ID A0A176WRP2_MARPO Unreviewed; 2086 AA.
AC A0A176WRP2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE35798.1};
GN ORFNames=AXG93_4225s1010 {ECO:0000313|EMBL:OAE35798.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE35798.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE35798.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE35798.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000256|ARBA:ARBA00008049}.
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:OAE35798.1}.
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DR EMBL; LVLJ01000057; OAE35798.1; -; Genomic_DNA.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
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; IPR037975; MyosinXI_CBD.
DR InterPro; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF792; MYOSIN-9; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
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}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000077202};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..148
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 153..823
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1693..2007
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 704..726
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1157..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1007..1041
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1066..1131
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1624..1651
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1385..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2086 AA; 233124 MW; 23C9CA92C0D9D4CB CRC64;
MANVPLGIAL VILDILPFVI LLVQGLSGYW RSWTGLGSTS HDETTARRSA AIRVLGALVR
SQDRNLARPG GTALDIGQLK KALDTSALSL EFKATANISI GSQVWVEDSN LAWVEAEVLD
FDGKQVKART INGTTVVASV SNVHAKDSDS QPGGVDDMTK LAYLHEPGVL YNLASRYELD
EIYTYTGNIL IAVNPFAKLP HLYDNHMMEQ YRGAPLGELS PHVFAVADSS YRAMINEKRS
QSILVSGESG AGKTETTKLI MQYLAYMGGR ANTDGRTVEQ QVLESNPLLE AFGNAKTSRN
DNSSRFGKFV EIQFDRNGRI SGAAVRTYLL ERSRVVQIAD PERNYHCFYQ LCASPEDSEK
YRLGDPRSFH YLNQSPVFEL NNVNNGREYI KTRRAMDIVG ISPEEQEAIF RVVAAILHLG
NVEFTTGKEA DSSIPKDEKS KFHLSVVAEL LRCNSKSLLD SLCERIIVTR DENITKTLDA
YSATTNRDTL AKTIYSRLFD WLVDKVNKSI GQDPDSTTLV GVLDIYGFES FKVNSFEQFC
INLANEKLQQ HFNQHVFKME QEEYTKEAIN WSYIEFVDNQ DVLDLIEKKP VGIIALLDEA
CMFPKSTNET FATKLFQSFN RNKRFSKPKL SRTDFTISHY AGDVTYQTDL FLDKNKDYVV
AEHQALLGSS SCSFVAGLFP PPSDESSKSS YKFSSIGTRF KQQLQALMET LNQTEPHYIR
CVKPNMVNKP GRFENVNVLQ QLRCGGVLEA VRISCAGYPT RRTFDEFIDR FGLLAPELLN
GNYDEKTVTE KLLEKMGLVN FQVGQTKVFL RAGQMATLDG KRSELLSNAA RTIQRQVRTF
LARREFTKKR KAAVKIQACW RGRMARKQYE DLRKEAAAVC IQKHVRRWLA QKSYAKTRKA
AIFVQAGVRG MIARKEFRRR RQTKAAIIIQ TRFRGYKARS DYQKLRKAAV VFQCQWRGRV
ARQALKKLKM AAKETGALQA AKTMLEKRCD ELTWRLQLEK RMRTDLEEAK AQEISKLQAS
LQDMQLQVQA ASDSLIQERE QNKMALGQAV LAAERVPSVE VTDAKVEKLV AECDRLKALV
ETLEARAAEA TEAEKKYAAA KKESDERLLR AEEAEAKIEQ MQEAVHRLAI SLRRPMWGLA
SRRDGLVPSA RDSVLCSDSL EGSRSPPSRD VYTTKQSGFS VPVDSSSLTS QLHLLELACE
TACETPEDWL VPLSSHLLSL LPEGSLPNLR ASLHDSGRVA CRHCGDRVQP ILRSGSLEGP
TRQEIENSLS QALSKLPRLH GRDSQSPRSK PVTKVLTATE AGTLKLRLKV REPLRVVETV
QTTKLSKDSR SGYDTVSEVS SLETAVPVSP PAPFPYLMKG GIRSDQLSQG PGISRPETPK
SDRVSSRTRN PSPLVTPRGT RSPSLTSRKL PSSPRPNSIL PEAPGARRPS PSRSSTRKPS
PSPSPRFSFS LNPPSNRKSS PAPSRGISSH TTSATRKPSQ APSPRFSLSQ TSSSSPAPSP
QVNASDTPSP LPKPSPSAST RLNPPPSPSF LRKPNPSLST RRTDSPMGPT RRHPSPPPNL
KGRLEEKLQN MESENQVLRQ QTLVLSPTKG LGSRFKTTVF QRSPDNGYLA NGEHRQATLE
TPSTAQIERE HSEAEQRRQK LLIDRQQENQ DALLQCVMQD VGFSHDRPVA ACIIYKSLLQ
WRSFEAERTN VFDRIIQTIG TAIESQENND VLAYWLSNTS TLLFLLQRTL KASGAAGGTP
QRRRPSSVTL FGRMTQGFRS SPSGGVSFGN GGIMGGLEVL RQVEAKYPAL LFKQQLTAYV
EKIYGMIRDN LKKEISPLLS LCIQAPRTSR ATLSKVASRT SPIANMSTQQ VLSSHWHSII
SSLSSLLSTL RANHVPPFLV RKLFTQIFSF INVQLFNSLL LRRECCSFSN GEYVKAGLAE
LEHWIYDATE EYAGSSWDEL KYIRQAVGFL VIHQKPKKSL DEITHDLCPV LSVQQLYRIS
TMYWDDKYGT HSVSPEVIAN MRVLMTEDSN SAVSNSFLLD DDSSIPFTVD DISKSMSDID
LSDVDAPPLL RDNAAFNFLQ PQHEWIFHTA VVLRKKSLMD FWVEED
//
