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Conserved domains on  [gi|22327992|ref|NP_200901|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

KISc_KIF4 and Rcc_KIF21 domain-containing protein( domain architecture ID 12916601)

KISc_KIF4 and Rcc_KIF21 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
6-361 1.72e-179

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: 533.06  E-value: 1.72e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    6 CVRVAVNIRPLITPELLNGCTDCITVAPKEPQVHIG-SHTFTYDFVYGnGGYPCSEIYNHCVAPLVDALFKGYNATVLAY 84
Cdd:cd01372    2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGtDKSFTFDYVFD-PSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   85 GQTGSGKTYTMGTNYSGDCTNG--GVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSallkndsgvq 162
Cdd:cd01372   81 GQTGSGKTYTMGTAYTAEEDEEqvGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETD---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  163 akhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKKIAGGSC 242
Cdd:cd01372  151 ------KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  243 TTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkeGGHVPYRDSKLTRLLQ 322
Cdd:cd01372  225 PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKK--GAHVPYRDSKLTRLLQ 302
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 22327992  323 DSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQ 361
Cdd:cd01372  303 DSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
529-845 2.70e-10

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 2.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    529 DKVMDVTDELEfqeKEIEHCSLQEK-------LDMELKELDK-----RLEEKEAEMKRFSSggtsvLKQHYEKKVYDLEQ 596
Cdd:TIGR02168  189 DRLEDILNELE---RQLKSLERQAEkaerykeLKAELRELELallvlRLEELREELEELQE-----ELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    597 EKRALQREIEGLRHNLASIpSGPGDGAQKLKEEYVQKLNTLETQVSVLKKKQD--------AQAQLMRQKQKSDDaaikL 668
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleeLEAQLEELESKLDE----L 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    669 QDEIHRIKSQKVQLQQKIKQESEQFRawKASREKEVMQLKKEGRRNEYEmhklmALNQKQKLVLQRKTEEASQVtkrlkE 748
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELE--ELEAELEELESRLEELEEQLE-----TLRSKVAQLELQIASLNNEI-----E 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    749 LLDNRKASSRETLSGANGPGTQALMQAIEHEI-EVTVRVHEVRSEYERQTEERARMAKEVARLREENELLKNAKISVHGD 827
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
                          330
                   ....*....|....*...
gi 22327992    828 TMSpgaRNSRIFALENML 845
Cdd:TIGR02168  484 LAQ---LQARLDSLERLQ 498
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
6-361 1.72e-179

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: 533.06  E-value: 1.72e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    6 CVRVAVNIRPLITPELLNGCTDCITVAPKEPQVHIG-SHTFTYDFVYGnGGYPCSEIYNHCVAPLVDALFKGYNATVLAY 84
Cdd:cd01372    2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGtDKSFTFDYVFD-PSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   85 GQTGSGKTYTMGTNYSGDCTNG--GVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSallkndsgvq 162
Cdd:cd01372   81 GQTGSGKTYTMGTAYTAEEDEEqvGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETD---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  163 akhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKKIAGGSC 242
Cdd:cd01372  151 ------KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  243 TTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkeGGHVPYRDSKLTRLLQ 322
Cdd:cd01372  225 PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKK--GAHVPYRDSKLTRLLQ 302
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 22327992  323 DSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQ 361
Cdd:cd01372  303 DSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
7-367 3.51e-137

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: 421.98  E-value: 3.51e-137
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992       7 VRVAVNIRPLITPELLNGCTDCITVAPKEPQV--------HIGSHTFTYDFVYGnggYPCS--EIYNHCVAPLVDALFKG 76
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspknRQGEKKFTFDKVFD---ATASqeDVFEETAAPLVDSVLEG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992      77 YNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSALlk 156
Cdd:smart00129   79 YNATIFAYGQTGSGKTYTM----IGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL-- 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     157 ndsgvqakhtalsrapiQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKK 236
Cdd:smart00129  153 -----------------EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKI 215
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     237 iaggscttTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkegGHVPYRDSK 316
Cdd:smart00129  216 --------KNSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS---RHIPYRDSK 284
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 22327992     317 LTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVIN 367
Cdd:smart00129  285 LTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
13-360 9.67e-134

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 412.35  E-value: 9.67e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     13 IRPLITPELLNGCTDCITVAPKEPQVHIGS--------HTFTYDFVYGnggyPCS---EIYNHCVAPLVDALFKGYNATV 81
Cdd:pfam00225    2 VRPLNEREKERGSSVIVSVESVDSETVESShltnknrtKTFTFDKVFD----PEAtqeDVYEETAKPLVESVLEGYNVTI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     82 LAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSallkndsgv 161
Cdd:pfam00225   78 FAYGQTGSGKTYTM----EGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNK--------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    162 qakhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKKiaggs 241
Cdd:pfam00225  145 -------NKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRN----- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    242 ctTTEDGGEDILCAKLHLVDLAGSERAKRTG-ADGMRLKEGIHINKGLLALGNVISALGDEKKrkegGHVPYRDSKLTRL 320
Cdd:pfam00225  213 --RSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS----KHIPYRDSKLTRL 286
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 22327992    321 LQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNI 360
Cdd:pfam00225  287 LQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
60-621 2.69e-85

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 289.72  E-value: 2.69e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   60 EIYNHCVAPLVDALFKGYNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIF 139
Cdd:COG5059   72 DVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM----SGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIY 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  140 KEEVFDLLDSNSSALLkndsgvqakhtalsrapiqIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNS 219
Cdd:COG5059  148 NEKIYDLLSPNEESLN-------------------IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIND 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  220 QSSRSHAIFTITLEQKKIAGGsctTTEDGgedilcaKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALG 299
Cdd:COG5059  209 ESSRSHSIFQIELASKNKVSG---TSETS-------KLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALG 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  300 DEKKRkegGHVPYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVINrdpATAQMQRmr 379
Cdd:COG5059  279 DKKKS---GHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN---SSSDSSR-- 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  380 sQIEQLQTELLFYR-GDSGAFDELQILKHKISLleasnRELHNELQERRVASEHFSKRAYDAQVEKDKLIMIIESVRNGK 458
Cdd:COG5059  351 -EIEEIKFDLSEDRsEIEILVFREQSQLSQSSL-----SGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKKLLKEE 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  459 SLDEIESCQNEDVGLVNKyVSKIQELEGELLHIKNLKKTSNHQYSDdsydvgprsnnvlfpssNESSDCEDKvmdvtdeL 538
Cdd:COG5059  425 GWKYKSTLQFLRIEIDRL-LLLREEELSKKKTKIHKLNKLRHDLSS-----------------LLSSIPEET-------S 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  539 EFQEKEIEHcSLQEKLDMELKELDKRLEEKEAEMKRFSsggTSVLKQHYEKKVYDLEQEKRALQREIEGLRH--NLASIP 616
Cdd:COG5059  480 DRVESEKAS-KLRSSASTKLNLRSSRSHSKFRDHLNGS---NSSTKELSLNQVDLAGSERKVSQSVGELLREtqSLNKSL 555

                 ....*
gi 22327992  617 SGPGD 621
Cdd:COG5059  556 SSLGD 560
PLN03188 PLN03188
kinesin-12 family protein; Provisional
7-396 2.03e-64

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 240.61  E-value: 2.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     7 VRVAVNIRPLITPELlngcTDCITVAPKEPQVHIGSHTFTYDFVyGNGGYPCSEIYNHCVAPLVDALFKGYNATVLAYGQ 86
Cdd:PLN03188  100 VKVIVRMKPLNKGEE----GEMIVQKMSNDSLTINGQTFTFDSI-ADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    87 TGSGKTYTM--------GTNYSGDctNGGVIPNVMEDIFRRV--ETTKDSSELL---IRVSFIEIFKEEVFDLLDSnssa 153
Cdd:PLN03188  175 TGSGKTYTMwgpangllEEHLSGD--QQGLTPRVFERLFARIneEQIKHADRQLkyqCRCSFLEIYNEQITDLLDP---- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   154 llkndsgvqakhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLE 233
Cdd:PLN03188  249 ---------------SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVE 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   234 QKkiaggsCTTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRKEGGHVPYR 313
Cdd:PLN03188  314 SR------CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYR 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   314 DSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVINrDPATAQMQRMRSQIEQLQTELLFYR 393
Cdd:PLN03188  388 DSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN-EVMQDDVNFLREVIRQLRDELQRVK 466

                  ...
gi 22327992   394 GDS 396
Cdd:PLN03188  467 ANG 469
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
529-845 2.70e-10

