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Conserved domains on  [gi|1622836834|ref|XP_028683175|]
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kinesin-like protein KIF3B isoform X1 [Macaca mulatta]

Protein Classification

kinesin-like protein( domain architecture ID 12916170)

kinesin-like protein such as KIF3A/3B/3C, which are microtubule-based anterograde translocators for membranous organelles

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-340 0e+00

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: 692.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:cd01371     1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  88 FNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 1622836834 327 TLTTLRYANRAKNI 340
Cdd:cd01371   321 TLSTLRYANRAKNI 334
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
355-581 7.48e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 355 LREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGddkddywREQQEKLEIEKRAIVEDHSL 434
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-------QAEEYELLAELARLEQDIAR 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 435 VAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQME 514
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-----------EAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836834 515 SQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELK 581
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
 
Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-340 0e+00

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: 692.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:cd01371     1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  88 FNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 1622836834 327 TLTTLRYANRAKNI 340
Cdd:cd01371   321 TLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
15-340 2.25e-172

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 497.48  E-value: 2.25e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  15 RCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKgTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFA 94
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVESSHL-TNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  95 YGQTGTGKTYTMEGirgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQTK--RLELKERPD 171
Cdd:pfam00225  80 YGQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIqKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrKLRIREDPK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 172 TGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSER 251
Cdd:pfam00225 157 KGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 252 QAKTG-AQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTT 330
Cdd:pfam00225 237 ASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLST 316
                         330
                  ....*....|
gi 1622836834 331 LRYANRAKNI 340
Cdd:pfam00225 317 LRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-347 5.33e-167

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: 484.00  E-value: 5.33e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834    9 SVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQ-VSVKNPKGTAHEmpKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKtLTVRSPKNRQGE--KKFTFDKVFDATASQEDVFEETAAPLVDSVLEG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   88 FNGTIFAYGQTGTGKTYTMEGirgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQtKRLEL 166
Cdd:smart00129  79 YNATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIdKREEGWQFSVKVSYLEIYNEKIRDLLNPSS-KKLEI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGlDGENHIRVGKLNLVDL 246
Cdd:smart00129 155 REDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:smart00129 234 AGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLE 313
                          330       340
                   ....*....|....*....|..
gi 1622836834  326 ETLTTLRYANRAKNIKNKPRVN 347
Cdd:smart00129 314 ETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
54-347 1.14e-87

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 287.02  E-value: 1.14e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  54 PKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPekrGVIPNSFDHIFTHIS-R 132
Cdd:COG5059    55 EGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEdL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 133 SQNQQYLVRASYLEIYQEEIRDLLSKDqTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHS 212
Cdd:COG5059   132 SMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDES 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 213 SRSHAIFVITIECSEVGLDgenHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIP 291
Cdd:COG5059   211 SRSHSIFQIELASKNKVSG---TSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIP 287
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836834 292 YRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVN 347
Cdd:COG5059   288 YRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
PLN03188 PLN03188
kinesin-12 family protein; Provisional
6-367 2.27e-82

