NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|113678899|ref|NP_001038441|]
View 

kinesin-like protein KIF14 [Danio rerio]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
39-389 0e+00

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: 562.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHPD---------TKQTHKFTFDFSFCSINEADASFSSQQLIYEKLAR 109
Cdd:cd01365     3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKqadknnkatREVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  110 PLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKEMSCHLEMSYFEVYNEKIHDLLVAK 189
Cdd:cd01365    83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLNPK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  190 DEQNqkKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFveEE 269
Cdd:cd01365   163 PKKN--KGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDA--ET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  270 EHDHCITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQ---SRKKVFTPYRESVLTWLLKES 346
Cdd:cd01365   239 NLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgksKKKSSFIPYRDSVLTWLLKEN 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 113678899  347 LGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVN 389
Cdd:cd01365   319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
475-582 3.28e-72

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 235.62  E-value: 3.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  475 FKVDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNG 554
Cdd:cd22707     1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 113678899  555 HLVSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
Kinesin_assoc super family cl24686
Kinesin-associated;
386-504 1.29e-13

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 70.26  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   386 AKVNEDTNAKLIRDLKAEVEKLRAAQMSsQGVE--------PEKMRLFQQEIAALK------------------------ 433
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYA-QGLGdiidtiahPTKKRANTPAANASAataamagaspspslsalssraasv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   434 -----------------NKLCQQEHEMAEAHRTWKEKLEEAERRKREEAKELQRAGVTFKVDN---------RLPNLVNL 487
Cdd:pfam16183   80 sslherimftpgseeaiERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGgtlgvfspkKTPHLVNL 159
                          170
                   ....*....|....*..
gi 113678899   488 NEDPQLSEMLLYMIKEG 504
Cdd:pfam16183  160 NEDPLMSECLLYYIKDG 176
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
606-752 2.00e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  606 AKNELLSAQRAQLEAEIQEARLKAKE-----EMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHK 680
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899  681 QRAASQIEQLQSVKTLLEKEVsshkRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1196   333 EELEEELEELEEELEEAEEEL----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
39-389 0e+00

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: 562.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHPD---------TKQTHKFTFDFSFCSINEADASFSSQQLIYEKLAR 109
Cdd:cd01365     3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKqadknnkatREVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  110 PLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKEMSCHLEMSYFEVYNEKIHDLLVAK 189
Cdd:cd01365    83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLNPK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  190 DEQNqkKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFveEE 269
Cdd:cd01365   163 PKKN--KGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDA--ET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  270 EHDHCITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQ---SRKKVFTPYRESVLTWLLKES 346
Cdd:cd01365   239 NLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgksKKKSSFIPYRDSVLTWLLKEN 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 113678899  347 LGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVN 389
Cdd:cd01365   319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
38-389 8.33e-145

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: 442.40  E-value: 8.33e-145
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899     38 AVTVAVRVRPFSSREKIEKACQVIFMENQD----TLVQHPDTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARPLLE 113
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVgktlTVRSPKNRQGEKKFTFDKVF-------DATASQEDVFEETAAPLVD 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    114 RAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSEtKEMSCHLEMSYFEVYNEKIHDLLvakdeqN 193
Cdd:smart00129   74 SVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE-EGWQFSVKVSYLEIYNEKIRDLL------N 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    194 QKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEfveeEEHDH 273
Cdd:smart00129  147 PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN----SSSGS 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    274 CITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQSRkkvFTPYRESVLTWLLKESLGGNSKT 353
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR---HIPYRDSKLTRLLQDSLGGNSKT 299
                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 113678899    354 AMIATLSPAASNMEESLSTLRYAQQARMIINIAKVN 389
Cdd:smart00129  300 LMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
44-382 1.69e-138

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 425.06  E-value: 1.69e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    44 RVRPFSSREKIEKACQVIFMENQDTLVQH----PDTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARPLLERAFEGF 119
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshlTNKNRTKTFTFDKVF-------DPEATQEDVYEETAKPLVESVLEGY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   120 NTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKeMSCHLEMSYFEVYNEKIHDLLVAKdeqNQKKMPL 199
Cdd:pfam00225   74 NVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKER-SEFSVKVSYLEIYNEKIRDLLSPS---NKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   200 RVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFVEEEEHdhcITSRI 279
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV---KTGKL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   280 NLVDLAGSERCTSAQTS-GDRLREGASINKSLLTLGKVISSLSEQsqsrKKVFTPYRESVLTWLLKESLGGNSKTAMIAT 358
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALADK----KSKHIPYRDSKLTRLLQDSLGGNSKTLMIAN 302
                          330       340
                   ....*....|....*....|....
gi 113678899   359 LSPAASNMEESLSTLRYAQQARMI 382
Cdd:pfam00225  303 ISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
80-393 3.32e-76

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 263.91  E-value: 3.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   80 KFTFDFSFcsineadASFSSQQLIYEKLARPLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRL- 158
Cdd:COG5059    57 TYAFDKVF-------GPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLe 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  159 ARSETKEMSchLEMSYFEVYNEKIHDLLVAKDEQnqkkmpLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRAT 238
Cdd:COG5059   130 DLSMTKDFA--VSISYLEIYNEKIYDLLSPNEES------LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  239 AATGMNDKSSRSHSVFTLVMTQTKTEFVEEEehdhciTSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVIS 318
Cdd:COG5059   202 ASTEINDESSRSHSIFQIELASKNKVSGTSE------TSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVIN 275
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113678899  319 SLSEQSQSRKKvftPYRESVLTWLLKESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVNEDTN 393
Cdd:COG5059   276 ALGDKKKSGHI---PYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSD 347
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
475-582 3.28e-72

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 235.62  E-value: 3.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  475 FKVDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNG 554
Cdd:cd22707     1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 113678899  555 HLVSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
PLN03188 PLN03188
kinesin-12 family protein; Provisional
23-409 6.72e-67

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 248.70  E-value: 6.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   23 KMSELQTQELKMENSAVTVAVRVRPFSSREKIEKACQVIfmeNQDTLVQHPDTkqthkFTFDfsfcSINEADasfSSQQL 102
Cdd:PLN03188   84 KLSAETAPENGVSDSGVKVIVRMKPLNKGEEGEMIVQKM---SNDSLTINGQT-----FTFD----SIADPE---STQED 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  103 IYEKLARPLLERAFEGFNTCLFAYGQTGSGKSYTMMG----------FGEETGVIPRFCEELFSRLARSETKEMSCHLEM 172
Cdd:PLN03188  149 IFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEEQIKHADRQLKY 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  173 ----SYFEVYNEKIHDLLvakdEQNQKKmpLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSS 248
Cdd:PLN03188  229 qcrcSFLEIYNEQITDLL----DPSQKN--LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESS 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  249 RSHSVFTLVmtqtktefVEEeehdHCI----------TSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVIS 318
Cdd:PLN03188  303 RSHSVFTCV--------VES----RCKsvadglssfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLIN 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  319 SLSEQSQSRKKVFTPYRESVLTWLLKESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVNE----DTN- 393
Cdd:PLN03188  371 ILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNf 450
                         410
                  ....*....|....*..
gi 113678899  394 -AKLIRDLKAEVEKLRA 409
Cdd:PLN03188  451 lREVIRQLRDELQRVKA 467
Kinesin_assoc pfam16183
Kinesin-associated;
386-504 1.29e-13

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 70.26  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   386 AKVNEDTNAKLIRDLKAEVEKLRAAQMSsQGVE--------PEKMRLFQQEIAALK------------------------ 433
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYA-QGLGdiidtiahPTKKRANTPAANASAataamagaspspslsalssraasv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   434 -----------------NKLCQQEHEMAEAHRTWKEKLEEAERRKREEAKELQRAGVTFKVDN---------RLPNLVNL 487
Cdd:pfam16183   80 sslherimftpgseeaiERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGgtlgvfspkKTPHLVNL 159
                          170
                   ....*....|....*..
gi 113678899   488 NEDPQLSEMLLYMIKEG 504
Cdd:pfam16183  160 NEDPLMSECLLYYIKDG 176
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
606-752 2.00e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  606 AKNELLSAQRAQLEAEIQEARLKAKE-----EMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHK 680
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899  681 QRAASQIEQLQSVKTLLEKEVsshkRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1196   333 EELEEELEELEEELEEAEEEL----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
604-762 1.24e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 56.29  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   604 EFAKNELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKElsEQKSLYEIKIRALERELKEESERK------REQE 677
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEERAREMERVRLEEQERQqqverlRQQE 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   678 LHKQRAASQIEQLQSVKTLLEKEvssHKRRLQMEAQATRQAMADHDvRHAKIV---------AALEAEKRKIAED--LAQ 746
Cdd:pfam17380  470 EERKRKKLELEKEKRDRKRAEEQ---RRKILEKELEERKQAMIEEE-RKRKLLekemeerqkAIYEEERRREAEEerRKQ 545
                          170
                   ....*....|....*.
gi 113678899   747 IEMKRALKVTQTPKMA 762
Cdd:pfam17380  546 QEMEERRRIQEQMRKA 561
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
501-579 3.40e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  501 IKEGQTKVGKlksESAHDIQLSGALIADQHCVISSVKGTVSIKPMpNAK--TFVNGHLVSECTVLHHGDRVILgGDHYFR 578
Cdd:COG1716    18 LDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRL-GKTELR 92

