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Database: UniProt
Entry: A0A1S3MJI6_SALSA
LinkDB: A0A1S3MJI6_SALSA
Original site: A0A1S3MJI6_SALSA 
ID   A0A1S3MJI6_SALSA        Unreviewed;      2459 AA.
AC   A0A1S3MJI6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE            EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN   Name=LOC106573174 {ECO:0000313|RefSeq:XP_014003388.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014003388.1};
RN   [1] {ECO:0000313|RefSeq:XP_014003388.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014003388.1};
RG   RefSeq;
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the Mical family.
CC       {ECO:0000256|ARBA:ARBA00008223}.
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DR   RefSeq; XP_014003388.1; XM_014147913.1.
DR   OrthoDB; 5399346at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa16.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
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:SF51; [F-ACTIN]-MONOOXYGENASE MICAL3; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          526..632
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1078..1140
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          2298..2447
FT                   /note="BMERB"
FT                   /evidence="ECO:0000259|PROSITE:PS51848"
FT   REGION          672..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1223..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1389..1517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1564..1694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1961..1991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2010..2043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2074..2256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2282..2335
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        675..735
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1256..1275
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1352
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1415..1434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1481..1503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1569..1590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1646..1693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1718..1732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1798..1834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1835..1849
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1850..1866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1884..1898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2024..2043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2074..2098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2109..2140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2151..2175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2183..2199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2200..2217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2218..2251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2459 AA;  274843 MW;  9A94A8F33FFDADE0 CRC64;
     MGTMGDLGGF TTTGERVNPA HILFDRFVQA STCKVTLKAF QELCDHLELK PCEYRVFYHK
     LKSRLNYWKA KALWAKLDKR AGQKEYKKGR ACTNSKCLII GAGPCGLRTA IELGFLGAKV
     VLLEKRDAFS RNNVLHLWPF TIQDLRGLGA KKFYGKFCAG AIDHISIRQL QLMLLKVALL
     LGIEIHVNTE FKGLIEPPED QENERIGWRA EVLPRTHPVN ELEFDVIIGA DGRRNTLAGF
     RRKEFRGKLA IAITANFINR NTTAEAKVEE ISGVAFIFNQ KFFQDLREAT GIDLENIVYY
     KDDTHYFVMT AKKQSLLEKG VILHDYADTE MLLSRANVDQ AALLSYAREA ADFSTNHQLP
     TLDFAINHYG QPDVAMFDFT CMYASENAAL VRQRNGRQLL VSLVGDSLLE PFWPMGTGIA
     RGFLAAMDSG WMVKSWAQGN PSLDVLAERE SIYRLLPQTT PENINKNFSH YSVDPTTRYP
     NISLHFLRPN QVRHLIDTGD SSREMLIEME NVVNSSTPKL TRNESIARSS KLLNWCQRQT
     EGYRKVSVTD LTMSWKSGMA LCALIHRYRP DLIDFDSLDE RDQQKNNQLG FDVAEREFGI
     SPCMTGKEMS QVSEPDKLSM VMYLSQFYEM FKDTVPPGAG GDQNMSPEEK AALINSTKSP
     ISFLSKLGQS IAISRKRNPK DKKEKEVDGL GKRRKTSQAD NSEDEEVLRG NRDDRPSNST
     ALTERKMKEE SAAVGNHNKV KSMATQLLAK FEENAPAESK GLKRQGDSLP SLGLVLALPP
     PPASLDPPRE PVRLAPVPAW RQKRTQQQEQ LSFRYKEKVK CQTLPIRGEQ PRSGTEWCSG
     SRSCPKKTIL LSSTSSLSLH SQHCDREGLE EEETTQNQTP QAHRKWEPMQ LEEPEPIHIP
     SIQERSAWLI AKFKGKPEKP KLKKKPSRFF IEQWHLSART LSQNTQNLLS SPEALGQEIE
     PLRSDDQMPL HVLSVQERAE QLASQFQGKL ANSQSMKKAL HFCVQKRHLS HSQKPESPLS
     SPETLRPRYL KMYTGEVSLL AEQIANQLQP QEEPKPLLDK WELGSLRKEF PQNIGGSDVC
     FFCQKRVYVM ERLSAEGKFF HRSCFKCDYC GTTLRLSSYA FDVEDGKFYC KPHYCYRSSG
     QAQRKRPAPT PALLNAKDNQ ASLPAAVTVD SPGRGAMASP SPTERRSSVP EVNGLQEPSL
     AKRLRGTPER IELENYRLSL QREEDLEEVP EETLAEHNLS SVLDKDAHAD LGSSSSESDM
     EEEDQEEEEQ HEEEEQQDPP SPSDLGGVPW KEAVELHAKL KTDSDPGAEG EDGEGEDETH
     GHIARDLEVE EEEDDEEEEE DDEAESTDEG EYCPWELELQ SGIWLENLQD EEDTCRFKAR
     NLQIQQVLQP VDPTGIKNLR RVSVLSEGDK EEPPASASQP STMLTQSPST APAHTSARHE
     AVRVWLESVS GEPCEDDDPE AEVGSHDFEP GTEMDQEDIP SDAEAEARLH QSELSDALPE
     EDKKSQSQGI AYSIEQTSVS PVKLVGEVAL SPVKPLTPQP DLQMSHTSPP YLVKSPGMRF
     FPDPFASENI TIPQRTVQTP NAKSPQYATP APSPIHSPLQ SPIRSQPIPL PETVTPKSPV
     NSPPCSCPST GNPLSPICAQ PLPCHEPSSP LTSDSPVRTQ PVPAITSTPL AKPDSSDRTT
     PEPQKSLNLT DETPVKKTDI IEEFWLKSAE IRKSLGLTPL DRSSSSSSKA PEKCPVTVGK
     VPTPDSPSTK SYTPEDLSEE LRPSPSPFTG RSVIRRLNIT VEGQVISPAE PKSNGSDRRD
     LSSSSGLGLN GSTATNQTSQ AASDSYHTSD STMLTPPSSP PPPPPNEEPA TLRQQQKHQV
     SWDNGIDGPT TPEPAKAAPT KTNSPVPAPR TQISPVSMPV SAPKPAPRTT PVTSPVTSPV
     TAPVTPLVVM RREKSSKPRR EEVRKSFVEC VAEIPFADDV EDTYDERTPD TTMDRFYTPP
     SSKPNREREK RPLHLALAME NGKPIFPVNQ QASKSQKAQQ FSPEAKEIAE ERMRAREKSI
     KSQALKEAMA KQLNKMKETD TAKGAAAAAK VVWNVASSET SGKSTKKSSG SPKTSAVKSL
     ESKKAETLPE RFFSSQGNKS LDSSTVSSDG SASGGKSKKR SSLFSPRKNK KEKKAKNESQ
     LSVKHGTDET PSPPKHKSLW KVVFSGYKKD KKKNKDDKSC PSTPSSSNTN DSGKKRLSPL
     GRSSDLKSRR NLSFSEDSDL SCDDVLERSS QKSRTDSVYV PHALAFKRAY ATKKTYTEEE
     LNAKLTRRVQ KAARRQAKQE ELKRLHRAQT IQRQLEQVEE KQRQLEERGV AVEKALRGEA
     GMGKKDDPKL MQEWFKLVQE KNALVRYESE LMIFARELEL EDRQSRLQQD LRERMAIEDH
     LKTEVELAQE KRILNEMLEV VEQRDSLVAL LEEQRLREKE EDKDLESVML SKGFNLNWA
//
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