ID A0A3Q0H0K9_ALLSI Unreviewed; 1801 AA.
AC A0A3Q0H0K9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN Name=MICAL2 {ECO:0000313|RefSeq:XP_025063970.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025063970.1};
RN [1] {ECO:0000313|RefSeq:XP_025063970.1}
RP IDENTIFICATION.
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 -!- 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 RefSeq; XP_025063970.1; XM_025208185.1.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000189705};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 516..622
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 854..916
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1640..1789
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 665..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1621..1735
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 665..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1801 AA; 205182 MW; 67FCD74FE9D4AEA0 CRC64;
MGENDDEKCT QAGHIFENFV QASTCKGTIQ AFNILTRQLE LDPLDNRNFY IKLKSKITSW
KAKALWNKLD KRASHKEYKR GKSCMNTKCL IVGGGPCGLR TAIELAFLGA KVVVVEKRDT
FSRNNVLHLW PYTIHDLRGL GAKKFYGKFC AGSIDHISIW QLQLILFKVA LMLGVEIHVN
LEFVKVLEPP EDQENQKIGW RAEFLPVDHP LSEFEFDVII GADGRRNTLE GFRRKEFRGK
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDSTHYFV
MTAKKQSLLD KGVIINDYID TEMLLCGENV NQENLLSYAR EAADFATNYQ LPSLDFAINH
YGQSDVAMFD FTSMYASENA ALVRERQRHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TAWMVKSWSQ GKPPLEILAE RESIYRLLPQ TTPENINKNF DQYTIDPGTR YPNLNSSCVR
SHQVRHLYVT NELQQCPLER VSSIRRSVNL SRHESDIRPN KLLTWCQKQT EGYRNVDVTD
LTTSWRSGLA LCAIMHRFRP DLIDFDSLNE EDAVKNNQLA FDIAEREFGI PPVTTGKEMA
SAGEPDKLSM VMYLSKFYEL FRGTPLRAVD AVDKQNGENN DLSSAKSSNS IFNYINLTLP
RKRVPKVERK EENETKKRRR KGLSSGFEEA SSFSNQETNS GKDQGDGREG VNKNKVKSMA
TQLLAKFEEN APNTSLRRQE LVDKPALLSS CHPPVKPCFA KPQDPSPPPQ PKWQMTVGKV
SRGIGAVAEV LVSLYMNDHR PKPQFSFQEL NQSLDGDISS FPTSCSVSPT CASTIQSCQV
SLRKEFPQTV GGSDICYFCK KRVYVMERLS AEGHFFHREC FKCDVCSTTL RLGIYAFDVE
EGKFYCKPHF THCKISNKHR KRRATLPIQE KGDAEMWKKE ESKPPETTTE STLTTVSSSE
DRPPDYYLLI ADEPTSPKKP KNVTELSDFE SICPSLSPEW ASVRVIPEEE MTERNLMAIR
VMVTSDGSSS EPESDFYGDS SNSEVSEGKI SLPEAISSTN PRKYASSTRS SEEEEEYHEK
SKVADALQRA NSFRSSSSNK YQNWRRKLQS NFPLLYSKKP GLHSKENSGS IQSALEDDLP
PTQLMSNNKP PEITRHFKPY SPIFKRKSKT RETPEEIPLY VLHHPVQNSI GDSFLKHSES
VSPDANLYNY EYEDGNAEEY KLETWNENIR EQEPLAERGA SRRKIVDLSS LNLEEKDEKN
SRHPKEKAEL NEIKKRITRK LMLSSEQQFK LNVSNNADLS GTKPGYQSNR ALEISEQKDA
DNNARENSIS VLSPFENEAL PIVPVNAKDI QKSLDNTGGE QLPSQPKSPL KLIASAIKKS
ILEPLISPSE SIKKSSDSKR KPHSEHTFFS FPNNASHSVS LNNSNGGQPQ GSSVPRHPGE
ESELRNSSKT SSNIFTSLEE KSPYGYTEVH FPACSLHTSP SKPEKSSYTK IEDVPRLLEK
FTLKETPLRS SGDDMLTSKQ KNLSVSSLRL KNKISKDNTV DPSQRSDIRT FFTNFRTKVT
EREKKDPSKS SVPINRFFPE EVLSHPSTGS EHLAVRKQVT ECYSSSSDNE IEHKPSLAFK
VKRSLKRKKK LEKETKQLIK QEQLRRLHKA QAIQRQLEEL EERQTALETR GVKLERELRG
ESDSGTQDET QLLHEWFELA LEKNKLMRYE SELLVLAQEL ELEDHQSRLE QELREKMAID
DSLKDEKDLK EENEIFIKMM RVIAERDKLV SSLEQQRLKK KAEDQHFESF MLPREYPLNR
T
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