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Conserved domains on  [gi|240256264|ref|NP_196285|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

KISc_CENP_E and Smc domain-containing protein( domain architecture ID 12917181)

KISc_CENP_E and Smc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
66-394 8.94e-172

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: 503.40  E-value: 8.94e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEEIAWYADGETIVRnENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsvn 145
Cdd:cd01374    1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYL-VEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYN------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 146 sttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRREFLLRVSYFEIYNEVVNDLLNPAGQNLRIRED- 224
Cdd:cd01374   74 ---GTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDv 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 225 EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGdNNEGGAVHLSQLNLIDLAGS 304
Cdd:cd01374  151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERG-ELEEGTVRVSTLNLIDLAGS 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 305 ESSKAETS-GLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNSEETH 382
Cdd:cd01374  230 ERAAQTGAaGVRRKEGSHINKSLLTLGTVISKLSEgKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETL 309
                        330
                 ....*....|..
gi 240256264 383 NTLKFAHRAKHI 394
Cdd:cd01374  310 NTLKFASRAKKI 321
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
638-953 4.54e-08

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: 57.25  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 638 LREQQKTLSEEmAQQSRSFKLLSEEAAKApQNEEIKAEIINLNGDIKAKNDQIATLgkqildfviashdELDKSDIVQAV 717
Cdd:COG1196  198 LERQLEPLERQ-AEKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAELEEL-------------EAELEELEAEL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 718 SEMRAQLNEKcfELEVKAADNRIIQEQLTEktsfcEDLQEEVANLKQQLSDALELgdinsvtchmqqssqspNKNEEKVI 797
Cdd:COG1196  263 AELEAELEEL--RLELEELELELEEAQAEE-----YELLAELARLEQDIARLEER-----------------RRELEERL 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 798 EAQAFEIEELKLKAAELSELNEQLEIRNKKLAEE-SSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQKSSVT 876
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256264 877 tpQGKTGNLRNGRRESVSKRKEQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLENELA 953
Cdd:COG1196  399 --AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
 
Name Accession Description Interval E-value
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
66-394 8.94e-172

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: 503.40  E-value: 8.94e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEEIAWYADGETIVRnENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsvn 145
Cdd:cd01374    1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYL-VEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYN------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 146 sttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRREFLLRVSYFEIYNEVVNDLLNPAGQNLRIRED- 224
Cdd:cd01374   74 ---GTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDv 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 225 EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGdNNEGGAVHLSQLNLIDLAGS 304
Cdd:cd01374  151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERG-ELEEGTVRVSTLNLIDLAGS 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 305 ESSKAETS-GLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNSEETH 382
Cdd:cd01374  230 ERAAQTGAaGVRRKEGSHINKSLLTLGTVISKLSEgKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETL 309
                        330
                 ....*....|..
gi 240256264 383 NTLKFAHRAKHI 394
Cdd:cd01374  310 NTLKFASRAKKI 321
Kinesin pfam00225
Kinesin motor domain;
72-394 4.41e-132

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 401.18  E-value: 4.41e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   72 RFRPLSPREIRKGEEIAWYADG------ETIVRNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNVTlsvn 145
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESvdsetvESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVT---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  146 sttgtIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETP-RREFLLRVSYFEIYNEVVNDLLNPAGQN---LRI 221
Cdd:pfam00225  77 -----IFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKeRSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  222 REDEQ-GTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLgDNNEGGAVHLSQLNLID 300
Cdd:pfam00225 152 REDPKkGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR-STGGEESVKTGKLNLVD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  301 LAGSESSKA--ETSGLRRKEGSYINKSLLTLGTVISKLTDRRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNS 378
Cdd:pfam00225 231 LAGSERASKtgAAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNY 310
                         330
                  ....*....|....*.
gi 240256264  379 EETHNTLKFAHRAKHI 394
Cdd:pfam00225 311 EETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
66-401 6.84e-117

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: 361.50  E-value: 6.84e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264    66 NVTVTVRFRPLSPREIRKGEEIAWYADG----ETIVRNENN--QSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVN 139
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDkvgkTLTVRSPKNrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   140 vtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQE-TPRREFLLRVSYFEIYNEVVNDLLNPAGQN 218
Cdd:smart00129  81 ---------ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   219 LRIREDEQ-GTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLgdNNEGGAVHLSQLN 297
Cdd:smart00129 152 LEIREDEKgGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIK--NSSSGSGKASKLN 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   298 LIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPAS 375
Cdd:smart00129 230 LVDLAGSErAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSS 309
                          330       340
                   ....*....|....*....|....*.
gi 240256264   376 SNSEETHNTLKFAHRAKHIEIQAAQN 401
Cdd:smart00129 310 SNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
53-485 1.95e-66

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 233.86  E-value: 1.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  53 KPQLPPKPLQSKENVTVTVRFRPlspreiRKGEEIAWYADGETIVRNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVN 132
Cdd:COG5059   10 KSRLSSRNEKSVSDIKSTIRIIP------GELGERLINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 133 GAMAGVNvtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRR-EFLLRVSYFEIYNEVVNDL 211
Cdd:COG5059   84 SLLLGYN---------CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTkDFAVSISYLEIYNEKIYDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 212 LNPAGQNLRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSplgdNNEGGA 290
Cdd:COG5059  155 LSPNEESLNIREDsLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASK----NKVSGT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 291 VHLSQLNLIDLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLI 368
Cdd:COG5059  231 SETSKLSLVDLAGSERaARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVI 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 369 CTVTPASSNSEETHNTLKFAHRAKHIE--IQAAQNKIIDEKSLIKKYQYEIrqLKEELEQLKQGIkpVSQLKDISGDDID 446
Cdd:COG5059  311 CTISPSSNSFEETINTLKFASRAKSIKnkIQVNSSSDSSREIEEIKFDLSE--DRSEIEILVFRE--QSQLSQSSLSGIF 386
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 240256264 447 IVLLKQKLEEEedakaALLSRIQRLTKLILVSNKTPQTS 485
Cdd:COG5059  387 AYMQSLKKETE-----TLKSRIDLIMKSIISGTFERKKL 420
PLN03188 PLN03188
kinesin-12 family protein; Provisional
53-428 1.49e-54

