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Conserved domains on  [gi|947207764|ref|XP_014441149|]
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kinesin-like protein KIF12 isoform X5 [Tupaia chinensis]

Protein Classification

KISc and PHA02682 domain-containing protein( domain architecture ID 12884047)

protein containing domains KISc, PHA03247, and PHA02682

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 117-356 2.76e-97

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


:

Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 301.87  E-value: 2.76e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 117 PPSLAGIMQRTFAWLLDRVQRL---GSQVTLRASYLEIYNEQVRDLLSLGSSRPLPVRWNKTRGFYVEQLREVEFGSLEA 193
Cdd:cd00106   99 DPEQRGIIPRALEDIFERIDKRketKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLED 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 194 LMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASlvpqspqlppadaGEPPAGGKLCFVDLAGSEKVTATGS 273
Cdd:cd00106  179 ALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS-------------GESVTSSKLNLVDLAGSERAKKTGA 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 274 RGELMLEANSINRSLLALGHCISLLLDPQRKqsHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYAS 353
Cdd:cd00106  246 EGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFAS 323


                 ...
gi 947207764 354 RAQ 356
Cdd:cd00106  324 RAK 326
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 466-544 1.08e-03

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.39  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 947207764 466 SICHLRHSGPGPAPPCACWMGPAHPCYALPPLCSCPCChLCPLAHWACPRrehhlQQVPSPEPPGGLPLSARPPPCVPP 544
Cdd:PHA02682  70 SACMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAV-TCPAPAPACPP-----ATAPTCPPPAVCPAPARPAPACPP 142
 
Name Accession Description Interval E-value
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 117-356 2.76e-97

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 301.87  E-value: 2.76e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 117 PPSLAGIMQRTFAWLLDRVQRL---GSQVTLRASYLEIYNEQVRDLLSLGSSRPLPVRWNKTRGFYVEQLREVEFGSLEA 193
Cdd:cd00106   99 DPEQRGIIPRALEDIFERIDKRketKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLED 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 194 LMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASlvpqspqlppadaGEPPAGGKLCFVDLAGSEKVTATGS 273
Cdd:cd00106  179 ALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS-------------GESVTSSKLNLVDLAGSERAKKTGA 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 274 RGELMLEANSINRSLLALGHCISLLLDPQRKqsHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYAS 353
Cdd:cd00106  246 EGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFAS 323


                 ...
gi 947207764 354 RAQ 356
Cdd:cd00106  324 RAK 326
Kinesin pfam00225
Kinesin motor domain;
117-358 4.09e-95

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 296.02  E-value: 4.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  117 PPSLAGIMQRTFAWLLDRVQRLGSQV--TLRASYLEIYNEQVRDLLSLG--SSRPLPVRWNKTRGFYVEQLREVEFGSLE 192
Cdd:pfam00225  94 SDEQPGIIPRALEDLFDRIQKTKERSefSVKVSYLEIYNEKIRDLLSPSnkNKRKLRIREDPKKGVYVKGLTEVEVSSAE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  193 ALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASLVPQSPQlppadageppagGKLCFVDLAGSEKVTATG 272
Cdd:pfam00225 174 EVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKT------------GKLNLVDLAGSERASKTG 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  273 SR-GELMLEANSINRSLLALGHCISLLLDPQrkQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRY 351
Cdd:pfam00225 242 AAgGQRLKEAANINKSLSALGNVISALADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRF 319


                  ....*..
gi 947207764  352 ASRAQRV 358
Cdd:pfam00225 320 ASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 117-363 2.20e-84