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 286.06  E-value: 2.27e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834    6 SSESVRVVVRCRPMNGKEKaasydkvvdvdvklGQVSVKNPKGTAHEM-PKTFTFDAVYDWNAKQFELYDETFRPLVDSV 84
Cdd:PLN03188    96 SDSGVKVIVRMKPLNKGEE--------------GEMIVQKMSNDSLTInGQTFTFDSIADPESTQEDIFQLVGAPLVENC 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   85 LQGFNGTIFAYGQTGTGKTYTM---------EGIRGDpeKRGVIPNSFDHIFTHISRSQNQ------QYLVRASYLEIYQ 149
Cdd:PLN03188   162 LAGFNSSVFAYGQTGSGKTYTMwgpanglleEHLSGD--QQGLTPRVFERLFARINEEQIKhadrqlKYQCRCSFLEIYN 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  150 EEIRDLLSKDQtKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIE--CSE 227
Cdd:PLN03188   240 EQITDLLDPSQ-KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrCKS 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  228 VGlDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD----GKSTHIPYRDSKLTRLLQD 303
Cdd:PLN03188   319 VA-DGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQE 397
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  304 SLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKD------ALLREFQEEIARLKA 367
Cdd:PLN03188   398 SLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
355-581 7.48e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 355 LREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGddkddywREQQEKLEIEKRAIVEDHSL 434
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-------QAEEYELLAELARLEQDIAR 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 435 VAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQME 514
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-----------EAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836834 515 SQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELK 581
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
437-602 2.16e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 437 EEKMRLLKEKEKKMEDLRRE----KDAAEMLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQ 512
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKEnqsyKQEIKNLESQINDLESKIQ-----------NQEKLNQQKDEQIKKLQQEKELLEKE 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 513 MESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTR-ELKLKHLIIENfI 591
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkEKELKKLNEEK-K 506
                         170
                  ....*....|.
gi 1622836834 592 PLEEKSKIMNR 602
Cdd:TIGR04523 507 ELEEKVKDLTK 517
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
415-628 2.35e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEDHSLVAEekmrlLKEKEKKMEDLRREKdaAEMLGAKIKAMESKLlvggKNIVDHTNEQQKILEQ 494
Cdd:pfam02463  769 LSLKEKELAEEREKTEKLKVEEE-----KEEKLKAQEEELRAL--EEELKEEAELLEEEQ----LLIEQEEKIKEEELEE 837
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  495 KRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQN 574
Cdd:pfam02463  838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622836834  575 ELTRELKLKHLIIENFIPLEEKSKIMNRAFFDEEEDHwklHPITRLENQQMMKR 628
Cdd:pfam02463  918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---KEEEEERNKRLLLA 968
PRK12704 PRK12704
phosphodiesterase; Provisional
436-598 2.38e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 436 AEEKM-RLLKEKEKKMEDLRREKdaaeMLGAKIKAMESKllvggknivdhtNEQQKILEQKRQEIAEQKRREREIQQQME 514
Cdd:PRK12704   36 AEEEAkRILEEAKKEAEAIKKEA----LLEAKEEIHKLR------------NEFEKELRERRNELQKLEKRLLQKEENLD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 515 SQDEEtLELKEtysslqQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHikeRQELEQTQNeLTRElKLKHLIIENfipLE 594
Cdd:PRK12704  100 RKLEL-LEKRE------EELEKKEKELEQKQQELEKKEEELEELIEEQ---LQELERISG-LTAE-EAKEILLEK---VE 164

                  ....
gi 1622836834 595 EKSK 598
Cdd:PRK12704  165 EEAR 168
 
Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-340 0e+00

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: 692.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:cd01371     1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  88 FNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 1622836834 327 TLTTLRYANRAKNI 340
Cdd:cd01371   321 TLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
15-340 2.25e-172

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 497.48  E-value: 2.25e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  15 RCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKgTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFA 94
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVESSHL-TNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  95 YGQTGTGKTYTMEGirgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQTK--RLELKERPD 171
Cdd:pfam00225  80 YGQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIqKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrKLRIREDPK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 172 TGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSER 251
Cdd:pfam00225 157 KGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 252 QAKTG-AQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTT 330
Cdd:pfam00225 237 ASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLST 316
                         330
                  ....*....|
gi 1622836834 331 LRYANRAKNI 340
Cdd:pfam00225 317 LRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
9-338 8.16e-170

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: 491.00  E-value: 8.16e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGKEkAASYDKVVDVDVKlGQVSVKNPKGTaHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGF 88
Cdd:cd00106     1 NVRVAVRVRPLNGRE-ARSAKSVISVDGG-KSVVLDPPKNR-VAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  89 NGTIFAYGQTGTGKTYTMEGIrgDPEKRGVIPNSFDHIFTHIS--RSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd00106    78 NGTIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDkrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGEnHIRVGKLNLVDL 246
Cdd:cd00106   156 REDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE-SVTSSKLNLVDL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd00106   235 AGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEE 314
                         330
                  ....*....|..
gi 1622836834 327 TLTTLRYANRAK 338
Cdd:cd00106   315 TLSTLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-347 5.33e-167

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: 484.00  E-value: 5.33e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834    9 SVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQ-VSVKNPKGTAHEmpKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKtLTVRSPKNRQGE--KKFTFDKVFDATASQEDVFEETAAPLVDSVLEG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   88 FNGTIFAYGQTGTGKTYTMEGirgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQtKRLEL 166
Cdd:smart00129  79 YNATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIdKREEGWQFSVKVSYLEIYNEKIRDLLNPSS-KKLEI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGlDGENHIRVGKLNLVDL 246
Cdd:smart00129 155 REDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:smart00129 234 AGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLE 313
                          330       340
                   ....*....|....*....|..
gi 1622836834  326 ETLTTLRYANRAKNIKNKPRVN 347
Cdd:smart00129 314 ETLSTLRFASRAKEIKNKPIVN 335
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
9-341 2.39e-131