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: 65.08  E-value: 2.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    529 DKVMDVTDELEfqeKEIEHCSLQEK-------LDMELKELDK-----RLEEKEAEMKRFSSggtsvLKQHYEKKVYDLEQ 596
Cdd:TIGR02168  189 DRLEDILNELE---RQLKSLERQAEkaerykeLKAELRELELallvlRLEELREELEELQE-----ELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    597 EKRALQREIEGLRHNLASIpSGPGDGAQKLKEEYVQKLNTLETQVSVLKKKQD--------AQAQLMRQKQKSDDaaikL 668
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleeLEAQLEELESKLDE----L 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    669 QDEIHRIKSQKVQLQQKIKQESEQFRawKASREKEVMQLKKEGRRNEYEmhklmALNQKQKLVLQRKTEEASQVtkrlkE 748
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELE--ELEAELEELESRLEELEEQLE-----TLRSKVAQLELQIASLNNEI-----E 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    749 LLDNRKASSRETLSGANGPGTQALMQAIEHEI-EVTVRVHEVRSEYERQTEERARMAKEVARLREENELLKNAKISVHGD 827
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
                          330
                   ....*....|....*...
gi 22327992    828 TMSpgaRNSRIFALENML 845
Cdd:TIGR02168  484 LAQ---LQARLDSLERLQ 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
558-825 6.06e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 6.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  558 LKELDKRLE--EKEAEM-KRFssggtsvLKQHYEKKVYDLE---QEKRALQREIEGLRHNLASipsgpgdgAQKLKEEYV 631
Cdd:COG1196  195 LGELERQLEplERQAEKaERY-------RELKEELKELEAElllLKLRELEAELEELEAELEE--------LEAELEELE 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  632 QKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKlqdEIHRIKSQKVQLQQKIKQESEQfrawKASREKEVMQLKKEG 711
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEER----LEELEEELAELEEEL 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  712 RRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRLKELLDNRKASSRETLSGAngpgtQALMQAIEHEIEVTVRVHEVRS 791
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-----EELLEALRAAAELAAQLEELEE 407
                        250       260       270
                 ....*....|....*....|....*....|....
gi 22327992  792 EYERQTEERARMAKEVARLREENELLKNAKISVH 825
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEE 441
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
524-821 3.74e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   524 SSDCEDKVMDVTDELEFQEKEI-EHCSLQEKLDMELKELDKRLEEKEAEMKRFSSggtsvlkqhYEKKVYDLEQEKRALQ 602
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREInEISSELPELREELEKLEKEVKELEELKEEIEE---------LEKELESLEGSKRKLE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   603 REIEGLRHNLASipsgpgdgaqklKEEYVQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQL 682
Cdd:PRK03918  259 EKIRELEERIEE------------LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   683 QQKIKQESEqfrawKASREKEVMQLKKEGRRneyemhKLMALNQKQKLVlqrktEEASQVTKRLKELLDNRKASSRETls 762
Cdd:PRK03918  327 EERIKELEE-----KEERLEELKKKLKELEK------RLEELEERHELY-----EEAKAKKEELERLKKRLTGLTPEK-- 388
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   763 gangpgtqalmqaIEHEIE-VTVRVHEVRSEYERQTEERARMAKEVARLREENELLKNAK 821
Cdd:PRK03918  389 -------------LEKELEeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
398-824 3.54e-05

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: 48.18  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    398 AFDELQILKhkisllEASNRELHNELQERRVASEHFSKRaYDAQV---EKDKLIMIIESVRNGKSLDEIESCQNEDVGLV 474
Cdd:pfam05483  198 AFEELRVQA------ENARLEMHFKLKEDHEKIQHLEEE-YKKEIndkEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    475 NKYVSKIQelegelLHIKNLKKTSNHQYsddsydvgprsnnvlfpssNESSDCEDKVMDVTDELEFQEkeiehcSLQEKL 554
Cdd:pfam05483  271 NQLEEKTK------LQDENLKELIEKKD-------------------HLTKELEDIKMSLQRSMSTQK------ALEEDL 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    555 DMELKELDKRLEEKEAEMKRFSSGGT--SVLKQHYEKKVYDLEQEKRALQREIEGLRHNLASIPSGPGDGAQKLkEEYVQ 632
Cdd:pfam05483  320 QIATKTICQLTEEKEAQMEELNKAKAahSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTK 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    633 KLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQESEQFRAWKASRE---KEVMQLKK 709
Cdd:pfam05483  399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKT 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    710 EGRRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRLK----ELLDNRKASSRetlsgangpgtqaLMQAIE--HEIEVT 783
Cdd:pfam05483  479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKkhqeDIINCKKQEER-------------MLKQIEnlEEKEMN 545
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 22327992    784 VR--VHEVRSEYERQTEE---RARMAKEVARLREENELLKNAKISV 824
Cdd:pfam05483  546 LRdeLESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKI 591
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
6-361 1.72e-179

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: 533.06  E-value: 1.72e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    6 CVRVAVNIRPLITPELLNGCTDCITVAPKEPQVHIG-SHTFTYDFVYGnGGYPCSEIYNHCVAPLVDALFKGYNATVLAY 84
Cdd:cd01372    2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGtDKSFTFDYVFD-PSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   85 GQTGSGKTYTMGTNYSGDCTNG--GVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSallkndsgvq 162
Cdd:cd01372   81 GQTGSGKTYTMGTAYTAEEDEEqvGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETD---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  163 akhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKKIAGGSC 242
Cdd:cd01372  151 ------KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  243 TTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkeGGHVPYRDSKLTRLLQ 322
Cdd:cd01372  225 PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKK--GAHVPYRDSKLTRLLQ 302
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 22327992  323 DSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQ 361
Cdd:cd01372  303 DSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
7-367 3.51e-137

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: 421.98  E-value: 3.51e-137
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992       7 VRVAVNIRPLITPELLNGCTDCITVAPKEPQV--------HIGSHTFTYDFVYGnggYPCS--EIYNHCVAPLVDALFKG 76
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspknRQGEKKFTFDKVFD---ATASqeDVFEETAAPLVDSVLEG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992      77 YNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSALlk 156
Cdd:smart00129   79 YNATIFAYGQTGSGKTYTM----IGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL-- 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     157 ndsgvqakhtalsrapiQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKK 236
Cdd:smart00129  153 -----------------EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKI 215
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     237 iaggscttTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkegGHVPYRDSK 316
Cdd:smart00129  216 --------KNSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS---RHIPYRDSK 284
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 22327992     317 LTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVIN 367
Cdd:smart00129  285 LTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
13-360 9.67e-134

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 412.35  E-value: 9.67e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     13 IRPLITPELLNGCTDCITVAPKEPQVHIGS--------HTFTYDFVYGnggyPCS---EIYNHCVAPLVDALFKGYNATV 81
Cdd:pfam00225    2 VRPLNEREKERGSSVIVSVESVDSETVESShltnknrtKTFTFDKVFD----PEAtqeDVYEETAKPLVESVLEGYNVTI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     82 LAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSallkndsgv 161
Cdd:pfam00225   78 FAYGQTGSGKTYTM----EGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNK--------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    162 qakhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKKiaggs 241
Cdd:pfam00225  145 -------NKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRN----- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    242 ctTTEDGGEDILCAKLHLVDLAGSERAKRTG-ADGMRLKEGIHINKGLLALGNVISALGDEKKrkegGHVPYRDSKLTRL 320
Cdd:pfam00225  213 --RSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS----KHIPYRDSKLTRL 286
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 22327992    321 LQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNI 360
Cdd:pfam00225  287 LQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
7-358 6.45e-122

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: 380.83  E-value: 6.45e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELlNGCTDCITVAPKE-------PQVHIGSHTFTYDFVYGnGGYPCSEIYNHCVAPLVDALFKGYNA 79
Cdd:cd00106    2 VRVAVRVRPLNGREA-RSAKSVISVDGGKsvvldppKNRVAPPKTFAFDAVFD-STSTQEEVYEGTAKPLVDSALEGYNG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   80 TVLAYGQTGSGKTYTMGTNYSGDctnGGVIPNVMEDIFRRVETTKD-SSELLIRVSFIEIFKEEVFDLLDSNSSAllknd 158
Cdd:cd00106   80 TIFAYGQTGSGKTYTMLGPDPEQ---RGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSPVPKK----- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  159 sgvqakhtalsraPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKKia 238
Cdd:cd00106  152 -------------PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN-- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  239 ggscttTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKrkegGHVPYRDSKLT 318
Cdd:cd00106  217 ------REKSGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLT 286
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 22327992  319 RLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRAR 358
Cdd:cd00106  287 RLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
5-360 8.84e-108

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: 343.29  E-value: 8.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    5 ECVRVAVNIRPLITPELLNGCTDCITVAPKEPQVHIGS---------HTFTYDFVYGnGGYPCSEIYNHCVAPLVDALFK 75
Cdd:cd01371    1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNpkataneppKTFTFDAVFD-PNSKQLDVYDETARPLVDSVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   76 GYNATVLAYGQTGSGKTYTMGTNySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSALL 155
Cdd:cd01371   80 GYNGTIFAYGQTGTGKTYTMEGK-REDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  156 kndsgvqakhtalsrapiQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEqk 235
Cdd:cd01371  159 ------------------ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIE-- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  236 kiaggSCTTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKrkegGHVPYRDS 315
Cdd:cd01371  219 -----CSEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKS----THIPYRDS 289
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 22327992  316 KLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNI 360
Cdd:cd01371  290 KLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
7-360 2.52e-104