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 268.29  E-value: 2.20e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764   117 PPSLAGIMQRTFAWLLDRVQRL--GSQVTLRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLEAL 194
Cdd:smart00129 100 TPDSPGIIPRALKDLFEKIDKReeGWQFSVKVSYLEIYNEKIRDLLN-PSSKKLEIREDEKGGVYVKGLTEISVSSFEEV 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764   195 MELLQKGLSRRRSSAHSLNQASSRSHALLTLHIcrpvspaslvpqsPQLPPADAGEPPAGGKLCFVDLAGSEKVTATGSR 274
Cdd:smart00129 179 YNLLEKGNKNRTVAATKMNEESSRSHAVFTITV-------------EQKIKNSSSGSGKASKLNLVDLAGSERAKKTGAE 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764   275 GELMLEANSINRSLLALGHCISLLLDPQrKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASR 354
Cdd:smart00129 246 GDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASR 324


                   ....*....
gi 947207764   355 AQRVTTRPQ 363
Cdd:smart00129 325 AKEIKNKPI 333
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
121-464 1.58e-58

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 206.90  E-value: 1.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 121 AGIMQRTFAWLLDRV--QRLGSQVTLRASYLEIYNEQVRDLLSLGSSRPLpVRWNKTRGFYVEQLREVEFGSLEALMELL 198
Cdd:COG5059  114 PGIIPLSLKELFSKLedLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLN-IREDSLLGVKVAGLTEKHVSSKEEILDLL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 199 QKGLSRRRSSAHSLNQASSRSHALLTLHicrpvspaslVPQSPQLPPadagePPAGGKLCFVDLAGSEKVTATGSRGELM 278
Cdd:COG5059  193 RKGEKNRTTASTEINDESSRSHSIFQIE----------LASKNKVSG-----TSETSKLSLVDLAGSERAARTGNRGTRL 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 279 LEANSINRSLLALGHCISLLLDPqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 358
Cdd:COG5059  258 KEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSI 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 359 TTRPQApKSPVAKQPQRLET--EVLQLQEENRRLRFQLDQMDPKASSSGpsgarvawaqrnLYGMLQEFMLENERLrKEK 436
Cdd:COG5059  337 KNKIQV-NSSSDSSREIEEIkfDLSEDRSEIEILVFREQSQLSQSSLSG------------IFAYMQSLKKETETL-KSR 402

                        330       340
                 ....*....|....*....|....*...
gi 947207764 437 SQLQRSRDLARNEQRILAQQVHELERRL 464
Cdd:COG5059  403 IDLIMKSIISGTFERKKLLKEEGWKYKS 430
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 122-427 4.10e-47

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 179.75  E-value: 4.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  122 GIMQRTFAWLLDRV---------QRLGSQVtlRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLE 192
Cdd:PLN03188  201 GLTPRVFERLFARIneeqikhadRQLKYQC--RCSFLEIYNEQITDLLD-PSQKNLQIREDVKSGVYVENLTEEYVKTMK 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  193 ALMELLQKGLSRRRSSAHSLNQASSRSHALLTlhiCrpvspaslVPQSPQLPPADAGEPPAGGKLCFVDLAGSEKVTATG 272
Cdd:PLN03188  278 DVTQLLIKGLSNRRTGATSINAESSRSHSVFT---C--------VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTG 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  273 SRGELMLEANSINRSLLALGHCISLLLDPQR--KQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLR 350
Cdd:PLN03188  347 AAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLR 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  351 YASRAQRVTTRpqapkspvAKQPQRLETEVLQLQEENRRLRFQLDQMdpKASSSGPSGARVA----WAQRNLYGMLQEFM 426
Cdd:PLN03188  427 FAQRAKAIKNK--------AVVNEVMQDDVNFLREVIRQLRDELQRV--KANGNNPTNPNVAystaWNARRSLNLLKSFG 496


                  .
gi 947207764  427 L 427
Cdd:PLN03188  497 L 497
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 466-544 1.08e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.39  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 947207764 466 SICHLRHSGPGPAPPCACWMGPAHPCYALPPLCSCPCChLCPLAHWACPRrehhlQQVPSPEPPGGLPLSARPPPCVPP 544
Cdd:PHA02682  70 SACMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAV-TCPAPAPACPP-----ATAPTCPPPAVCPAPARPAPACPP 142
 
Name Accession Description Interval E-value
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 117-356 2.76e-97

