ID A0A066X9Q4_COLSU Unreviewed; 2388 AA.
AC A0A066X9Q4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDN64414.1};
GN ORFNames=CSUB01_04456 {ECO:0000313|EMBL:KDN64414.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64414.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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:KDN64414.1}.
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DR EMBL; JMSE01001135; KDN64414.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066X9Q4; -.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_5_2_1; -.
DR OMA; QRAMDIE; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 109..159
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 163..855
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..756
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1119..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1605..1632
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1700..1727
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1916..2049
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2092..2337
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2388 AA; 273314 MW; 7FE9E7ED22C9F1AA CRC64;
MAQPRSNPFA RTSPGPSSSR PKSALFSSPS PLSAVSTPTS HVRNNSTAST APAAPAAPVM
FSGTGHFRHN RSDSRNSGSG TFAPSFIKAE EMRGDSNAVR GIEGENDFSG KRYVWLKDPQ
AAFVRGWVVE ETGGNKILVQ CDDGTQREVD VESVDKVNPA KFDKANDMAE LTHLNEASVV
HNLHMRYQAD LIYTYSGLFL VTVNPYCPLP IYTNEYINMY KGRSREDTKP HIFAMADHAF
RNLVDEGENQ SILVTGESGA GKTENTKKVI QYLAAVAHSE SPVKSKSQQS NLSQQILRAN
PILEAFGNAQ TVRNNNSSRF GKFIRIEFNR AGAICGAFID WYLLEKSRVV RINGHERNYH
IFYQLLKGAD KKLKQEFLLD DLDVEDFAYT RAGHDTIVGV SDREEWDLLM EAFNVMGFSD
KDQNSIIRTI AAVLHLGNIS VVKESRAADQ ARLAPDAKEQ AAKVCKLLGV PLDPFLQGLL
HPRVKAGREW VEKVQTPEQV RLGLDALSKG IYERGFGDLV TRINRQLDRT GMGLDDSRFI
GVLDIAGFEI FEENSFEQLC INYTNEKLQQ FFNHHMFVLE QEEYAREQIE WQFIDFGRDL
QPTIDLIELP NPIGIFSCLD EDCVMPKATD KSFTEKLNSL WDKKSNKYRP SRLGQGFILT
HYAAEVEYST DGWLEKNKDP LNDNITRLLA SSTDKHIADL FADCADVDDD PGASRNRVKK
GLFRTVAQRH KEQLHSLMAQ LHSTHPHFVR CILPNHKKKP KQFNKLLVLD QLRCNGVLEG
IRIARTGFPN RLPFAEFRQR YEVLCKNMPK GYQEGQAVAA MMLEKLGLDR SLYRVGLTKV
FFRAGVLAEL EEQRDALITE IMSRFQSVAR GYIQRRVAYK RLFRTEATRI IQKNFNTYLD
LMENPWWQLV SKMKPLLGAT RSATEVKKRD AMIRQLQDKM RQEADDRHKL EEDRRNVHSE
MIRIQQTLES ERALALDKEE IFKRLQVREA ELEEKLSGAI EDQERLEDQL DDLLEAKRRA
EQDVEKYRAQ LEQAALLIAR LEQEKSELSA RTEELERSIE EISQKQSERS EQERLLEEEI
KMLQSQLNLK DRKARDLESK LLKVDQDLEV KLQAAQKELQ SSKSRESQLA SENRQVQQQL
SELSKTSTDY EDLVRKKESE LSVLRDDNKK YETERRTFEE QKKSLVSEKE NAAAKLREVQ
AEITAIKSQQ SQLEREAEDA KKLLETRLSE DAQADKNRQV LEAQIKDLKD ELFNIQKELS
RERQSRDDVV LLSEHKFNAL QEEYDHLNES KIIIEKELYV QQDNLRRTKE ARDTAERERD
EARQEIRRLR VAKTQAEEAR MQAEIEGERA ASRAAREREE SLRKDLDAAQ ERLKWFEDEC
ANLNRQVEDL NKLILSSGEF GLKNDQEKER LERELVTVKG RLKASENDNR ALLNKLQQKG
LEIARSSSRA SEASRSQVLG LQREKARADE QNTQLNKQLG EAQLTIAGLE KKVEKLQLNL
EDLNHEVARE AKASRNAEKT ASTATAQLAE ANRTVESERQ LRTQAQATVR TLQSTMEARE
KELQELRAQM LKVLKTVDPG VVIPPQADGT NEGALSKNFD LVRKVEDLQQ NLRVQTAART
NAEAQLAELR SARVDSPVRS KLEEISPNEA PFNGSPTFRR SKLQARQYSN NSTPTRRIES
EPLDSARSDK TADILSFNNR MDLKAEVEEL QNQLQIAQMQ NRHLQSQLER SSSPLEDFDE
NSSVLRVQKL EKVNSRLHDM LDDSAKKVSA LERSVRTGEL SLRDIQTRSH EEILDALNSQ
EEARRSLLHS HRDAISELSD VKNHFERMRH DRAAIEVELR DTRSELEEMT MAREQEAASR
SQLLQEFSDL QIRLDNETSK LADVGASLNL YKSRADEYFS KLEQAEIAVL KANRAEQFAK
TQAKEAEETY AEIMSEREKM DSTIEDLQRQ NQRLEEKLED LSTDLDAATQ AKKRLQHELE
DYRNQRANDI EDKEMSIEQT RKKYQAEFAT LTKELDLARE EKLFKQAEIA RLREELDELR
SKWDDEVLNS STWSKEKARL ESTLADVVSS RDEAVNAHSD AQGKIVTLLS QVRSLRASVD
EITSERDSLV REKRSIEARL EEAKAGLEDL TNGDSASLRD AANIDKEMLE LKSSLAQKED
IAAAAVEKMR RAEALASEMQ KEAMVEREAS AQLQKDKAAL EKALNEIQIR CVDLETKGYS
SASHDIKFLH KRIQELESQL EEHENERNKS QRSVRNVDRI VKDLQGQIDR KDKQNTQLQD
DVARMRDKAE KLLQTIEELQ SSESENQLQA RRAERELREE KERAMRLERE LEGIKALRFE
KGAASAMGSV RGAWRTGFSV DDDTASIISV PKRKSSLSRA PSLTKGFL
//
