ID A0A0L8HGF6_OCTBM Unreviewed; 2622 AA.
AC A0A0L8HGF6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN ORFNames=OCBIM_22015048mg {ECO:0000313|EMBL:KOF88338.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF88338.1};
RN [1] {ECO:0000313|EMBL:KOF88338.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF88338.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF88338.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR EMBL; KQ418194; KOF88338.1; -; Genomic_DNA.
DR RefSeq; XP_014772482.1; XM_014916996.1.
DR EnsemblMetazoa; Ocbimv22015036m; Ocbimv22015036m.p; Ocbimv22015048m.g.
DR EnsemblMetazoa; XM_014916996.1; XP_014772482.1; LOC106870794.
DR GeneID; 106870794; -.
DR OrthoDB; 5399346at2759; -.
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 CDD; cd22198; CH_MICAL_EHBP-like; 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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF54; [F-ACTIN]-MONOOXYGENASE MICAL; 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 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); 1.
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 LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 517..622
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 774..839
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 2412..2594
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 839..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1845..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1945..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2117..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2181..2329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2370..2419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1586..1635
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 839..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..956
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1036
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1992..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2010..2024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2040..2069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2181..2221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2293..2329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2622 AA; 295855 MW; 66E52724D14F6520 CRC64;
METSAPESGY SGDPNVLFDQ FVNAGTCKSI LHTFQLLCDA LDIKQTDHRH FYRRLKLRLT
SWKAQSLWAK LDKRASHKEY RKGEACTNTK VLIIGSGPCG LRTAIEIALL GGKAVVLEKR
DSFSRNNVLH LWPFLITDLK NFGAKKFFGK FCAGSIDHIS IRQLQCILLK VALIFGVEVH
YNVSFENLLE PPADQSKEKI GWRALVNPAN HPVSEYQFDV LIGADGKRNT LEGFQRKEFR
GKLAIAVTAN FINRNTQAEA RVEEISGVAF IYNQKFFHQL KEKTGIDLEN IVYYKDATHY
FVMTAKKQSL LDKGVLKHDY SDTGSLLSRS NVDQEALLSY AREAADFSTN HQLPHMDYAV
NHYGQADVAM FDFTSLFQAE NACRILSKHN HKMIMALVGD SLLEPFWPTG SGCARGFLSA
LDSAWMIRSW AGGKLTPLQV IAERESIYRL LSQTKPENIN KNYNAYTIDP NTRYPNLNSN
YFRSEQVRPL YICDEEDEYL KNEINELPLK KPRNDDFIDS YTLLRWCQRV LNTGRHQSVN
IIDFTSSWKS GLALCALIHT FRPDLIDFNS LNKSEVVKNN QLAFDLAEKE FGISPVMTGQ
EMAECDVPDK LAMVSYLSQF YVIFKKEKHP KLENIALTPE EGPKPYRSPS HRLSLLQKIS
NRFSKHKRLS RSREDEHLTF GTGHATGELK ENRAPVELKS YSKLPINEIS NRLTSNWRFE
DMKKDRREVQ SKVNVSAMAE ILASKFKADL QPPPPAIKRI TSNPTLLAAQ PASEFCYFCK
RRVYIMERMS AEGLFFHRGC LRCEHCKNNL RLSNYSCDRT ITGEVRFYCF RHVGMMRQRR
KRSLTEEPTK DEQDLTPGTS PPRIPPLAET YKNTPSTSPS IKKKGAPKVK DDSQLNLKNT
PERVEFENYI EGVSEETEEE QFEHNLRPSL SSQELLEASD EEENSSDSDE ELSDLELSDF
LSQWTSEDDA DVEDLDDDAS HILTWEEACL LAETLQERQA RESIPSKLAD KCRLQLEDTD
STEESSDDET ETEKGFSSDD ADDTMKDQTT PDTENKTLLD EMADARTDQR LSRLRPTSKI
EPLSPLRSPT SPASQMEARA KFFASPPEPV RLDAKLLFGI DKSEKAGEKT PTSSENVNNA
KDEAVTPSTT DVTIGQVPDT VDTKVEDSNL DKDALKDAIA KSDITVEEDY FEGSEESETE
TLEEVASEEA DTNDEIDDII EENVVDDREA VGQAMEEVLT SLERRSTSSE EDEEMTPAKA
WEGMQDDDDV FMKESTNIRD SAYNGEAMEN GTYEDNENED IYKGRAVEGD VIKGVAIVRN
TVEDDNIGEN IEDDNIVNDT EQILEADVKT DVLDEMKEEE LQLNNSSEDE SKSTETTNTE
KAVLRSVSAM SDDTIVDSED STLQSVLRSL ERMDEPSTPV LESEPWNKLD ERFITKRKKK
PKKDDGGSES DTSFTLSTPS KSIHSSLSSL NDALQYNKQI LLETAANNSD NELLNEFQQV
IEERLDEVNN EAENIAIEAN SEEAPQENDV TLTEDTFSEL PEESVKAEEE LQKIKVIDVS
VVSKDEDKVT EPLHEEMEVE EAPKNLEMEL EEISELPEKI VEQEEEDVIV TKNVNANLEM
VENESEQILA DLNNENLPLS STRKEDITEL LDNKVPEKTP NEIISDLDKK TVITPSNKLL
NKIEMYESKE SELQPCSPRE EKMVHSVSVT EKIKQSTPQS TFSPKKNKLA DKKPVLVDIA
DRHPLFANKK LTVNTPSKVD VESSAAAIPT TTTITSTPTT TTTTTADDNV DAANTPTTPT
EVKYRNSIPI KPPRSARPLT TEFDSRRPLS DLILESQPIA ARSSDRIQSN KTSANKQVTR
ASSLPRESHM EKYLSSVDVE MRKKPEYLWK GDRDNWKRYS DLPENNGNYD MTVVSKQLPD
NITRKNYSHS KSLDRNFVAG SRELSPAPKA TLDESPTDLT PVPKPRRILP EVTELKRSLP
PLKPLAPTPA SRTSLKAKSA GSTPVSTATK EPEENKKQPF IPTKLEEKMK PNASLTVPPE
GRNDKRRKIP VDASLKKPQK ENHLDKQSSV VESIDDIPFA DESDSDALTT ISISSVEQFP
GTLIKSKPVR RVSHSAFKKR ILPAAPKKEP ATPIVPTDST KPPEPKKKER VISLTKMIPT
NKRDSYNQDI PASVLLSTPY TTSPFWKMSP TPNTPIPSTY SDQTPVKQQS LTTNQSAFSP
KVPSPTPKPF LSWSQSTSTK KPEKPKEGTQ SEGSSTASTP KKEKKRSLLS MFLPSKSRNK
STSSGSESSD KQKTPTSSKE KKLGQKPSKT VNDKKDKGMK HTDSKDLDFD LSRDMTDLSI
KSVFHVKDRP HITAEQKLRI LESGLKAIIP PRGDDEFSDS GESFLSTDTS VSRRSKLSDP
KKIQQAARKQ QKRQQQQRLR RAQEIQRRLE EVDVQQKELE DRGVIVEKAL RGEGLEYGFI
NICLACAFTP LQGRGINQIS TLLKGQQKAG RNEGELMQEW FNLVHEKNVL LRYESELMVQ
AKELELEDRQ ARLETELRNK MTTDDEKSKT SDQVEAEKRI LAELLEVVEE RDALVSMLEE
DRLREREEDR DLEGIMLTKG FELSPLSCIR PPKGPTRLGT TS
//