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 301.87  E-value: 2.76e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 117 PPSLAGIMQRTFAWLLDRVQRL---GSQVTLRASYLEIYNEQVRDLLSLGSSRPLPVRWNKTRGFYVEQLREVEFGSLEA 193
Cdd:cd00106   99 DPEQRGIIPRALEDIFERIDKRketKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLED 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 194 LMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASlvpqspqlppadaGEPPAGGKLCFVDLAGSEKVTATGS 273
Cdd:cd00106  179 ALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS-------------GESVTSSKLNLVDLAGSERAKKTGA 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 274 RGELMLEANSINRSLLALGHCISLLLDPQRKqsHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYAS 353
Cdd:cd00106  246 EGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFAS 323


                 ...
gi 947207764 354 RAQ 356
Cdd:cd00106  324 RAK 326
Kinesin pfam00225
Kinesin motor domain;
117-358 4.09e-95

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 296.02  E-value: 4.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  117 PPSLAGIMQRTFAWLLDRVQRLGSQV--TLRASYLEIYNEQVRDLLSLG--SSRPLPVRWNKTRGFYVEQLREVEFGSLE 192
Cdd:pfam00225  94 SDEQPGIIPRALEDLFDRIQKTKERSefSVKVSYLEIYNEKIRDLLSPSnkNKRKLRIREDPKKGVYVKGLTEVEVSSAE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  193 ALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASLVPQSPQlppadageppagGKLCFVDLAGSEKVTATG 272
Cdd:pfam00225 174 EVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKT------------GKLNLVDLAGSERASKTG 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  273 SR-GELMLEANSINRSLLALGHCISLLLDPQrkQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRY 351
Cdd:pfam00225 242 AAgGQRLKEAANINKSLSALGNVISALADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRF 319


                  ....*..
gi 947207764  352 ASRAQRV 358
Cdd:pfam00225 320 ASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 117-363 2.20e-84

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 268.29  E-value: 2.20e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764   117 PPSLAGIMQRTFAWLLDRVQRL--GSQVTLRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLEAL 194
Cdd:smart00129 100 TPDSPGIIPRALKDLFEKIDKReeGWQFSVKVSYLEIYNEKIRDLLN-PSSKKLEIREDEKGGVYVKGLTEISVSSFEEV 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764   195 MELLQKGLSRRRSSAHSLNQASSRSHALLTLHIcrpvspaslvpqsPQLPPADAGEPPAGGKLCFVDLAGSEKVTATGSR 274
Cdd:smart00129 179 YNLLEKGNKNRTVAATKMNEESSRSHAVFTITV-------------EQKIKNSSSGSGKASKLNLVDLAGSERAKKTGAE 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764   275 GELMLEANSINRSLLALGHCISLLLDPQrKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASR 354
Cdd:smart00129 246 GDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASR 324


                   ....*....
gi 947207764   355 AQRVTTRPQ 363
Cdd:smart00129 325 AKEIKNKPI 333
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 109-355 2.08e-69

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 229.52  E-value: 2.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 109 AGGEGVPVPPSLAGIMQRTFAWLLDRVQRLGSQV--TLRASYLEIYNEQVRDLLSLGSSR--PLPVRWNKTRGFYVEQLR 184
Cdd:cd01372   92 GTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDTFefQLKVSFLEIYNEEIRDLLDPETDKkpTISIREDSKGGITIVGLT 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 185 EVEFGSLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASLVPQSpqlppADAGEPPAGGKLCFVDLAG 264
Cdd:cd01372  172 EVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS-----ADDKNSTFTSKFHFVDLAG 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 265 SEKVTATGSRGELMLEANSINRSLLALGHCISLLLDPQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPE 344
Cdd:cd01372  247 SERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEE 326

                        250
                 ....*....|.
gi 947207764 345 TLSTLRYASRA 355
Cdd:cd01372  327 TLNTLKYANRA 337
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 26-355 4.47e-69