                  .
gi 113678899  579 F 579
Cdd:COG1716    93 F 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
601-814 7.73e-07

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: 53.91  E-value: 7.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   601 KDFEFAKNELLSAQRAQLEAEIQ----EARLKAKEEMMQGIQVAK-EMAQKELSEQKSLYE--IKIRALERELKEESERK 673
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEEleelTAELQELEEKLEELRLEVsELEEEIEELQKELYAlaNEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   674 REQELHKQRAASQIEQLQSVKTLLEKEVSSHKRRLQmEAQATRQAM-ADHDVRHAKIVAA----------LEAEKRKIAE 742
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLeAELEELEAELEELesrleeleeqLETLRSKVAQ 390
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899   743 DLAQIEMKRALKVTQTPKMAIPQWDAMKLSLMIEEANKISGKLRKHTVFSRHEAADKEVEGGDAQLQVQVQN 814
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
506-571 2.16e-06

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 46.42  E-value: 2.16e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113678899   506 TKVGklkSESAHDIQLSGALIADQHCVISSVKG-TVSIKPM-PNAKTFVNGHLVS-ECTVLHHGDRVIL 571
Cdd:pfam00498    1 VTIG---RSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVIRL 66
PTZ00121 PTZ00121
MAEBL; Provisional
608-787 3.06e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  608 NELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQI 687
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  688 EQLQSVKTLLEKEVSSHKRRlqmeAQATRQAMADHDVRHAKIVAALEAEKRKiAEDLAQIEMKRALKVTQTPKMAIPQWD 767
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKK-AEEAKKAEEDEKKAAEALKKEAEEAKK 1703
                         170       180
                  ....*....|....*....|
gi 113678899  768 AMKLSLMIEEANKISGKLRK 787
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKK 1723
Prefoldin_beta_GimC cd23162
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ...
609-681 2.71e-05

Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467478 [Multi-domain]  Cd Length: 102  Bit Score: 44.39  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQEARlKAKEEM-----------MQG---IQVAKEMAQKELSEQKSLYEIKIRALERelKEESERKR 674
Cdd:cd23162    14 QAVLLQKQQLEAELREIE-RALEELeklpddaevykSVGtilVKVDKEEVIKELKERKETLELRLKTLEK--QEERLRKQ 90

                  ....*..
gi 113678899  675 EQELHKQ 681
Cdd:cd23162    91 LEELQKK 97
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
506-557 3.37e-04

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 39.47  E-value: 3.37e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 113678899    506 TKVGKlkSESAHDIQLSGALIADQHCVISSVKGT-VSIKPMP-NAKTFVNGHLV 557
Cdd:smart00240    1 VTIGR--SSEDCDIQLDGPSISRRHAVIVYDGGGrFYLIDLGsTNGTFVNGKRI 52
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
39-389 0e+00

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: 562.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHPD---------TKQTHKFTFDFSFCSINEADASFSSQQLIYEKLAR 109
Cdd:cd01365     3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKqadknnkatREVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  110 PLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKEMSCHLEMSYFEVYNEKIHDLLVAK 189
Cdd:cd01365    83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLNPK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  190 DEQNqkKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFveEE 269
Cdd:cd01365   163 PKKN--KGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDA--ET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  270 EHDHCITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQ---SRKKVFTPYRESVLTWLLKES 346
Cdd:cd01365   239 NLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgksKKKSSFIPYRDSVLTWLLKEN 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 113678899  347 LGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVN 389
Cdd:cd01365   319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
38-389 8.33e-145

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: 442.40  E-value: 8.33e-145
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899     38 AVTVAVRVRPFSSREKIEKACQVIFMENQD----TLVQHPDTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARPLLE 113
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVgktlTVRSPKNRQGEKKFTFDKVF-------DATASQEDVFEETAAPLVD 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    114 RAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSEtKEMSCHLEMSYFEVYNEKIHDLLvakdeqN 193
Cdd:smart00129   74 SVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE-EGWQFSVKVSYLEIYNEKIRDLL------N 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    194 QKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEfveeEEHDH 273
Cdd:smart00129  147 PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN----SSSGS 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    274 CITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQSRkkvFTPYRESVLTWLLKESLGGNSKT 353
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR---HIPYRDSKLTRLLQDSLGGNSKT 299
                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 113678899    354 AMIATLSPAASNMEESLSTLRYAQQARMIINIAKVN 389
Cdd:smart00129  300 LMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
44-382 1.69e-138

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 425.06  E-value: 1.69e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    44 RVRPFSSREKIEKACQVIFMENQDTLVQH----PDTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARPLLERAFEGF 119
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshlTNKNRTKTFTFDKVF-------DPEATQEDVYEETAKPLVESVLEGY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   120 NTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKeMSCHLEMSYFEVYNEKIHDLLVAKdeqNQKKMPL 199
Cdd:pfam00225   74 NVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKER-SEFSVKVSYLEIYNEKIRDLLSPS---NKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   200 RVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFVEEEEHdhcITSRI 279
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV---KTGKL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   280 NLVDLAGSERCTSAQTS-GDRLREGASINKSLLTLGKVISSLSEQsqsrKKVFTPYRESVLTWLLKESLGGNSKTAMIAT 358
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALADK----KSKHIPYRDSKLTRLLQDSLGGNSKTLMIAN 302
                          330       340
                   ....*....|....*....|....
gi 113678899   359 LSPAASNMEESLSTLRYAQQARMI 382
Cdd:pfam00225  303 ISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
38-380 1.21e-118

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: 372.36  E-value: 1.21e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   38 AVTVAVRVRPFSSREKiEKACQVIFMENQDTLVQHP---DTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARPLLER 114
Cdd:cd00106     1 NVRVAVRVRPLNGREA-RSAKSVISVDGGKSVVLDPpknRVAPPKTFAFDAVF-------DSTSTQEEVYEGTAKPLVDS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  115 AFEGFNTCLFAYGQTGSGKSYTMMG-FGEETGVIPRFCEELFSRLARSETKEMSCHLEMSYFEVYNEKIHDLLvakdeQN 193
Cdd:cd00106    73 ALEGYNGTIFAYGQTGSGKTYTMLGpDPEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL-----SP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  194 QKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEfveeEEHDH 273
Cdd:cd00106   148 VPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNRE----KSGES 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  274 CITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQsqsrKKVFTPYRESVLTWLLKESLGGNSKT 353
Cdd:cd00106   224 VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADG----QNKHIPYRDSKLTRLLQDSLGGNSKT 299
                         330       340
                  ....*....|....*....|....*..
gi 113678899  354 AMIATLSPAASNMEESLSTLRYAQQAR 380
Cdd:cd00106   300 IMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
37-382 1.35e-102

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: 329.68  E-value: 1.35e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   37 SAVTVAVRVRPFSSREKIEKA-CQVIFMENQDTLVQHPDtkqtHKFTFDFSFcsineadASFSSQQLIYEKLARPLLERA 115
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCrICVSFVPGEPQVTVGTD----KSFTFDYVF-------DPSTEQEEVYNTCVAPLVDGL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  116 FEGFNTCLFAYGQTGSGKSYTM-MGFG-----EETGVIPRFCEELFSRLA-RSETKEMSchLEMSYFEVYNEKIHDLLva 188
Cdd:cd01372    70 FEGYNATVLAYGQTGSGKTYTMgTAYTaeedeEQVGIIPRAIQHIFKKIEkKKDTFEFQ--LKVSFLEIYNEEIRDLL-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  189 kDEQNQKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTK-----T 263
Cdd:cd01372   146 -DPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKkngpiA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  264 EFVEEEEHDHcITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSeqSQSRKKVFTPYRESVLTWLL 343
Cdd:cd01372   225 PMSADDKNST-FTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALG--DESKKGAHVPYRDSKLTRLL 301
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 113678899  344 KESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMI 382
Cdd:cd01372   302 QDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
38-382 8.07e-100