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: 392.85  E-value: 2.39e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVknpkGTAhempKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGF 88
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTV----GTD----KSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  89 NGTIFAYGQTGTGKTYTMEG---IRGDPEKRGVIPNSFDHIFTHISRSQNQ-QYLVRASYLEIYQEEIRDLLSK--DQTK 162
Cdd:cd01372    74 NATVLAYGQTGSGKTYTMGTaytAEEDEEQVGIIPRAIQHIFKKIEKKKDTfEFQLKVSFLEIYNEEIRDLLDPetDKKP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 163 RLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIE-------CSEVGLDGENH 235
Cdd:cd01372   154 TISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpIAPMSADDKNS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 236 IRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNAKTVM 313
Cdd:cd01372   234 TFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDEskKGAHVPYRDSKLTRLLQDSLGGNSHTLM 313
                         330       340
                  ....*....|....*....|....*...
gi 1622836834 314 VANVGPASYNVEETLTTLRYANRAKNIK 341
Cdd:cd01372   314 IACVSPADSNFEETLNTLKYANRARNIK 341
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
10-349 6.53e-127

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: 382.06  E-value: 6.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFN 89
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  90 GTIFAYGQTGTGKTYTMEGIRGD--------PEKRGVIPNSFDHIFTHISrSQNQQYLVRASYLEIYQEEIRDLLS--KD 159
Cdd:cd01364    84 CTIFAYGQTGTGKTYTMEGDRSPneeytwelDPLAGIIPRTLHQLFEKLE-DNGTEYSVKVSYLEIYNEELFDLLSpsSD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 160 QTKRLELKERPDT--GVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIR 237
Cdd:cd01364   163 VSERLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 238 VGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDgKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANV 317
Cdd:cd01364   243 IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIATI 321
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1622836834 318 GPASYNVEETLTTLRYANRAKNIKNKPRVNED 349
Cdd:cd01364   322 SPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
9-340 1.22e-126

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: 380.14  E-value: 1.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGKEKAASYDKVVDVDvklgqvsvknPKGTAH----EMPKTFTFDAVYDWNAKQFELYDETFRPLVDSV 84
Cdd:cd01369     3 NIKVVCRFRPLNELEVLQGSKSIVKFD----------PEDTVViatsETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  85 LQGFNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRS-QNQQYLVRASYLEIYQEEIRDLLSKdQTKR 163
Cdd:cd01369    73 LNGYNGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMdENLEFHVKVSYFEIYMEKIRDLLDV-SKTN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 164 LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVgLDGEnhIRVGKLNL 243
Cdd:cd01369   152 LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENV-ETEK--KKSGKLYL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 244 VDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYN 323
Cdd:cd01369   229 VDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYN 308
                         330
                  ....*....|....*..
gi 1622836834 324 VEETLTTLRYANRAKNI 340
Cdd:cd01369   309 ESETLSTLRFGQRAKTI 325
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
10-342 8.55e-126

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: 378.09  E-value: 8.55e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEmpktFTFDAVYDWNAKQFELYDETfRPLVDSVLQGFN 89
Cdd:cd01366     4 IRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAKQKE----FSFDKVFDPEASQEDVFEEV-SPLVQSALDGYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  90 GTIFAYGQTGTGKTYTMEGirgDPEKRGVIPNSFDHIFTHISRSQNQ--QYLVRASYLEIYQEEIRDLLSKD--QTKRLE 165
Cdd:cd01366    79 VCIFAYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgwSYTIKASMLEIYNETIRDLLAPGnaPQKKLE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 166 LKERPDTG-VYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEcsevgldGEN----HIRVGK 240
Cdd:cd01366   156 IRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS-------GRNlqtgEISVGK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 241 LNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKStHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPA 320
Cdd:cd01366   229 LNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS-HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPA 307
                         330       340
                  ....*....|....*....|..
gi 1622836834 321 SYNVEETLTTLRYANRAKNIKN 342
Cdd:cd01366   308 ESNLNETLNSLRFASKVNSCEL 329
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
8-347 6.47e-124

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: 374.38  E-value: 6.47e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKlgQVSVKNPKGTAHEM------PKTFTFDAVYdWN--------AKQFELY 73
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGK--ETTLKNPKQADKNNkatrevPKSFSFDYSY-WShdsedpnyASQEQVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  74 DETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMegiRGDPEKRGVIPNSFDHIFTHISRSQNQ--QYLVRASYLEIYQEE 151
Cdd:cd01365    78 EDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTM---MGTQEQPGIIPRLCEDLFSRIADTTNQnmSYSVEVSYMEIYNEK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 152 IRDLLSKDQTKR---LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEC--- 225
Cdd:cd01365   155 VRDLLNPKPKKNkgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQkrh 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 226 -SEVGLDGEnhiRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-------GKSTHIPYRDSKL 297
Cdd:cd01365   235 dAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622836834 298 TRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVN 347
Cdd:cd01365   312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
9-340 1.47e-120