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 228.77  E-value: 4.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  26 IQVVLRVRPMSAAELRRGEQSVLHCSGTRTL----QNARPSTAPSPGEPPGRGPRRGVPLRrgagrdaHAGGRV------ 95
Cdd:cd01370    2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLvfdpKDEEDGFFHGGSNNRDRRKRRNKELK-------YVFDRVfdetst 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  96 ----------PGVRRAAPGRACA-----AGGEG----VPVPPSLAGIMQRTFAWLLDRVQRLGS--QVTLRASYLEIYNE 154
Cdd:cd01370   75 qeevyeettkPLVDGVLNGYNATvfaygATGAGkthtMLGTPQEPGLMVLTMKELFKRIESLKDekEFEVSMSYLEIYNE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 155 QVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPA 234
Cdd:cd01370  155 TIRDLLN-PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 235 SLVPQSPQlppadageppagGKLCFVDLAGSEKVTATGSRGELMLEANSINRSLLALGHCISLLLDPQRKQSHIPFRDSK 314
Cdd:cd01370  234 SINQQVRQ------------GKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSK 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 947207764 315 LTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRA 355
Cdd:cd01370  302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRA 342
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 117-359 1.28e-63

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 213.61  E-value: 1.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 117 PPSLAGIMQRTFAWLLDRVQRLGSQ---VTLRASYLEIYNEQVRDLLSLGSSRPLP--VRWNKTRG-FYVEQLREVEFGS 190
Cdd:cd01366   98 PPESPGIIPRALQELFNTIKELKEKgwsYTIKASMLEIYNETIRDLLAPGNAPQKKleIRHDSEKGdTTVTNLTEVKVSS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 191 LEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRpvspaslvpQSPQLPPAdageppAGGKLCFVDLAGSEKVTA 270
Cdd:cd01366  178 PEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG---------RNLQTGEI------SVGKLNLVDLAGSERLNK 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 271 TGSRGELMLEANSINRSLLALGHCISLLLdpqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLR 350
Cdd:cd01366  243 SGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLR 319


                 ....*....
gi 947207764 351 YASRAQRVT 359
Cdd:cd01366  320 FASKVNSCE 328
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 26-358 8.61e-63

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 211.55  E-value: 8.61e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  26 IQVVLRVRPMSAAELRRGEQSVLHC---SGTRTLQNARPStapsPGEPP----------GRGPRRGVplrrgagRDAHAG 92
Cdd:cd01371    3 VKVVVRCRPLNGKEKAAGALQIVDVdekRGQVSVRNPKAT----ANEPPktftfdavfdPNSKQLDV-------YDETAR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  93 GRVPGVRRAAPGRACAAGG---------EGVPVPPSLAGIMQRTFAWLLDRVQRLGS--QVTLRASYLEIYNEQVRDLLS 161
Cdd:cd01371   72 PLVDSVLEGYNGTIFAYGQtgtgktytmEGKREDPELRGIIPNSFAHIFGHIARSQNnqQFLVRVSYLEIYNEEIRDLLG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 162 LGSSRPLPVRWNKTRGFYVEQLREVEFGSLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRpvspaslvpqsp 241
Cdd:cd01371  152 KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC------------ 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 242 qlppADAGEPPAG----GKLCFVDLAGSEKVTATGSRGELMLEANSINRSLLALGHCISLLLDPqrKQSHIPFRDSKLTK 317
Cdd:cd01371  220 ----SEKGEDGENhirvGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTR 293

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 947207764 318 LLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 358
Cdd:cd01371  294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 26-364 2.31e-61