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: 333.15  E-value: 2.52e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLiTPELLNGCTDCITVAPKEP--QVHIGSHTFTYDFVYGnGGYPCSEIYNHCVAPLVDALFKGYNATVLAY 84
Cdd:cd01374    2 ITVTVRVRPL-NSREIGINEQVAWEIDNDTiyLVEPPSTSFTFDHVFG-GDSTNREVYELIAKPVVKSALEGYNGTIFAY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   85 GQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSsELLIRVSFIEIFKEEVFDLLDSNSSallkndsgvqak 164
Cdd:cd01374   80 GQTSSGKTFTM----SGDEDEPGIIPLAIRDIFSKIQDTPDR-EFLLRVSYLEIYNEKINDLLSPTSQ------------ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  165 htalsraPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEqkkiaggSCTT 244
Cdd:cd01374  143 -------NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIE-------SSER 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  245 TEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKrkeGGHVPYRDSKLTRLLQDS 324
Cdd:cd01374  209 GELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKV---GGHIPYRDSKLTRILQPS 285
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 22327992  325 LGGNSKTVMIACVSPADTNAEETLNTLKYANRARNI 360
Cdd:cd01374  286 LGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
7-360 3.10e-102

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: 328.53  E-value: 3.10e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITVA--------PKE-----------PQVHIGSHT----FTYDFVYGNGGYPcSEIYN 63
Cdd:cd01370    2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdPKDeedgffhggsnNRDRRKRRNkelkYVFDRVFDETSTQ-EEVYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   64 HCVAPLVDALFKGYNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEV 143
Cdd:cd01370   81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTM----LGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  144 FDLLDSNSsallkndsgvqakhtalsrAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSR 223
Cdd:cd01370  157 RDLLNPSS-------------------GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  224 SHAIFTITLEQKkiaggscTTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKK 303
Cdd:cd01370  218 SHAVLQITVRQQ-------DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGK 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327992  304 RKEggHVPYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNI 360
Cdd:cd01370  291 KNK--HIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
7-367 3.77e-99

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: 320.84  E-value: 3.77e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITVAPKEPQVHIGS-------------HTFTYDFVY----GNGGYPCSE--IYNHCVA 67
Cdd:cd01365    3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKqadknnkatrevpKSFSFDYSYwshdSEDPNYASQeqVYEDLGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   68 PLVDALFKGYNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVE-TTKDSSELLIRVSFIEIFKEEVFDL 146
Cdd:cd01365   83 ELLQHAFEGYNVCLFAYGQTGSGKSYTM----MGTQEQPGIIPRLCEDLFSRIAdTTNQNMSYSVEVSYMEIYNEKVRDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  147 LDSNssallkndsgvqakhTALSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHA 226
Cdd:cd01365  159 LNPK---------------PKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  227 IFTITLEQKKIAGGSCTTTEdggediLCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRKE 306
Cdd:cd01365  224 VFTIVLTQKRHDAETNLTTE------KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327992  307 GGH---VPYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVIN 367
Cdd:cd01365  298 KKKssfIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
7-369 1.68e-97

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: 315.80  E-value: 1.68e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITVAP--KEPQVHIGSH-------TFTYDFVYGNGGyPCSEIYNHCVAPLVDALFKGY 77
Cdd:cd01364    4 IQVVVRCRPFNLRERKASSHSVVEVDPvrKEVSVRTGGLadksstkTYTFDMVFGPEA-KQIDVYRSVVCPILDEVLMGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   78 NATVLAYGQTGSGKTYTMgtnySGDCTN-----------GGVIPNVMEDIFRRVETTKdsSELLIRVSFIEIFKEEVFDL 146
Cdd:cd01364   83 NCTIFAYGQTGTGKTYTM----EGDRSPneeytweldplAGIIPRTLHQLFEKLEDNG--TEYSVKVSYLEIYNEELFDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  147 LDSNSSallkndsgvqakhtalSRAPIQIRETAS--GGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRS 224
Cdd:cd01364  157 LSPSSD----------------VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRS 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  225 HAIFTITLEQKKiaggsctTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKkr 304
Cdd:cd01364  221 HSVFSITIHIKE-------TTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERA-- 291
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327992  305 kegGHVPYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVINRD 369
Cdd:cd01364  292 ---PHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
7-360 1.21e-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: 309.65  E-value: 1.21e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITVAPkEPQVHIGS----HTFTYDFVYgnggYPCS---EIYNHCVAPLVDALFKGYNA 79
Cdd:cd01369    4 IKVVCRFRPLNELEVLQGSKSIVKFDP-EDTVVIATsetgKTFSFDRVF----DPNTtqeDVYNFAAKPIVDDVLNGYNG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   80 TVLAYGQTGSGKTYTM-GTNysGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDsnssallknd 158
Cdd:cd01369   79 TIFAYGQTSSGKTYTMeGKL--GDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  159 sgvqakhtaLSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKkia 238
Cdd:cd01369  147 ---------VSKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--- 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  239 ggsctTTEDGgeDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkeggHVPYRDSKLT 318
Cdd:cd01369  215 -----NVETE--KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLT 283
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 22327992  319 RLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNI 360
Cdd:cd01369  284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
6-362 1.26e-94

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: 307.21  E-value: 1.26e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    6 CVRVAVNIRPLITPELLNGCTdCITVAPKEPQVH------IGSHTFTYDFVYGnggyPCS---EIYNHcVAPLVDALFKG 76
Cdd:cd01366    3 NIRVFCRVRPLLPSEENEDTS-HITFPDEDGQTIeltsigAKQKEFSFDKVFD----PEAsqeDVFEE-VSPLVQSALDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   77 YNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSS-ELLIRVSFIEIFKEEVFDLLDSNSSALL 155
Cdd:cd01366   77 YNVCIFAYGQTGSGKTYTM----EGPPESPGIIPRALQELFNTIKELKEKGwSYTIKASMLEIYNETIRDLLAPGNAPQK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  156 KNDsgvqakhtalsrapiqIRET-ASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQ 234
Cdd:cd01366  153 KLE----------------IRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  235 KKIAGGSCTTtedggedilcAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALgdekkRKEGGHVPYRD 314
Cdd:cd01366  217 RNLQTGEISV----------GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL-----RQKQSHIPYRN 281
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 22327992  315 SKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQN 362
Cdd:cd01366  282 SKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
60-621 2.69e-85

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 289.72  E-value: 2.69e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   60 EIYNHCVAPLVDALFKGYNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIF 139
Cdd:COG5059   72 DVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM----SGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIY 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  140 KEEVFDLLDSNSSALLkndsgvqakhtalsrapiqIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNS 219
Cdd:COG5059  148 NEKIYDLLSPNEESLN-------------------IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIND 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  220 QSSRSHAIFTITLEQKKIAGGsctTTEDGgedilcaKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALG 299
Cdd:COG5059  209 ESSRSHSIFQIELASKNKVSG---TSETS-------KLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALG 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  300 DEKKRkegGHVPYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVINrdpATAQMQRmr 379
Cdd:COG5059  279 DKKKS---GHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN---SSSDSSR-- 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  380 sQIEQLQTELLFYR-GDSGAFDELQILKHKISLleasnRELHNELQERRVASEHFSKRAYDAQVEKDKLIMIIESVRNGK 458
Cdd:COG5059  351 -EIEEIKFDLSEDRsEIEILVFREQSQLSQSSL-----SGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKKLLKEE 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  459 SLDEIESCQNEDVGLVNKyVSKIQELEGELLHIKNLKKTSNHQYSDdsydvgprsnnvlfpssNESSDCEDKvmdvtdeL 538
Cdd:COG5059  425 GWKYKSTLQFLRIEIDRL-LLLREEELSKKKTKIHKLNKLRHDLSS-----------------LLSSIPEET-------S 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  539 EFQEKEIEHcSLQEKLDMELKELDKRLEEKEAEMKRFSsggTSVLKQHYEKKVYDLEQEKRALQREIEGLRH--NLASIP 616
Cdd:COG5059  480 DRVESEKAS-KLRSSASTKLNLRSSRSHSKFRDHLNGS---NSSTKELSLNQVDLAGSERKVSQSVGELLREtqSLNKSL 555

                 ....*
gi 22327992  617 SGPGD 621
Cdd:COG5059  556 SSLGD 560
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
7-369 7.56e-83

