ID M7B2C0_CHEMY Unreviewed; 2055 AA.
AC M7B2C0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=LIM domain and actin-binding protein 1 {ECO:0000313|EMBL:EMP31209.1};
GN ORFNames=UY3_11631 {ECO:0000313|EMBL:EMP31209.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP31209.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB546351; EMP31209.1; -; Genomic_DNA.
DR STRING; 8469.M7B2C0; -.
DR eggNOG; ENOG502S05D; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09485; LIM_Eplin_alpha_beta; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR028740; EPLIN_Lim_dom.
DR InterPro; IPR049146; FAM186A_B_C.
DR InterPro; IPR049144; FAM186A_B_N.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206:SF95; LIM ZINC-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24206; OS06G0237300 PROTEIN; 1.
DR Pfam; PF20865; FAM186A-B_C; 1.
DR Pfam; PF20870; FAM186A-B_N; 2.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
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:UP000031443};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 1678..1738
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..2055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 250..277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..2022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2055 AA; 236383 MW; C93F18E4D4D5AC6C CRC64;
MAVQESSSSS LSSGSSYESE TNSEPEPEAA ASTLELTISP LTEIPPSVKN ILDKIDAAQL
SRARKEVFKQ LFVILDNVNR VCNCFKGDQG MDPEIEEQFF LSGTWAERKR RALLLDKVAI
LLKASTAQGK DLKFVLESLK EWVVPKTGMW RAWREKVAQK PQEAQPLSPE QMLEDESVIF
SRTSELLTML QEFVESTVLN KAEAVVVKYI VTMVANLTKA FTLLTKQCRG LQAKYDTLAS
QESRKQEVQY VNFQKEVQML NEKKASLEAR VQSIEDKYKM LLVANEAMQK VLHKVKENAA
VNIEPSLRDM KFGARASFEW KSQEDDDNDL SRKKDAVLSA EKLSWKSQAD LGKSPCRKRE
AKVPDKKQLQ RPLAERTEDT SDKQETKLLD KKPALKASIE RGEDISDKQD AKLLDKNPLR
KVLVERGEGT SDKQETKLLD KKPALKGSIE RGEDISDKQK VPVERTQDTV VKWDAVIPVE
KQEETSGDLA GRRHEQPLDS EQTEAADKWD VSLLGGTQEV VEDVTGEWHE ILPEEHELKA
DSEEEIERLP SPTELPYQGI SRKGKQRRKK ESLYTEETHT EMPQSPISRS KLEPSTALYG
FNSAILAYLE QKMEKLWKCP SPGKRQAERM LPKDPEAQRL YMALERKLEE CFSKMKIKYS
SSLEEQKLPR SLELTEGHDE EAKLSDPDSP FLESKVPVIS RWGLPAALWK DPNVSARFQF
PKQWQEEGQE PWQEQAQEPW QGEAQEWFKK IQKEQQCQMQ SPQPEEQLQQ QLQGVKEKVE
VEQLEEEQLQ QEEHQFEELQ PQQEPRQEGQ KEWQEEKQKQ WKKWLEEQAE EQRLCQQQQR
VQQEEEQRLW QQQRAQQEEV QRLWQQRAQQ EEEQRLRQQQ EEEQRLWQQQ RAQQEEVQRL
WQQRAQQEEE QRLRQQQRAQ QEEVERLGEA AQGGEETXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXGRQWQQQ EAKQQEQERL WQQQWQEQLQ QLHEQQELQQ KQTQQEQYLT
PRPKTVPSTR EPGTLEHSTK QIPRRPRREI AKEEVLLYKY FQPSAQQMVP TQSKVSLHSQ
AQSTEETSWL PTLAQKTKGK SLVPSSLSEK RYWVDVEAQR ENLVLLGQAT QKCRLPPYLH
MQAKEVITET LHTDVERLAL LFHKYISFCH LHHVRQTLMS RLEAARAVND GAEVRNLYTY
VERVDAYRKK VLQCWVAKQK TAERARQHCL GKMISLFAQL RLSAELHLSS PSPLMIKAVD
EMKKEFPSSA RARSKSPGYP SPLASVKKVR DFMHPAGVSE QLCDQIESVW RTDVISHGFP
IVPKPPVSLL WSQAGGFPDI PRFLELDVSS VRSKPFRTLQ TRYFCFHKME PSPFNRRQWT
SHSLRITAKE LSLVNKNKSS ALLERFSKYQ KAAEEATAEK KRNNTENLPP HFKRGTLSVL
KKKWENPILG TQSGTETLQS NCTEVRQKVA SPSVGVETNT ASEAETDQTS RVYTRSQLRS
PSGAFGQLKY PSVDSKESKI HSLESDKMEN CVRESRQVGK PEASENPDSS GKIEKYSIPL
NKLKMMFEKG EATQTKNEIQ ASDSEIKSYK SEQKENVPPS PEDSISHQDG DKVFFSEKSL
GFHSNLSEDG TIELNSQSET EAKRRVYAKQ QSSDSKPANQ TDPSPPKVIK KFQLPVKETC
VACQKTVYPM ERLFANQQVF HISCFRCSHC NSKLSLGTYA SLRGNIYCKP HFNQLFKSKG
NYDEGFGHKQ HKELWVSKTE NEESLEKSAH TENTIEGPQS PGVEDAPIAK VGVLAASMEA
KVAALPGREE KPAETKKLRI AWPPPSELGS QGSALEEGIK VFKPKWPPED EVSKPDVQED
VDLDLRKLRR TSSLKERSRP FTVAASFRTM SVKGHKTENV SSPSKADRVM FKQSEELESE
AVMERKQKGK KAENGNIQNT QEKNKELEEE RGREVPDIKA DREENWIQNG QVGMETDDEE
NATMQQPSPN EEIFDSNSPK RISLSNMVTA KELSPSQNSK SKDDVFWEGE DVEDLSVEEQ
IKRNRYYEEE DEDEE
//