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 208.75  E-value: 2.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  26 IQVVLRVRPMSAAELRRGEQSVLHCSGTR-TLQNARPSTAPspgeppgRGPRRGVPLRRG--------AGRDAHAG---- 92
Cdd:cd01365    3 VKVAVRVRPFNSREKERNSKCIVQMSGKEtTLKNPKQADKN-------NKATREVPKSFSfdysywshDSEDPNYAsqeq 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  93 -----GRvPGVRRAAPGRACA--AGGE----------GVPVPPslaGIMQRTFAWLLDRVQRLGSQ---VTLRASYLEIY 152
Cdd:cd01365   76 vyedlGE-ELLQHAFEGYNVClfAYGQtgsgksytmmGTQEQP---GIIPRLCEDLFSRIADTTNQnmsYSVEVSYMEIY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 153 NEQVRDLLS---LGSSRPLPVRWNKTRGFYVEQLREVEFGSLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLhicr 229
Cdd:cd01365  152 NEKVRDLLNpkpKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTI---- 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 230 pvspaslvpQSPQLPPADAGEPPAG--GKLCFVDLAGSEKVTATGSRGELMLEANSINRSLLALGHCISLLLDPQR---- 303
Cdd:cd01365  228 ---------VLTQKRHDAETNLTTEkvSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgksk 298

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 947207764 304 -KQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQA 364
Cdd:cd01365  299 kKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVV 360
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
121-464 1.58e-58

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 206.90  E-value: 1.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 121 AGIMQRTFAWLLDRV--QRLGSQVTLRASYLEIYNEQVRDLLSLGSSRPLpVRWNKTRGFYVEQLREVEFGSLEALMELL 198
Cdd:COG5059  114 PGIIPLSLKELFSKLedLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLN-IREDSLLGVKVAGLTEKHVSSKEEILDLL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 199 QKGLSRRRSSAHSLNQASSRSHALLTLHicrpvspaslVPQSPQLPPadagePPAGGKLCFVDLAGSEKVTATGSRGELM 278
Cdd:COG5059  193 RKGEKNRTTASTEINDESSRSHSIFQIE----------LASKNKVSG-----TSETSKLSLVDLAGSERAARTGNRGTRL 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 279 LEANSINRSLLALGHCISLLLDPqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 358
Cdd:COG5059  258 KEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSI 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 359 TTRPQApKSPVAKQPQRLET--EVLQLQEENRRLRFQLDQMDPKASSSGpsgarvawaqrnLYGMLQEFMLENERLrKEK 436
Cdd:COG5059  337 KNKIQV-NSSSDSSREIEEIkfDLSEDRSEIEILVFREQSQLSQSSLSG------------IFAYMQSLKKETETL-KSR 402

                        330       340
                 ....*....|....*....|....*...
gi 947207764 437 SQLQRSRDLARNEQRILAQQVHELERRL 464
Cdd:COG5059  403 IDLIMKSIISGTFERKKLLKEEGWKYKS 430
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 118-363 8.14e-58

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 199.09  E-value: 8.14e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 118 PSLAGIMQRTFAWLLDRVQRLGSQVTLRASYLEIYNEQVRDLLSLGSSRPLPVR----WNKTRGFYVEQLREVEFGSLEA 193
Cdd:cd01364  115 DPLAGIIPRTLHQLFEKLEDNGTEYSVKVSYLEIYNEELFDLLSPSSDVSERLRmfddPRNKRGVIIKGLEEITVHNKDE 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 194 LMELLQKGLSRRRSSAHSLNQASSRSHAL--LTLHIcrpvspaslVPQSPqlppaDAGEPPAGGKLCFVDLAGSEKVTAT 271
Cdd:cd01364  195 VYQILEKGAAKRKTAATLMNAQSSRSHSVfsITIHI---------KETTI-----DGEELVKIGKLNLVDLAGSENIGRS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 272 GSRGELMLEANSINRSLLALGHCISLLLDpqrKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRY 351
Cdd:cd01364  261 GAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEY 337

                        250
                 ....*....|..
gi 947207764 352 ASRAQRVTTRPQ 363
Cdd:cd01364  338 AHRAKNIKNKPE 349
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 112-358 1.83e-55