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: 275.16  E-value: 7.56e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITVAPKEPQVHIG--SHTFTYDFVYGNGGYPcSEIYNHCVAPLVDALFKGYNATVLAY 84
Cdd:cd01373    3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkpPKTFTFDHVADSNTNQ-ESVFQSVGKPIVESCLSGYNGTIFAY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   85 GQTGSGKTYTM-GTNYSGDCTNG---GVIPNVMEDIFRRV----ETTKDSSELLIRVSFIEIFKEEVFDLLDSNSSALlk 156
Cdd:cd01373   82 GQTGSGKTYTMwGPSESDNESPHglrGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  157 ndsgvqakhtalsrapiQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLEQKK 236
Cdd:cd01373  160 -----------------KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  237 iaGGSCTTTedggedILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRKEGgHVPYRDSK 316
Cdd:cd01373  223 --KKACFVN------IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQR-HVCYRDSK 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22327992  317 LTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVINRD 369
Cdd:cd01373  294 LTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
7-356 1.43e-82

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: 273.40  E-value: 1.43e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITVAPK-EPQVH-----------IGSHTFTYDFVYGnGGYPCSEIYNHCVAPLVDALF 74
Cdd:cd01367    2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKlTLIVHepklkvdltkyIENHTFRFDYVFD-ESSSNETVYRSTVKPLVPHIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   75 KGYNATVLAYGQTGSGKTYTMGTNYSGDCTNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLLDsnssal 154
Cdd:cd01367   81 EGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  155 lkndsgvqakhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLeq 234
Cdd:cd01367  155 --------------RKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  235 kkiaggsctttEDGGEDILCAKLHLVDLAGSER-AKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKrkeggHVPYR 313
Cdd:cd01367  219 -----------RDRGTNKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKA-----HIPFR 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 22327992  314 DSKLTRLLQDSL-GGNSKTVMIACVSPADTNAEETLNTLKYANR 356
Cdd:cd01367  283 GSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
7-354 3.39e-76

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


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 256.17  E-value: 3.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCITV---------APKEPQVHIGSHT-------FTYDFVYGNGgYPCSEIYNHCVAPLV 70
Cdd:cd01368    3 VKVYLRVRPLSKDELESEDEGCIEVinsttvvlhPPKGSAANKSERNggqketkFSFSKVFGPN-TTQKEFFQGTALPLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   71 DALFKGYNATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRrveTTKDSSellIRVSFIEIFKEEVFDLLDSN 150
Cdd:cd01368   82 QDLLHGKNGLLFTYGVTNSGKTYTM----QGSPGDGGILPRSLDVIFN---SIGGYS---VFVSYIEIYNEYIYDLLEPS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  151 SSALLKNdsgvqakhtalsRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTI 230
Cdd:cd01368  152 PSSPTKK------------RQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  231 TLEQkkIAGGSCTTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRKEGGHV 310
Cdd:cd01368  220 KLVQ--APGDSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMV 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 22327992  311 PYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYA 354
Cdd:cd01368  298 PFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
7-358 1.25e-68

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: 233.93  E-value: 1.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    7 VRVAVNIRPLITPELLNGCTDCI------TVAPKEPQVHIGSHTFTYDFVYGNggyPCS--EIYNHCVAPLVDALFKGYN 78
Cdd:cd01376    2 VRVAVRVRPFVDGTAGASDPSCVsgidscSVELADPRNHGETLKYQFDAFYGE---ESTqeDIYAREVQPIVPHLLEGQN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   79 ATVLAYGQTGSGKTYTMgtnySGDCTNGGVIPNVMEDIFRRVETTKDSSELLIrvSFIEIFKEEVFDLLDSNSSALLknd 158
Cdd:cd01376   79 ATVFAYGSTGAGKTFTM----LGSPEQPGLMPLTVMDLLQMTRKEAWALSFTM--SYLEIYQEKILDLLEPASKELV--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  159 sgvqakhtalsrapiqIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITL-EQKKI 237
Cdd:cd01376  150 ----------------IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVdQRERL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  238 AGGSCTTTedggedilcaKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRkegghVPYRDSKL 317
Cdd:cd01376  214 APFRQRTG----------KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR-----IPYRDSKL 278
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 22327992  318 TRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRAR 358
Cdd:cd01376  279 TRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
61-358 1.04e-66

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: 229.00  E-value: 1.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   61 IYNHCVAPLVDALFKGYNATVLAYGQTGSGKTYTM---GTNYSgdctNGGVIPNVMEDIFRRVEttKDSSELL-IRVSFI 136
Cdd:cd01375   64 VYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMtggTENYK----HRGIIPRALQQVFRMIE--ERPTKAYtVHVSYL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  137 EIFKEEVFDLLDSNSSALLKNDsgvqakhtalsraPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTN 216
Cdd:cd01375  138 EIYNEQLYDLLSTLPYVGPSVT-------------PMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  217 MNSQSSRSHAIFTITLEQKkiaggsctTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVIS 296
Cdd:cd01375  205 MNKNSSRSHCIFTIHLEAH--------SRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAII 276
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327992  297 ALGDEKKRkeggHVPYRDSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRAR 358
Cdd:cd01375  277 ALSDKDRT----HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
7-396 2.03e-64

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 240.61  E-value: 2.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992     7 VRVAVNIRPLITPELlngcTDCITVAPKEPQVHIGSHTFTYDFVyGNGGYPCSEIYNHCVAPLVDALFKGYNATVLAYGQ 86
Cdd:PLN03188  100 VKVIVRMKPLNKGEE----GEMIVQKMSNDSLTINGQTFTFDSI-ADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    87 TGSGKTYTM--------GTNYSGDctNGGVIPNVMEDIFRRV--ETTKDSSELL---IRVSFIEIFKEEVFDLLDSnssa 153
Cdd:PLN03188  175 TGSGKTYTMwgpangllEEHLSGD--QQGLTPRVFERLFARIneEQIKHADRQLkyqCRCSFLEIYNEQITDLLDP---- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   154 llkndsgvqakhtalSRAPIQIRETASGGITLAGVTEAEVKTKEEMGSFLARGSLSRATGSTNMNSQSSRSHAIFTITLE 233
Cdd:PLN03188  249 ---------------SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVE 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   234 QKkiaggsCTTTEDGGEDILCAKLHLVDLAGSERAKRTGADGMRLKEGIHINKGLLALGNVISALGDEKKRKEGGHVPYR 313
Cdd:PLN03188  314 SR------CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYR 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   314 DSKLTRLLQDSLGGNSKTVMIACVSPADTNAEETLNTLKYANRARNIQNKAVINrDPATAQMQRMRSQIEQLQTELLFYR 393
Cdd:PLN03188  388 DSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN-EVMQDDVNFLREVIRQLRDELQRVK 466

                  ...
gi 22327992   394 GDS 396
Cdd:PLN03188  467 ANG 469
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
28-339 1.77e-13

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: 69.68  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   28 CITVAP-KEPQVHIGSHTFTYDFVYGNGGYPcSEIYNHCvAPLVDALFKGYN-ATVLAYGQTGSGKTYTMgtnysgdctn 105
Cdd:cd01363    2 LVRVNPfKELPIYRDSKIIVFYRGFRRSESQ-PHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  106 GGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEevfdLLDSNSSAllkndsgvQAKHTAlsrapiqiretasggitl 185
Cdd:cd01363   70 KGVIPYLASVAFNGINKGETEGWVYLTEITVTLEDQ----ILQANPIL--------EAFGNA------------------ 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  186 agvteaevktkeemgsflargslsratgSTNMNSQSSRSHAIFTItleqkkiaggsctttedggedilcaklhLVDLAGS 265
Cdd:cd01363  120 ----------------------------KTTRNENSSRFGKFIEI----------------------------LLDIAGF 143
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327992  266 ERakrtgadgmrlkegihINKGLLALGNVISAlgdekkrkegghvpyrdskltrllqdslggnSKTVMIACVSP 339
Cdd:cd01363  144 EI----------------INESLNTLMNVLRA-------------------------------TRPHFVRCISP 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
529-845 2.70e-10

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: 65.08  E-value: 2.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    529 DKVMDVTDELEfqeKEIEHCSLQEK-------LDMELKELDK-----RLEEKEAEMKRFSSggtsvLKQHYEKKVYDLEQ 596
Cdd:TIGR02168  189 DRLEDILNELE---RQLKSLERQAEkaerykeLKAELRELELallvlRLEELREELEELQE-----ELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    597 EKRALQREIEGLRHNLASIpSGPGDGAQKLKEEYVQKLNTLETQVSVLKKKQD--------AQAQLMRQKQKSDDaaikL 668
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleeLEAQLEELESKLDE----L 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    669 QDEIHRIKSQKVQLQQKIKQESEQFRawKASREKEVMQLKKEGRRNEYEmhklmALNQKQKLVLQRKTEEASQVtkrlkE 748
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELE--ELEAELEELESRLEELEEQLE-----TLRSKVAQLELQIASLNNEI-----E 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    749 LLDNRKASSRETLSGANGPGTQALMQAIEHEI-EVTVRVHEVRSEYERQTEERARMAKEVARLREENELLKNAKISVHGD 827
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
                          330
                   ....*....|....*...
gi 22327992    828 TMSpgaRNSRIFALENML 845
Cdd:TIGR02168  484 LAQ---LQARLDSLERLQ 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
558-825 6.06e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 6.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  558 LKELDKRLE--EKEAEM-KRFssggtsvLKQHYEKKVYDLE---QEKRALQREIEGLRHNLASipsgpgdgAQKLKEEYV 631
Cdd:COG1196  195 LGELERQLEplERQAEKaERY-------RELKEELKELEAElllLKLRELEAELEELEAELEE--------LEAELEELE 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  632 QKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKlqdEIHRIKSQKVQLQQKIKQESEQfrawKASREKEVMQLKKEG 711
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEER----LEELEEELAELEEEL 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  712 RRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRLKELLDNRKASSRETLSGAngpgtQALMQAIEHEIEVTVRVHEVRS 791
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-----EELLEALRAAAELAAQLEELEE 407
                        250       260       270
                 ....*....|....*....|....*....|....
gi 22327992  792 EYERQTEERARMAKEVARLREENELLKNAKISVH 825
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEE 441
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
373-813 6.96e-09