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: 321.20  E-value: 8.07e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   38 AVTVAVRVRPFSSREKIEKAcQVIFMENQDTLVQHPDTKQthKFTFDFSFcsineadASFSSQQLIYEKLARPLLERAFE 117
Cdd:cd01374     1 KITVTVRVRPLNSREIGINE-QVAWEIDNDTIYLVEPPST--SFTFDHVF-------GGDSTNREVYELIAKPVVKSALE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  118 GFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKEMSchLEMSYFEVYNEKIHDLLvakDEQNQkkm 197
Cdd:cd01374    71 GYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFL--LRVSYLEIYNEKINDLL---SPTSQ--- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  198 PLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKtefVEEEEHDHCITS 277
Cdd:cd01374   143 NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSE---RGELEEGTVRVS 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  278 RINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEqsqSRKKVFTPYRESVLTWLLKESLGGNSKTAMIA 357
Cdd:cd01374   220 TLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIIC 296
                         330       340
                  ....*....|....*....|....*
gi 113678899  358 TLSPAASNMEESLSTLRYAQQARMI 382
Cdd:cd01374   297 TITPAESHVEETLNTLKFASRAKKI 321
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
38-382 7.77e-99

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: 319.02  E-value: 7.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   38 AVTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHPDTKQTHK-----FTFDFSFcsineaDASfSSQQLIYEKLARPLL 112
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANeppktFTFDAVF------DPN-SKQLDVYDETARPLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  113 ERAFEGFNTCLFAYGQTGSGKSYTMMG---FGEETGVIPRFCEELFSRLARSETKEMSChLEMSYFEVYNEKIHDLLvAK 189
Cdd:cd01371    75 DSVLEGYNGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIARSQNNQQFL-VRVSYLEIYNEEIRDLL-GK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  190 DEQnqKKMPLRvrEHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLvmTQTKTEFVEEE 269
Cdd:cd01371   153 DQT--KRLELK--ERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTI--TIECSEKGEDG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  270 EhDHCITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQsqsrKKVFTPYRESVLTWLLKESLGG 349
Cdd:cd01371   227 E-NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG----KSTHIPYRDSKLTRLLQDSLGG 301
                         330       340       350
                  ....*....|....*....|....*....|...
gi 113678899  350 NSKTAMIATLSPAASNMEESLSTLRYAQQARMI 382
Cdd:cd01371   302 NSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
44-384 1.53e-93

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: 304.13  E-value: 1.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   44 RVRPFSSREKIE-KACQVIFMENQDTL-VQHPDTKQtHKFTFDFSFcsineadASFSSQQLIYEKLArPLLERAFEGFNT 121
Cdd:cd01366     9 RVRPLLPSEENEdTSHITFPDEDGQTIeLTSIGAKQ-KEFSFDKVF-------DPEASQEDVFEEVS-PLVQSALDGYNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  122 CLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLARSETKEMSCHLEMSYFEVYNEKIHDLLvAKDEQNQKKMPLRv 201
Cdd:cd01366    80 CIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLL-APGNAPQKKLEIR- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  202 REHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVM----TQTKTefveeeehdhCITS 277
Cdd:cd01366   158 HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnLQTGE----------ISVG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  278 RINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLseqsqSRKKVFTPYRESVLTWLLKESLGGNSKTAMIA 357
Cdd:cd01366   228 KLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL-----RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFV 302
                         330       340
                  ....*....|....*....|....*..
gi 113678899  358 TLSPAASNMEESLSTLRYAQQARMIIN 384
Cdd:cd01366   303 NISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
38-392 4.05e-89

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: 292.88  E-value: 4.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   38 AVTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHpdTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARPLLERAFE 117
Cdd:cd01373     2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLH--SKPPKTFTFDHVA-------DSNTNQESVFQSVGKPIVESCLS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  118 GFNTCLFAYGQTGSGKSYTMMG--------FGEETGVIPRFCEELFSRLARSETK-----EMSChlEMSYFEVYNEKIHD 184
Cdd:cd01373    73 GYNGTIFAYGQTGSGKTYTMWGpsesdnesPHGLRGVIPRIFEYLFSLIQREKEKagegkSFLC--KCSFLEIYNEQIYD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  185 LLvakdeqNQKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVmtqtkte 264
Cdd:cd01373   151 LL------DPASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCT------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  265 fVEEEEHDHCI----TSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQSRKKvFTPYRESVLT 340
Cdd:cd01373   218 -IESWEKKACFvnirTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQR-HVCYRDSKLT 295
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 113678899  341 WLLKESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVNEDT 392
Cdd:cd01373   296 FLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNEDT 347
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
39-382 1.71e-87

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: 288.09  E-value: 1.71e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHPDTKQTHKFTFDFSFCSINEA---------DASF---SSQQLIYEK 106
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRKRrnkelkyvfDRVFdetSTQEEVYEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  107 LARPLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLaRSETKEMSCHLEMSYFEVYNEKIHDLL 186
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI-ESLKDEKEFEVSMSYLEIYNETIRDLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  187 VAKDEqnqkkmPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTL-VMTQTKTEF 265
Cdd:cd01370   161 NPSSG------PLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQItVRQQDKTAS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  266 VEEEEHdhciTSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSqsRKKVFTPYRESVLTWLLKE 345
Cdd:cd01370   235 INQQVR----QGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPG--KKNKHIPYRDSKLTRLLKD 308
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 113678899  346 SLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMI 382
Cdd:cd01370   309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
36-391 6.95e-86

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: 283.83  E-value: 6.95e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   36 NSAVTVAVRVRPFSSREKIEKACQVIFMEN--QDTLVQH---PDTKQTHKFTFDFSFcsineadASFSSQQLIYEKLARP 110
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPvrKEVSVRTgglADKSSTKTYTFDMVF-------GPEAKQIDVYRSVVCP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  111 LLERAFEGFNTCLFAYGQTGSGKSYTMMG-----------FGEETGVIPRFCEELFSRLARSETKEMschLEMSYFEVYN 179
Cdd:cd01364    74 ILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTEYS---VKVSYLEIYN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  180 EKIHDLLvakDEQNQKKMPLRVREHP--VYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTlV 257
Cdd:cd01364   151 EELFDLL---SPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS-I 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  258 MTQTKTEFVEEEEHDHCitSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEqsqsrKKVFTPYRES 337
Cdd:cd01364   227 TIHIKETTIDGEELVKI--GKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-----RAPHVPYRES 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 113678899  338 VLTWLLKESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVNED 391
Cdd:cd01364   300 KLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
37-382 4.42e-84

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: 277.67  E-value: 4.42e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   37 SAVTVAVRVRPFSSREkIEKACQVIFMENQDTLVQHPDTKQTHKFTFDFSFcsineaDASfSSQQLIYEKLARPLLERAF 116
Cdd:cd01369     2 CNIKVVCRFRPLNELE-VLQGSKSIVKFDPEDTVVIATSETGKTFSFDRVF------DPN-TTQEDVYNFAAKPIVDDVL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  117 EGFNTCLFAYGQTGSGKSYTMMGFGEET---GVIPRFCEELFSRLaRSETKEMSCHLEMSYFEVYNEKIHDLLVAKdeqn 193
Cdd:cd01369    74 NGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETI-YSMDENLEFHVKVSYFEIYMEKIRDLLDVS---- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  194 qkKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEfveeeeHDH 273
Cdd:cd01369   149 --KTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE------TEK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  274 CITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEqsqsRKKVFTPYRESVLTWLLKESLGGNSKT 353
Cdd:cd01369   221 KKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD----GKKTHIPYRDSKLTRILQDSLGGNSRT 296
                         330       340
                  ....*....|....*....|....*....
gi 113678899  354 AMIATLSPAASNMEESLSTLRYAQQARMI 382
Cdd:cd01369   297 TLIICCSPSSYNESETLSTLRFGQRAKTI 325
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
80-393 3.32e-76

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 263.91  E-value: 3.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   80 KFTFDFSFcsineadASFSSQQLIYEKLARPLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRL- 158
Cdd:COG5059    57 TYAFDKVF-------GPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLe 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  159 ARSETKEMSchLEMSYFEVYNEKIHDLLVAKDEQnqkkmpLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRAT 238
Cdd:COG5059   130 DLSMTKDFA--VSISYLEIYNEKIYDLLSPNEES------LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  239 AATGMNDKSSRSHSVFTLVMTQTKTEFVEEEehdhciTSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVIS 318
Cdd:COG5059   202 ASTEINDESSRSHSIFQIELASKNKVSGTSE------TSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVIN 275
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113678899  319 SLSEQSQSRKKvftPYRESVLTWLLKESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVNEDTN 393
Cdd:COG5059   276 ALGDKKKSGHI---PYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSD 347
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
39-376 9.54e-73

