ID A0A2A2JDI5_9BILA Unreviewed; 1408 AA.
AC A0A2A2JDI5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WR25_21273 {ECO:0000313|EMBL:PAV59691.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV59691.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV59691.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV59691.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV59691.1}.
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DR EMBL; LIAE01010510; PAV59691.1; -; Genomic_DNA.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
DR CDD; cd21188; CH_PLEC-like_rpt1; 1.
DR CDD; cd21189; CH_PLEC-like_rpt2; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR049538; PCN-like_spectrin-like_rpt.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; ENVOPLAKIN; 1.
DR PANTHER; PTHR23169:SF23; SHORT STOP, ISOFORM H; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF00435; Spectrin; 1.
DR Pfam; PF21020; Spectrin_4; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 5.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 228..331
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 342..449
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 867..924
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT COILED 1055..1082
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1176..1230
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1408 AA; 164529 MW; 7B8E4E8E1C3DD991 CRC64;
MGAKCCAPRP DKLQLRMLEE ERYVPSRSGS MDNNVNRRGE MNPAYQKERV TTKEMYRHTL
ERSENLHASS RSLPANAAGA VFPPQRTVYY QNGGTLPRES STSRLASTEV RTMQTREIPP
TQPAMQQYHT TTGSIESRLD DISGGSTIPQ PRAPPGREWS QPLLTYQYKV GSSERRLEYR
YHSESRIDDD EIRKRHEIEQ WTHTQPVQVL RLDQKEREVH MLQDERDKIQ KKTFTKWVNK
HLIKSGRKVD DLFVDLRDGY SLIALLEVLT GERIPKENGY TRFHRIQNVQ YCLDFLRNKK
IKLVNIRPED IVEGNGKLTL GLIWTIILNF QVSEALLGSD AKSARDALLE WARRVTAGYP
RVNVTNFSSS WRDGLAFNAI LHRYRPNLID WNKISDPSVS NRERLANAFA AAEREFGVER
LLDPEDVDTE NPDEKSIITY VSSLYNALPH LPELSKGNLN DLISRLTRGI GITNEKLDLI
LQRIEDVEAR IDTSPPGLIE RQVGEIVDEL NVLEAPINGF FDDVETLKSH NHPEANDFYR
QVYGLHQRRT AYLDRLTNQI LVRLGVRTDT LRKENASRLE GIRQSTFSRV EECIEWVRTR
MEKLSNMEFL EDLETLEEMF EQHKLDNRDI QDFRQNVDEC IARQAEVSAE DTYEYCELLR
TLESEYQQLR DLSAGRMLDL DSLIAFVRAA QLELVWVSER EDIEVTRNWS DIKQLDLPML
TNYYKQLLHE MELREKQYND VHNQGAALLN QGHPAVHVIE VYLRTMQNQW DWLLALSKCL
EEHLRDALNL KSFLEEASDA EAWMEEQSQR LENNYNRTDF SLEEGERYLR ELDEIKEILN
KYHSVLMALT ERCATISPLW QRGERIQRPI TVQALCDYSD KGITIKTGDE VTLLDNSDLI
KWVIRDLSGV EGIVPSVVFR IPPPDPKLTN LLSRLLQQFE KLKKLWEKKH RMVRFNMVLN
TMKTIQGWDQ DTFDAIDPEQ RDAILKALID DTNKLLSELD PNDPLALRLK EELKKTIEHF
MKDEYSNMFD QKCAELLRKL EEAWRKLTET VGRPISRSTE ELERVIREHK AFEDALQALD
VDVANVKELF RMLPHPNPTQ IHNHEALNVN WENIWDLSRM YVERIKVLEM VLNGVIEVKD
IVRAHEITLN SFNDMPAALD KLRGHHAQLL EINMVLKQQQ TVIEQMNKNM AVLRQHVART
RINENHHPDV DALEEEVQRL NVRWENVNQQ VAERLIAAEK ALQIQMVYRS EYETELAWLD
SVEETINRLR RPEDLHPEEY QQQLEVLIHE YAQLQEHTAA IEKVNREGGQ YIREAKTFDA
KMAQYGDAIV GIHGSDIRLE FRRTKPQPKN GAQIVTEELE KLNRRFAELS SLILERRNTM
QVLIQNWKRQ KQVRQKFDCV WRRLPGAC
//
