ID A0A183CEG3_GLOPA Unreviewed; 1245 AA.
AC A0A183CEG3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000313|WBParaSite:GPLIN_001126700};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001126700};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_001126700}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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 AlphaFoldDB; A0A183CEG3; -.
DR WBParaSite; GPLIN_001126700; GPLIN_001126700; GPLIN_001126700.
DR Proteomes; UP000050741; 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 CDD; cd00014; CH_SF; 1.
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}.
FT DOMAIN 189..318
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1111..1245
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 982..1009
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 138845 MW; EEE6A83AC35D384E CRC64;
MENEQNNRKS RTTAMTRSSS CSSSNSSRHI ANVANYIPEE GKMKASLKWL VSRVYGDNYV
PDGLRELFFS DVDGHLQPSP PLIASLVNGF LYCQAASRIF QDAAIAAAPQ HNIGAVFSAL
SREGIDVRDL DGNGIVEETL LQSNPFNIGA HLHMTDALMT AHLRSLVSIE KIVQAISNYT
SVEKREEPLD CVDALLFWIN KICLLVRDDI ERNGLLGVDE LPIIPEMEDL YEDLCDGTCI
CALISFYRSD ELPLREICFN DPMTVNDCRF NLEILRKFCA SCLPWNPFHF ETEDILYLHE
SLQPNINVFL ADFFQFFESH SLMPPAEPTP ASLQQRRFVP IQSIPDLRTQ DIAYSNKGKF
GVRNSNNRPV MANTRDRASS LASEDSFGTN STLQTKDSLA ASTPRPSNLD PNAPNVTHFA
AFNVGHDSSN DTPPQQQNSA QKQQRTLRNT AEIRLQMEEM RRQLAQRQQI EMAKQGQRRC
EAGKDAFFRV MSKSANIELP QAQSSPIVQN HPTDLLSPNN DETLVAQFQQ MPTYFGSQQN
MAPNATTQCY ERPQQQIWTP QQQRLIPPQT VTGGPFTQQT PNAMMQTSTP QMGSVGAVSS
SHPMLSPIAN YTLKAHNGSS FAVDPSSLMG PASSQQHFGG AAHQFAMTPH PSSIAQQRQQ
LTEQSQYAVP TDLHPTHQHQ QHQFATISPY GVGSPSFGVG PLQSSSQPMH LHMINQQIPT
PFSYPQQPPL HHQSQQQFHQ PFYQQNPQQF PPNHMAFQQH QLQQNYVPSP LPPPINTASM
FPSAEAFQMP PPLPPHQTQL FGGAHCQPEE SSTATFRLHQ ANAPASRLDP QLDLNRDLTN
WSQMTYRDGD RPQRKTWAQK QSETDKSIQN LNFSPGNGGP SAGSRGRTVA QLSGGSGEES
AVNSPEKGKL LVLNQTYTKS LTDASVALLS PTTVANGSAS SNNHSGESVL ENVSEPNSEM
AKRRAILASQ IRRKERMMAK SEEKESVDID RLQVKMQRME QAEMRKMERG QRRQKLLEDY
KRKKMEQELL EPSSARTCAS STISLNRGHS QPPPFGRPKS QSNMNLDCAG GTLSRRFGRA
QSNMGNENAD NEQNGGTSTA RANVPSMAEP SLKLYAKQQP KSNRGLIMNA LQYSVFPGHV
SNDQRQKAQA AIAQSDSKHF LVLFRDHKCQ YRGLYTWDQF SDTVHKIDGL GPKICKEPMM
TIMFKYDSGA KSFGHIPTKH LSVTIDGFVV ADQYWQKPKI PHSGR
//