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: 246.05  E-value: 9.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIEKACQVIFMENQDTLVQH-PDTK-------QTHKFTFDFSFcsineaDASFSSQQLiYEKLARP 110
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHePKLKvdltkyiENHTFRFDYVF------DESSSNETV-YRSTVKP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  111 LLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCE----ELFSRLARSeTKEMSCHLEMSYFEVYNEKIHDLL 186
Cdd:cd01367    75 LVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYAlaarDVFRLLNKL-PYKDNLGVTVSFFEIYGGKVFDLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  187 vakdeqnQKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEfv 266
Cdd:cd01367   154 -------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTN-- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  267 eeeehdhCITSRINLVDLAGSERC--TSAQTSgDRLREGASINKSLLTLGKVISSLseqsqSRKKVFTPYRESVLTWLLK 344
Cdd:cd01367   225 -------KLHGKLSFVDLAGSERGadTSSADR-QTRMEGAEINKSLLALKECIRAL-----GQNKAHIPFRGSKLTQVLK 291
                         330       340       350
                  ....*....|....*....|....*....|...
gi 113678899  345 ESL-GGNSKTAMIATLSPAASNMEESLSTLRYA 376
Cdd:cd01367   292 DSFiGENSKTCMIATISPGASSCEHTLNTLRYA 324
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
475-582 3.28e-72

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 235.62  E-value: 3.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  475 FKVDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNG 554
Cdd:cd22707     1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 113678899  555 HLVSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
39-380 5.56e-72

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: 244.23  E-value: 5.56e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIEKACQVIFMENQDTLVQHPDT------------KQTHKFTFDFSFcsineadASFSSQQLIYEK 106
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKgsaanksernggQKETKFSFSKVF-------GPNTTQKEFFQG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  107 LARPLLERAFEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELFSRLarsetKEMSchLEMSYFEVYNEKIHDLL 186
Cdd:cd01368    76 TALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSI-----GGYS--VFVSYIEIYNEYIYDLL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  187 -VAKDEQNQKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFT--LVMTQTKT 263
Cdd:cd01368   149 ePSPSSPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTikLVQAPGDS 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  264 EFVEEEEHDHCITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQSQSRKKVFTPYRESVLTWLL 343
Cdd:cd01368   229 DGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLF 308
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 113678899  344 KESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQAR 380
Cdd:cd01368   309 QNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
23-409 6.72e-67

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 248.70  E-value: 6.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   23 KMSELQTQELKMENSAVTVAVRVRPFSSREKIEKACQVIfmeNQDTLVQHPDTkqthkFTFDfsfcSINEADasfSSQQL 102
Cdd:PLN03188   84 KLSAETAPENGVSDSGVKVIVRMKPLNKGEEGEMIVQKM---SNDSLTINGQT-----FTFD----SIADPE---STQED 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  103 IYEKLARPLLERAFEGFNTCLFAYGQTGSGKSYTMMG----------FGEETGVIPRFCEELFSRLARSETKEMSCHLEM 172
Cdd:PLN03188  149 IFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEEQIKHADRQLKY 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  173 ----SYFEVYNEKIHDLLvakdEQNQKKmpLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSS 248
Cdd:PLN03188  229 qcrcSFLEIYNEQITDLL----DPSQKN--LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESS 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  249 RSHSVFTLVmtqtktefVEEeehdHCI----------TSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVIS 318
Cdd:PLN03188  303 RSHSVFTCV--------VES----RCKsvadglssfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLIN 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  319 SLSEQSQSRKKVFTPYRESVLTWLLKESLGGNSKTAMIATLSPAASNMEESLSTLRYAQQARMIINIAKVNE----DTN- 393
Cdd:PLN03188  371 ILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNf 450
                         410
                  ....*....|....*..
gi 113678899  394 -AKLIRDLKAEVEKLRA 409
Cdd:PLN03188  451 lREVIRQLRDELQRVKA 467
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
38-380 3.27e-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: 227.46  E-value: 3.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   38 AVTVAVRVRPFSSRE----KIEKACQVIFMENQDTLVQHPDTKQTHKFTFDFsfcsineaDASF--SSQQLIYEKLARPL 111
Cdd:cd01375     1 KVQAFVRVRPTDDFAhemiKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKF--------DGVLhnASQELVYETVAKDV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  112 LERAFEGFNTCLFAYGQTGSGKSYTMMGFGE---ETGVIPRFCEELFSRLARSETKEMSCHLemSYFEVYNEKIHDLLVA 188
Cdd:cd01375    73 VSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFRMIEERPTKAYTVHV--SYLEIYNEQLYDLLST 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  189 KDEQNQKKMPLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFVEE 268
Cdd:cd01375   151 LPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  269 EehdhCITSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSEQsqsrKKVFTPYRESVLTWLLKESLG 348
Cdd:cd01375   231 K----YITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK----DRTHVPFRQSKLTHVLRDSLG 302
                         330       340       350
                  ....*....|....*....|....*....|..
gi 113678899  349 GNSKTAMIATLSPAASNMEESLSTLRYAQQAR 380
Cdd:cd01375   303 GNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
39-380 1.44e-64

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


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 221.99  E-value: 1.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   39 VTVAVRVRPFSSREKIE--KACqVIFMENQDTLVQHPDTKQ-THKFTFDFSFcsineadASFSSQQLIYEKLARPLLERA 115
Cdd:cd01376     2 VRVAVRVRPFVDGTAGAsdPSC-VSGIDSCSVELADPRNHGeTLKYQFDAFY-------GEESTQEDIYAREVQPIVPHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  116 FEGFNTCLFAYGQTGSGKSYTMMGFGEETGVIPRFCEELfsrLARSETKEMSCHLEMSYFEVYNEKIHDLLVAKDEQnqk 195
Cdd:cd01376    74 LEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDL---LQMTRKEAWALSFTMSYLEIYQEKILDLLEPASKE--- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  196 kmpLRVREHPVYGPYVADLSTNVVSSYSDIKTWLELGNKQRATAATGMNDKSSRSHSVftLVMTQTKTEFVEEEEHdhcI 275
Cdd:cd01376   148 ---LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAV--LLIKVDQRERLAPFRQ---R 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  276 TSRINLVDLAGSERCTSAQTSGDRLREGASINKSLLTLGKVISSLSeQSQSRkkvfTPYRESVLTWLLKESLGGNSKTAM 355
Cdd:cd01376   220 TGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALN-KNLPR----IPYRDSKLTRLLQDSLGGGSRCIM 294
                         330       340
                  ....*....|....*....|....*
gi 113678899  356 IATLSPAASNMEESLSTLRYAQQAR 380
Cdd:cd01376   295 VANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
481-581 4.67e-43

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 152.00  E-value: 4.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  481 LPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNGHLVSEC 560
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
                          90       100
                  ....*....|....*....|.
gi 113678899  561 TVLHHGDRVILGGDHYFRFNH 581
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
482-582 2.43e-37

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 135.81  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  482 PNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKP-MPNAKTFVNGHLVSEC 560
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPvSPGAKVIVNGVPVTGE 80
                          90       100
                  ....*....|....*....|..
gi 113678899  561 TVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22709    81 TELHHLDRVILGSNHLYVFVGP 102
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
484-582 2.11e-32

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 121.63  E-value: 2.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  484 LVNLNEDPQLSEMLLYMIKEgQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNGHLVSECTVL 563
Cdd:cd22706     4 LVNLNADPSLNELLVYYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQL 82
                          90
                  ....*....|....*....
gi 113678899  564 HHGDRVILGGDHYFRFNHP 582
Cdd:cd22706    83 RHGDRILWGNNHFFRLNCP 101
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
482-586 1.76e-31

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 119.65  E-value: 1.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  482 PNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGT-----VSIKPMPNAKTFVNGHL 556
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 113678899  557 VSECTVLHHGDRVILGGDHYFRFNHPAEVQ 586
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQAR 111
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
482-584 3.40e-31

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 118.60  E-value: 3.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  482 PNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGT-----VSIKPMPNAKTFVNGHL 556
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNngeviVTLEPCERSETYVNGKR 82
                          90       100
                  ....*....|....*....|....*...
gi 113678899  557 VSECTVLHHGDRVILGGDHYFRFNHPAE 584
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
477-582 1.20e-28

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 111.21  E-value: 1.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  477 VDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNGHL 556
Cdd:cd22708     4 LDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVNGQV 83
                          90       100
                  ....*....|....*....|....*.
gi 113678899  557 VSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22708    84 ITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
482-581 2.16e-28

