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Database: UniProt
Entry: A0A443SRP7_9ACAR
LinkDB: A0A443SRP7_9ACAR
Original site: A0A443SRP7_9ACAR 
ID   A0A443SRP7_9ACAR        Unreviewed;      1330 AA.
AC   A0A443SRP7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 2-like protein {ECO:0000313|EMBL:RWS30210.1};
GN   ORFNames=B4U80_10462 {ECO:0000313|EMBL:RWS30210.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS30210.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS30210.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS30210.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
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}.
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:RWS30210.1}.
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DR   EMBL; NCKV01000593; RWS30210.1; -; Genomic_DNA.
DR   STRING; 299467.A0A443SRP7; -.
DR   EnsemblMetazoa; LDEU001830-RA; LDEU001830-PA; LDEU001830.
DR   VEuPathDB; VectorBase:LDEU001830; -.
DR   Proteomes; UP000288716; 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   Gene3D; 3.10.20.360; CKK domain; 1.
DR   InterPro; IPR032940; CAMSAP.
DR   InterPro; IPR022613; CAMSAP-like_CH_dom.
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; 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:UP000288716}.
FT   DOMAIN          148..279
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1196..1329
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          291..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1014..1044
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        291..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..786
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..987
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1078
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1330 AA;  150978 MW;  63D7D85E509E33A3 CRC64;
     MQAKQKSSIL WILSKAYNNE IPPDLLDPYY KDNEEQDKLK PQIVQSLANT EIYCLSLSNI
     YADPNYSCLN HHEIMQLLMR KGIYVVEPND TSLTETVLLQ TAPIRLSAHM VIIEAIMALY
     IKEVLIPEKL VEVVSRFIAI DPEEPLPSDP EEAAIFWMNK SCIRMKQRMD DELFHLGNDN
     VVSPPLLVLE DLADLSDGCS LATLLSFYCP EQLNWTEICF NESMGMADSI YNLQLVQYFC
     QEKLPHNICF LSLEDFLYLH ETIRPNVLAF IADLLFLFEI KPSPFVRRPG TKEELGFSDS
     EEETFKGLPD LPTPAEMKSK SLQHSGWANS DYRNSREDSK SQRSFQRSLR RLERSDEEDT
     FQHCSMESGV PSDRYPDVIF SKPYDTVSVS NFSKPLTKYK FQELQRSHSA SKSRSPTRSE
     KSDTVSDISS VEKEKHSPTL TTNFMKISRS KDVNGSQSEN HSENQTTPVI NIAFKQKDAN
     EYSMNSIRAS QKPFQLNDGS SIKDIFNQKP NQTNIVEQEK SSDDVQTLLR DIRLKLEAKR
     HKLEAENKNV NQAWKQQALL KAVKTQKDDK EVEVKDDEKC NGGGDNVDVE ELKHDLEEMS
     KRLAEHEKLS TLRRVSNSDK QTPDKKIDPE SASEAHQQKP NYNAQHERFE LNSSEIPSSL
     PNQIRFDNSS QHLGNSPHAA AFNEPQMIPK RSKWGQPSVP FAANDLEYQW TVASIPPQVE
     HPFYPRYPAN PYEHMYSMHM YPTHAPLQPR SVYGYQHPET YYRPHLPPQT SNHGHPIYSQ
     PNEMYRTPDN RDFVPFSPPT HHLNYSQNVG SNVNPPTVVE HNEDSLKSRN RLLNQSVNNE
     SRKLKDSRSN HDLRKDLSNT FQERSPTLTQ TITRSSHRTS SSCEPSQGIN RKKSVDSEAS
     SSDSIHNKNG SSSDSLSNKD DDLTFTQKGF FIHFGDDDSK PKPKPAVRPK LRSQQKPQLA
     IESDFTRQHE NHRESVKSSK EKKPSNEVKL SPVSQGVGFV IGQDLVDPDP CLELEMAKKK
     EKKKEEASKK KEEERLRRQI ILEQYRQRKI QEEADKNGLS GAVSSVSSKD SSRNNTVVLH
     RPARGRPNSS GTKPRPKSYH VSASQMQDFV SLDPKASRIT DDVDAVYNFG SSMSSVVGSS
     CSRPQSALSG TTTMPRRLPS PPSRLPAIPS NLLGRHRGPP SDGASDAGST FSEYTGPKLF
     VKPTQKSNRG LIINASNVVL AGAVNAETKK RVLEEINVSD SKHFVILFRG AGMQFRAIYS
     YNPDREEVFK LYGTGPKTIN NDMIDKFYKY NSGTKSFNEV QTKHLTVTID AFTIHNTLWS
     GKRMSTKNIF
//
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