ID A0A452IW10_9SAUR Unreviewed; 1575 AA.
AC A0A452IW10;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000032279.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000032279.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000032279.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSGAGT00000036596.1; ENSGAGP00000032279.1; ENSGAGG00000023101.1.
DR Proteomes; UP000291020; 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 CDD; cd21278; CH_LIMCH1; 1.
DR CDD; cd08368; LIM; 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; IPR001781; Znf_LIM.
DR PANTHER; PTHR15551:SF3; LIM AND CALPONIN HOMOLOGY DOMAINS-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR15551; LIM DOMAIN ONLY 7; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 2.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00889; CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 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:UP000291020};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 22..139
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1503..1569
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..922
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1269..1307
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 186..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1575 AA; 178327 MW; 0A67FCA8E2294E11 CRC64;
MASPRLELEE IQPLQQDAAR PEPAVAEARH WIEQVTGRSF GDKDFRSGLE NGILLCELLN
AIKPGLVKKI NRLSTPIAGL DNTILFLRGC KELGLKESQL FDPGDLQDTS NRITVKNIEN
SRKLKNVLVT IYWLGKAANR CTSYSGATLN LKEFEGLLAQ MRKETEDIES PKRNIRDSGY
IDCWDSERSD SLSPPRHGRD DSFDSLDSFG SRSQQTPSPD VVLRGSSDGR GSDSESDLPH
RKMPDVKKDD MSARRTSYGE PKSVVPFNQY LPNKSNQTAY VPAPLRKKKA EREEYRKSWS
TATSPLGGEK PFSQKQIYED REPTPDIILH KEKPSMMHCQ GKDSGSEDEA VCRVPDLEKD
DFAARRARLN QPKLTVSFNR FLVGPCTNKD KGKLEGVKKP LQKEKQEYAR ANQVHMASAR
QIVTRKENPF LQSQDNESEE EEQVKVPDIQ RDDLAKRKTQ SNLTQQQESP VSVKASITQA
DLETWDRLKV SEQLSEEDLR CSKDPEPSSE IAVEAAVHDD FASCKARAYK KASSPKQRFV
HFGPVTEIDQ QKWEKVSIAR AISNSETTEE TGRERAERQI CHETFASATA CSLTTIEHNN
EVSRPQNDSS SFPLNCTMEQ HHGTVSPVFM GCNVTRDESH EKLKDQSRGG TEHQVRLPDP
RDDMMARRTG AFLKQPGPSV KQFLPVPFSK QQSSQERAKK LVKPGKKMKS TTTTGSFITE
KCPQICANSP QRLAVQPQHR EEKEQERQHL PDTGQDVAFT IHMSSHSLDQ IHSDQTSQLQ
EVPERNKVVS SRDEQLQIFG PRTAVSDDAE SVSMFDMRCE DEAVMQPHSK ARHEKLQHIH
NQLKEDEDRW QDDLARWKSR RRSASQDLIK KEAERKKMER LLSGGDGTSE RRKSIKTYRE
IVEEKERREK ELHEAYKNAK SREEAESILQ QYIERFTISE AVLEHLEMPK ILERSHSVEP
NSSSPPKDPN PMRYLRQQSL PPPKYTATIE ATIVPISESE ATVSTGQTSP SKTVVSKAVP
VLTPKPYAQP KNTQQVLKTF KVDGKVSMNG ETFNGLEEKD KECTTVIFAP LLRRSPKFEG
VARVDESLVE LKQDTTSVEL SLKRPATHTV HRELTASFTE DIKPANQKDE TDSGRPEMMN
SGFASPAAEQ KQFKTTVTCA HPVVPSMEFP PSTHSEEAAS KDKDLKKPET EQQKEAEVLV
TEKVVKSKAP EQEGSILFPF LKKVPETSQV ILQNSAQQAD SDNSDKSNRF SFWSWDPEEE
RKRQERWQHE QERLLQERYQ KEQNKLKEEW EKAQKEVEEE ERRYCEEERK IIEDTVVPFT
VSSSSAEPLS TSSSVSEGNG IMTMMELSNS HEEEKQKEIK REKKLPWEQE SASLAKNKRS
EPCLEKKSSV NKVPTEHPET ILQTESEQDH QVSVAERSSP VILNLPLTQD VSWSQQLLTK
QSPHISEEVR QKTSLDQSIG QQDNSPGERR RTGYHENFRP GLSSPCSPTP QNHSPNRSVS
GKKLCSACRL PLGKGAAMII ETLGLYFHIH CFRCGICKGQ LGDAASGTDV RIRNGLLNCN
DCYIRSRTAG QPTTL
//