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: 364.35  E-value: 1.47e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGKEKAASYDK--VVDVDVklgqVSVKNPKGTAhempktFTFDAVYDWNAKQFELYDETFRPLVDSVLQ 86
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVawEIDNDT----IYLVEPPSTS------FTFDHVFGGDSTNREVYELIAKPVVKSALE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  87 GFNGTIFAYGQTGTGKTYTMegiRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKdQTKRLEL 166
Cdd:cd01374    71 GYNGTIFAYGQTSSGKTFTM---SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSP-TSQNLKI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01374   147 RDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGK-STHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:cd01374   227 AGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVE 306
                         330
                  ....*....|....*
gi 1622836834 326 ETLTTLRYANRAKNI 340
Cdd:cd01374   307 ETLNTLKFASRAKKI 321
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
9-340 3.75e-119

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: 361.66  E-value: 3.75e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGKEKAASYDKVVDV--------------DVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYD 74
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdpkdeeDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  75 ETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPekrGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIR 153
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIeSLKDEKEFEVSMSYLEIYNETIR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 154 DLLSKdQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGE 233
Cdd:cd01370   158 DLLNP-SSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASIN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 234 NHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNAKT 311
Cdd:cd01370   237 QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPgkKNKHIPYRDSKLTRLLKDSLGGNCRT 316
                         330       340
                  ....*....|....*....|....*....
gi 1622836834 312 VMVANVGPASYNVEETLTTLRYANRAKNI 340
Cdd:cd01370   317 VMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
10-349 3.56e-110

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: 338.33  E-value: 3.56e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPkgtahemPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFN 89
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKP-------PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  90 GTIFAYGQTGTGKTYTMEGIRGDPEK-----RGVIPNSFDHIFTHISRSQ-----NQQYLVRASYLEIYQEEIRDLLskD 159
Cdd:cd01373    76 GTIFAYGQTGSGKTYTMWGPSESDNEsphglRGVIPRIFEYLFSLIQREKekageGKSFLCKCSFLEIYNEQIYDLL--D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 160 QTKR-LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGlDGENHIRV 238
Cdd:cd01373   154 PASRnLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKK-ACFVNIRT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 239 GKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVA 315
Cdd:cd01373   233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622836834 316 NVGPASYNVEETLTTLRYANRAKNIKNKPRVNED 349
Cdd:cd01373   313 NVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
54-347 1.14e-87

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 287.02  E-value: 1.14e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  54 PKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPekrGVIPNSFDHIFTHIS-R 132
Cdd:COG5059    55 EGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEdL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 133 SQNQQYLVRASYLEIYQEEIRDLLSKDqTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHS 212
Cdd:COG5059   132 SMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDES 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 213 SRSHAIFVITIECSEVGLDgenHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIP 291
Cdd:COG5059   211 SRSHSIFQIELASKNKVSG---TSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIP 287
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836834 292 YRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVN 347
Cdd:COG5059   288 YRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
9-338 2.90e-84

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: 270.61  E-value: 2.90e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGK--------EKAASYDKVVDVDVKLGQVsvkNPKGTAHempkTFTFDAVYDwNAKQFELYDETFRPL 80
Cdd:cd01375     1 KVQAFVRVRPTDDFahemikygEDGKSISIHLKKDLRRGVV---NNQQEDW----SFKFDGVLH-NASQELVYETVAKDV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  81 VDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSK-- 158
Cdd:cd01375    73 VSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTlp 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 159 ---DQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLdGENH 235
Cdd:cd01375   153 yvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTL-SSEK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 236 IRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVA 315
Cdd:cd01375   232 YITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVA 311
                         330       340
                  ....*....|....*....|...
gi 1622836834 316 NVGPASYNVEETLTTLRYANRAK 338
Cdd:cd01375   312 NIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
10-338 1.37e-82

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: 265.52  E-value: 1.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  10 VRVVVRCRP-MNGKEKAASYDKVVDVDVKlgQVSVKNPkgTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGF 88
Cdd:cd01376     2 VRVAVRVRPfVDGTAGASDPSCVSGIDSC--SVELADP--RNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  89 NGTIFAYGQTGTGKTYTMEgirGDPEKRGVIPNSFDHIFTHiSRSQNQQYLVRASYLEIYQEEIRDLLSKdQTKRLELKE 168
Cdd:cd01376    78 NATVFAYGSTGAGKTFTML---GSPEQPGLMPLTVMDLLQM-TRKEAWALSFTMSYLEIYQEKILDLLEP-ASKELVIRE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 169 RPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIecSEVGLDGENHIRVGKLNLVDLAG 248
Cdd:cd01376   153 DKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--DQRERLAPFRQRTGKLNLIDLAG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 249 SERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKStHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETL 328
Cdd:cd01376   231 SEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTL 309
                         330
                  ....*....|
gi 1622836834 329 TTLRYANRAK 338
Cdd:cd01376   310 STLNFAARSR 319
PLN03188 PLN03188
kinesin-12 family protein; Provisional
6-367 2.27e-82