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 207.09  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   53 KPQLPPKPLQSK------------EN------VTVTVRFRPLSpreirKGEEiawyadGETIVRNENNQSIA-----YAY 109
Cdd:PLN03188   68 KSPLPPRPPSSNplkrklsaetapENgvsdsgVKVIVRMKPLN-----KGEE------GEMIVQKMSNDSLTingqtFTF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  110 DRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsvnsttGTIFAYGVTSSGKTHTM------------HGNQRspGIIPL 177
Cdd:PLN03188  137 DSIADPESTQEDIFQLVGAPLVENCLAGFN---------SSVFAYGQTGSGKTYTMwgpanglleehlSGDQQ--GLTPR 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  178 AVKDAFSIIQETPRR------EFLLRVSYFEIYNEVVNDLLNPAGQNLRIREDEQ-GTYIEGIKEEVVLSPAHVLSLIAA 250
Cdd:PLN03188  206 VFERLFARINEEQIKhadrqlKYQCRCSFLEIYNEQITDLLDPSQKNLQIREDVKsGVYVENLTEEYVKTMKDVTQLLIK 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  251 GEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGDNNEGGAVHLSQLNLIDLAGSESSKAE-TSGLRRKEGSYINKSLLTL 329
Cdd:PLN03188  286 GLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTgAAGDRLKEAGNINRSLSQL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  330 GTVISKLTD----RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNSEETHNTLKFAHRAKHIEIQAAQNKIID 405
Cdd:PLN03188  366 GNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQ 445
                         410       420
                  ....*....|....*....|...
gi 240256264  406 EKslIKKYQYEIRQLKEELEQLK 428
Cdd:PLN03188  446 DD--VNFLREVIRQLRDELQRVK 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
638-953 4.54e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 638 LREQQKTLSEEmAQQSRSFKLLSEEAAKApQNEEIKAEIINLNGDIKAKNDQIATLgkqildfviashdELDKSDIVQAV 717
Cdd:COG1196  198 LERQLEPLERQ-AEKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAELEEL-------------EAELEELEAEL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 718 SEMRAQLNEKcfELEVKAADNRIIQEQLTEktsfcEDLQEEVANLKQQLSDALELgdinsvtchmqqssqspNKNEEKVI 797
Cdd:COG1196  263 AELEAELEEL--RLELEELELELEEAQAEE-----YELLAELARLEQDIARLEER-----------------RRELEERL 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 798 EAQAFEIEELKLKAAELSELNEQLEIRNKKLAEE-SSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQKSSVT 876
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256264 877 tpQGKTGNLRNGRRESVSKRKEQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLENELA 953
Cdd:COG1196  399 --AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
712-952 1.08e-06

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: 52.75  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   712 DIVQAVSEMRAQLNEKCFELEVKAADNRIIQEQLTEKTSFCEDLQEEVANLKQQLSDALElgDINSVTcHMQQSSQSPNK 791
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLE-ERIAQLSKELT 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   792 NEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQ 871
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   872 KSSVTTPQGKTGNlrNGRRESVSK-RKEQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLEN 950
Cdd:TIGR02168  838 RRLEDLEEQIEEL--SEDIESLAAeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                   ..
gi 240256264   951 EL 952
Cdd:TIGR02168  916 EL 917
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
597-950 1.14e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 597 EGSALADQIiETMENREahEDSFHEIETPETRIKMI-DQMEILREQQKTLsEEMAQQSRsfkllsEEAAKAPQN-EEIKA 674
Cdd:PRK02224 308 DAEAVEARR-EELEDRD--EELRDRLEECRVAAQAHnEEAESLREDADDL-EERAEELR------EEAAELESElEEARE 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 675 EIINLNGDIKAKNDQIATLGKQI------LDFVIASHDEL--DKSDIVQAVSEMRAQLNE---------------KCFEL 731
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFgdapvdLGNAEDFLEELreERDELREREAELEATLRTarerveeaealleagKCPEC 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 732 EVKAADNRIIqEQLTEKTSFCEDLQEEVANLKQQ---LSDALELGDINSVTCHMQQSSQSPNKNEEKVIEAQAFEIEELK 808
Cdd:PRK02224 458 GQPVEGSPHV-ETIEEDRERVEELEAELEDLEEEveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 809 LKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLaADLAAVQkSSVTTPQGKTGNLRNg 888
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLL-AAIADAEDEIERLRE- 613
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256264 889 RRESVSKRKEQENSLMELKRELTvsKEREVSFEAALIEKIQreaelqrtvEESKQREAYLEN 950
Cdd:PRK02224 614 KREALAELNDERRERLAEKRERK--RELEAEFDEARIEEAR---------EDKERAEEYLEQ 664
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
593-944 1.83e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.48  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  593 SRLSEGSALADQIIETMENREAHEDSfhEIETpetrIKMIDQMEIlrEQQKTLSEEMAQQSRSFKLLSEEA--------- 663
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTK--ELED----IKMSLQRSM--STQKALEEDLQIATKTICQLTEEKeaqmeelnk 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  664 AKAPQN---EEIKAEIINLNGDIKAKNDQIATLGKQILDFVIashdELDKSDivQAVSEMRAQLNEKCFELEVKAADNRI 740
Cdd:pfam05483 343 AKAAHSfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKS--SELEEMTKFKNNKEVELEELKKILAE 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  741 IQEQLTEKTSFcEDLQEEVANLKQQLSDALELGDINSVTCHMQ-QSSQSPNKNEEKVIEAQAFEIEELKLKAAELSELNE 819
Cdd:pfam05483 417 DEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREKEIHDLEIQlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  820 QLEIRNKKLAEEssyakelASAAAIELKALSEEIARLMNHNERLAADLAAVQKSSVttpqgktgNLRNgrrESVSKRKEQ 899
Cdd:pfam05483 496 KLLLENKELTQE-------ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM--------NLRD---ELESVREEF 557
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 240256264  900 ENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQR 944
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
ClyA_MakA-like cd22655
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ...
599-697 7.56e-03

Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.


Pssm-ID: 439153 [Multi-domain]  Cd Length: 342  Bit Score: 39.57  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 599 SALADQIIETMEnreAHEDSFheieTPETRIKMIDQMEILREQQKTLSEEMAQQSRSFKLLSEEAAKAP----------Q 668
Cdd:cd22655   74 SAATSQILNIFK---ALPTAP----DDAQVEQIIALLQALQKPVQEIISNIAAYQGKLKAWGDKMQAAHdnlttgaaqiQ 146
                         90       100       110
                 ....*....|....*....|....*....|.
gi 240256264 669 NEE--IKAEIINLNGDIKAKNDQIATLGKQI 697
Cdd:cd22655  147 AAEtdLQADIDKINNAIANLNAEIAKDNKAI 177
 
Name Accession Description Interval E-value
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
66-394 8.94e-172

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: 503.40  E-value: 8.94e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEEIAWYADGETIVRnENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsvn 145
Cdd:cd01374    1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYL-VEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYN------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 146 sttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRREFLLRVSYFEIYNEVVNDLLNPAGQNLRIRED- 224
Cdd:cd01374   74 ---GTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDv 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 225 EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGdNNEGGAVHLSQLNLIDLAGS 304
Cdd:cd01374  151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERG-ELEEGTVRVSTLNLIDLAGS 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 305 ESSKAETS-GLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNSEETH 382
Cdd:cd01374  230 ERAAQTGAaGVRRKEGSHINKSLLTLGTVISKLSEgKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETL 309
                        330
                 ....*....|..
gi 240256264 383 NTLKFAHRAKHI 394
Cdd:cd01374  310 NTLKFASRAKKI 321
Kinesin pfam00225
Kinesin motor domain;
72-394 4.41e-132

