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Database: UniProt
Entry: A0A3Q0H0K9_ALLSI
LinkDB: A0A3Q0H0K9_ALLSI
Original site: A0A3Q0H0K9_ALLSI 
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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