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 286.06  E-value: 2.27e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834    6 SSESVRVVVRCRPMNGKEKaasydkvvdvdvklGQVSVKNPKGTAHEM-PKTFTFDAVYDWNAKQFELYDETFRPLVDSV 84
Cdd:PLN03188    96 SDSGVKVIVRMKPLNKGEE--------------GEMIVQKMSNDSLTInGQTFTFDSIADPESTQEDIFQLVGAPLVENC 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   85 LQGFNGTIFAYGQTGTGKTYTM---------EGIRGDpeKRGVIPNSFDHIFTHISRSQNQ------QYLVRASYLEIYQ 149
Cdd:PLN03188   162 LAGFNSSVFAYGQTGSGKTYTMwgpanglleEHLSGD--QQGLTPRVFERLFARINEEQIKhadrqlKYQCRCSFLEIYN 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  150 EEIRDLLSKDQtKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIE--CSE 227
Cdd:PLN03188   240 EQITDLLDPSQ-KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrCKS 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  228 VGlDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD----GKSTHIPYRDSKLTRLLQD 303
Cdd:PLN03188   319 VA-DGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQE 397
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  304 SLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKD------ALLREFQEEIARLKA 367
Cdd:PLN03188   398 SLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
10-338 8.61e-80

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: 258.38  E-value: 8.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLgQVSVKNPKGTAHEMPK----TFTFDAVYDWNAKQFELYDETFRPLVDSVL 85
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKL-TLIVHEPKLKVDLTKYienhTFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  86 QGFNGTIFAYGQTGTGKTYTMEG-IRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDqtKR 163
Cdd:cd01367    81 EGGKATCFAYGQTGSGKTYTMGGdFSGQEESKGIYALAARDVFRLLNKLPyKDNLGVTVSFFEIYGGKVFDLLNRK--KR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 164 LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEcsevglDGENHIRVGKLNL 243
Cdd:cd01367   159 VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR------DRGTNKLHGKLSF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 244 VDLAGSERQAKTGAQG-ERLKEATKINLSLSALGNVISALVDGKStHIPYRDSKLTRLLQDSL-GGNAKTVMVANVGPAS 321
Cdd:cd01367   233 VDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA-HIPFRGSKLTQVLKDSFiGENSKTCMIATISPGA 311
                         330
                  ....*....|....*..
gi 1622836834 322 YNVEETLTTLRYANRAK 338
Cdd:cd01367   312 SSCEHTLNTLRYADRVK 328
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
8-338 6.84e-79

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: 256.55  E-value: 6.84e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   8 ESVRVVVRCRPMNGKEKAASYDKVVDVdVKLGQVSVKNPKGT-AHEMPKT-------FTFDAVYDWNAKQFELYDETFRP 79
Cdd:cd01368     1 DPVKVYLRVRPLSKDELESEDEGCIEV-INSTTVVLHPPKGSaANKSERNggqketkFSFSKVFGPNTTQKEFFQGTALP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  80 LVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPekrGVIPNSFDHIFTHIsrsqnQQYLVRASYLEIYQEEIRDLL--- 156
Cdd:cd01368    80 LVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSI-----GGYSVFVSYIEIYNEYIYDLLeps 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 157 SKDQTKR---LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGE 233
Cdd:cd01368   152 PSSPTKKrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 234 -----NHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISAL----VDGKSTHIPYRDSKLTRLLQDS 304
Cdd:cd01368   232 vdqdkDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLFQNY 311
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622836834 305 LGGNAKTVMVANVGPASYNVEETLTTLRYANRAK 338
Cdd:cd01368   312 FDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
55-281 1.10e-21

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 92.79  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  55 KTFTFDAVYDWNAKQFELYDETfRPLVDSVLQGFNG-TIFAYGQTGTGKTYTMEGIrgdpekrgvIPNSFDHIFTHISRS 133
Cdd:cd01363    18 KIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNNqSIFAYGESGAGKTETMKGV---------IPYLASVAFNGINKG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 134 QNQqylvrasyLEIYQEEIRDLLSKdqtkrlelkerpdtgvyvkdlssfvtksvkEIEHVMNVGNQNRsVGATNMNEHSS 213
Cdd:cd01363    88 ETE--------GWVYLTEITVTLED------------------------------QILQANPILEAFG-NAKTTRNENSS 128
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622836834 214 RSHAIFVItiecsevgldgenhirvgklnLVDLAGSERqaktgaqgerlkeatkINLSLSALGNVISA 281
Cdd:cd01363   129 RFGKFIEI---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
9-156 1.50e-21