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 401.18  E-value: 4.41e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   72 RFRPLSPREIRKGEEIAWYADG------ETIVRNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNVTlsvn 145
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESvdsetvESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVT---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  146 sttgtIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETP-RREFLLRVSYFEIYNEVVNDLLNPAGQN---LRI 221
Cdd:pfam00225  77 -----IFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKeRSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  222 REDEQ-GTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLgDNNEGGAVHLSQLNLID 300
Cdd:pfam00225 152 REDPKkGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR-STGGEESVKTGKLNLVD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  301 LAGSESSKA--ETSGLRRKEGSYINKSLLTLGTVISKLTDRRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNS 378
Cdd:pfam00225 231 LAGSERASKtgAAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNY 310
                         330
                  ....*....|....*.
gi 240256264  379 EETHNTLKFAHRAKHI 394
Cdd:pfam00225 311 EETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
66-401 6.84e-117

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: 361.50  E-value: 6.84e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264    66 NVTVTVRFRPLSPREIRKGEEIAWYADG----ETIVRNENN--QSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVN 139
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDkvgkTLTVRSPKNrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   140 vtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQE-TPRREFLLRVSYFEIYNEVVNDLLNPAGQN 218
Cdd:smart00129  81 ---------ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   219 LRIREDEQ-GTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLgdNNEGGAVHLSQLN 297
Cdd:smart00129 152 LEIREDEKgGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIK--NSSSGSGKASKLN 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   298 LIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPAS 375
Cdd:smart00129 230 LVDLAGSErAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSS 309
                          330       340
                   ....*....|....*....|....*.
gi 240256264   376 SNSEETHNTLKFAHRAKHIEIQAAQN 401
Cdd:smart00129 310 SNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
66-392 1.49e-107

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: 336.92  E-value: 1.49e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEEIAWYADGETIV----RNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvt 141
Cdd:cd00106    1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVldppKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 142 lsvnsttGTIFAYGVTSSGKTHTMHGNQRS-PGIIPLAVKDAFSIIQETP--RREFLLRVSYFEIYNEVVNDLLNPAGQN 218
Cdd:cd00106   79 -------GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKRKetKSSFSVSASYLEIYNEKIYDLLSPVPKK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 219 -LRIREDE-QGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGDnnEGGAVHLSQL 296
Cdd:cd00106  152 pLSLREDPkRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK--SGESVTSSKL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 297 NLIDLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTDRRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPAS 375
Cdd:cd00106  230 NLVDLAGSERaKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSS 309
                        330
                 ....*....|....*..
gi 240256264 376 SNSEETHNTLKFAHRAK 392
Cdd:cd00106  310 ENFEETLSTLRFASRAK 326
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
66-394 2.45e-95

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: 304.25  E-value: 2.45e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEE-IAWYADGETIVRNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsv 144
Cdd:cd01369    3 NIKVVCRFRPLNELEVLQGSKsIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYN----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 145 nsttGTIFAYGVTSSGKTHTMHG---NQRSPGIIPLAVKDAFSIIQETPRR-EFLLRVSYFEIYNEVVNDLLNPAGQNLR 220
Cdd:cd01369   78 ----GTIFAYGQTSSGKTYTMEGklgDPESMGIIPRIVQDIFETIYSMDENlEFHVKVSYFEIYMEKIRDLLDVSKTNLS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 221 IREDE-QGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESsplgDNNEGGAVHLSQLNLI 299
Cdd:cd01369  154 VHEDKnRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ----ENVETEKKKSGKLYLV 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 300 DLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTDRRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNS 378
Cdd:cd01369  230 DLAGSEKvSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNE 309
                        330
                 ....*....|....*.
gi 240256264 379 EETHNTLKFAHRAKHI 394
Cdd:cd01369  310 SETLSTLRFGQRAKTI 325
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
67-395 2.35e-91

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: 294.24  E-value: 2.35e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  67 VTVTVRFRPLSPREIRKGEEIAW-YADGETIVRNENNQSiaYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNVTlsvn 145
Cdd:cd01372    3 VRVAVRVRPLLPKEIIEGCRICVsFVPGEPQVTVGTDKS--FTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNAT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 146 sttgtIFAYGVTSSGKTHTMHG--NQRSP----GIIPLAVKDAFSIIQETPRR-EFLLRVSYFEIYNEVVNDLLNPAGQ- 217
Cdd:cd01372   77 -----VLAYGQTGSGKTYTMGTayTAEEDeeqvGIIPRAIQHIFKKIEKKKDTfEFQLKVSFLEIYNEEIRDLLDPETDk 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 218 --NLRIREDEQG-TYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGDNNEGGAVHL- 293
Cdd:cd01372  152 kpTISIREDSKGgITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDk 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 294 -----SQLNLIDLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTD--RRASHVPYRDSKLTRLLESSLSGHGRV 365
Cdd:cd01372  232 nstftSKFHFVDLAGSERlKRTGATGDRLKEGISINSGLLALGNVISALGDesKKGAHVPYRDSKLTRLLQDSLGGNSHT 311
                        330       340       350
                 ....*....|....*....|....*....|
gi 240256264 366 SLICTVTPASSNSEETHNTLKFAHRAKHIE 395
Cdd:cd01372  312 LMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
65-394 2.17e-90

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: 291.67  E-value: 2.17e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  65 ENVTVTVRFRPLSPREIRKGEEIAWYAD---GETIVRNENNQSI----AYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAG 137
Cdd:cd01371    1 ENVKVVVRCRPLNGKEKAAGALQIVDVDekrGQVSVRNPKATANeppkTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 138 VNvtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSP---GIIPLAVKDAFSIIQETP-RREFLLRVSYFEIYNEVVNDLL- 212
Cdd:cd01371   81 YN---------GTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLg 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 213 NPAGQNLRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGDNNEGgAV 291
Cdd:cd01371  152 KDQTKRLELKERpDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGEN-HI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 292 HLSQLNLIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKLTDRRASHVPYRDSKLTRLLESSLSGHGRVSLICT 370
Cdd:cd01371  231 RVGKLNLVDLAGSErQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCAN 310
                        330       340
                 ....*....|....*....|....
gi 240256264 371 VTPASSNSEETHNTLKFAHRAKHI 394
Cdd:cd01371  311 IGPADYNYDETLSTLRYANRAKNI 334
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
66-394 8.14e-83

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: 271.53  E-value: 8.14e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKG-------------------EEIAWYADGETIVRNENNQS--IAYAYDRVFGPTTTTRNVYD 124
Cdd:cd01370    1 SLTVAVRVRPFSEKEKNEGfrrivkvmdnhmlvfdpkdEEDGFFHGGSNNRDRRKRRNkeLKYVFDRVFDETSTQEEVYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 125 VAAQHVVNGAMAGVNvtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQET-PRREFLLRVSYFEI 203
Cdd:cd01370   81 ETTKPLVDGVLNGYN---------ATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLkDEKEFEVSMSYLEI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 204 YNEVVNDLLNPAGQNLRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPL 282
Cdd:cd01370  152 YNETIRDLLNPSSGPLELREDaQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 283 GDNNEGGaVHLSQLNLIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKLTD--RRASHVPYRDSKLTRLLESSL 359
Cdd:cd01370  232 TASINQQ-VRQGKLSLIDLAGSErASATNNRGQRLKEGANINRSLLALGNCINALADpgKKNKHIPYRDSKLTRLLKDSL 310
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 240256264 360 SGHGRVSLICTVTPASSNSEETHNTLKFAHRAKHI 394
Cdd:cd01370  311 GGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
65-401 2.78e-82

