ID A0A151NKU6_ALLMI Unreviewed; 1330 AA.
AC A0A151NKU6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=LIM domain only protein 7 isoform D {ECO:0000313|EMBL:KYO37426.1};
GN Name=LMO7 {ECO:0000313|EMBL:KYO37426.1};
GN ORFNames=Y1Q_0017237 {ECO:0000313|EMBL:KYO37426.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO37426.1};
RN [1] {ECO:0000313|EMBL:KYO37426.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO37426.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO37426.1}.
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DR EMBL; AKHW03002722; KYO37426.1; -; Genomic_DNA.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR CDD; cd08368; LIM; 1.
DR CDD; cd00136; PDZ; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR029978; LMO-7.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR46767; LIM DOMAIN ONLY PROTEIN 7; 1.
DR PANTHER; PTHR46767:SF1; LIM DOMAIN ONLY PROTEIN 7; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR00889; CALPONIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 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:UP000050525};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 12..129
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 642..723
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1259..1325
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 215..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 827..877
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 289..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 150152 MW; 1198BDABD0E01B30 CRC64;
MESGEEPAGG CEAAFAEAQR WVEAVTGKSF GTKSFRAALE NGVLLCDLIN KIKPGIIKKI
NRLSTPIAGL DNINVFLKAC ENIGLKEAQL FHPGDLQDLS NRVTVKPEET NRRVKNVLIT
LYWLGRKAQS NPHYNGPYLN LKAFEKLLGQ ALTKALEESS SLKRSGRDSG YGDIWSIDRG
EAFSSISHKR DDSFDSLDSF GSRSSASFSS DITLKGGSEG CGSDTDSELP YKMHNSHKDD
MSYRRLSAVE PKPLTDFNRF LPSKSKPSAY MPAPLRKKRI EKNEDNRRSW ASPVSTESDG
TLSRSKSLTD ISADELQSMR KIRFEELQKI KAQLQEQDQR WQDDLAKWKS RRKSFTSDLQ
KKKEEREDIE RKTSEVSVRN TKSLKEMQRD REKRDHETYG DNQRTTERKW IYSSYDDVFS
EEKTSSRSSV AKDYLVEKDT TDVFKNNEKP LAAPTSKENL QKWESYATVN AQTGSARVSA
SLPRSYQKTD TSRLTSVVTP RPFGVHTRGI SSLPRSFTMD DAQKYNGEVD RAKRAPALFT
SNSFSQPETR QPLSTTALKS GNEDAEDEEE EEEEEKEEDI KRTYSPISVA SAVSQDQDAG
SHGLKSEYYT SPDSVTVAPS AERRSLPEPE VSRSRDQYSE MRISINQKPG KSHNFGFTAN
WNTSGVFVQS IEKGSPADLC QLHVDDEIIT VSGTKVSHMD PAEGEEAIAN ALETGNLVMD
VRRYGKNGTS ENKWIDATSG DHFPTTSSDI STKTDFNSSL QNSDTGAKVI NGMQADLCSN
EQKESESISL KNLKRRSQFF EQGGSESAIS DLSVPSITVP SRRVWDQEEE RKRQEKWQKE
QERLLQEKYK REQEKLREEW LRAQEEAEKE SSKYQDEEQC VLTADTMSIT AHVPLASSWR
TVMGGDADVP EGGGGSEQGS QQQQNEKEKD EERRWLQEEQ GLEEKEILHL KQKSELQELE
LEQRRKEIEQ QYTEDQKRWA EAEEQHQRFY KHYDEPKTIE DRSGHFLADR SKSRSTSELD
DYTTNRNGQY EKPLGGIARG LLQDELNQKQ SVKMQQETKE PEQKAPRRQM LYHMKYNNPK
QAGTNNKYLE KSRNVPDSQK GSQKEPAMSQ AEAERQQILQ EMRKRTSLHT DNSWIRQRSS
SVYKEPITVH NTLMRRGESL DNLDSSRTSS WRHHSWMNQS VSSSQDYTRP APPAGSTSNR
AYTCTPSSNV APSSTSSVRT ASSTHTLPSA PSPVPCAQSP TSASQSGSQT RNKSISGKKI
CSYCNNVLGK GAAMIIESLG LCYHLHCFKC VACKCNLGGS GSGAEVRIRN NELFCNDCYI
RFKTGQPTSM
//