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 91.51  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834   9 SVRVVVRCRPMNGKEKAASYDkvvDVDVKLGQVSVKNpkgtahempKTFTFDAVYDWNAKQFELYDEtFRPLVDSVLQGF 88
Cdd:pfam16796  21 NIRVFARVRPELLSEAQIDYP---DETSSDGKIGSKN---------KSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGY 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836834  89 NGTIFAYGQTGTGKTytmegirgdpekRGVIPNSFDHIFTHISRSQNQ-QYLVRASYLEIYQEEIRDLL 156
Cdd:pfam16796  88 NVCIFAYGQTGSGSN------------DGMIPRAREQIFRFISSLKKGwKYTIELQFVEIYNESSQDLL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
355-581 7.48e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 355 LREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGddkddywREQQEKLEIEKRAIVEDHSL 434
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-------QAEEYELLAELARLEQDIAR 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 435 VAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQME 514
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-----------EAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836834 515 SQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELK 581
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
415-588 8.35e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 8.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 415 REQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQ 494
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 495 KRQEIAEQKRREREIQQQmESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQN 574
Cdd:COG1196   406 EEAEEALLERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
                         170
                  ....*....|....
gi 1622836834 575 ELTRELKLKHLIIE 588
Cdd:COG1196   485 ELAEAAARLLLLLE 498
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
92-285 8.97e-06

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 48.97  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  92 IFAYGQTGTGKTYTMEgirgdpEKRGVIPNSFD-HIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERP 170
Cdd:COG5059   385 IFAYMQSLKKETETLK------SRIDLIMKSIIsGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIH 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 171 DTGVYVKDLSSFVTKSVKEIEH-VMNVGNQ-NRSVGATNMNEHSSRSHaifviTIECSEvgLDGENHIR-VGKLNLVDLA 247
Cdd:COG5059   459 KLNKLRHDLSSLLSSIPEETSDrVESEKASkLRSSASTKLNLRSSRSH-----SKFRDH--LNGSNSSTkELSLNQVDLA 531
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622836834 248 GSERQAKTgAQGERLKEATKINLSLSALGNVISALVDG 285
Cdd:COG5059   532 GSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHALGSK 568
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
437-602 2.16e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 437 EEKMRLLKEKEKKMEDLRRE----KDAAEMLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQ 512
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKEnqsyKQEIKNLESQINDLESKIQ-----------NQEKLNQQKDEQIKKLQQEKELLEKE 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 513 MESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTR-ELKLKHLIIENfI 591
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkEKELKKLNEEK-K 506
                         170
                  ....*....|.
gi 1622836834 592 PLEEKSKIMNR 602
Cdd:TIGR04523 507 ELEEKVKDLTK 517
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
414-588 2.75e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 414 WREQQEKLEIEKRAI-VEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEmlgAKIKAMESKLlvggknivdhtNEQQKIL 492
Cdd:COG1196   218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELE---AELEELRLEL-----------EELELEL 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 493 EQKRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQT 572
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                         170
                  ....*....|....*.
gi 1622836834 573 QNELTRELKLKHLIIE 588
Cdd:COG1196   364 EEALLEAEAELAEAEE 379
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
415-580 2.96e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDA-AEMLGAKIKAMESKLLVGGKNIvdhtNEQQKILE 493
Cdd:TIGR02168  216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAeLQELEEKLEELRLEVSELEEEI----EELQKELY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  494 QKRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIK---ERQELE 570
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELEELE 371
                          170
                   ....*....|
gi 1622836834  571 QTQNELTREL 580
Cdd:TIGR02168  372 SRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
442-609 3.02e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 442 LLKEKEKKMEDLRREKDAAE---MLGAKIKAMESKLLVGGKNIVDHT-NEQQKILEQKRQEIAEQKRREREIQQQMESQD 517
Cdd:COG1196   194 ILGELERQLEPLERQAEKAEryrELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 518 EETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKS 597
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                         170
                  ....*....|..
gi 1622836834 598 KIMNRAFFDEEE 609
Cdd:COG1196   354 EEAEAELAEAEE 365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
436-615 6.88e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  436 AEEKMRLLKEK----EKKMEDLRREKDAAEMLGAKIKA----MESKLLVGGKNIVDHTNEQQKILEQKRQ---EIAEQKR 504
Cdd:TIGR02168  682 LEEKIEELEEKiaelEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLARLEAEVEQLEERIAQlskELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  505 REREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKH 584
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622836834  585 LIIENFIPLEEKSKIMNRAFFDEEEDHWKLH 615
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELE 872
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
352-533 2.34e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  352 DALLREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGDDKDDYWREQQEKLEIEKRAIVED 431
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  432 HSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKllvggknivdhtneqqkiLEQKRQEIAEQKRREREIQQ 511
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE------------------KEDKALEIKKQEWKLEQLAA 462
                          170       180
                   ....*....|....*....|..
gi 1622836834  512 QMESQDEETLELKETYSSLQQE 533
Cdd:TIGR02169  463 DLSKYEQELYDLKEEYDRVEKE 484
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
415-628 2.35e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEDHSLVAEekmrlLKEKEKKMEDLRREKdaAEMLGAKIKAMESKLlvggKNIVDHTNEQQKILEQ 494
Cdd:pfam02463  769 LSLKEKELAEEREKTEKLKVEEE-----KEEKLKAQEEELRAL--EEELKEEAELLEEEQ----LLIEQEEKIKEEELEE 837
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  495 KRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQN 574
Cdd:pfam02463  838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622836834  575 ELTRELKLKHLIIENFIPLEEKSKIMNRAFFDEEEDHwklHPITRLENQQMMKR 628
Cdd:pfam02463  918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---KEEEEERNKRLLLA 968
PRK12704 PRK12704
phosphodiesterase; Provisional
436-598 2.38e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 436 AEEKM-RLLKEKEKKMEDLRREKdaaeMLGAKIKAMESKllvggknivdhtNEQQKILEQKRQEIAEQKRREREIQQQME 514
Cdd:PRK12704   36 AEEEAkRILEEAKKEAEAIKKEA----LLEAKEEIHKLR------------NEFEKELRERRNELQKLEKRLLQKEENLD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 515 SQDEEtLELKEtysslqQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHikeRQELEQTQNeLTRElKLKHLIIENfipLE 594
Cdd:PRK12704  100 RKLEL-LEKRE------EELEKKEKELEQKQQELEKKEEELEELIEEQ---LQELERISG-LTAE-EAKEILLEK---VE 164

