ID A0A0L0H5M2_SPIPD Unreviewed; 3040 AA.
AC A0A0L0H5M2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPPG_08355 {ECO:0000313|EMBL:KNC96201.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KNC96201.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KNC96201.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KNC96201.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ257470; KNC96201.1; -; Genomic_DNA.
DR RefSeq; XP_016604241.1; XM_016756513.1.
DR STRING; 645134.A0A0L0H5M2; -.
DR GeneID; 27691524; -.
DR VEuPathDB; FungiDB:SPPG_08355; -.
DR eggNOG; KOG0517; Eukaryota.
DR InParanoid; A0A0L0H5M2; -.
DR OMA; ERIRTWI; -.
DR OrthoDB; 2729759at2759; -.
DR Proteomes; UP000053201; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR Gene3D; 1.20.58.60; -; 2.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 3.30.920.20; Gas2-like domain; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF02187; GAS2; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00243; GAS2; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF143575; GAS2 domain-like; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS51460; GAR; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000053201};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 69..196
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 251..468
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2905..2977
FT /note="GAR"
FT /evidence="ECO:0000259|PROSITE:PS51460"
FT REGION 8..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2281..2301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2825..2891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2829..2877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3040 AA; 337313 MW; 558605C793683605 CRC64;
MSWIKRIASR RSSRDDNNKS ISGSDGNSDF GSLSRRGSKE SLGGSRRGSV AAVEEADTKV
DSLRTDYLLV QKKTFTKWCN VQLAKARNKN VDTLGDEFVI RDLGQDLRDG IRLAHLIETL
SDEKLPKPER AVSRVASSGN AGALTRIYSI VNVDKCLKFL QTKLREPLSN IGSEDIVDGN
LKLTMGLVWV LILRFRIEAI AMKDKRVSVQ SVASVSDPGM RLESPNLDPN SPISQDTPSL
TSNRPAALSA AGGKAALLNW CQQILAPYVD VGVIPRITNF SEAWQSGMAF LCLVHTYNHE
LLPELTEICR RYGESKALAG RAARSSVISR SSVGSSAPSS PDIPGKSSLR YSLSSEFSLG
SLDPFGPSSP KPSGPRDPPF TLSPRNSTSS GLASPPSSPV MRARLSMTSY LYSTNPADWR
VSLSKAFALA EERMGIPQLL DVEDIANVDR PDEMVIMTYV SEIYWVLRDR PFPAPTAFRV
MVSEGERNDA SPTARCERLI AMYVNHANRL GSWLAKQTQD LLRLSEVLAS GADISNVAVS
EESWIRPILN AWADPGTNVD NLKRTIETQV SLIERELANA FTSVAEQDSV HLDEIYGAAL
MPHLLRLYDD VKRAEQDLIS GNEGAAPDTR KVEERHRYLK SRLQVFAKET FPTFVSSMKS
YLELLAERSA KVQQIEAELV GLDWRGGLRE EAQRFVRDIK AMGKDLHAAQ KNEDKLIDFE