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: 270.76  E-value: 2.78e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  65 ENVTVTVRFRPLSPREIRKGEEIAWYADG-ETIVRNEN----------NQSIAYAYDRVF------GPT-TTTRNVYDVA 126
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGkETTLKNPKqadknnkatrEVPKSFSFDYSYwshdseDPNyASQEQVYEDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 127 AQHVVNGAMAGVNVTLsvnsttgtiFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRRE--FLLRVSYFEIY 204
Cdd:cd01365   81 GEELLQHAFEGYNVCL---------FAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNmsYSVEVSYMEIY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 205 NEVVNDLLNP----AGQNLRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIES 279
Cdd:cd01365  152 NEKVRDLLNPkpkkNKGNLKVREHpVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 280 SPLGDNNEGGAVHLSQLNLIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKLTD-------RRASHVPYRDSKL 351
Cdd:cd01365  232 KRHDAETNLTTEKVSKISLVDLAGSErASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVL 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 240256264 352 TRLLESSLSGHGRVSLICTVTPASSNSEETHNTLKFAHRAKHIEIQAAQN 401
Cdd:cd01365  312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
66-394 9.39e-82

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: 269.20  E-value: 9.39e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEEIAWYADG---ETIVRNENNQSIA----YAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGV 138
Cdd:cd01364    3 NIQVVVRCRPFNLRERKASSHSVVEVDPvrkEVSVRTGGLADKSstktYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 139 NVTlsvnsttgtIFAYGVTSSGKTHTMHGNQRS-----------PGIIPLAVKDAFSIIQETpRREFLLRVSYFEIYNEV 207
Cdd:cd01364   83 NCT---------IFAYGQTGTGKTYTMEGDRSPneeytweldplAGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 208 VNDLLNPAGQN---LRIRED---EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTI---E 278
Cdd:cd01364  153 LFDLLSPSSDVserLRMFDDprnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIhikE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 279 SSPLGDNneggAVHLSQLNLIDLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTDRrASHVPYRDSKLTRLLES 357
Cdd:cd01364  233 TTIDGEE----LVKIGKLNLVDLAGSENiGRSGAVDKRAREAGNINQSLLTLGRVITALVER-APHVPYRESKLTRLLQD 307
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 240256264 358 SLSGHGRVSLICTVTPASSNSEETHNTLKFAHRAKHI 394
Cdd:cd01364  308 SLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNI 344
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
64-396 7.20e-80

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: 262.92  E-value: 7.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  64 KENVTVTVRFRPLSPREIRKGEEIAWYADGET---IVRNENNQSIAYAYDRVFGPTTTTRNVYdVAAQHVVNGAMAGVNV 140
Cdd:cd01366    1 KGNIRVFCRVRPLLPSEENEDTSHITFPDEDGqtiELTSIGAKQKEFSFDKVFDPEASQEDVF-EEVSPLVQSALDGYNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 141 TlsvnsttgtIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQE--TPRREFLLRVSYFEIYNEVVNDLLNPA--- 215
Cdd:cd01366   80 C---------IFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLAPGnap 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 216 GQNLRIRED--EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIEssplGDNNEGGAVHL 293
Cdd:cd01366  151 QKKLEIRHDseKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS----GRNLQTGEISV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 294 SQLNLIDLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTDRRaSHVPYRDSKLTRLLESSLSGHGRVSLICTVT 372
Cdd:cd01366  227 GKLNLVDLAGSERlNKSGATGDRLKETQAINKSLSALGDVISALRQKQ-SHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
                        330       340
                 ....*....|....*....|....
gi 240256264 373 PASSNSEETHNTLKFAHRAKHIEI 396
Cdd:cd01366  306 PAESNLNETLNSLRFASKVNSCEL 329
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
66-403 3.20e-73

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: 245.50  E-value: 3.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEEIAWYADGETIVRNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsvn 145
Cdd:cd01373    2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYN------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 146 sttGTIFAYGVTSSGKTHTMHGNQRSP--------GIIPLAVKDAFSIIQ-----ETPRREFLLRVSYFEIYNEVVNDLL 212
Cdd:cd01373   76 ---GTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 213 NPAGQNLRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESspLGDNNEGGAV 291
Cdd:cd01373  153 DPASRNLKLREDiKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES--WEKKACFVNI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 292 HLSQLNLIDLAGSESSK-AETSGLRRKEGSYINKSLLTLGTVISKLTDR---RASHVPYRDSKLTRLLESSLSGHGRVSL 367
Cdd:cd01373  231 RTSRLNLVDLAGSERQKdTHAEGVRLKEAGNINKSLSCLGHVINALVDVahgKQRHVCYRDSKLTFLLRDSLGGNAKTAI 310
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 240256264 368 ICTVTPASSNSEETHNTLKFAHRAKHIEIQAAQNKI 403
Cdd:cd01373  311 IANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
65-392 4.19e-71

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: 239.60  E-value: 4.19e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  65 ENVTVTVRFRPLSPREIRKGEEIAWYA-DGETIV-------------RNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHV 130
Cdd:cd01368    1 DPVKVYLRVRPLSKDELESEDEGCIEViNSTTVVlhppkgsaankseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 131 VNGAMAGVNvtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQEtprreFLLRVSYFEIYNEVVND 210
Cdd:cd01368   81 VQDLLHGKN---------GLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-----YSVFVSYIEIYNEYIYD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 211 LLNPAG-------QNLRIREDEQG-TYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPL 282
Cdd:cd01368  147 LLEPSPssptkkrQSLRLREDHNGnMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 283 GDNNEGGA----VHLSQLNLIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKL----TDRRASHVPYRDSKLTR 353
Cdd:cd01368  227 DSDGDVDQdkdqITVSQLSLVDLAGSErTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTH 306
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 240256264 354 LLESSLSGHGRVSLICTVTPASSNSEETHNTLKFAHRAK 392
Cdd:cd01368  307 LFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
53-485 1.95e-66

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 233.86  E-value: 1.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  53 KPQLPPKPLQSKENVTVTVRFRPlspreiRKGEEIAWYADGETIVRNENNQSIAYAYDRVFGPTTTTRNVYDVAAQHVVN 132
Cdd:COG5059   10 KSRLSSRNEKSVSDIKSTIRIIP------GELGERLINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 133 GAMAGVNvtlsvnsttGTIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRR-EFLLRVSYFEIYNEVVNDL 211
Cdd:COG5059   84 SLLLGYN---------CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTkDFAVSISYLEIYNEKIYDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 212 LNPAGQNLRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSplgdNNEGGA 290
Cdd:COG5059  155 LSPNEESLNIREDsLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASK----NKVSGT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 291 VHLSQLNLIDLAGSES-SKAETSGLRRKEGSYINKSLLTLGTVISKLTD-RRASHVPYRDSKLTRLLESSLSGHGRVSLI 368
Cdd:COG5059  231 SETSKLSLVDLAGSERaARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVI 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 369 CTVTPASSNSEETHNTLKFAHRAKHIE--IQAAQNKIIDEKSLIKKYQYEIrqLKEELEQLKQGIkpVSQLKDISGDDID 446
Cdd:COG5059  311 CTISPSSNSFEETINTLKFASRAKSIKnkIQVNSSSDSSREIEEIKFDLSE--DRSEIEILVFRE--QSQLSQSSLSGIF 386
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 240256264 447 IVLLKQKLEEEedakaALLSRIQRLTKLILVSNKTPQTS 485
Cdd:COG5059  387 AYMQSLKKETE-----TLKSRIDLIMKSIISGTFERKKL 420
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
66-392 1.56e-64