                  ....
gi 1622836834 595 EKSK 598
Cdd:PRK12704  165 EEAR 168
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
414-585 3.52e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 414 WREQQEKLEIEKRAIVEDHSLVaeEKMRLLKEKEKKMEDLRREKDAaemLGAKIKAMESKLlvggknivDHTNEQQKILE 493
Cdd:COG4717   100 LEEELEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAE---LPERLEELEERL--------EELRELEEELE 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 494 QKRQEIAEQKRREREIQQQMESQDEETLE-LKETYSSLQQEVdiktkklkklfsklQAVKAEIHDLQEEHIKERQELEQT 572
Cdd:COG4717   167 ELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRL--------------AELEEELEEAQEELEELEEELEQL 232
                         170
                  ....*....|...
gi 1622836834 573 QNELTRELKLKHL 585
Cdd:COG4717   233 ENELEAAALEERL 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
415-596 6.01e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 6.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEkraivedhslvaeekmrllKEKEKKMEDLRREKDAAE--MLGAKIKAMESKLLVGGKNIVDHTNEQQKI- 491
Cdd:TIGR02169  197 RQQLERLRRE-------------------REKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLt 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  492 --LEQKRQEIAEQKRREREIQQQ-MESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQE 568
Cdd:TIGR02169  258 eeISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
                          170       180
                   ....*....|....*....|....*...
gi 1622836834  569 LEQTQNELTRELKLKHLIIENFIPLEEK 596
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEEYAELKEE 365
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
415-614 6.77e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEDhslvAEEKMRLLKEKEKKMEDLRREKDAAemLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQ 494
Cdd:TIGR02169  250 EEELEKLTEEISELEKR----LEEIEQLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEER 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  495 KRQ---EIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDiktkklkKLFSKLQAVKAEIHDLQEEHIKERQELEQ 571
Cdd:TIGR02169  324 LAKleaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE-------DLRAELEEVDKEFAETRDELKDYREKLEK 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622836834  572 TQNELTRELKLKHLIIENFIPLEEKSKIMNRAFFDEEEDHWKL 614
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
454-579 7.95e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 7.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  454 RREKDAAEMLGAKIKAMESKLlvggKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQE 533
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1622836834  534 VDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRE 579
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
415-578 1.15e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIvedHSLVAEEKMRLLKEKEKKME-DLRREKDAAEMLGAKIKAMESKLL--------VGGKNIVDHT 485
Cdd:COG4913    268 RERLAELEYLRAAL---RLWFAQRRLELLEAELEELRaELARLEAELERLEARLDALREELDeleaqirgNGGDRLEQLE 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  486 NEqqkiLEQKRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDiktKKLKKLFSKLQAVKAEIHDLQEEHIKE 565
Cdd:COG4913    345 RE----IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAALRDL 417
                          170
                   ....*....|...
gi 1622836834  566 RQELEQTQNELTR 578
Cdd:COG4913    418 RRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
442-580 1.26e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  442 LLKEKEKKMEDLRREKDAAEMLgAKIKAMESKLLVGgkNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESQDEETL 521
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERY-KELKAELRELELA--LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622836834  522 ELKETYSSLQQEVDiktkklkKLFSKLQAVKAEIHDL--QEEHIKERQE-LEQTQNELTREL 580
Cdd:TIGR02168  271 ELRLEVSELEEEIE-------ELQKELYALANEISRLeqQKQILRERLAnLERQLEELEAQL 325
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
415-585 1.53e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEDhslvAEEKMRLLKEKEKKMEDLRREKDAaemLGAKIKAME---SKLLVGGKNIVDHTNEQQ-K 490
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKER----LEELEEDLSSLEQEIENVKSELKE---LEARIEELEedlHKLEEALNDLEARLSHSRiP 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  491 ILEQKRQEIAEQKRREREIQQQMEsQDEETLELKETYssLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELE 570
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIE-QKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
                          170
                   ....*....|....*..
gi 1622836834  571 QTQNELtREL--KLKHL 585
Cdd:TIGR02169  872 ELEAAL-RDLesRLGDL 887
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
415-572 2.63e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 415 REQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNivdhtneqqKILEQ 494
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN---------KEYEA 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622836834 495 KRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQT 572
Cdd:COG1579    94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
415-578 2.69e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEdhslvaeEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIvdhtNEQQKILEQ 494
Cdd:TIGR02168  294 ANEISRLEQQKQILRE-------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL----ESLEAELEE 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  495 KRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVdiktkklkklfsklQAVKAEIHDLQEEHIKERQELEQTQN 574
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI--------------ERLEARLERLEDRRERLQQEIEELLK 428