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 110.35  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  482 PNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSesahDIQLSGALIADQHCVISSVKG-----TVSIKPMPNAKTFVNGHL 556
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77
                          90       100
                  ....*....|....*....|....*
gi 113678899  557 VSECTVLHHGDRVILGGDHYFRFNH 581
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
484-582 8.63e-28

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 108.46  E-value: 8.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  484 LVNLNEDPQLSEMLLYMIKEgQTKVGklkSESAHDIQLSGALIADQHCVIS-SVKGTVSIKPMPNAKTFVNGHLVSECTV 562
Cdd:cd22730     4 LVNLNADPALNELLVYYLKE-HTLIG---SADSQDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
                          90       100
                  ....*....|....*....|
gi 113678899  563 LHHGDRVILGGDHYFRFNHP 582
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
472-584 2.29e-25

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 102.16  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  472 GVTfkVDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTF 551
Cdd:cd22731     1 GVT--IDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 113678899  552 VNGHLVSECTVLHHGDRVILGGDHYFRFNHPAE 584
Cdd:cd22731    79 VNGREVTESCRLSQGAVIVLGKTHKFRFNHPAE 111
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
484-582 3.65e-23

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 95.34  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  484 LVNLNEDPQLSEMLLYMIKeGQTKVGklkSESAHDIQLSGALIADQHCVIS-SVKGTVSIKPMPNAKTFVNGHLVSECTV 562
Cdd:cd22729     4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
                          90       100
                  ....*....|....*....|
gi 113678899  563 LHHGDRVILGGDHYFRFNHP 582
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLP 99
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
41-319 2.15e-21

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


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 92.41  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   41 VAVRVRPFSSREKIEKACQVIFMEnqdtlVQHPDTKQTHKFtfdfsfcsineadasfssqqliyeKLARPLLERAFEGFN 120
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVFYR-----GFRRSESQPHVF------------------------AIADPAYQSMLDGYN 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  121 -TCLFAYGQTGSGKSYTMMgfgeetGVIPRFCEELFSRLARSETKEMSCHLEMSyfevynekihdllvakdeqnqkkmpl 199
Cdd:cd01363    52 nQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLTEIT-------------------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  200 rvrehpvygpyvadlstnvVSSYSDIKTWLELGNKQRaTAATGMNDKSSRSHSVFTLVmtqtktefveeeehdhcitsri 279
Cdd:cd01363   100 -------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEIL---------------------- 137
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 113678899  280 nlVDLAGSERctsaqtsgdrlregasINKSLLTLGKVISS 319
Cdd:cd01363   138 --LDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
477-584 2.31e-21

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 90.76  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  477 VDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKTFVNGHL 556
Cdd:cd22732     4 LDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVNGVQ 83
                          90       100
                  ....*....|....*....|....*...
gi 113678899  557 VSECTVLHHGDRVILGGDHYFRFNHPAE 584
Cdd:cd22732    84 ITEATQLNQGAVILLGRTNMFRFNHPKE 111
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
481-582 1.27e-19

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 85.45  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  481 LPNLVNLNEDPQLSEML-LYMIKEGQTKVGKLKSE--SAHDIQLSGALIADQHCVISSVKGTVSIKPM-PNAKTFVNGHL 556
Cdd:cd22711     1 LPYLLELSPDGSDRDKPrRHRLQPNVTEVGSERSPanSGQFIQLFGPDILPRHCVITHMEGVVTVTPAsQDAETYVNGQR 80
                          90       100
                  ....*....|....*....|....*.
gi 113678899  557 VSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22711    81 IYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
471-586 6.87e-16

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 75.06  E-value: 6.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  471 AGVTFKVDNRLPNLVNLNEDPQLSEMLLYMIKEGQTKVGklkSESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAKT 550
Cdd:cd22713     6 TGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIG---TAASDIISLQGPGVEPEHCYIENINGTVTLYPCGNLCS 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 113678899  551 fVNGHLVSECTVLHHGDRVILGGDHYFRFNHPAEVQ 586
Cdd:cd22713    83 -VDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
24-186 3.78e-15

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 73.79  E-value: 3.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    24 MSELQTQELKMENS------AVTVAVRVRPFSSREkiekaCQVIFMENQDTLVQhpDTKQTHKFTFDFSFcsineadASF 97
Cdd:pfam16796    1 LEEEETLRRKLENSiqelkgNIRVFARVRPELLSE-----AQIDYPDETSSDGK--IGSKNKSFSFDRVF-------PPE 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899    98 SSQQLIYEKLaRPLLERAFEGFNTCLFAYGQTGSgksytmmgfGEETGVIPRFCEELFsRLARSETKEMSCHLEMSYFEV 177
Cdd:pfam16796   67 SEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQTGS---------GSNDGMIPRAREQIF-RFISSLKKGWKYTIELQFVEI 135

                   ....*....
gi 113678899   178 YNEKIHDLL 186
Cdd:pfam16796  136 YNESSQDLL 144
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
484-579 8.83e-14

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 68.07  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  484 LVNLNEDPQLSEmllYMIKEGQTKVGklkSESAHDIQLSGALIADQHCVISSVKGTVSIKPM-PNAKTFVNGHLVSECTV 562
Cdd:cd00060     2 LIVLDGDGGGRE---FPLTKGVVTIG---RSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLgSTNGTFVNGKRITPPVP 75
                          90
                  ....*....|....*..
gi 113678899  563 LHHGDRVILgGDHYFRF 579
Cdd:cd00060    76 LQDGDVIRL-GDTTFRF 91
Kinesin_assoc pfam16183
Kinesin-associated;
386-504 1.29e-13

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 70.26  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   386 AKVNEDTNAKLIRDLKAEVEKLRAAQMSsQGVE--------PEKMRLFQQEIAALK------------------------ 433
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYA-QGLGdiidtiahPTKKRANTPAANASAataamagaspspslsalssraasv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   434 -----------------NKLCQQEHEMAEAHRTWKEKLEEAERRKREEAKELQRAGVTFKVDN---------RLPNLVNL 487
Cdd:pfam16183   80 sslherimftpgseeaiERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGgtlgvfspkKTPHLVNL 159
                          170
                   ....*....|....*..
gi 113678899   488 NEDPQLSEMLLYMIKEG 504
Cdd:pfam16183  160 NEDPLMSECLLYYIKDG 176
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
606-752 2.00e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  606 AKNELLSAQRAQLEAEIQEARLKAKE-----EMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHK 680
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899  681 QRAASQIEQLQSVKTLLEKEVsshkRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1196   333 EELEEELEELEEELEEAEEEL----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
501-579 1.34e-08

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 53.37  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  501 IKEGQTKVGklkSESAHDIQLSGALIADQHCVIS-SVKGTVSIKPMPNAK-TFVNGHLVSECTVLHHGDrVILGGDHYFR 578
Cdd:cd22673    18 LTKKSCTFG---RDLSCDIRIQLPGVSREHCRIEvDENGKAYLENLSTTNpTLVNGKAIEKSAELKDGD-VITIGGRSFR 93

                  .
gi 113678899  579 F 579
Cdd:cd22673    94 F 94
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
482-582 1.60e-08

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 54.23  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  482 PNLVNLNEDPQLSEMLLYMIKEGQTKVGK-LKSESAHDIQLSGALIADQHCVI---------------SSVKGTVSIKPM 545
Cdd:cd22712     4 PYLLTLRGFSPKQDLLVYPLLEQVILVGSrTEGARKVDISLRAPDILPQHCWIrrkpeplsddedsdkESADYRVVLSPL 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 113678899  546 PNAKTFVNGHLVSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22712    84 RGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
480-582 1.05e-07

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 51.72  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  480 RLPNLVNLNEDPQLSEMLLYMIKEGQTKVGKLKSESAHDIQLSGALIADQHCVISSVKGTVS-------IKPMPNAKTFV 552
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPKHrseeklvLEPIPGAHVSV 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 113678899  553 NGHLVSECTVLHHGDRVILGGDHYFRFNHP 582
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
604-762 1.24e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 56.29  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   604 EFAKNELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKElsEQKSLYEIKIRALERELKEESERK------REQE 677
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEERAREMERVRLEEQERQqqverlRQQE 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   678 LHKQRAASQIEQLQSVKTLLEKEvssHKRRLQMEAQATRQAMADHDvRHAKIV---------AALEAEKRKIAED--LAQ 746
Cdd:pfam17380  470 EERKRKKLELEKEKRDRKRAEEQ---RRKILEKELEERKQAMIEEE-RKRKLLekemeerqkAIYEEERRREAEEerRKQ 545
                          170
                   ....*....|....*.
gi 113678899   747 IEMKRALKVTQTPKMA 762
Cdd:pfam17380  546 QEMEERRRIQEQMRKA 561
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
611-754 1.28e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  611 LSAQRAQLEAEIQE------------ARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQEL 678
Cdd:COG1196   314 LEERLEELEEELAEleeeleeleeelEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113678899  679 HKQRAASQIEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRALK 754
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
501-579 3.40e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  501 IKEGQTKVGKlksESAHDIQLSGALIADQHCVISSVKGTVSIKPMpNAK--TFVNGHLVSECTVLHHGDRVILgGDHYFR 578
Cdd:COG1716    18 LDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRL-GKTELR 92