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: 220.45  E-value: 1.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRK-GEEIAWYADGETI-VRNENNQ--SIAYAYDRVFGPTTTTRNVYDVAAQHVVNGAMAGVNVT 141
Cdd:cd01376    1 NVRVAVRVRPFVDGTAGAsDPSCVSGIDSCSVeLADPRNHgeTLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 142 lsvnsttgtIFAYGVTSSGKTHTMHGNQRSPGIIPLAVKDAFSIIQETPRREFLLrVSYFEIYNEVVNDLLNPAGQNLRI 221
Cdd:cd01376   81 ---------VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEAWALSFT-MSYLEIYQEKILDLLEPASKELVI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 222 REDEQGT-YIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMftLTIESSPLGDNNEGGAVHlSQLNLID 300
Cdd:cd01376  151 REDKDGNiLIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAV--LLIKVDQRERLAPFRQRT-GKLNLID 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 301 LAGSESSK-AETSGLRRKEGSYINKSLLTLGTVISKLtDRRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNSE 379
Cdd:cd01376  228 LAGSEDNRrTGNEGIRLKESGAINSSLFVLSKVVNAL-NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQ 306
                        330
                 ....*....|...
gi 240256264 380 ETHNTLKFAHRAK 392
Cdd:cd01376  307 DTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
66-392 4.77e-63

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: 216.78  E-value: 4.77e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  66 NVTVTVRFRPLSPREIRKGEE-IAWYADGETIVRNENNQSI---------AYAYDRVFGPTTTTRNVYDVAA----QHVV 131
Cdd:cd01367    1 KIKVCVRKRPLNKKEVAKKEIdVVSVPSKLTLIVHEPKLKVdltkyienhTFRFDYVFDESSSNETVYRSTVkplvPHIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 132 NGAMAgvnvtlsvnsttgTIFAYGVTSSGKTHTMHG----NQRSPGIIPLAVKDAFSIIQETPRREFL-LRVSYFEIYNE 206
Cdd:cd01367   81 EGGKA-------------TCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLgVTVSFFEIYGG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 207 VVNDLLNPaGQNLRIREDEQG-TYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSplGDN 285
Cdd:cd01367  148 KVFDLLNR-KKRVRLREDGKGeVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDR--GTN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 286 NEGGavhlsQLNLIDLAGSE--SSKAETSGLRRKEGSYINKSLLTLGTVISKLtDRRASHVPYRDSKLTRLLESSLSG-H 362
Cdd:cd01367  225 KLHG-----KLSFVDLAGSErgADTSSADRQTRMEGAEINKSLLALKECIRAL-GQNKAHIPFRGSKLTQVLKDSFIGeN 298
                        330       340       350
                 ....*....|....*....|....*....|
gi 240256264 363 GRVSLICTVTPASSNSEETHNTLKFAHRAK 392
Cdd:cd01367  299 SKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
67-392 7.96e-56

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: 196.65  E-value: 7.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  67 VTVTVRFRPLSPREirkGEEIAWYADGETIVRNE---------NNQSIAYAY--DRVFgPTTTTRNVYDVAAQHVVNGAM 135
Cdd:cd01375    2 VQAFVRVRPTDDFA---HEMIKYGEDGKSISIHLkkdlrrgvvNNQQEDWSFkfDGVL-HNASQELVYETVAKDVVSSAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 136 AGVNvtlsvnsttGTIFAYGVTSSGKTHTMHG---NQRSPGIIPLAVKDAFSIIQETPRREFLLRVSYFEIYNEVVNDLL 212
Cdd:cd01375   78 AGYN---------GTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 213 NP---AGQN---LRIRED-EQGTYIEGIKEEVVLSPAHVLSLIAAGEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGDN 285
Cdd:cd01375  149 STlpyVGPSvtpMTILEDsPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 286 NEggAVHLSQLNLIDLAGSE-SSKAETSGLRRKEGSYINKSLLTLGTVISKLTDRRASHVPYRDSKLTRLLESSLSGHGR 364
Cdd:cd01375  229 SE--KYITSKLNLVDLAGSErLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCN 306
                        330       340
                 ....*....|....*....|....*...
gi 240256264 365 VSLICTVTPASSNSEETHNTLKFAHRAK 392
Cdd:cd01375  307 TVMVANIYGEAAQLEETLSTLRFASRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
53-428 1.49e-54

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 207.09  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   53 KPQLPPKPLQSK------------EN------VTVTVRFRPLSpreirKGEEiawyadGETIVRNENNQSIA-----YAY 109
Cdd:PLN03188   68 KSPLPPRPPSSNplkrklsaetapENgvsdsgVKVIVRMKPLN-----KGEE------GEMIVQKMSNDSLTingqtFTF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  110 DRVFGPTTTTRNVYDVAAQHVVNGAMAGVNvtlsvnsttGTIFAYGVTSSGKTHTM------------HGNQRspGIIPL 177
Cdd:PLN03188  137 DSIADPESTQEDIFQLVGAPLVENCLAGFN---------SSVFAYGQTGSGKTYTMwgpanglleehlSGDQQ--GLTPR 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  178 AVKDAFSIIQETPRR------EFLLRVSYFEIYNEVVNDLLNPAGQNLRIREDEQ-GTYIEGIKEEVVLSPAHVLSLIAA 250
Cdd:PLN03188  206 VFERLFARINEEQIKhadrqlKYQCRCSFLEIYNEQITDLLDPSQKNLQIREDVKsGVYVENLTEEYVKTMKDVTQLLIK 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  251 GEEHRHIGSTSFNLLSSRSHTMFTLTIESSPLGDNNEGGAVHLSQLNLIDLAGSESSKAE-TSGLRRKEGSYINKSLLTL 329
Cdd:PLN03188  286 GLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTgAAGDRLKEAGNINRSLSQL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  330 GTVISKLTD----RRASHVPYRDSKLTRLLESSLSGHGRVSLICTVTPASSNSEETHNTLKFAHRAKHIEIQAAQNKIID 405
Cdd:PLN03188  366 GNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQ 445
                         410       420
                  ....*....|....*....|...
gi 240256264  406 EKslIKKYQYEIRQLKEELEQLK 428
Cdd:PLN03188  446 DD--VNFLREVIRQLRDELQRVK 466
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
98-334 4.95e-11