                   ....
gi 1622836834  575 ELTR 578
Cdd:TIGR02168  429 KLEE 432
PTZ00121 PTZ00121
MAEBL; Provisional
408-598 3.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  408 DDKDDYWREQQEKLEIEKRAIVEDHSLVAEEK------MRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGK-- 479
Cdd:PTZ00121  1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElk 1653
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  480 -----NIVDHTNEQQKILEQKRQeiAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAE 554
Cdd:PTZ00121  1654 kaeeeNKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622836834  555 IHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSK 598
Cdd:PTZ00121  1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
489-580 3.51e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 489 QKILEQKRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVdiktkklkklfsklQAVKAEIHDLQEEHIKERQE 568
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--------------AALEAELAELEKEIAELRAE 98
                          90
                  ....*....|..
gi 1622836834 569 LEQTQNELTREL 580
Cdd:COG4942    99 LEAQKEELAELL 110
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
415-581 5.57e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 415 REQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMeskLLVGGKNIVDH---------- 484
Cdd:COG4942    68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAvrrlqylkyl 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 485 TNEQQKILEQKRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQeehiK 564
Cdd:COG4942   145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----Q 220
                         170
                  ....*....|....*..
gi 1622836834 565 ERQELEQTQNELTRELK 581
Cdd:COG4942   221 EAEELEALIARLEAEAA 237
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
416-609 8.56e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 416 EQQEKLEIEKRA-IVEDHSLVAEEKMRLL-----KEKEKKMEDLRREKDAAEMlgAKIKAMESKLLVGGKNIVDHTNE-- 487
Cdd:pfam17380 322 EKARQAEMDRQAaIYAEQERMAMERERELerirqEERKRELERIRQEEIAMEI--SRMRELERLQMERQQKNERVRQEle 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834 488 ---QQKILEQKRQ-EIAEQKR------------REREIQQQMESQDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAV 551
Cdd:pfam17380 400 aarKVKILEEERQrKIQQQKVemeqiraeqeeaRQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622836834 552 KAEIHDLQEEHIKERQELEQTQNELTR---ELKLKHLIIENfiPLEEKSKimnrAFFDEEE 609
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEKELEERKQamiEEERKRKLLEK--EMEERQK----AIYEEER 534
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
415-602 8.59e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  415 REQQEKLEIEKRAIVEdhslVAEEKMRLLKEKEKKMEDLRREKDAAEmlgAKIKAMESKLlvggknivdhtNEQQKILEQ 494
Cdd:TIGR02169  853 EKEIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELE---AQLRELERKI-----------EELEAQIEK 914
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836834  495 KRQEIAEQKRREREIQQQMESQDEETLELKETYSSLQQEVDIktkklkklFSKLQAVKAEIHDLQEEHIKERQELEQTQN 574
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--------QAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
                          170       180
                   ....*....|....*....|....*...
gi 1622836834  575 ELTrELKLKHLIIEnfiplEEKSKIMNR 602
Cdd:TIGR02169  987 RLD-ELKEKRAKLE-----EERKAILER 1008
 
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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