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 191.77  E-value: 1.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 112 EGVPVPPSLAGIMQRTFAWLLDRVQRL--GSQVTLRASYLEIYNEQVRDLLSLgSSRPLPVRWNKTRGFYVEQLREVEFG 189
Cdd:cd01369   95 EGKLGDPESMGIIPRIVQDIFETIYSMdeNLEFHVKVSYFEIYMEKIRDLLDV-SKTNLSVHEDKNRGPYVKGATERFVS 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 190 SLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHIC-RPVSPASLVpqspqlppadageppaGGKLCFVDLAGSEKV 268
Cdd:cd01369  174 SPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKqENVETEKKK----------------SGKLYLVDLAGSEKV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 269 TATGSRGELMLEANSINRSLLALGHCISLLLDpqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLST 348
Cdd:cd01369  238 SKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315

                        250
                 ....*....|
gi 947207764 349 LRYASRAQRV 358
Cdd:cd01369  316 LRFGQRAKTI 325
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 121-358 9.50e-53

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 184.07  E-value: 9.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 121 AGIMQRTFAWLLDRVQRL-GSQVTLRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLEALMELLQ 199
Cdd:cd01374   97 PGIIPLAIRDIFSKIQDTpDREFLLRVSYLEIYNEKINDLLS-PTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIA 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 200 KGLSRRRSSAHSLNQASSRSHALLTLHIcrpvspaslvpQSPQLPPaDAGEPPAGGKLCFVDLAGSEKVTATGSRGELML 279
Cdd:cd01374  176 RGEKNRHVGETDMNERSSRSHTIFRITI-----------ESSERGE-LEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRK 243

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 947207764 280 EANSINRSLLALGHCISLLLDpQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 358
Cdd:cd01374  244 EGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 111-362 8.52e-51

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 179.63  E-value: 8.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 111 GEGVPVPPSLAGIMQRTFAWLLDRVQR------LGSQVTLRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLR 184
Cdd:cd01373   97 ESDNESPHGLRGVIPRIFEYLFSLIQRekekagEGKSFLCKCSFLEIYNEQIYDLLD-PASRNLKLREDIKKGVYVENLV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 185 EVEFGSLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRPVSPASLVPQSPqlppadageppagGKLCFVDLAG 264
Cdd:cd01373  176 EEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVNIRT-------------SRLNLVDLAG 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 265 SEKVTATGSRGELMLEANSINRSLLALGHCISLLLD-PQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLP 343
Cdd:cd01373  243 SERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFG 322

                        250
                 ....*....|....*....
gi 947207764 344 ETLSTLRYASRAQRVTTRP 362
Cdd:cd01373  323 ETLSTLRFAQRAKLIKNKA 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 122-427 4.10e-47

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 179.75  E-value: 4.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  122 GIMQRTFAWLLDRV---------QRLGSQVtlRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLE 192
Cdd:PLN03188  201 GLTPRVFERLFARIneeqikhadRQLKYQC--RCSFLEIYNEQITDLLD-PSQKNLQIREDVKSGVYVENLTEEYVKTMK 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  193 ALMELLQKGLSRRRSSAHSLNQASSRSHALLTlhiCrpvspaslVPQSPQLPPADAGEPPAGGKLCFVDLAGSEKVTATG 272
Cdd:PLN03188  278 DVTQLLIKGLSNRRTGATSINAESSRSHSVFT---C--------VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTG 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  273 SRGELMLEANSINRSLLALGHCISLLLDPQR--KQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLR 350
Cdd:PLN03188  347 AAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLR 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764  351 YASRAQRVTTRpqapkspvAKQPQRLETEVLQLQEENRRLRFQLDQMdpKASSSGPSGARVA----WAQRNLYGMLQEFM 426
Cdd:PLN03188  427 FAQRAKAIKNK--------AVVNEVMQDDVNFLREVIRQLRDELQRV--KANGNNPTNPNVAystaWNARRSLNLLKSFG 496


                  .
gi 947207764  427 L 427
Cdd:PLN03188  497 L 497
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 121-356 8.85e-47