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: 62.36  E-value: 4.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  98 RNENNQSIAYAYDRVFGPTTTTRNVYDVAAQhVVNGAMAGVNVTlsvnsttgTIFAYGVTSSGKTHTMHgnqrspGIIPL 177
Cdd:cd01363   11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNQ--------SIFAYGESGAGKTETMK------GVIPY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 178 AVKDAFSiiqetprrefllrvsyfeiynevvndllnpagqNLRIREDEQGTYIEgikEEVVLSPAHVLSLIAAGEEHRHi 257
Cdd:cd01363   76 LASVAFN---------------------------------GINKGETEGWVYLT---EITVTLEDQILQANPILEAFGN- 118
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256264 258 GSTSFNLLSSRSHTMFTLtiessplgdnneggavhlsqlnLIDLAGSEsskaetsglrrkegsYINKSLLTLGTVIS 334
Cdd:cd01363  119 AKTTRNENSSRFGKFIEI----------------------LLDIAGFE---------------IINESLNTLMNVLR 158
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
64-212 5.39e-11

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 61.47  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   64 KENVTVTVRFRPLSPREIrkgeeIAWYADGETIVRNENNQSIAYAYDRVFGPTTTTRNVYDvAAQHVVNGAMAGVNVTls 143
Cdd:pfam16796  19 KGNIRVFARVRPELLSEA-----QIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQ-EISQLVQSCLDGYNVC-- 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  144 vnsttgtIFAYGVTSSGKThtmhgnqrsPGIIPLAVKDAFSIIQETPR-REFLLRVSYFEIYNEVVNDLL 212
Cdd:pfam16796  91 -------IFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKgWKYTIELQFVEIYNESSQDLL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
638-953 4.54e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 638 LREQQKTLSEEmAQQSRSFKLLSEEAAKApQNEEIKAEIINLNGDIKAKNDQIATLgkqildfviashdELDKSDIVQAV 717
Cdd:COG1196  198 LERQLEPLERQ-AEKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAELEEL-------------EAELEELEAEL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 718 SEMRAQLNEKcfELEVKAADNRIIQEQLTEktsfcEDLQEEVANLKQQLSDALELgdinsvtchmqqssqspNKNEEKVI 797
Cdd:COG1196  263 AELEAELEEL--RLELEELELELEEAQAEE-----YELLAELARLEQDIARLEER-----------------RRELEERL 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 798 EAQAFEIEELKLKAAELSELNEQLEIRNKKLAEE-SSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQKSSVT 876
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256264 877 tpQGKTGNLRNGRRESVSKRKEQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLENELA 953
Cdd:COG1196  399 --AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
712-952 1.08e-06

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: 52.75  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   712 DIVQAVSEMRAQLNEKCFELEVKAADNRIIQEQLTEKTSFCEDLQEEVANLKQQLSDALElgDINSVTcHMQQSSQSPNK 791
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLE-ERIAQLSKELT 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   792 NEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQ 871
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   872 KSSVTTPQGKTGNlrNGRRESVSK-RKEQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLEN 950
Cdd:TIGR02168  838 RRLEDLEEQIEEL--SEDIESLAAeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                   ..
gi 240256264   951 EL 952
Cdd:TIGR02168  916 EL 917
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
597-950 1.14e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 597 EGSALADQIiETMENREahEDSFHEIETPETRIKMI-DQMEILREQQKTLsEEMAQQSRsfkllsEEAAKAPQN-EEIKA 674
Cdd:PRK02224 308 DAEAVEARR-EELEDRD--EELRDRLEECRVAAQAHnEEAESLREDADDL-EERAEELR------EEAAELESElEEARE 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 675 EIINLNGDIKAKNDQIATLGKQI------LDFVIASHDEL--DKSDIVQAVSEMRAQLNE---------------KCFEL 731
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFgdapvdLGNAEDFLEELreERDELREREAELEATLRTarerveeaealleagKCPEC 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 732 EVKAADNRIIqEQLTEKTSFCEDLQEEVANLKQQ---LSDALELGDINSVTCHMQQSSQSPNKNEEKVIEAQAFEIEELK 808
Cdd:PRK02224 458 GQPVEGSPHV-ETIEEDRERVEELEAELEDLEEEveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 809 LKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLaADLAAVQkSSVTTPQGKTGNLRNg 888
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLL-AAIADAEDEIERLRE- 613
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256264 889 RRESVSKRKEQENSLMELKRELTvsKEREVSFEAALIEKIQreaelqrtvEESKQREAYLEN 950
Cdd:PRK02224 614 KREALAELNDERRERLAEKRERK--RELEAEFDEARIEEAR---------EDKERAEEYLEQ 664
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
634-871 1.41e-05

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: 49.30  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   634 QMEILREQQKTLSEEMAQQSRSFKLLSEEAakapqnEEIKAEIINLNGDIKAKNDQIATLGKQILDFviasHDELDKSDI 713
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEI------ENVKSELKELEARIEELEEDLHKLEEALNDL----EARLSHSRI 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   714 VQAVSEMRAqLNEKCFELEVKAADnriIQEQLTEKTSFCEDLQEEVANLKQQLSDAlelgdinsvtchmqqssQSPNKNE 793
Cdd:TIGR02169  794 PEIQAELSK-LEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDL-----------------KEQIKSI 852
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256264   794 EKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQ 871
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
658-872 1.48e-05

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: 48.61  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 658 LLSEEAAKAPQNEEIKAEIINLNGDIKAKNDQIATLGKQIldfvIASHDELDKSDivQAVSEMRAQLNEkcFELEVKAAD 737
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE----KALLKQLAALE--RRIAALARRIRA--LEQELAALE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 738 NRIIQEQlTEKTSFCEDLQEEVANLKQQLSDALELGDINSVTCHMqqSSQSPNKNE------EKVIEAQAFEIEELKLKA 811
Cdd:COG4942   83 AELAELE-KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLL--SPEDFLDAVrrlqylKYLAPARREQAEELRADL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256264 812 AELSELNEQLE--------------IRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQK 872
Cdd:COG4942  160 AELAALRAELEaeraeleallaeleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
648-838 3.61e-05

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 47.93  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 648 EMAQQSRSFKLLSEEAAKApqnEEIKAEI------INLNGDIKAKndqIATLGKQILDFVIASHDELD---KSDIVQAVS 718
Cdd:PLN03229 538 DMLNEFSRAKALSEKKSKA---EKLKAEInkkfkeVMDRPEIKEK---MEALKAEVASSGASSGDELDddlKEKVEKMKK 611
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 719 EMRAQLNE--KCFELEVKAADNRiiQEQLTEKTSFcEDLQEEVANLKQQLSDALE--------LGDINSVTCHMQQSSQS 788
Cdd:PLN03229 612 EIELELAGvlKSMGLEVIGVTKK--NKDTAEQTPP-PNLQEKIESLNEEINKKIErvirssdlKSKIELLKLEVAKASKT 688
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 240256264 789 PNKNEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKEL 838
Cdd:PLN03229 689 PDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAES 738
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
739-965 5.78e-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: 47.36  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   739 RIIQEQLTEKTSFCEDLQEEVANLKQQLSDAL-ELGDINSVTCHMQQSSQSPNKNEEKVIEAQAFEIEELKLKAAELSEL 817
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   818 NEQLEIRNKKLAEESSYAKELASaaaiELKALSEEIARLMNHNERLAADLAAVQKssvttpqgKTGNLRNGRRESVSKRK 897
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRA--------ELTLLNEEAANLRERLE 827
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256264   898 EQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLENELANMWGLVAKLRSQ 965
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
791-971 1.60e-04