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: 60.47  E-value: 6.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    373 AQMQRMRSQIEQLQTELlfyrgdSGAFDELQILKHKISLLEASNRELHNELQERrvasehfSKRAYDAQVEKDKLIMIIE 452
Cdd:TIGR02169  674 AELQRLRERLEGLKREL------SSLQSELRRIENRLDELSQELSDASRKIGEI-------EKEIEQLEQEEEKLKERLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    453 SVRngkslDEIESCQNEdvglVNKYVSKIQELEGEL----LHIKNLKKTSNHQYSDDSydvgprsnnvlfpssnessdcE 528
Cdd:TIGR02169  741 ELE-----EDLSSLEQE----IENVKSELKELEARIeeleEDLHKLEEALNDLEARLS---------------------H 790
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    529 DKVMDVTDELEFQEKEIEhcslqeKLDMELKELDKRLEEKEAEMKRFSSggtsvLKQHYEKKVYDLEQEKRALQREIEGL 608
Cdd:TIGR02169  791 SRIPEIQAELSKLEEEVS------RIEARLREIEQKLNRLTLEKEYLEK-----EIQELQEQRIDLKEQIKSIEKEIENL 859
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    609 RHNLASIpsgpgdgAQKLkEEYVQKLNTLETQVSVLKKKQD-AQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIK 687
Cdd:TIGR02169  860 NGKKEEL-------EEEL-EELEAALRDLESRLGDLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    688 QESEqfrawkasrekevmqLKKEGRRNEYEMHKLMALNQKQKlVLQRKTEEAsqvtkrlkelldnrkassrETLSGANgp 767
Cdd:TIGR02169  932 ELSE---------------IEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEI-------------------RALEPVN-- 974
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 22327992    768 gtqalMQAIEHEIEVTVRVHEVRSEYERQTEERARMAKEVARLREE 813
Cdd:TIGR02169  975 -----MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
542-876 1.37e-08

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: 59.70  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    542 EKEIEHCSLQEKL-DMELKELDKRLEEKEAEmkrfssggtsvlKQHYEKKVYDLEQEKRALQREIEGLRHNLASIPSGPG 620
Cdd:TIGR02169  208 EKAERYQALLKEKrEYEGYELLKEKEALERQ------------KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    621 DGAQKLKEEYVQKLNTLETQVSVLKKK----QDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQESEQFRAW 696
Cdd:TIGR02169  276 ELNKKIKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    697 K---ASREKEVMQLKkegRRNEYEMHKLMALNQKQKlvlQRKtEEASQVTKRLKELLDN--RKASSRETLSGANGPGTQA 771
Cdd:TIGR02169  356 TeeyAELKEELEDLR---AELEEVDKEFAETRDELK---DYR-EKLEKLKREINELKREldRLQEELQRLSEELADLNAA 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    772 LMQAIEHEIEVTVRVHEVRSEYERQTEERARMAKEVARLREEnellknakisvhgdtmspgarnsrIFALENMLATSSST 851
Cdd:TIGR02169  429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE------------------------LYDLKEEYDRVEKE 484
                          330       340
                   ....*....|....*....|....*
gi 22327992    852 LVSMASQLSEAEERERVFGGRGRWN 876
Cdd:TIGR02169  485 LSKLQRELAEAEAQARASEERVRGG 509
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
6-147 2.25e-08

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 54.15  E-value: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992      6 CVRVAVNIRPLITPELlngCTDCITVAPKEPQVHIGSHTFTYDFVYGNGGyPCSEIYNHCVApLVDALFKGYNATVLAYG 85
Cdd:pfam16796   21 NIRVFARVRPELLSEA---QIDYPDETSSDGKIGSKNKSFSFDRVFPPES-EQEDVFQEISQ-LVQSCLDGYNVCIFAYG 95
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327992     86 QTGSGKtytmgtnysgdctNGGVIPNVMEDIFRRVETTKDSSELLIRVSFIEIFKEEVFDLL 147
Cdd:pfam16796   96 QTGSGS-------------NDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
554-765 1.29e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  554 LDMELKELDKRLEEKEAEMKRF--SSGGTSV--LKQHYEKKVYDLEQEKRALQREIEGLRHNLASIPSGPGDGAQKLKEe 629
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFrqKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE- 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  630 yvqkLNTLETQVSVLKKKQDAQAQLMRQKQKSDD---AAIKLQDEIHRIKSQKVQLQQKIKQESEQFRAWKASREKEVmq 706
Cdd:COG3206  259 ----LLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL-- 332
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327992  707 lkkEGRRNEYEmHKLMALNQKQK--LVLQRKTEEASQVtkrLKELLDNRK-ASSRETLSGAN 765
Cdd:COG3206  333 ---QAQLAQLE-ARLAELPELEAelRRLEREVEVAREL---YESLLQRLEeARLAEALTVGN 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
443-754 2.43e-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: 52.37  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    443 EKDKLIMIIESVRNGKSLDEIESCQNEDVGLVNKYVSKIQELEGEL----LHIKNLKKTSNHQYSDdsydvgprsnnvLF 518
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKE------------LY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    519 PSSNESSDCEDKVMDVTDELEFQEKEIEHCSLQ--------EKLDMELKELDKRLEEKEAEMKRFSSGGTSvlkqhYEKK 590
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQleelesklDELAEELAELEEKLEELKEELESLEAELEE-----LEAE 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    591 VYDLEQEKRALQREIEGLRHNLASIpsgpgdgaqklkeeyVQKLNTLETQVSVLK-KKQDAQAQLMRQKQKSDDAAIKLQ 669
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQL---------------ELQIASLNNEIERLEaRLERLEDRRERLQQEIEELLKKLE 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    670 ----DEIHRIKSQKVQLQQKIKQESEQFRAWKASREKEVMQLKKEGRRNEYEMHKLmalnQKQKLVLQRKTEEASQVTKR 745
Cdd:TIGR02168  432 eaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARLDSLERLQENLEGFSEG 507

                   ....*....
gi 22327992    746 LKELLDNRK 754
Cdd:TIGR02168  508 VKALLKNQS 516
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
524-821 3.74e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   524 SSDCEDKVMDVTDELEFQEKEI-EHCSLQEKLDMELKELDKRLEEKEAEMKRFSSggtsvlkqhYEKKVYDLEQEKRALQ 602
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREInEISSELPELREELEKLEKEVKELEELKEEIEE---------LEKELESLEGSKRKLE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   603 REIEGLRHNLASipsgpgdgaqklKEEYVQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQL 682
Cdd:PRK03918  259 EKIRELEERIEE------------LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   683 QQKIKQESEqfrawKASREKEVMQLKKEGRRneyemhKLMALNQKQKLVlqrktEEASQVTKRLKELLDNRKASSRETls 762
Cdd:PRK03918  327 EERIKELEE-----KEERLEELKKKLKELEK------RLEELEERHELY-----EEAKAKKEELERLKKRLTGLTPEK-- 388
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   763 gangpgtqalmqaIEHEIE-VTVRVHEVRSEYERQTEERARMAKEVARLREENELLKNAK 821
Cdd:PRK03918  389 -------------LEKELEeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
401-752 5.08e-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: 51.21  E-value: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    401 ELQILKHKISLLEASNRELHNELQERRVASEHFSKRAYDAQVEKDKLIMIIESVRNGKSLDEIEscqnedvglVNKYVSK 480
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE---------VEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    481 IQELEGELLHIKNLKKTSnhqysddsydvgprsnnvlfpssnessdcEDKVMDVTDELEFQEKEIEhcSLQEKLD---ME 557
Cdd:TIGR02168  749 IAQLSKELTELEAEIEEL-----------------------------EERLEEAEEELAEAEAEIE--ELEAQIEqlkEE 797
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    558 LKELDKRLEEKEAEMKRFSSGGTSVL--KQHYEKKVYDLEQEKRALQREIEGLRHNLASipsgpgdgAQKLKEEYVQKLN 635
Cdd:TIGR02168  798 LKALREALDELRAELTLLNEEAANLRerLESLERRIAATERRLEDLEEQIEELSEDIES--------LAAEIEELEELIE 869
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    636 TLETQVSVLKKKQDAQAQLMRQKQksdDAAIKLQDEIHRIKSQKVQLQQKI---KQESEQFRAWKASREKEVMQLkKEGR 712
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLR---SELEELSEELRELESKRSELRRELeelREKLAQLELRLEGLEVRIDNL-QERL 945
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 22327992    713 RNEYEMHKLMALNQKQKLVLQrkTEEASQVTKRLKELLDN 752
Cdd:TIGR02168  946 SEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKE 983
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
550-710 6.14e-06