                  .
gi 113678899  579 F 579
Cdd:COG1716    93 F 93
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
609-748 4.40e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQ--EARLKAKEEMMQGIQVAKEMAQKELSE--------QKSLYEI--KIRALERELKEESERKREQ 676
Cdd:COG1196   235 RELEAELEELEAELEelEAELEELEAELAELEAELEELRLELEEleleleeaQAEEYELlaELARLEQDIARLEERRREL 314
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899  677 ELHKQRAASQIEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMAdhdvRHAKIVAALEAEKRKIAEDLAQIE 748
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
601-814 7.73e-07

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: 53.91  E-value: 7.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   601 KDFEFAKNELLSAQRAQLEAEIQ----EARLKAKEEMMQGIQVAK-EMAQKELSEQKSLYE--IKIRALERELKEESERK 673
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEEleelTAELQELEEKLEELRLEVsELEEEIEELQKELYAlaNEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   674 REQELHKQRAASQIEQLQSVKTLLEKEVSSHKRRLQmEAQATRQAM-ADHDVRHAKIVAA----------LEAEKRKIAE 742
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLeAELEELEAELEELesrleeleeqLETLRSKVAQ 390
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899   743 DLAQIEMKRALKVTQTPKMAIPQWDAMKLSLMIEEANKISGKLRKHTVFSRHEAADKEVEGGDAQLQVQVQN 814
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
607-752 7.96e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 7.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  607 KNELLSAQRAQLEAEIQEARLKAKEEmmqgiqvakEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQ 686
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEEL---------EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113678899  687 IEQLQSVKTLLEKEVSSHKRRLQmEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
506-571 2.16e-06

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 46.42  E-value: 2.16e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113678899   506 TKVGklkSESAHDIQLSGALIADQHCVISSVKG-TVSIKPM-PNAKTFVNGHLVS-ECTVLHHGDRVIL 571
Cdd:pfam00498    1 VTIG---RSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVIRL 66
PTZ00121 PTZ00121
MAEBL; Provisional
608-787 3.06e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  608 NELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQI 687
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  688 EQLQSVKTLLEKEVSSHKRRlqmeAQATRQAMADHDVRHAKIVAALEAEKRKiAEDLAQIEMKRALKVTQTPKMAIPQWD 767
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKK-AEEAKKAEEDEKKAAEALKKEAEEAKK 1703
                         170       180
                  ....*....|....*....|
gi 113678899  768 AMKLSLMIEEANKISGKLRK 787
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKK 1723
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
607-752 4.25e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  607 KNELLSAQRAQLEAEIQEA------------RLKAKEEMMQGIQVAKEMAQKE---LSEQKSLYEI--KIRALERELKEE 669
Cdd:COG4717    65 KPELNLKELKELEEELKEAeekeeeyaelqeELEELEEELEELEAELEELREElekLEKLLQLLPLyqELEALEAELAEL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  670 SERKREQELHKQRAASQIEQLQSvktlLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEM 749
Cdd:COG4717   145 PERLEELEERLEELRELEEELEE----LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                  ...
gi 113678899  750 KRA 752
Cdd:COG4717   221 ELE 223
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
609-681 8.35e-06

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 46.42  E-value: 8.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQEARlKAKEE-----------MMQG---IQVAKEMAQKELSEQKSLYEIKIRALERElkEESERKR 674
Cdd:COG1382    24 QAVAAQKQQVESELKEAE-KALEEleklpddaevyKSVGnllVKTDKEEVIKELEEKKETLELRLKTLEKQ--EERLQKQ 100

                  ....*..
gi 113678899  675 EQELHKQ 681
Cdd:COG1382   101 LEELQEK 107
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
605-742 1.35e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   605 FAKNELLSAQRAQLEAEIQEarLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAA 684
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEE--LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113678899   685 SQIEQL--------QSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAE 742
Cdd:TIGR02168  407 ARLERLedrrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
PRK12704 PRK12704
phosphodiesterase; Provisional
614-738 2.11e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  614 QRAQLEAEI--QEARLKAKEEMMQgiqvAKEMAQKELSEQKSLY---EIKIRALERELKEESE--RKREQELHKQRA--A 684
Cdd:PRK12704   45 EEAKKEAEAikKEALLEAKEEIHK----LRNEFEKELRERRNELqklEKRLLQKEENLDRKLEllEKREEELEKKEKelE 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113678899  685 SQIEQLQSVKTLLEKEVSSHKRRL-----------------QMEAQATRQAMadHDVRHAKIVAALEAEKR 738
Cdd:PRK12704  121 QKQQELEKKEEELEELIEEQLQELerisgltaeeakeilleKVEEEARHEAA--VLIKEIEEEAKEEADKK 189
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
613-754 2.29e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.99  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   613 AQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEEsERKREqelhKQRAASQIEQLQS 692
Cdd:pfam13868  162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK-ERQKE----REEAEKKARQRQE 236
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   693 VKTLLEKEVSSHKRRLQMEAQ---ATRQAMADHDVRHAKIVAALEAEKRKIAEDLA-----QIEMKRALK 754
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEreeEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRrelekQIEEREEQR 306
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
613-752 2.43e-05

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: 47.23  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  613 AQRAQLEAEIQE--ARLKAKEEMMQGIQVAKEMAQKELSEqkslYEIKIRALERELKEESERKREQElhkqraasqiEQL 690
Cdd:COG1579    17 SELDRLEHRLKElpAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYE----------EQL 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113678899  691 QSVKTL-----LEKEVSSHKRR----------LQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1579    83 GNVRNNkeyeaLQKEIESLKRRisdledeileLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
Prefoldin_beta_GimC cd23162
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ...
609-681 2.71e-05

Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467478 [Multi-domain]  Cd Length: 102  Bit Score: 44.39  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQEARlKAKEEM-----------MQG---IQVAKEMAQKELSEQKSLYEIKIRALERelKEESERKR 674
Cdd:cd23162    14 QAVLLQKQQLEAELREIE-RALEELeklpddaevykSVGtilVKVDKEEVIKELKERKETLELRLKTLEK--QEERLRKQ 90

