ID A0A2K1JII6_PHYPA Unreviewed; 1396 AA.
AC A0A2K1JII6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYPA_018732 {ECO:0000313|EMBL:PNR41329.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR41329.1};
RN [1] {ECO:0000313|EMBL:PNR41329.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c14_19550V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR41329.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c14_19550V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c14_19550V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
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DR EMBL; ABEU02000014; PNR41329.1; -; Genomic_DNA.
DR STRING; 3218.A0A2K1JII6; -.
DR PaxDb; 3218-PP1S34_101V6-1; -.
DR EnsemblPlants; Pp3c14_19550V3.1; Pp3c14_19550V3.1; Pp3c14_19550.
DR EnsemblPlants; Pp3c14_19550V3.2; Pp3c14_19550V3.2; Pp3c14_19550.
DR EnsemblPlants; Pp3c14_19550V3.3; Pp3c14_19550V3.3; Pp3c14_19550.
DR EnsemblPlants; Pp3c14_19550V3.4; Pp3c14_19550V3.4; Pp3c14_19550.
DR EnsemblPlants; Pp3c14_19550V3.5; Pp3c14_19550V3.5; Pp3c14_19550.
DR EnsemblPlants; Pp3c14_19550V3.6; Pp3c14_19550V3.6; Pp3c14_19550.
DR EnsemblPlants; Pp3c14_19550V3.7; Pp3c14_19550V3.7; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.1; Pp3c14_19550V3.1; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.2; Pp3c14_19550V3.2; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.3; Pp3c14_19550V3.3; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.4; Pp3c14_19550V3.4; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.5; Pp3c14_19550V3.5; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.6; Pp3c14_19550V3.6; Pp3c14_19550.
DR Gramene; Pp3c14_19550V3.7; Pp3c14_19550V3.7; Pp3c14_19550.
DR InParanoid; A0A2K1JII6; -.
DR OrthoDB; 54358at2759; -.
DR Proteomes; UP000006727; Chromosome 14.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR CDD; cd21203; CH_AtKIN14-like; 1.
DR CDD; cd01366; KISc_C_terminal; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 100..221
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 644..973
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 242..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..567
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 980..1007
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1055..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 729..736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1396 AA; 154220 MW; 946E2C7795AB3B11 CRC64;
MDVARMGYDN GSSAVLSSVE GTMPHGLGLP VNSWHGGNET YYASEKRILD IERPKGQVCE
HMNQEQMDHT TASIVNATVS SAGVRLSDTH LASRKAEEAA TRRQHAIMWL QEIVGNVGLS
SDSTEEDLRL CLRNGIVLCK LINKVQPGAV HKVVANPILS NHPDGAQSAF QYFENVRNFL
VAVEEMSLPS FEVSDLEQGS MSSSSSAKLV DCILALKSYH DWKQGGALGF WRLKSPSHPT
GNMSKSISKF SASKNVNKSG NARKQWANPD QESHDDTILA SASNHSKGFE PGESVSGHES
LTNDLSGENC SSVGDGEEVV FINNSAGSKS TWLEHLGDKF HEVLQVSAKS MQRVSDSAPF
TTDGYAGGPT TALDNVPSQS LLRLINAILC DKSVEEVSMA VEFMLRKVME EFQRHLVTQR
KQVTKMRTSM KEILSREDKL ALQNSVLVAL AGGTQEEIKL YAQMLHKLEV EMNKLKEEKR
VKEEEVCRLL QENKEQQLAV QVLRNELDHI KRADKEMLQL LESQNKEFEQ ECKETIQSLE
LQLQDSYDKL KELKINADKE MSSLKLKDNQ YQTFLSSQLL ECRDLRLAQV NTKDEFMRMQ
TEWNNQFSML EEQLQSMARA ASGYHKVLAE NRMLYNEVQD LKGNIRVYCR VRPFLTEEAG
RLTTLDYIGE NGQLMLVNPL KPGAKDSRKS FTFNKCFAPN ASQEEVFLDT QPLIRSVLDG
FNVCIFAYGQ TGSGKTYTMS GPNNMAPVDW GVNYRALHDL FSTTQSRLDV FRYEIGVQML
EIYNEQVRDL LAADGVQKKL EIRNNSQLNG LNVPDASMMS VRSTEDVLDL MKVGQKNRAV
GATALNERSS RSHSVLTVHV QGTDLESGAI LRGSLHLVDL AGSERVDRSE ATGDRLKEAQ
HINKSLSALG DVIAALAQKN GHVPYRNSKL TQLLQDSLGG QAKTLMFVHI SPDVESFGET
ISTLKFAERV STVELGAARS NKESGEIQNL KEQVALLKEA AAKKDAEIAH LQTFKERHDR
GESGVGVEKY KSRILKPSAR VRASPDVSPA PKLRMVQNES GSETTETRAI TRKLPGQPKS
PIRVAVGSSH ESEDPAEHLL SSSACSPAGS STEQGLGSFD VMEDGANNVD EKLKRSSSKH
QRNGSGTGFS SWTSQIHNSK DSDGGQMKAT EGSRQHEAVL ANHVESASSD IKQEVTTREL
PERSQIVRED IDNFFLETEK QAIYSNSGYL HESNADFESL RSACSSQRSL PGLEEQFESD
GLFDLRDGHD DSSSLFSESG LSVVADLSLS SQLDYTKKVQ SSPAQVRNER RALLQTQVPR
PPISAIRKSS SVMNRKSVGA PLHSRPRRYS NIGISSSTEK LLSKRNASLG AVASPDFECS
GNRRVAIGAG SSTSWR
//