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: 49.15  E-value: 6.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  550 LQEkLDMELKELDKRLEEKEAEMKRFSSggtsvLKQHYEKKVYDLEQEKRALQREIEGLRHNLASipsgpgdgAQKLKEE 629
Cdd:COG1579   12 LQE-LDSELDRLEHRLKELPAELAELED-----ELAALEARLEAAKTELEDLEKEIKRLELEIEE--------VEARIKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  630 YVQKLNTLET--QVSVLKKKQDAQAqlmRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQESEQFRAWKASREKEVMQL 707
Cdd:COG1579   78 YEEQLGNVRNnkEYEALQKEIESLK---RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

                 ...
gi 22327992  708 KKE 710
Cdd:COG1579  155 EAE 157
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
354-867 6.37e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  354 ANRARNIQNK--------AVINRDPATAQMQRMRSQIEQLQTELlfyrgdsgafdelQILKHKISLLEASNRELHNELQE 425
Cdd:COG1196  212 AERYRELKEElkeleaelLLLKLRELEAELEELEAELEELEAEL-------------EELEAELAELEAELEELRLELEE 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  426 RRVASEHFSKRAYDAQVEKDKLIMIIESV-----RNGKSLDEIESCQNEDVGLVNKYVSKIQELEGELLHIKNLKKTSNH 500
Cdd:COG1196  279 LELELEEAQAEEYELLAELARLEQDIARLeerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  501 QYSDDsydvgprsnnvlfpSSNESSDCEDKVMDVTDELEFQEKEIEHCSLQEKLDMELKELDKRLEEKEAEMKRfssggt 580
Cdd:COG1196  359 ELAEA--------------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER------ 418
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  581 svlkqhyekkvydLEQEKRALQREIEGLRHNLASIpsgpgdgAQKLKEEYVQKLNTLETQVSVLKKKQDAQAQLMRQKQK 660
Cdd:COG1196  419 -------------LEEELEELEEALAELEEEEEEE-------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  661 SDDaaikLQDEIHRIKSQKVQLQQKIKQESEQFRAWKASREKEVMQLKKE------GRRNEYEMHKLMALNQKQKLVLQR 734
Cdd:COG1196  479 LAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavavliGVEAAYEAALEAALAAALQNIVVE 554
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  735 KTEEASQVTKRLKE------------LLDNRKASSRETLSGANGPGTQALMQAIEHEIEVTVRVHEVRSEyERQTEERAR 802
Cdd:COG1196  555 DDEVAAAAIEYLKAakagratflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG-RTLVAARLE 633
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327992  803 MAKEVARLREENELLKnakiSVHGDTMSPGARNSRIFALENmlATSSSTLVSMASQLSEAEERER 867
Cdd:COG1196  634 AALRRAVTLAGRLREV----TLEGEGGSAGGSLTGGSRREL--LAALLEAEAELEELAERLAEEE 692
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
551-764 1.59e-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: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  551 QEKLDMELKELDKRLEEKEAEMKRFSSGGTSVLKQ---------HYEKKVYDLEQEKRALQREIEGLRHNLASIpsgpGD 621
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalerriaALARRIRALEQELAALEAELAELEKEIAEL----RA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  622 GAQKLKEEYVQKLNTLETQ-----VSVLKKKQDAQ-----AQLMRQKQKSDDAAIK-LQDEIHRIKSQKVQLQQKiKQES 690
Cdd:COG4942   98 ELEAQKEELAELLRALYRLgrqppLALLLSPEDFLdavrrLQYLKYLAPARREQAEeLRADLAELAALRAELEAE-RAEL 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327992  691 EQFRAWKASREKEVMQLKKEGRRNEYEMHKLMALNQKQklvLQRKTEEASQVTKRLKELLDNRKASSRETLSGA 764
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
398-824 3.54e-05

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: 48.18  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    398 AFDELQILKhkisllEASNRELHNELQERRVASEHFSKRaYDAQV---EKDKLIMIIESVRNGKSLDEIESCQNEDVGLV 474
Cdd:pfam05483  198 AFEELRVQA------ENARLEMHFKLKEDHEKIQHLEEE-YKKEIndkEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    475 NKYVSKIQelegelLHIKNLKKTSNHQYsddsydvgprsnnvlfpssNESSDCEDKVMDVTDELEFQEkeiehcSLQEKL 554
Cdd:pfam05483  271 NQLEEKTK------LQDENLKELIEKKD-------------------HLTKELEDIKMSLQRSMSTQK------ALEEDL 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    555 DMELKELDKRLEEKEAEMKRFSSGGT--SVLKQHYEKKVYDLEQEKRALQREIEGLRHNLASIPSGPGDGAQKLkEEYVQ 632
Cdd:pfam05483  320 QIATKTICQLTEEKEAQMEELNKAKAahSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTK 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    633 KLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQESEQFRAWKASRE---KEVMQLKK 709
Cdd:pfam05483  399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKT 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    710 EGRRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRLK----ELLDNRKASSRetlsgangpgtqaLMQAIE--HEIEVT 783
Cdd:pfam05483  479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKkhqeDIINCKKQEER-------------MLKQIEnlEEKEMN 545
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 22327992    784 VR--VHEVRSEYERQTEE---RARMAKEVARLREENELLKNAKISV 824
Cdd:pfam05483  546 LRdeLESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKI 591
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
594-817 1.48e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.27  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    594 LEQEKRALQREIEGLRHNLASIPSGPGDGAQKLKEEyVQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIH 673
Cdd:pfam05557   11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRE-SDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    674 RIKSQKVQLQQKIKQEseqfrawKASREKEVMQLKKEGRRNEYEM----HKLMALNQKQKLvLQRKTEEASQVTKRLKEL 749
Cdd:pfam05557   90 KKLNEKESQLADAREV-------ISCLKNELSELRRQIQRAELELqstnSELEELQERLDL-LKAKASEAEQLRQNLEKQ 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327992    750 LDNRKASSRETlsgangpgtQALMQAIEHEIEVTVRVHEVRSEYERQTEerarMAKEVARLREENELL 817
Cdd:pfam05557  162 QSSLAEAEQRI---------KELEFEIQSQEQDSEIVKNSKSELARIPE----LEKELERLREHNKHL 216
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
558-692 1.48e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   558 LKELDKRLEEKEAEMKRfssggtsvLKQHYEKKVYDLEQEKRALQREIEGLRhnlasipsgpgdgaQKLKEEYVQKLNTL 637
Cdd:PRK00409  525 LEELERELEQKAEEAEA--------LLKEAEKLKEELEEKKEKLQEEEDKLL--------------EEAEKEAQQAIKEA 582
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327992   638 etqvsvlKKKQDAQAQLMRQKQKSDDAAIKLQD--EIHRIKSQKVQLQQKIKQESEQ 692
Cdd:PRK00409  583 -------KKEADEIIKELRQLQKGGYASVKAHEliEARKRLNKANEKKEKKKKKQKE 632
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
528-703 6.67e-04

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: 43.60  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  528 EDKVMDVTDELEFQEKEIEhcslqeKLDMELKELDKRLEEKEAEMKR-----FSSGGTSVLK--------QHYEKKVYDL 594
Cdd:COG4942   68 ARRIRALEQELAALEAELA------ELEKEIAELRAELEAQKEELAEllralYRLGRQPPLAlllspedfLDAVRRLQYL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  595 EQEKRALQREIEGLRHNLASIpsgpgdgaQKLKEEYVQKLNTLETQvsvLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHR 674
Cdd:COG4942  142 KYLAPARREQAEELRADLAEL--------AALRAELEAERAELEAL---LAELEEERAALEALKAERQKLLARLEKELAE 210
                        170       180
                 ....*....|....*....|....*....
gi 22327992  675 IKSQKVQLQQKIKQESEQFRAWKASREKE 703
Cdd:COG4942  211 LAAELAELQQEAEELEALIARLEAEAAAA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
593-823 7.46e-04