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 168.73  E-value: 8.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 121 AGIMQRTFAWLLDRVQRLGSQVtlraSYLEIYNEQVRDLLSLGSS------RPLPVRWNKTRGFYVEQLREVEFGSLEAL 194
Cdd:cd01368  113 GGILPRSLDVIFNSIGGYSVFV----SYIEIYNEYIYDLLEPSPSsptkkrQSLRLREDHNGNMYVAGLTEIEVKSTEEA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 195 MELLQKGLSRRRSSAHSLNQASSRSHALLTLHICRpvSPASLVPQSPQLPpadagEPPAGGKLCFVDLAGSEKVTATGSR 274
Cdd:cd01368  189 RKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ--APGDSDGDVDQDK-----DQITVSQLSLVDLAGSERTSRTQNT 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 275 GELMLEANSINRSLLALGHCISLLLDPQ--RKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYA 352
Cdd:cd01368  262 GERLKEAGNINTSLMTLGTCIEVLRENQlqGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341


                 ....
gi 947207764 353 SRAQ 356
Cdd:cd01368  342 AIAQ 345
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 146-354 2.28e-44

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 161.69  E-value: 2.28e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 146 ASYLEIYNEQVRDLLSlgSSRPLPVRWNKTRGFYVEQLREVEFGSLEALMELLQKGLSRRRSSAHSLNQASSRSHALLTL 225
Cdd:cd01367  139 VSFFEIYGGKVFDLLN--RKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 226 hICRpvspaslvpqspqlppaDAGEPPAGGKLCFVDLAGSEKVTATGSRG-ELMLEANSINRSLLALGHCISLLldpQRK 304
Cdd:cd01367  217 -ILR-----------------DRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRAL---GQN 275

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 947207764 305 QSHIPFRDSKLTKLLADSL-GGRGVTLMVACVSPSAQCLPETLSTLRYASR 354
Cdd:cd01367  276 KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 122-354 3.08e-44

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 161.21  E-value: 3.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 122 GIMQRTFAWLLDRVQRLGSQV-TLRASYLEIYNEQVRDLLS-----LGSSRPLPVRWNKTRGFYVEQLREVEFGSLEALM 195
Cdd:cd01375  109 GIIPRALQQVFRMIEERPTKAyTVHVSYLEIYNEQLYDLLStlpyvGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEAL 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 196 ELLQKGLSRRRSSAHSLNQASSRSHALLTLHI-CRPVSPASlvpqspqlppadagEPPAGGKLCFVDLAGSEKVTATGSR 274
Cdd:cd01375  189 SLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeAHSRTLSS--------------EKYITSKLNLVDLAGSERLSKTGVE 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 275 GELMLEANSINRSLLALGHCISLLLDPQRkqSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASR 354
Cdd:cd01375  255 GQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 118-356 4.20e-41

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 152.27  E-value: 4.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 118 PSLAGIMQRTFAWLLDRVQRLGSQVTLRASYLEIYNEQVRDLLSlGSSRPLPVRWNKTRGFYVEQLREVEFGSLEALMEL 197
Cdd:cd01376   99 PEQPGLMPLTVMDLLQMTRKEAWALSFTMSYLEIYQEKILDLLE-PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEA 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947207764 198 LQKGLSRRRSSAHSLNQASSRSHALLTLHIcrpVSPASLVPQSPQLppadageppagGKLCFVDLAGSEKVTATGSRGEL 277
Cdd:cd01376  178 FLPASKNRTVAATRLNDNSSRSHAVLLIKV---DQRERLAPFRQRT-----------GKLNLIDLAGSEDNRRTGNEGIR 243

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 947207764 278 MLEANSINRSLLALGHCISLLLdpqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQ 356
Cdd:cd01376  244 LKESGAINSSLFVLSKVVNALN---KNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 466-544 1.08e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.39  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 947207764 466 SICHLRHSGPGPAPPCACWMGPAHPCYALPPLCSCPCChLCPLAHWACPRrehhlQQVPSPEPPGGLPLSARPPPCVPP 544
Cdd:PHA02682  70 SACMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAV-TCPAPAPACPP-----ATAPTCPPPAVCPAPARPAPACPP 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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