ID A0A176W2I2_MARPO Unreviewed; 1040 AA.
AC A0A176W2I2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=AXG93_641s1030 {ECO:0000313|EMBL:OAE26662.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE26662.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE26662.1, 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:OAE26662.1};
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. Kinesin family. Ungrouped subfamily.
CC {ECO:0000256|ARBA:ARBA00010103}.
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:OAE26662.1}.
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DR EMBL; LVLJ01002136; OAE26662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W2I2; -.
DR SMR; A0A176W2I2; -.
DR OrthoDB; 463662at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd00106; KISc; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR047149; KIF11-like.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47970:SF31; ARMADILLO REPEAT-CONTAINING KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 80..427
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 782..824
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 823..866
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 675..716
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1040 AA; 115264 MW; 76C957D61634F9AF CRC64;
MAFASSPHKN GTGLNARSTG RLDNRPGSVN STIKPVTPPA PATASPPMRP KSASPSSSVN
TGTRRGSGKN GSDNGGVPGR VRVAVRLRPR NGEEMVADMD FADCVELQPE LKRLKLRKNN
WDCETYQFDE ILTETASQKR VYEVVAKPVV ESVLEGYNGT VMAYGQTGTG KTFTLGRLGE
EDTADRGIMV RAMEDILANV SSVDDTVTVS YLQLYMETVQ DLLAPEKDNI AIVEDPKTGD
VSVPSATHVE LQDQRSFVRL LQAGEANRFA ANTKLNTESS RSHAILLVNV RKVVKPKTGD
RELIVLNENG GSPQVGKNIR APTVRKSKLL IVDLAGSERV DKSGSEGHTL EEAKSINLSL
TALGKCINAL AENSPHVPIR DSKLTRMLRD SFGGTARTSL IVTIGPSPRH RGETASTIMF
GQRAMKVENM VKLKEEFDYK SLCRRLETEL DRLVAENERQ VKARQDEEEE NERKLEDTRE
CAAEAESKLA AAMESIEAER KKFQQDLAEA HQNLEKAEKE LKNISQDYQH EKKERNSHAE
KLKLQRDLTD AMQKHQKELT DEKQRQQKEL ADAIQNLELE RGQRKRLEQE LNQATQELNE
ATQHLHVKNE SLEQGNEVLE LKLLLEKETQ LREELEQEIQ TLKSQPPKLP NGIEVVFPTT
VCLILFLSLL LGLFKAKHNE ELLALRRRLD EELKHRERLE EEVRTLREQL TVLSDEGEES
RKIIDKVGSG RSSEGSQSPS VHKPTSHMRD TINGQRATIA KLFEQGEGLF LLLLCFMVSS
AVGLQKILSL LESEDVDVRV HAVKVVANLA AEEANQEKIV EAGGLGSLLM LLQSSEDETI
RRVAAGAVAN LAMNETNQEL IMAQGGIGLL ARTADDAEDP QTLRMVAGAI ANLCGNDKLQ
IKLREEGGIR ALLGMVRSRH PDVLAQVARG IANFAKCESR GAAQGYKTGR SLLIDDGALP
WIVANANNDA SPIRRHIELA LCHLAQHEVN AKDLVAGGAL WELVRISREC SREDIRNLAQ
RTLNASNTFQ TELKRLQLVY
//