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: 43.60  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  593 DLEQEKRALQREIEGLRHNLASIpsgpgdgaQKLKEEYVQKLNTLETQVSVLKKKQDAqaqlmrqkqksddaaikLQDEI 672
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAAL--------KKEEKALLKQLAALERRIAALARRIRA-----------------LEQEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  673 HRIKSQKVQLQQKIKQESEQFRAWKASREKEVMQLKKEGRR-------------------------NEYEMHKLMALNQK 727
Cdd:COG4942   79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRAD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  728 QKLvLQRKTEEASQVTKRLKELLDNRKASSRETLSGANgpGTQALMQAIEHEIEvtvrvhEVRSEYERQTEERARMAKEV 807
Cdd:COG4942  159 LAE-LAALRAELEAERAELEALLAELEEERAALEALKA--ERQKLLARLEKELA------ELAAELAELQQEAEELEALI 229
                        250
                 ....*....|....*.
gi 22327992  808 ARLREENELLKNAKIS 823
Cdd:COG4942  230 ARLEAEAAAAAERTPA 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
537-695 8.98e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  537 ELEFQEKEIEHC-SLQEKLDMELKELDKRLEEKEAEM-----KRFSSGGTSVlkQHYEKKVYDLEQEKRALQREIEGLRH 610
Cdd:COG4913  289 RLELLEAELEELrAELARLEAELERLEARLDALREELdeleaQIRGNGGDRL--EQLEREIERLERELEERERRRARLEA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  611 NLASIPSGPGDGAQKLKEEYVQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQlqqkIKQES 690
Cdd:COG4913  367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN----IPARL 442

                 ....*
gi 22327992  691 EQFRA 695
Cdd:COG4913  443 LALRD 447
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
352-820 1.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   352 KYANRARNIQNKAVINRDPATAQMQR---MRSQIEQLQTELlfyrgdSGAFDELQILKHKISLLEASNRELHNELQERRV 428
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKELEEVLREineISSELPELREEL------EKLEKEVKELEELKEEIEELEKELESLEGSKRK 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   429 ASEHFSKRAYDAQVEKDKLIMIIESVRNGKSLDEIESCQNEDVGLVNKYVSKIQELEGELLHIKNLKKTSNHQYSddsyd 508
Cdd:PRK03918  257 LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----- 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   509 vgprsnnvlfpssnESSDCEDKVMDVTDELEFQEKEIEHCSLQEKLDMELKELDKRLEEKEAEMKRFSSGGTSVL----- 583
Cdd:PRK03918  332 --------------ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEleele 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   584 --KQHYEKKVYDLEQEKRALQREIEGLRHNLASIPSGPG-----------DGAQKLKEEYVQKLNTLETQvsvlKKKQDA 650
Cdd:PRK03918  398 kaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteEHRKELLEEYTAELKRIEKE----LKEIEE 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   651 QAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQ-----------QKIKQESEQFRAWKasreKEVMQLKKEGRRNEYEMH 719
Cdd:PRK03918  474 KERKLRKELRELEKVLKKESELIKLKELAEQLKeleeklkkynlEELEKKAEEYEKLK----EKLIKLKGEIKSLKKELE 549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   720 KLMALNqKQKLVLQRKTEEASQVTKRLKELLDNRKASSRETLSGAngpgtqalMQAIEHEIEVTVRVHEVRSEYERQTEE 799
Cdd:PRK03918  550 KLEELK-KKLAELEKKLDELEEELAELLKELEELGFESVEELEER--------LKELEPFYNEYLELKDAEKELEREEKE 620
                         490       500
                  ....*....|....*....|.
gi 22327992   800 RARMAKEVARLREENELLKNA 820
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKR 641
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
567-733 1.40e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 41.57  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    567 EKEAEMKRFSSGGTSVLKQHyekkvydlEQEKRALQREIEGLRHNLAsipsgpgDGAQKLKEEYVQKLNTLETQVSVLKK 646
Cdd:pfam15665   46 GEELDLKRRIQTLEESLEQH--------ERMKRQALTEFEQYKRRVE-------ERELKAEAEHRQRVVELSREVEEAKR 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    647 KQDAQ----AQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQES---EQFRAWKASREkEVMQLKKEGRRNEYEMH 719
Cdd:pfam15665  111 AFEEKlesfEQLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASslaEQEKLEELHKA-ELESLRKEVEDLRKEKK 189
                          170
                   ....*....|....
gi 22327992    720 KLMALNQKQKLVLQ 733
Cdd:pfam15665  190 KLAEEYEQKLSKAQ 203
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
565-778 1.75e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.73  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   565 LEEKEAEMKRfssggtsvlKQHYEKKVYDLEQEKRALQREIEGLRHNLASIPSGPgdGAQKLKEEYVQKLNTLETQVSVL 644
Cdd:PRK10929   57 LEERKGSLER---------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNM--STDALEQEILQVSSQLLEKSRQA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   645 KKKQDaqaqlmRQKQKSDDAAI--KLQDEIHRIKSQ-KVQLQQKIKQESEQFRAWKASREKEVMQLKkeGRRNEYEMHKL 721
Cdd:PRK10929  126 QQEQD------RAREISDSLSQlpQQQTEARRQLNEiERRLQTLGTPNTPLAQAQLTALQAESAALK--ALVDELELAQL 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327992   722 MAlNQKQKLVLQRkteeaSQVTKRLKELLDNRKASSRETLsgaNGPGTQALMQAIEH 778
Cdd:PRK10929  198 SA-NNRQELARLR-----SELAKKRSQQLDAYLQALRNQL---NSQRQREAERALES 245
PRK12704 PRK12704
phosphodiesterase; Provisional
623-803 1.99e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   623 AQKLKEEYVQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDdaaikLQDEIHRIKSQKVQLQQKIKQESEQFrawkaSREK 702
Cdd:PRK12704   33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNE-----FEKELRERRNELQKLEKRLLQKEENL-----DRKL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   703 EvmQLKKEGRRNEyemHKLMALNQKQKLVLQRKTEEASQVTKRLKELldnrkassrETLSG-----AngpgTQALMQAIE 777
Cdd:PRK12704  103 E--LLEKREEELE---KKEKELEQKQQELEKKEEELEELIEEQLQEL---------ERISGltaeeA----KEILLEKVE 164
                         170       180
                  ....*....|....*....|....*...
gi 22327992   778 HEI--EVTVRVHEVRSEYERQTEERARM 803
Cdd:PRK12704  165 EEArhEAAVLIKEIEEEAKEEADKKAKE 192
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
458-760 2.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    458 KSLDEIESCQNEDVGLVNKYVSKIQELEGELLHIKNLKKTSNHQYSDDSYDvgprsnnvLFPSSNESSDCEDKVMDVTDE 537
Cdd:TIGR04523   54 KELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD--------LSKINSEIKNDKEQKNKLEVE 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    538 LEFQEKEIEHCSLQEKLDM-ELKELDKRLEEKEAEMKRFssggtsvlkqhyEKKVYDLEQEKRALQREIEGLRHNLASIP 616
Cdd:TIGR04523  126 LNKLEKQKKENKKNIDKFLtEIKKKEKELEKLNNKYNDL------------KKQKEELENELNLLEKEKLNIQKNIDKIK 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    617 SgpgdgaqklkeeyvqKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQESEQFRAW 696
Cdd:TIGR04523  194 N---------------KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327992    697 KASREKEVMQLKKegRRNEYEMHKLMaLNQKQKLVLQRKTE-------EASQVTKRLKELLDNRKASSRET 760
Cdd:TIGR04523  259 KDEQNKIKKQLSE--KQKELEQNNKK-IKELEKQLNQLKSEisdlnnqKEQDWNKELKSELKNQEKKLEEI 326
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
588-815 2.85e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  588 EKKVYDLEQEKRALQREIEGLRHNLASipsgpgdgAQKLKEEYVQKLNTLETQvsvLKKKQDAQAQLMRQKQKSDDAAIK 667
Cdd:COG4372   44 QEELEQLREELEQAREELEQLEEELEQ--------ARSELEQLEEELEELNEQ---LQAAQAELAQAQEELESLQEEAEE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  668 LQDEIHRIKSQKVQLQQ---KIKQESEQFRAWKASREKEVMQLKKEGRRNEYEMHKLMALNQkqklvlQRKTEEASQVTK 744
Cdd:COG4372  113 LQEELEELQKERQDLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ------ALSEAEAEQALD 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327992  745 RLKELLDNRKASSRETLSGANGPGTQALMQAIEHEIEVTVRVHEVRSEYERQTEERARMAKEVARLREENE 815
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
523-771 3.15e-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: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  523 ESSDCEDKVMDVTDELEFQEKEIEhcslqeKLDMELKELDKRLEEKEAEMKRFssggtsvlkqhyEKKVYDLEQEKRALQ 602
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELD------ALQAELEELNEEYNELQAELEAL------------QAEIDKLQAEIAEAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  603 REIEGLRHNLASI---------PSGPGD---GAQKLkEEYVQKLNTLET----QVSVLKKKQDAQAQLMRQKQKSDDAAI 666
Cdd:COG3883   79 AEIEERREELGERaralyrsggSVSYLDvllGSESF-SDFLDRLSALSKiadaDADLLEELKADKAELEAKKAELEAKLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  667 KLQDEIHRIKSQKVQLQQKIKQeseqfrawkasREKEVMQLKKEGRRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRL 746
Cdd:COG3883  158 ELEALKAELEAAKAELEAQQAE-----------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
                        250       260
                 ....*....|....*....|....*
gi 22327992  747 KELLDNRKASSRETLSGANGPGTQA 771
Cdd:COG3883  227 AAAAAAAAAAAAAAAAAASAAGAGA 251
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
528-783 3.51e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  528 EDKVMDVTDELEFQEKEIEhcSLQEKLDMELKELDKR--LEEKEAEMKRFSSGGT-SVLKQHYEKKVYDL----EQEKRA 600
Cdd:COG5185  274 AESSKRLNENANNLIKQFE--NTKEKIAEYTKSIDIKkaTESLEEQLAAAEAEQElEESKRETETGIQNLtaeiEQGQES 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  601 LQREIEGLRHNLASIPsgpGDGAQKLKEEyvqKLNTLETQVSVLKKKQDAQAQlmRQKQKSDDAAIKLQDEIHRIKSQKV 680
Cdd:COG5185  352 LTENLEAIKEEIENIV---GEVELSKSSE---ELDSFKDTIESTKESLDEIPQ--NQRGYAQEILATLEDTLKAADRQIE 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  681 QLQQKIKQESEQFRAwkASREKEVMQLKKEGRRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRLKElLDNRKASSRET 760
Cdd:COG5185  424 ELQRQIEQATSSNEE--VSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQ-IESRVSTLKAT 500
                        250       260
                 ....*....|....*....|...
gi 22327992  761 LSGANGPGTQALMQAIEHEIEVT 783
Cdd:COG5185  501 LEKLRAKLERQLEGVRSKLDQVA 523
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
536-695 3.74e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  536 DELEFQEKEIEHCSLQEKLDMELKELDKRLEEKEAEMKRFSsggtsvlkqhyekkvyDLEQEKRALQREIEGLRHNLASI 615
Cdd:COG4717  119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR----------------ELEEELEELEAELAELQEELEEL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  616 PSGPGDGAQKLKEEYVQKLNTLETQVSVLKKK-QDAQAQLMRQKQKSDDAAIKLQDEihriksqkvQLQQKIKQESEQFR 694
Cdd:COG4717  183 LEQLSLATEEELQDLAEELEELQQRLAELEEElEEAQEELEELEEELEQLENELEAA---------ALEERLKEARLLLL 253