DARRAAQRVK AMKDVVFERL GGGLVQWEPP SRDYVQEYEQ SMQVLQELLE KVESTFALRM
QLLRTRTTEL ILVLEKDIMN SSSPATSASL KTSIKFTSVP SFLSAKIQKL VDTGNNDILV
FIAQEMAPLL STRRAQVAEQ VESACLRRNE EEGREAQLRT SAVSVTKAYC VQVRRVDEAI
KRWREELAQW TNEGNDRMAN AHQDDNWIAT AEKWWEERMA TVRECVEGGA NVGMSLAALD
NIWETVVASA STGLLNVSAP FVAIPHQHLR SSAKALLEAM SLFKTEILER ARGAVAEKRE
ALVTQWGQVA DEVERVVKAL GGESNSIDFV DAAIKSSLEN CLMTRRNMIT GMKEASRWDV
ILGIADTSSA AIHKSKEEVG KFVKDIVGRV RAIEADAAVF EETRWSPFVA RTESLLQALA
SEPNFHSRIQ TRFAQLRQSF EQALVRRSST MPELQTREKI MLEAYTWLQQ FLTAERTWLG
NASEAESSID SIEFDQNRVM AAMRTVIYNT GYGQVMGQEE ALTLHETTAT SIEQHLVEEL
TPLVSTVAET PFSSEWTRTP PKELAWARDE LFTGRNDFVK NVIERLQTKH SALLERAPVL
KARLSLERTI GKFTREAATL LSLLERHLKI EKDRQVPHGL DPEVSQDHYA SLLRDIAKEE
DETKRLVGSL RQVGNQCVEL VRGDPECHFV PIAVQKKMDE VERVLASIAD ATQISTEQIE
AGIKILKQVR IPGKKVNDAC KEIHAAVSEV AVAAAQDEAA LDIIANIRVL AERAGSLVPT
LEEMDKSVDE TSDLKVKAFV EELRGQAKAV REQTEEAGRE TIRAIVENWE NDVAAEIVTL
NKDLDSRIRS TPEVEVDGID LAGHASKVIE AVEAKYSNLV TDLQHLTPKL TDFETATEIV
IRGLREWEGR RGGPEADRRS SMPLLGVSSI PRPESLQARY IEIRSKADAL PRAVREGSSF
VRIATRFAEQ ATTCAALIKD FETQQLPALT TGAVDDSGGK LSQDLERRLS DLERTSLNTD
LAVLLDELNA HPGASSIAKD HAVVVQACTR RFEGLLDDVQ RVRGLLVGSK RTRDAVEAYL
RQAEEVYSWV RARVENLEAV ERDATAEAVQ VTAAISGDTL DDCIEHAAAR AVDRQTGIAS
AEAALERYAR AYEHLQGYSR TVIEGCVNDT GAAETVRRKQ EDVDLAWTAL RDKLRQVRRR
LEWQRKVFTW ARRCGKEVLR GIEETTKKIT EDKVGIGMGS VGGVDGPEVG LDNLGGFVEE
VIRAYQSDSL SWKQQAEAVL NFVSELDWET FAYNETGDKS PMDARDQQLL ENLTIHMRGR
VEASSAKLQA GVQQREATLS KWNAGVQAFL ASLTECEPLL EDAVRGLRER LYRGRSNTGS
RSLAGSRQSL LLSTDDLGTN PLLSRHLVIT GDDETDKDNL NDWIKNQERL EAQLANEGTQ
RIKELQIVGA QVVSSCEEVG GQIAVGIKED IKQRTDQLQE RWREATRLVA EEKVGIERAK
KYQHWHAMLA RLEFEASSVA ERLANLVPGQ GNLEYEAELE DMRTKLGALE LTMSMFFKMT
EQDKDTRPPS TVAAESPKDR SMRRHRSLVS LQVVGFAEEI NASHLKERTD GISGTIVKLT
AAVTEYSQEM SDQKQKKTVK EEMDKVLSWC ERVCARLGDR SGVLPPRALI GSHSADDKPN
ETVNVQKILL DAVKLSAGID VELGQHRLAV EQLVGQATEN ELRLMRDRLV TVETLVKAEK
ARIEDTKRLL ALDKAMTNVR TWIAAAKVAA DDIAQTQRSL AEGGSDGATE LSDEEQRLAA
TFEEVTELED RLKVFESTVN GFMNVAKTAK DEFGAVPVAY GGSDMVEGSR KEIERRIGRV
RAEWDALILT VANLRGSSVD RRREIEFNEA VEEVWQMVEE TKATLSGEFG PLTPEVLCDV
EDVLDGKALP RAIELRDTAD SAARDAKERK RFLTKQRALE DQIRVLLEHV ESQNNSADPV
LLERRVARLI EEIEMLNAEF SGFVQKAAAA AAAALALAEG VKLPAGEIVA PTDAECETMA
INLETHFGSF DGRVRLLLER LESAARAVNE MPKHIELVAR WEGVRAWKNE VKEDLLRPIL
AKRTPKKSSI PVPNRSRSPS WSIRSGSATP TGGLRLSPHG TKSPSPTPTT LSGGRSSPIS
PAPPVRTASG PVRIYLPSPN NYVPDPRNPL DVALANVINH HPSAIRVERA DEPGRYWFGE
TLRRQCFCRL VRNSVMVRIG GGWQELNIFL TEHTDLEHRI PTVRSFSTGG PDEGNELHEV
IELDPSQVAN PYALVSRRAP RKLASALARV AAKGYGGGKK
//