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: 45.82  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   791 KNEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAV 870
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   871 QKSSVTTPQgKTGNLRNGRRESVSKRKEQENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLEN 950
Cdd:TIGR02168  760 EAEIEELEE-RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
                          170       180
                   ....*....|....*....|.
gi 240256264   951 ELANMWGLVAKLRSQGAANSG 971
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAA 859
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
593-944 1.83e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.48  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  593 SRLSEGSALADQIIETMENREAHEDSfhEIETpetrIKMIDQMEIlrEQQKTLSEEMAQQSRSFKLLSEEA--------- 663
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTK--ELED----IKMSLQRSM--STQKALEEDLQIATKTICQLTEEKeaqmeelnk 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  664 AKAPQN---EEIKAEIINLNGDIKAKNDQIATLGKQILDFVIashdELDKSDivQAVSEMRAQLNEKCFELEVKAADNRI 740
Cdd:pfam05483 343 AKAAHSfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKS--SELEEMTKFKNNKEVELEELKKILAE 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  741 IQEQLTEKTSFcEDLQEEVANLKQQLSDALELGDINSVTCHMQ-QSSQSPNKNEEKVIEAQAFEIEELKLKAAELSELNE 819
Cdd:pfam05483 417 DEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREKEIHDLEIQlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  820 QLEIRNKKLAEEssyakelASAAAIELKALSEEIARLMNHNERLAADLAAVQKSSVttpqgktgNLRNgrrESVSKRKEQ 899
Cdd:pfam05483 496 KLLLENKELTQE-------ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM--------NLRD---ELESVREEF 557
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 240256264  900 ENSLMELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQR 944
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
616-923 3.42e-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: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   616 EDSFHEIETPETRIKMIDQM-EILREQQKTLSEEMAQQSRSFKLLS-----EEAAKAPQNEEIKAEIINLNGDIKAKNDQ 689
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIiDEKRQQLERLRREREKAERYQALLKekreyEGYELLKEKEALERQKEAIERQLASLEEE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   690 IATLGKQI-------------LDFVIASHDELDKSDIVQAVSEM--------RAQLNEKCFELEVKAADNRI------IQ 742
Cdd:TIGR02169  253 LEKLTEEIselekrleeieqlLEELNKKIKDLGEEEQLRVKEKIgeleaeiaSLERSIAEKERELEDAEERLakleaeID 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   743 EQLTEKTSFCED----------LQEEVANLKQQLSDAL-ELGDINSVTchmqQSSQSPNKNEEKVIEAQAFEIEELKLKA 811
Cdd:TIGR02169  333 KLLAEIEELEREieeerkrrdkLTEEYAELKEELEDLRaELEEVDKEF----AETRDELKDYREKLEKLKREINELKREL 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   812 AELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAVQKssvttpqgKTGNLRNGRRE 891
Cdd:TIGR02169  409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ--------ELYDLKEEYDR 480
                          330       340       350
                   ....*....|....*....|....*....|..
gi 240256264   892 SVSKRKEQENSLMELKRELTVSKEREVSFEAA 923
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERVRGGRAV 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
597-860 5.84e-04

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: 43.89  E-value: 5.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   597 EGSALADQIIETMENREAHEDsfhEIETPETRI-KMIDQMEILREQQKTLSEEMAQQSRSF--------KLLSEEAAKAP 667
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEA---EIEELEAQIeQLKEELKALREALDELRAELTLLNEEAanlrerleSLERRIAATER 838
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   668 QNEEIKAEIINLNGDIKAKNDQIATLGKQILdfviASHDELDK-SDIVQAVSEMRAQLNEkcfELEVKAADNRIIQEQLT 746
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEAlLNERASLEEALALLRS---ELEELSEELRELESKRS 911
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   747 EKTSFCEDLQEEVANLKQQLSDALelgdinsvtchmqqssqspnkneekvieaqaFEIEELKLKAAELSELNEQLEIRNK 826
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLE-------------------------------VRIDNLQERLSEEYSLTLEEAEALE 960
                          250       260       270
                   ....*....|....*....|....*....|....
gi 240256264   827 KLAEESSyakelaSAAAIELKALSEEIARLMNHN 860
Cdd:TIGR02168  961 NKIEDDE------EEARRRLKRLENKIKELGPVN 988
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
719-969 6.98e-04

