ID A0A158NF25_ATTCE Unreviewed; 1092 AA.
AC A0A158NF25;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=MICAL-like protein 1 {ECO:0008006|Google:ProtNLM};
GN Name=105619219 {ECO:0000313|EnsemblMetazoa:XP_012056133.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012056133.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012056133.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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DR EMBL; ADTU01013712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01013713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01013714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012056133.1; XM_012200743.1.
DR AlphaFoldDB; A0A158NF25; -.
DR STRING; 12957.A0A158NF25; -.
DR EnsemblMetazoa; XM_012200743.1; XP_012056133.1; LOC105619219.
DR GeneID; 105619219; -.
DR KEGG; acep:105619219; -.
DR eggNOG; ENOG502QWQX; Eukaryota.
DR InParanoid; A0A158NF25; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09400; LIM_like_1; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF46; ALPHA ACTININ 3; 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; PF00412; LIM; 1.
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 PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 4..110
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 150..211
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 864..1024
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 114..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 877..904
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 292..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 125312 MW; 210EF5CDD1EB3844 CRC64;
MSERRGTKAL ELWCRRITDG YPGVNVQNMT TSWRDGLAFC AMIHHFRPDL IDFNSLNKDD
VYRNNELAFR TAEQHLGIPA LLDAEDMASC MVPDRLSILT YLSQFYQTFG GSSPSRLATN
RTTESADDRI APVPESPKQK VGSRLGMRRD PCAACGLPVF LAEKLLIARA PYHRTCFRCA
RCCNQLTPGN YYETEEGQYC CETCPDEEET DSVHHKYAES TMSDTEREKN EPRSLSDEEK
TERKLCCVQS VLENAAVPDL ISHTSQMRKS FMTSHLLSEK FESTVKDTFA STKSDLDHRQ
ETNSRIDSAF PDDDENEEEE EEEEEEEEES HSSVTDSPDM EESNIERYDV HSALNSLDIR
SDKDQRSTAI SFHDIGKQRK EDNTKESPGC AGERANPETR LSLVQKRLQM FENRDKRDHV
DRTDQSNKRN PVAQDITMVQ GDSWDLSPDV LPMNEEERPE KRLEEDSIIK NTDKHKDSFE
DVGKQQKEDS KITNNEENFS KDFVRVNNED RLNKDKPQED SAKVRSIEKR KDNFTKIENE
RIENNKMDEE HYENAMGSRV LTAKGINLSD NENYPEDLNP FKSNEEDNAE KGKPRTVINS
SKSNKVSTNP FDSENEDIEE PEPPKPAIRN KPENRGTSVT KRVLAAPQIN LNPFWSDEEE
EHGSDEENRD RTPSGNVPIP KPRTIKITPE VNVRRVDLDR GGLYASNSSL TSSESTITPG
GTYRKKKPAP QPPVAKELFP SNQQSPILKS HNSTLPSYHD SSPRTTPRAR KTKPAPPPPM
PTSTPRNISI GKGLSLDESP IIKLRDDDRN LNMWEDQKTN KDEANRNRQS LSSISCTDSS
SYMSYTDKSV QGKWKRKKGP APPRPIPHRR KIKVISMKDV KLELDEIELQ QQGLERQGVR
LEQLIRDKCE SGPRTDDSSL GTDVEELVLE LFALVNEKNE LFRRQAELML LRRQQRLEEE
HVEVEYQIRC LMCQPEATKT DFDKQREEAL IQRLVEIVER RNEIVECLEM DRRREVEEDK
SINKHMGLFA ARNKNELANK GNDSSNAEKT KKGKTKEKVK EKKLKKATKK DADKDVDETE
VKLKRHGKRK WF
//