                  ....*..
gi 113678899  675 EQELHKQ 681
Cdd:cd23162    91 LEELQKK 97
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
603-748 2.85e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  603 FEFAKNELLSAQRAQLEAEIQ--EARLKAKEEMMQGIQVAKEMAQKELSEQKSlyeIKIRALERELKEESERKREQELHK 680
Cdd:COG4913   285 FAQRRLELLEAELEELRAELArlEAELERLEARLDALREELDELEAQIRGNGG---DRLEQLEREIERLERELEERERRR 361
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113678899  681 QRAASQIEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIE 748
Cdd:COG4913   362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
600-753 3.87e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  600 HKDFEFAKNEL--LSAQRAQLEAEIQEAR--LKAKEEMMQGIQVAKEMaqKELSEQKSLYEIKIRALERELKEESERKRE 675
Cdd:COG4717    87 EEEYAELQEELeeLEEELEELEAELEELReeLEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEERLEELRELEEE 164
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113678899  676 QELHKQRAASQIEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDvrhaKIVAALEAEKRKIAEDLAQIEMKRAL 753
Cdd:COG4717   165 LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE----EELEEAQEELEELEEELEQLENELEA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
601-752 4.37e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 4.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   601 KDFEFAKNELLSAQRAQLEAEIQEARLKAKEEmmqgiQVAKEMAQkeLSEQKSLYEIKIRALERELKEESERKREQELHK 680
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVE-----QLEERIAQ--LSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113678899   681 QRAASQIEQLQSVKTLLEKEVSShkrrLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDE----LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
625-760 4.47e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.49  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  625 ARLKAKEEMMQGIQVAKEMAQKELSEQKslyeiKIRALERELKEESERKREQELHKQRAASQIEQLQSvktllEKEVSSH 704
Cdd:PRK09510   74 AKRAEEQRKKKEQQQAEELQQKQAAEQE-----RLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEE-----AAAKAAA 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 113678899  705 KRRLQMEAQATR-QAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRALKVTQTPK 760
Cdd:PRK09510  144 AAKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK 200
PTZ00121 PTZ00121
MAEBL; Provisional
601-816 5.29e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  601 KDFEFAKNELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSE----QKSLYEIKIRALERELKEESERKREQ 676
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeelKKAEEENKIKAAEEAKKAEEDKKKAE 1678
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  677 ELHKQRAASQIEQLQSVKTLLE-KEVSSHKRRLQMEAQATRQAMADHDVRHAKIvaalEAEKRKIAEDLAQIEmkrALKV 755
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEaKKAEELKKKEAEEKKKAEELKKAEEENKIKA----EEAKKEAEEDKKKAE---EAKK 1751
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113678899  756 TQTPKMAIPQwdamklslMIEEANKISGKLRKHTVFSRHEAADKEVEGGDAQLQVQVQNTK 816
Cdd:PTZ00121 1752 DEEEKKKIAH--------LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
613-752 7.16e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.76  E-value: 7.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   613 AQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQ------ 686
Cdd:TIGR02794   50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEakakqa 129
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113678899   687 IEQLQSVKTLLE-KEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:TIGR02794  130 AEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKA 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
606-752 9.70e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  606 AKNELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKE-----LSEQKSLYEIKIRALERELK--EESERKREQEL 678
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeeleeLEEELEELEEELEEAEEELEeaEAELAEAEEAL 367
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113678899  679 HKQRAAsQIEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKivAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1196   368 LEAEAE-LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEE 438
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
613-752 9.95e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  613 AQRAQLEAEIQEARLKAKEemMQGIQVAKEMAQKELSEQkslyEIKIRALERELKEESERKREQELHKQRAASQIEQLQS 692
Cdd:COG1196   215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQA 288
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113678899  693 VKTLLEKEVSSH---KRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRA 752
Cdd:COG1196   289 EEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
609-754 1.01e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQ--EARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQ 686
Cdd:COG1196   284 EEAQAEEYELLAELArlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113678899  687 IEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRALK 754
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
612-768 1.03e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   612 SAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKE---LSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQIE 688
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDiesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   689 QLQSVktllEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDlAQIEMKRALKVTQTPKMAIPQWDA 768
Cdd:TIGR02168  898 ELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE-YSLTLEEAEALENKIEDDEEEARR 972
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
609-744 1.28e-04

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: 44.92  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQEARLKAKEemmqgiqvakemAQKELSEQKSLYEIKirALERELKEESERKREQELHKQRAASQIE 688
Cdd:COG1579    55 EDLEKEIKRLELEIEEVEARIKK------------YEEQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIE 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 113678899  689 QLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAEDL 744
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
FHA_EmbR-like cd22669
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ...
498-579 2.12e-04

forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438721 [Multi-domain]  Cd Length: 89  Bit Score: 41.63  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  498 LYMIKEGQTKVGKlksESAHDIQLSGALIADQHCVISSVKGTVSIKPMPNAK-TFVNGHLVSECTVLHHGDRVILgGDHY 576
Cdd:cd22669    10 GYPLQAAATRIGR---LHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNgVHVQHERIRSAVTLNDGDHIRI-CDHE 85

                  ...
gi 113678899  577 FRF 579
Cdd:cd22669    86 FTF 88
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
613-753 2.14e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.05  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  613 AQRAQLEAEIQEARLKAkEEMMQGIQVAKEMAQKELSEQkslyeikirALERELKEESERKREQELHKQrAASQIEQLQS 692
Cdd:COG1842    51 ANQKRLERQLEELEAEA-EKWEEKARLALEKGREDLARE---------ALERKAELEAQAEALEAQLAQ-LEEQVEKLKE 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  693 VKTLLEKEVSSHKRRLQM------EAQATRQ---AMADHDVRHAkiVAALEAEKRKIAEDLAQIEMKRAL 753
Cdd:COG1842   120 ALRQLESKLEELKAKKDTlkarakAAKAQEKvneALSGIDSDDA--TSALERMEEKIEEMEARAEAAAEL 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
612-757 2.69e-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: 44.75  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  612 SAQRAQLEAEIQEAR--LKAKEEMMQGIQVAKEMAQKELSEQkslyEIKIRALERELKEESERKREQELHKQRAASQIEQ 689
Cdd:COG4942    19 ADAAAEAEAELEQLQqeIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113678899  690 LQSVKTLLEKEVSSHKRRLQMEAQATR-------QAMADHDVR---HAKIVAALEAEKRKIAEDLAQIEMKRALKVTQ 757
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
PRK09343 PRK09343
prefoldin subunit beta; Provisional
609-681 2.96e-04

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 41.98  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQEARlKAKEEMMQG--------------IQVAKEMAQKELSEQKSLYEIKIRALERElkEESERKR 674
Cdd:PRK09343   24 ERLLQQKSQIDLELREIN-KALEELEKLpddtpiykivgnllVKVDKTKVEKELKERKELLELRSRTLEKQ--EKKLREK 100

                  ....*..
gi 113678899  675 EQELHKQ 681
Cdd:PRK09343  101 LKELQAK 107
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
506-557 3.37e-04

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 39.47  E-value: 3.37e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 113678899    506 TKVGKlkSESAHDIQLSGALIADQHCVISSVKGT-VSIKPMP-NAKTFVNGHLV 557
Cdd:smart00240    1 VTIGR--SSEDCDIQLDGPSISRRHAVIVYDGGGrFYLIDLGsTNGTFVNGKRI 52
PTZ00121 PTZ00121
MAEBL; Provisional
613-787 3.83e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  613 AQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSE-QKSLYEIKIRALERELKEESERKREQELHKQRAASQIEQLQ 691
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  692 SVKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAKivaaleaEKRKIAEDLAQIEMKRalKVTQTPKMAIPQWDAMKL 771
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-------EAKKAEEAKKKAEEAK--KADEAKKKAEEAKKADEA 1488
                         170
                  ....*....|....*.
gi 113678899  772 SLMIEEANKISGKLRK 787
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKK 1504
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
606-753 5.70e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  606 AKNELLSAQRAQLEAEIQEA-----RLKAKEEMMQGIQVAKEMAQKELSEQKSL--YEIKIRALERELKEESE------- 671
Cdd:COG4913   610 AKLAALEAELAELEEELAEAeerleALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDAssddlaa 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  672 -RKREQELHKQRAA--SQIEQLQSVKTLLEKEVSSHKRRLQmEAQATRQAMADHDVRHAkiVAALEAEKRKIAEDLAQIE 748
Cdd:COG4913   690 lEEQLEELEAELEEleEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLEL--RALLEERFAAALGDAVERE 766

                  ....*
gi 113678899  749 MKRAL 753
Cdd:COG4913   767 LRENL 771
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
609-731 5.80e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 43.50  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEI-QEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYeiKIRALERELKEESERKREQelhkqrAASQI 687
Cdd:COG1566    93 AAAEAQLARLEAELgAEAEIAAAEAQLAAAQAQLDLAQRELERYQALY--KKGAVSQQELDEARAALDA------AQAQL 164
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 113678899  688 EQLQSVKTLLEKEVSSHKRRLQMEAQ----ATRQAMADHDVRHAKIVA 731
Cdd:COG1566   165 EAAQAQLAQAQAGLREEEELAAAQAQvaqaEAALAQAELNLARTTIRA 212
PTZ00121 PTZ00121
MAEBL; Provisional
586-802 6.85e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  586 QSGKRASCWSSGDGHKDFEFAKNELLSAQRAQLEAEiqEARlKAkEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERE 665
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE--EAR-KA-DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  666 LKEESERKREQELHK----------------------QRAASQIEQLQSVKTLLEKEVSSHKRR---LQMEAQATRQA-- 718
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKadaakkkaeeakkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKadaAKKKAEEKKKAde 1395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  719 ---MADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRalKVTQTPKMAIPQWDAMKLSLMIEEANKISGKLRKHTVFSRHE 795
Cdd:PTZ00121 1396 akkKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473