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: 43.51  E-value: 6.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   719 EMRAQLNEKCFEL---EVKAADNRI--IQEQLTEKTSFCEDLQEEVANLKQQLSDaLELGdinsvtchMQQSSQSPNKNE 793
Cdd:TIGR02168  217 ELKAELRELELALlvlRLEELREELeeLQEELKEAEEELEELTAELQELEEKLEE-LRLE--------VSELEEEIEELQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   794 EKVIEAQAfEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAA---- 869
Cdd:TIGR02168  288 KELYALAN-EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleae 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   870 --VQKSSVTTPQGKTGNLRNGRRESVSKRKEQENSLMELKRELT---VSKEREVSFEAALIEKIQREA--ELQRTVEESK 942
Cdd:TIGR02168  367 leELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAElkELQAELEELE 446
                          250       260
                   ....*....|....*....|....*..
gi 240256264   943 QREAYLENELANMWGLVAKLRSQGAAN 969
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEA 473
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
575-914 1.40e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   575 SNSTPSTPQGEGSDFHTESRLSEGSALADQIIETMENREAHEDSFHEIETP--ETRIKMIDQ---MEILREQQKTLSEEM 649
Cdd:pfam15921  499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEceALKLQMAEKdkvIEILRQQIENMTQLV 578
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   650 AQQSRSF-KLLSEEAAKAPQNEEIKAEIINLNGDIKAKNDQIATLGKQILDFviashdELDKSDIVQAVSE-MRA--QLN 725
Cdd:pfam15921  579 GQHGRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL------ELEKVKLVNAGSErLRAvkDIK 652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   726 EKCFEL--EVKAADNRIiqEQLTE-----KTSF---CEDLQEEVANLKQQLSDAL-ELGDINSVTCHMQQSSQSPNK--- 791
Cdd:pfam15921  653 QERDQLlnEVKTSRNEL--NSLSEdyevlKRNFrnkSEEMETTTNKLKMQLKSAQsELEQTRNTLKSMEGSDGHAMKvam 730
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264   792 NEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLA--- 868
Cdd:pfam15921  731 GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnme 810
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 240256264   869 -AVQKSSvttpqgktgnLRNGRRESVSKRKEQENSLMELKRELTVSK 914
Cdd:pfam15921  811 vALDKAS----------LQFAECQDIIQRQEQESVRLKLQHTLDVKE 847
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
671-856 1.66e-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: 41.06  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 671 EIKAEIINLNGDIKAKNDQIATLGKQIldfviashdeldkSDIVQAVSEMRAQLNEKcfELEVKAADNRI--IQEQLTEK 748
Cdd:COG1579   21 RLEHRLKELPAELAELEDELAALEARL-------------EAAKTELEDLEKEIKRL--ELEIEEVEARIkkYEEQLGNV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 749 TSFCE--DLQEEVANLKQQLSDAlelgdinsvtchmqqssqspnknEEKVIEAQAfEIEELKlkaAELSELNEQLEIRNK 826
Cdd:COG1579   86 RNNKEyeALQKEIESLKRRISDL-----------------------EDEILELME-RIEELE---EELAELEAELAELEA 138
                        170       180       190
                 ....*....|....*....|....*....|
gi 240256264 827 KLAEESSYAKELASAAAIELKALSEEIARL 856
Cdd:COG1579  139 ELEEKKAELDEELAELEAELEELEAEREEL 168
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
711-884 2.27e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 711 SDIVQAVSEMRAQLNEKCFELEVKAADNRIIQEQLTEKTSFCEDLQEEVANLKQQLSDALE-LGDINSvtcHMQQSSQSP 789
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREeLGERAR---ALYRSGGSV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 790 N-------------------------KNEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAI 844
Cdd:COG3883  103 SyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 240256264 845 ELKALSEEIARLMNHNERLAADLAAVQKSSVTTPQGKTGN 884
Cdd:COG3883  183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
621-956 3.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 621 EIETPETRIKMIDQMEiLREQQKTLSEEMAQQSRSFKLLSEEAAKAPQNEEIKAEIINLNGDIKAKNDQIATLgkqildf 700
Cdd:COG4717   57 ELFKPQGRKPELNLKE-LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 701 viashdeldksDIVQAVSEMRAQLNEKCFELEvkAADNRIiqEQLTEKTSFCEDLQEEVANLKQQLSDALELGDInsvtc 780
Cdd:COG4717  129 -----------PLYQELEALEAELAELPERLE--ELEERL--EELRELEEELEELEAELAELQEELEELLEQLSL----- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 781 HMQQSSQSPNKNEEKVIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKE-------LASAAAIELKALSEEI 853
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllLIAAALLALLGLGGSL 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 854 ARLMNHNERLAADLAAVQKSSVTTPQGKTGNLRNGRRESVSKRKE---QENSLMELKRELTVSKEREVSFEAALIEKIQR 930
Cdd:COG4717  269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
                        330       340
                 ....*....|....*....|....*...
gi 240256264 931 EAELQRTVEESKQR--EAYLENELANMW 956
Cdd:COG4717  349 LQELLREAEELEEElqLEELEQEIAALL 376
PTZ00121 PTZ00121
MAEBL; Provisional
592-902 4.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  592 ESRLSEGSALADQIIETMENREAHEDSFHE--IETPETRIKMIDQMEILREQQKTLSEEMAQQSRSFKLLSEEAAKAPQN 669
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEeaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  670 EEIKAEIINLNGDIKAKNDQIATLGKQildfVIASHDELDKSDIVQAVSemRAQLNEKCFELEVKAADNRIIQEQLTEKT 749
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAE----EKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  750 SFCEDLQEEVANLKQQLSDALElgdinsvtcHMQQSSQSPNKNEEKVIEAQAF--EIEELKLKAAELS-ELNEQLEIRNK 826
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAE---------EKKKAEELKKAEEENKIKAEEAkkEAEEDKKKAEEAKkDEEEKKKIAHL 1762
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256264  827 KLAEESSYAKELASAAAIELKALSEEIARLMNHNERLAADLAAvqKSSVTTPQGKTGNLrngrreSVSKRKEQENS 902
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD--NFANIIEGGKEGNL------VINDSKEMEDS 1830
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
753-953 5.43e-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: 40.13  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 753 EDLQEEVANLKQQLSDALElgDINSVTCHMQQSSQSPNKNEEKV--IEAQAFEIE-ELKLKAAELSELNEQLEIRNKKLA 829
Cdd:COG4942   30 EQLQQEIAELEKELAALKK--EEKALLKQLAALERRIAALARRIraLEQELAALEaELAELEKEIAELRAELEAQKEELA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 830 EESSYAKELASAAAIELKALSEEIARLMNHNERLAA------DLAAVQKSSVTTPQGKTGNLRNGRRESVSKRKEQENSL 903
Cdd:COG4942  108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 240256264 904 MELKRELTVSKEREVSFEAALIEKIQREAELQRTVEESKQREAYLENELA 953
Cdd:COG4942  188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
151-333 7.03e-03

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 40.11  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 151 IFAYGVTSSGKTHTMhgNQRSPGIIPLAVKDAFSIIQETPRREFLLRV------SYFEIYNEVVNDLLNPAGQNLRIRED 224
Cdd:COG5059  385 IFAYMQSLKKETETL--KSRIDLIMKSIISGTFERKKLLKEEGWKYKStlqflrIEIDRLLLLREEELSKKKTKIHKLNK 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 225 EQGTYIEGIKEEVVLSPAHVLSLIAagEEHRHIGSTSFNLLSSRSHTMFTL-TIESSPLGDNNeggavhlsQLNLIDLAG 303
Cdd:COG5059  463 LRHDLSSLLSSIPEETSDRVESEKA--SKLRSSASTKLNLRSSRSHSKFRDhLNGSNSSTKEL--------SLNQVDLAG 532
                        170       180       190
                 ....*....|....*....|....*....|
gi 240256264 304 SESSKAETSGLRRKEGSYINKSLLTLGTVI 333
Cdd:COG5059  533 SERKVSQSVGELLRETQSLNKSLSSLGDVI 562
ClyA_MakA-like cd22655
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ...
599-697 7.56e-03

Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.


Pssm-ID: 439153 [Multi-domain]  Cd Length: 342  Bit Score: 39.57  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264 599 SALADQIIETMEnreAHEDSFheieTPETRIKMIDQMEILREQQKTLSEEMAQQSRSFKLLSEEAAKAP----------Q 668
Cdd:cd22655   74 SAATSQILNIFK---ALPTAP----DDAQVEQIIALLQALQKPVQEIISNIAAYQGKLKAWGDKMQAAHdnlttgaaqiQ 146
                         90       100       110
                 ....*....|....*....|....*....|.
gi 240256264 669 NEE--IKAEIINLNGDIKAKNDQIATLGKQI 697
Cdd:cd22655  147 AAEtdLQADIDKINNAIANLNAEIAKDNKAI 177
PTZ00121 PTZ00121
MAEBL; Provisional
636-951 8.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  636 EILREQQKTLSEEMAQQSRSFKLlSEEAAKAPQNEEIKAEIINLNGDIKAKNDQIATLGKQIldfviASHDELDKsdivq 715
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKK-ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-----KKADEAKK----- 1438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  716 avsemRAQLNEKCFELEVKAADNRIiQEQLTEKTSFCEDLQEevanLKQQLSDALELGDINSVTCHMQQSSQSPNKNEEK 795
Cdd:PTZ00121 1439 -----KAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKADE----AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  796 VIEAQAFEIEELKLKAAELSELNEQLEIRNKKLAEESSYAKELASAAAI---ELKALSEEIARL---MNHNERLAADLAA 869
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkaEEKKKAEEAKKAeedKNMALRKAEEAKK 1588
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256264  870 VQKSSVTTPQGKTGNLRNGRRESVSKRKEQENSLMELKRELTVSKEREVSFEAALIEKIQ-------------REAELQR 936
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeelkkaeeenkiKAAEEAK 1668
                         330
                  ....*....|....*
gi 240256264  937 TVEESKQREAYLENE 951
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKA 1683
 
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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