                 .
gi 22327992  695 A 695
Cdd:COG4717  254 I 254
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
533-824 4.50e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    533 DVTDELEFQEKEIEHCSLQ-----EKLDMELKELDKRLEEKEAEMKRFSSGGTSV---LKQHyEKKVYDLEQEKRALQRE 604
Cdd:pfam01576   75 EILHELESRLEEEEERSQQlqnekKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTeakIKKL-EEDILLLEDQNSKLSKE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    605 IEGLRHNLASIPSGPGD------GAQKLKEEYVQKLNTLETQvsvLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQ 678
Cdd:pfam01576  154 RKLLEERISEFTSNLAEeeekakSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    679 KVQLQQKIKQESEQFRAWKASREKEVMQlKKEGRRNEYEMHKLMALNQkQKLVLQRKTEEASQVTKR-LKELLDNRKASS 757
Cdd:pfam01576  231 IAELRAQLAKKEEELQAALARLEEETAQ-KNNALKKIRELEAQISELQ-EDLESERAARNKAEKQRRdLGEELEALKTEL 308
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327992    758 RETLSGANgpGTQALMQAIEHEIEVTVRV--HEVRSEYERQTEERARMAKEVARLREENELLKNAKISV 824
Cdd:pfam01576  309 EDTLDTTA--AQQELRSKREQEVTELKKAleEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANL 375
PTZ00121 PTZ00121
MAEBL; Provisional
536-970 6.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   536 DELEFQEKEIEHCSLQEKLDMELKELDKRLEEKEAEMKRfssgGTSVLKQHYEKKVYDlEQEKRALQREIEGLRHNLASi 615
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----KADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEE- 1313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   616 pSGPGDGAQKLKEEYVQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIKLQDEIHRIKSQKVQLQQKIKQESEQFRA 695
Cdd:PTZ00121 1314 -AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   696 WKASREKEVMQLKKEGRRNEYEMHKLMALNQKQKLVLQRKTEEASQVTKRLKELLDNRKASsrETLSGANGPGTQALMQA 775
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAK 1470
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   776 IEHEIEVTVRVHEVRSEYERQTEERARMAKEVARLREEN---ELLKNAKISVHGDTMSPGARNSRIFALENMLATSSSTL 852
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   853 VSMASQLSEAEERERVFGGR----GRWNQVRTLGDAKSI---------MNYLFNLASTARCLARDKEADCREKDVLIRDL 919
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKkaeeDKNMALRKAEEAKKAeearieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 22327992   920 KEKIVKFSSYVRYMEIQKADlvhQVKAQTSAMKKLSADENLKNEHSMKKQE 970
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
mukB PRK04863
chromosome partition protein MukB;
551-812 6.64e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   551 QEKLDM---ELKELDKRLEEKEaemkrfssggtSVLKQHYEKkVYDLEQEKRALQREIEGLRHNLASIPSGPgDGAQKLK 627
Cdd:PRK04863  347 QEKIERyqaDLEELEERLEEQN-----------EVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQAL-DVQQTRA 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   628 EEYVQKLNTLETQVSV-------LKKKQDAQAQLMRQKQKSDDAAIKLQ------DEIHRIKSQKVQLQQKIKQESEQFR 694
Cdd:PRK04863  414 IQYQQAVQALERAKQLcglpdltADNAEDWLEEFQAKEQEATEELLSLEqklsvaQAAHSQFEQAYQLVRKIAGEVSRSE 493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992   695 AWKASREKEvmqlkkegRRNEYEMHKLMALNQ-KQKLV-LQRKTEEASQVTKRLKELldNRKASSRETLSGANGPGTQAL 772
Cdd:PRK04863  494 AWDVARELL--------RRLREQRHLAEQLQQlRMRLSeLEQRLRQQQRAERLLAEF--CKRLGKNLDDEDELEQLQEEL 563
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 22327992   773 MQAIEHEIEVTVRVHEVRSEYERQTEE----RARMAKE----------VARLRE 812
Cdd:PRK04863  564 EARLESLSESVSEARERRMALRQQLEQlqarIQRLAARapawlaaqdaLARLRE 617
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
620-811 8.74e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  620 GDGAQKLKEEYvQKLNTLETQVSVLKKKQDAQAQLMRQKQKSDDAAIK----------------------LQDEIHRIKS 677
Cdd:COG4913  224 FEAADALVEHF-DDLERAHEALEDAREQIELLEPIRELAERYAAARERlaeleylraalrlwfaqrrlelLEAELEELRA 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992  678 QKVQLQQKIKQESEQFRAWKASREkevmQLKKEGRRNEYEmhKLMALNQKQKlVLQRKTEEASQVTKRLKELLDNRKAS- 756
Cdd:COG4913  303 ELARLEAELERLEARLDALREELD----ELEAQIRGNGGD--RLEQLEREIE-RLERELEERERRRARLEALLAALGLPl 375
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327992  757 --SRETLSGANGPGTQALMQAIEHEIEVTVRVHEVRSEYERQTEERARMAKEVARLR 811
Cdd:COG4913  376 paSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
537-759 9.87e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 40.27  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    537 ELEFQEKEIEhcslqeKLDMELKELDKRLEE---KEAEMKRFSSGGTSVLKQHyEKKVYDLEQEKRALQREIEGLRHNLA 613
Cdd:pfam15964  482 QLEIKDQEIE------KLGLELSESKQRLEQaqqDAARAREECLKLTELLGES-EHQLHLTRLEKESIQQSFSNEAKAQA 554
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327992    614 SipsgpgdGAQKLKEEYVQKLNTLETQvsvlKKKQDAQAQLMRQKQKSDDAaiKLQDEIHRIKSQKVQLQQKIKQESEQF 693
Cdd:pfam15964  555 L-------QAQQREQELTQKMQQMEAQ----HDKTVNEQYSLLTSQNTFIA--KLKEECCTLAKKLEEITQKSRSEVEQL 621
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327992    694 rawkaSREKEVMQ--LKKEGRRNEyEM------HKLMALNQKQKLVLQRKTEEAS-----QVTKRLKELLDNRKASSRE 759
Cdd:pfam15964  622 -----SQEKEYLQdrLEKLQKRNE-ELeeqcvqHGRMHERMKQRLRQLDKHCQATaqqlvQLLSKQNQLFKERQNLTEE 694
 
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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