                  ....*..
gi 113678899  796 AADKEVE 802
Cdd:PTZ00121 1474 EAKKKAE 1480
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
606-752 1.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  606 AKNELLSA--QRAQLE--AEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERK-------- 673
Cdd:COG4913   240 AHEALEDAreQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerlearld 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  674 ----REQELHKQRAAS---QIEQLQSVKTLLEKEVSSHKRR----------LQMEAQATRQAMADHDVRHAKIVAALEAE 736
Cdd:COG4913   320 alreELDELEAQIRGNggdRLEQLEREIERLERELEERERRrarleallaaLGLPLPASAEEFAALRAEAAALLEALEEE 399
                         170
                  ....*....|....*.
gi 113678899  737 KRKIAEDLAQIEMKRA 752
Cdd:COG4913   400 LEALEEALAEAEAALR 415
PTZ00121 PTZ00121
MAEBL; Provisional
601-787 1.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  601 KDFEFAKNELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRAleRELKEESERKREQELHK 680
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKK 1541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  681 ---QRAASQIEQLQSVKTLLEKEVSSHKRRlqmeaQATRQAMAdhdVRHAKIvaALEAEKRKIAEDLAQIEMKRALKVTQ 757
Cdd:PTZ00121 1542 aeeKKKADELKKAEELKKAEEKKKAEEAKK-----AEEDKNMA---LRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEE 1611
                         170       180       190
                  ....*....|....*....|....*....|
gi 113678899  758 TPKMAIPQWDAMKLSLMIEEANKISGKLRK 787
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
PTZ00121 PTZ00121
MAEBL; Provisional
613-809 1.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  613 AQRAQLEAEIQEARlkAKEEMMQGIQVAKEMAQKELSEQKSLYEIkiRALERELKEESERKREQElhkqRAASQIEQLQS 692
Cdd:PTZ00121 1163 ARKAEEARKAEDAK--KAEAARKAEEVRKAEELRKAEDARKAEAA--RKAEEERKAEEARKAEDA----KKAEAVKKAEE 1234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  693 VKTLLEKEVSSHKRRLQMEAQATRQAMADHDVRHAkivAALEAEKRKIAEDLAQIEMKRAL----------KVTQTPKMA 762
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ---AAIKAEEARKADELKKAEEKKKAdeakkaeekkKADEAKKKA 1311
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 113678899  763 IPQWDAMKLSLMIEEANKISGKLRKHTVFSRH--EAADKEVEGGDAQLQ 809
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKaaEAAKAEAEAAADEAE 1360
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
609-758 1.83e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  609 ELLSAQRAQLEAEIQEAR-----LKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRA 683
Cdd:COG3206   215 KLLLQQLSELESQLAEARaelaeAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113678899  684 ASQiEQLQSVKTLLEKEVSSHKRRLQMEAQATRQAMADhdvrHAKIVAALEAEKRKIAEDLAQI-EMKRALKVTQT 758
Cdd:COG3206   295 ALR-AQIAALRAQLQQEAQRILASLEAELEALQAREAS----LQAQLAQLEARLAELPELEAELrRLEREVEVARE 365
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
611-676 1.98e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 40.06  E-value: 1.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113678899  611 LSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQ 676
Cdd:PRK08476   57 VSEIEHEIETILKNAREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQ 122
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
601-778 2.08e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   601 KDFEFAKNELLSAQRAQLEAEIQEARLKAKEEMMQGIQV----------AKEMAQKELSEQKSLYEIKIRALERELKEES 670
Cdd:pfam13868   39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeqieereqKRQEEYEEKLQEREQMDEIVERIQEEDQAEA 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   671 ERKREQELHKQRAASQIEQLQSVKTLLEKEVSSHKRRLQMEAQATRQA-MADHDVRHAKIVAALEAEKRKIAEDLAQIEM 749
Cdd:pfam13868  119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAErEEEREAEREEIEEEKEREIARLRAQQEKAQD 198
                          170       180
                   ....*....|....*....|....*....
gi 113678899   750 KRAlkvtqtpkmaipQWDAMKLSLMIEEA 778
Cdd:pfam13868  199 EKA------------ERDELRAKLYQEEQ 215
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
611-752 2.31e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  611 LSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQ-----KELSEQKSLYEIKIRALERELK--EESERKREQELHKQ-- 681
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerriAALARRIRALEQELAALEAELAelEKEIAELRAELEAQke 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  682 ------RAASQIEQLQSVKTLLE-KEVSSHKRRLQMEAQATRQ------AMADHDVRHAKIVAALEAEKRKIAEDLAQIE 748
Cdd:COG4942   105 elaellRALYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPArreqaeELRADLAELAALRAELEAERAELEALLAELE 184

                  ....
gi 113678899  749 MKRA 752
Cdd:COG4942   185 EERA 188
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
607-848 4.09e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.18  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  607 KNELLSAQRAQLEAEIQEARLKAKEEMMQgiQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQ 686
Cdd:COG3064     1 AQEALEEKAAEAAAQERLEQAEAEKRAAA--EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  687 IEQLQSVKTLLEKEVSSHKRRLQMEAQAtrQAMADHDVRHAKIVAALEAEKRKIAEDLAQIEMKRALKVTQTPKMAIPQW 766
Cdd:COG3064    79 LAEAEKAAAEAEKKAAAEKAKAAKEAEA--AAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  767 DAMKLSLMIEEANKISGKLRKHTVFSRHEAADKEVEGGDAQLQVQVQNTKLGISTFWSLEKFQSNLAAMREIEQGESASK 846
Cdd:COG3064   157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236

                  ..
gi 113678899  847 DD 848
Cdd:COG3064   237 VE 238
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
613-753 4.09e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  613 AQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALER-ELKEESERKR---EQELHKQRA-ASQI 687
Cdd:COG2268   199 RDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKaEERREAETARaeaEAAYEIAEAnAERE 278
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113678899  688 EQLQSVKTLLEKEVS-SHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAED-LAQIEMKRAL 753
Cdd:COG2268   279 VQRQLEIAEREREIElQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKgLAEAEGKRAL 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
618-742 5.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  618 LEAEIQEARLKAKEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAASQIEQLQSVKTLL 697
Cdd:COG1196   647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 113678899  698 EKEVSSHKRRLQMEAQATRQAMADHDVRHAKIVAALEAEKRKIAE 742
Cdd:COG1196   727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
606-689 5.70e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 39.25  E-value: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   606 AKNELLSAQRAQLEAEIQEarlkakEEMMQGIQVAKEMAQKELSEQKSLYEIKIRALERELKEESERKREQELHKQRAAS 685
Cdd:pfam09756    9 AKLELKEAKRQQREAEEEE------REEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKSQF 82

                   ....
gi 113678899   686 QIEQ 689
Cdd:pfam09756   83 VVEE 86
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
607-709 6.52e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   607 KNELLSAQRAQLEAEIQEARLKAKEEMMQGIQVAKEMAQKELseQKSLYEIKIRALERELKEESERKREQELHKQRAASQ 686
Cdd:TIGR00618  394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL--QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
                           90       100
                   ....*....|....*....|...
gi 113678899   687 IEQLQSVKTLLEKEVSSHKRRLQ 709
Cdd:TIGR00618  472 EQQLQTKEQIHLQETRKKAVVLA 494
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
606-757 6.63e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 6.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   606 AKNELLSAQRAQLEAEiQEARLKAKEEMMQGIQVAKEMaQKELSEQKslyEIKIRALERELKEEsERKREQELHKQRAAS 685
Cdd:pfam13868  201 AERDELRAKLYQEEQE-RKERQKEREEAEKKARQRQEL-QQAREEQI---ELKERRLAEEAERE-EEEFERMLRKQAEDE 274
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113678899   686 QIEQLQSVKtllekevsshKRRLQME-AQATRQAMADhdvrHAKIVAALEAEKRKIAEDLAQIEMKRALKVTQ 757
Cdd:pfam13868  275 EIEQEEAEK----------RRMKRLEhRRELEKQIEE----REEQRAAEREEELEEGERLREEEAERRERIEE 333
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
606-746 7.29e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 40.89  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899   606 AKNELLSAQRAQLEAEIQEARL------KAKEEMMQGIQVAKEMA---QKELSEQKSLY----EIKIRALERELKEE-SE 671
Cdd:pfam07111  517 AERQQLSEVAQQLEQELQRAQEslasvgQQLEVARQGQQESTEEAaslRQELTQQQEIYgqalQEKVAEVETRLREQlSD 596
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113678899   672 RKR---EQELHKQRAASQIEQLQSvKTLLEKEVSSHKRRLQMEAQatrqamADHDVRHAKIVAALEAEKRKIAEDLAQ 746
Cdd:pfam07111  597 TKRrlnEARREQAKAVVSLRQIQH-RATQEKERNQELRRLQDEAR------KEEGQRLARRVQELERDKNLMLATLQQ 667
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
608-708 8.67e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113678899  608 NELLSAQRAQLEAEIQEARlkakeEMMQGIQVAKEMAQKELSEQKSLYEIK---IRALERELK----------EESERKR 674
Cdd:COG3096   986 NEKLRARLEQAEEARREAR-----EQLRQAQAQYSQYNQVLASLKSSRDAKqqtLQELEQELEelgvqadaeaEERARIR 1060
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 113678899  675 EQELHKQ--RAASQIEQLQSVKTLLEKEVSSHKRRL 708
Cdd:COG3096  1061 RDELHEElsQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH