ID A0A1J1J977_9DIPT Unreviewed; 1501 AA.
AC A0A1J1J977;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=CLUMA_CG020974, isoform D {ECO:0000313|EMBL:CRL08078.1};
GN ORFNames=CLUMA_CG020974 {ECO:0000313|EMBL:CRL08078.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL08078.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRL08078.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000256|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000256|PROSITE-
CC ProRule:PRU00841}.
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DR EMBL; CVRI01000074; CRL08078.1; -; Genomic_DNA.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR Gene3D; 3.10.20.360; CKK domain; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595:SF0; PATRONIN; 1.
DR PANTHER; PTHR21595; UNCHARACTERIZED; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50346; PRC-barrel domain; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000183832}.
FT DOMAIN 188..297
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1359..1494
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 356..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 555..586
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 652..689
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1090..1173
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 365..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1501 AA; 170485 MW; 143DC7CCE5CECAA3 CRC64;
MSLGVIPNSD ELKESSKNAK QRASICWLLS KAFNNQIPEQ LSEPFYTDHD GNLHLKPQIV
VGLGNASLYC QVLANIYCDP NYQNLNHWSI LQTLCRKGIS VFEEHSGVAP LTETLLIQQN
PLRINAHMIV IESLMILYAK EITSGDRIQS VVTRLSLGAT PDNLSSDQLL LHWLSHAMAA
LKHRLQKKLE LEELYDNKNR IKIPDIPTPV HDFASLCDGV CLAYLIAFYC PKILPWHQVR
ISYLPTIEDS LHNLSLVEKF SQHHLPYSIF HLLSEDVISL REHLKTNLVL LLADMFTLFE
IHPAECVDYP ELETSPGKRS GSATNVVTQH TSYAKNTSLS PENEFTVHKS KGITTLFQTK
ESSPGSSRHY KDKGKNDIKN DEKADKPAGR PSNWEDQRRP SFAGRRSRKN SFSEDSQLTI
ENFGGSQEQL NTIGMSFDQR SLDREKKPHE TSFASIEMTL PARSSIADAR GSLQIGYGDD
DDFLIKDREK PVLKSQHSNA SSSNSNINMQ EEKKKMPPLS SITPTTTTWR QQSLNLNQLN
EICDINQPYI DESKLSSVRL KLEEKRRHIE KEKRKIEAQM SKQLQKVGKA AFLQAINIKD
KPDPSQMRDN DSHANEKHIQ SQDVLDSESL GSKTLEREQN NNLSLEQYHQ SIAMMNSDLH
DIQEDIQKLA EQQNQIQVQT MQAQQLLQAQ QIASILNNQY SSQQNIAGLY HPVQQPDSNP
QLSLKSQAPQ YVNEQIHDIQ KLMPSQGSPR IIEDQYTSTP SKYLNQEQQL NIVKYVQDTN
HCRDQYETQR NQFFLHGDSS ASSPQTSSRR TWLQKGQQTM SKPEMSSWSQ QSAHKQAESL
SWNLMPSQKS KSNLGGFILH ENGKKQNEDD AHALFPVMHA SQREPSSKIN QVDDTMTPQS
ISFIGDEDGN DDIAMNFNDN KRDNRSSLQQ RHQNDINNVE ISLGKFNITS GSKTYRIPSP
TIKNHPGISP NSFHSVESQN GSEKQKGFYI SFDNETQPKR PKPPLRTKRS PKKSFDNLNN
FACDDEDDHE ISVRKFQAFD KHKENDHLMR TFDDSNDYKI IKNPTKSNDN KVLLVEANEK
NFDPEQMDEM QRKKEKIMLL SLQRRQQQEE VKVRKEIAAV QRKEKDQMKE EEKARKKEEQ
LARRTQILEQ HRLKKAIEEA EREGKVLDRA TAELITKQQQ MFSTQPKMRR LGTQRPRPKT
IHVETNSSFD MNQLEKKASN SNLTGIPSNT MRRDYYRGSQ DSLSTKEPQG NERGRTLNRL
SSVAKYGGAG ANFRGRKSNS LMNLCGDSDS GLGRATPPRR APSPGMGSRT SSGKHLPSPS
GPGSLPHPNL MIKRRGVGYD DGASDISSTH SSIFGDYSGP RLYKQPAAKS NRGILLNAVE
YCVFPGVVNR EAKQKVLEKI ARSEAKHFLI LFRDAGCQFR ALYSFDPETE AIIKLYGTGP
SHVYDVMFDK FFKYNSGGKC FAQVHTKHLT VTCDAFSIHN SLWQGKKTSH LPNKKDMALV
I
//
