRR RVEDQSHVTP LSLDSGSYSA TGSVQIHPPD
GPSSLPPEQL DKGQKRLPED TEIAVDALDA SCIVKSTTQD ATGSKGQSHA STKDHSNTKQ
NTRWKRKIRA TFPLIFIKHF QRSYKEGPET VPEADSDFEE ITTAEQQTVC DVTSKTSADS
PNQSKRREKS EKHSATAKAV CSPSPKKTRL KISPSEKEKL LNWDVEVTPE ETPVNADAKS
AQQHRDQVQA ETEADKPHTD SRQDGEPSQS QSPASSHSAF QLIANAFRRT FSVTNPSSSS
NAAVTMRPKR DGLHRQRPMS EGALNFSSFL SSVGPEPSAG QKKAGKREVR LASVGADPWG
GGRDLPSLLQ QVSLKGRRDS EGVFSDDMGS LPRRRVDLFS SLRLRKKQAS DSEGKDQEAQ
KEIRTILTNL RNKASSQQNL EELSSSDDEN ENENLPFSQE LCTERQRRKQ EKIVAQQTKR
EQLKRLHRAQ VIQRQLEEVG EKQRDLEERG VSIEKIIRGE TEPSQDEDSD EAQLYQSWFK
LVLEKNRLAR YESELMIFAQ ELELEDTQSR LQQDLRCRMA IEDTKKSASE LQEEQGILSE
IMTTVEKRDM LVSILEEQRL KERAEDKDLE SLVLSKGYEF HWAQADDSWG QEKLECEG
//
