NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2015229467|gb|KAG5201788|]
View 

hypothetical protein JEQ12_004551 [Ovis aries]

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_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-340 0e+00

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


:

Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 710.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:cd01371      1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   88 FNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd01371     81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01371    161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd01371    241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                          330
                   ....*....|....
gi 2015229467  327 TLTTLRYANRAKNI 340
Cdd:cd01371    321 TLSTLRYANRAKNI 334
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
912-1037 1.18e-34

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


:

Pssm-ID: 464041  Cd Length: 129  Bit Score: 129.72  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  912 KPATGQMKRNRGEEIDFETPGSILVNTNLRALINSRTFHALPSHFQQQLLFLLPEVDRQVGTDGLLRLS--SSALNNEFF 989
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTDDSRPalPSLRNNEFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2015229467  990 THAAQSWRERLADGEFTHEMQVRIRQEMEKEK-KVEQWKEKFFEDYYGQ 1037
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 super family cl16478
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
2177-2210 4.06e-20

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


The actual alignment was detected with superfamily member pfam13922:

Pssm-ID: 316444  Cd Length: 68  Bit Score: 86.11  E-value: 4.06e-20
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2015229467 2177 CACSLKAMIMCQGCGAFCHDDCIGPSKLCVLCLV 2210
Cdd:pfam13922   35 CACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
447-619 4.42e-06

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


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRRE----KDAAEVLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKET 522
Cdd:TIGR04523  373 EKLKKEnqsyKQEIKNLESQINDLESKIQ-----------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  523 YSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTR-ELKLKHLIIENfIPLEEKSKIMNR--S 599
Cdd:TIGR04523  442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkEKELKKLNEEK-KELEEKVKDLTKkiS 520
                          170       180
                   ....*....|....*....|.
gi 2015229467  600 FFDEEEDhwKLHP-ITRLENQ 619
Cdd:TIGR04523  521 SLKEKIE--KLESeKKEKESK 539
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1350-1631 8.31e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1350 PEPRGAPSAPGERASDLQRTQLLP-PCPLSGDHAQAETAVSRARREDLASLGKGKSCPLQkvldGPNSGLEDAFQLPVVP 1428
Cdd:PHA03247  2622 HAPDPPPPSPSPAANEPDPHPPPTvPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ----RPRRRAARPTVGSLTS 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1429 TRDPPcqalPPLPSRIPEPERLVEQLVLHPEGRTECGSGTTAWERGDEEPAPTIPSENSPVRALERPigleeGTGQAPDS 1508
Cdd:PHA03247  2698 LADPP----PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-----PTTAGPPA 2768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1509 SSNPtmKDLVNVTPSSIPESSLAScLQDRLFDDESELDDSGPPTRESASRQENLKTEAPVSPGAAPwrpglsndeAAGQP 1588
Cdd:PHA03247  2769 PAPP--AAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQP 2836
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015229467 1589 EPDSREEVPSAKSQVREKW------------EKAAPLIPASPAGLTAEEGLDPPV 1631
Cdd:PHA03247  2837 TAPPPPPGPPPPSLPLGGSvapggdvrrrppSRSPAAKPAAPARPPVRRLARPAV 2891
PHA03377 super family cl31823
EBNA-3C; Provisional
1580-2001 1.17e-03

EBNA-3C; Provisional


The actual alignment was detected with superfamily member PHA03377:

Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 44.27  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1580 SNDEAAGQPEPDSREEVPSAKSQVREKWEKAAPLIPASPAGlTAEEGLDPPVCLASLWTVPSGCVDSGGSDCKQLDGDKP 1659
Cdd:PHA03377   519 TTEEEESVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSD-RGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGP 597
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1660 RVNGDLEALSPHSESTDTASDceghlSEDSSEAEPSAALGLKRSLVAEQ--GEK------HNRNRCASLSKVNGNLSLVP 1731
Cdd:PHA03377   598 RQQAKCKDGPPASGPHEKQPP-----SSAPRDMAPSVVRMFLRERLLEQstGPKpksfweMRAGRDGSGIQQEPSSRRQP 672
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1732 RTDGMVAPQSWVSRVCAVPpKIPDSLLLASPEYQPRPVSLGRPTSSVE-------------------AANPLVMQLLQGH 1792
Cdd:PHA03377   673 ATQSTPPRPSWLPSVFVLP-SVDAGRAQPSEESHLSSMSPTQPISHEEqpryedpddpldlslhpdqAPPPSHQAPYSGH 751
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1793 LPLKKVLPPAHGGSKPEPPRLPLTAEQSPGGSlGVGSLQDPGEnrcgvgkSSPESLLPESCEASTGFARLeaSQAPGAPL 1872
Cdd:PHA03377   752 EEPQAQQAPYPGYWEPRPPQAPYLGYQEPQAQ-GVQVSSYPGY-------AGPWGLRAQHPRYRHSWAYW--SQYPGHGH 821
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1873 KMSKNAPSLDSLYPVTNPVAASGKAEVDFKEQL-----PPFSFEDQKEARDLSQCSISTAAPGVSlgnLTTSRAPLFSSP 1947
Cdd:PHA03377   822 PQGPWAPRPPHLPPQWDGSAGHGQDQVSQFPHLqsetgPPRLQLSQVPQLPYSQTLVSSSAPSWS---SPQPRAPIRPIP 898
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2015229467 1948 NAV--SSGPDQAGRALGDQNSAGGQGKKLFGSKNTAAALqcprlvepTPLPADAPH 2001
Cdd:PHA03377   899 TRFppPPMPLQDSMAVGCDSSGTACPSMPFASDYSQGAF--------TPLDINAQT 946
 
Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-340 0e+00

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


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 710.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:cd01371      1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   88 FNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd01371     81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01371    161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd01371    241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                          330
                   ....*....|....
gi 2015229467  327 TLTTLRYANRAKNI 340
Cdd:cd01371    321 TLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
15-340 8.54e-165

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 509.04  E-value: 8.54e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   15 RCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVaHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFA 94
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTN-KNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   95 YGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQTK--RLELKERPD 171
Cdd:pfam00225   80 YGQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIqKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrKLRIREDPK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  172 TGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSER 251
Cdd:pfam00225  157 KGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSER 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  252 QAKTG-AQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTT 330
Cdd:pfam00225  237 ASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLST 316
                          330
                   ....*....|
gi 2015229467  331 LRYANRAKNI 340
Cdd:pfam00225  317 LRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-347 1.30e-160

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: 497.48  E-value: 1.30e-160
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467     9 SVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQ-VSVKNPKGVAHEmpKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKtLTVRSPKNRQGE--KKFTFDKVFDATASQEDVFEETAAPLVDSVLEG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    88 FNGTIFAYGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQtKRLEL 166
Cdd:smart00129   79 YNATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIdKREEGWQFSVKVSYLEIYNEKIRDLLNPSS-KKLEI 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGlDGENHIRVGKLNLVDL 246
Cdd:smart00129  155 REDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDL 233
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:smart00129  234 AGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLE 313
                           330       340
                    ....*....|....*....|..
gi 2015229467   326 ETLTTLRYANRAKNIKNKPRVN 347
Cdd:smart00129  314 ETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
14-374 4.52e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 320.15  E-value: 4.52e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   14 VRCRPMNGKEKAASYDKVVDVDV--KLGQVSVK--NPKGVAHEM--PKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:COG5059      9 LKSRLSSRNEKSVSDIKSTIRIIpgELGERLINtsKKSHVSLEKskEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   88 FNGTIFAYGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHIS-RSQNQQYLVRASYLEIYQEEIRDLLSKDqTKRLEL 166
Cdd:COG5059     89 YNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEdLSMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEcSEVGLDGENHIrvGKLNLVDL 246
Cdd:COG5059    165 REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELA-SKNKVSGTSET--SKLSLVDL 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:COG5059    242 AGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFE 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2015229467  326 ETLTTLRYANRAKNIKNKPRVNE----DPKDALLR----EFQEEIARLKAQLEKRSI 374
Cdd:COG5059    322 ETINTLKFASRAKSIKNKIQVNSssdsSREIEEIKfdlsEDRSEIEILVFREQSQLS 378
PLN03188 PLN03188
kinesin-12 family protein; Provisional
6-367 5.36e-79

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 289.14  E-value: 5.36e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    6 SSESVRVVVRCRPMNGKEKaasydkvvdvdvklGQVSVKNPKGVAHEM-PKTFTFDAVYDWNAKQFELYDETFRPLVDSV 84
Cdd:PLN03188    96 SDSGVKVIVRMKPLNKGEE--------------GEMIVQKMSNDSLTInGQTFTFDSIADPESTQEDIFQLVGAPLVENC 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   85 LQGFNGTIFAYGQTGTGKTYTM---------EGVRGDpeKRGVIPNSFDHIFTHISRSQNQ------QYLVRASYLEIYQ 149
Cdd:PLN03188   162 LAGFNSSVFAYGQTGSGKTYTMwgpanglleEHLSGD--QQGLTPRVFERLFARINEEQIKhadrqlKYQCRCSFLEIYN 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  150 EEIRDLLSKDQtKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIE--CSE 227
Cdd:PLN03188   240 EQITDLLDPSQ-KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrCKS 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  228 VGlDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD----GKSTHIPYRDSKLTRLLQD 303
Cdd:PLN03188   319 VA-DGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQE 397
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  304 SLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKD------ALLREFQEEIARLKA 367
Cdd:PLN03188   398 SLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
912-1037 1.18e-34

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 129.72  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  912 KPATGQMKRNRGEEIDFETPGSILVNTNLRALINSRTFHALPSHFQQQLLFLLPEVDRQVGTDGLLRLS--SSALNNEFF 989
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTDDSRPalPSLRNNEFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2015229467  990 THAAQSWRERLADGEFTHEMQVRIRQEMEKEK-KVEQWKEKFFEDYYGQ 1037
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
2177-2210 4.06e-20

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 86.11  E-value: 4.06e-20
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2015229467 2177 CACSLKAMIMCQGCGAFCHDDCIGPSKLCVLCLV 2210
Cdd:pfam13922   35 CACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
447-619 4.42e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRRE----KDAAEVLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKET 522
Cdd:TIGR04523  373 EKLKKEnqsyKQEIKNLESQINDLESKIQ-----------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  523 YSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTR-ELKLKHLIIENfIPLEEKSKIMNR--S 599
Cdd:TIGR04523  442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkEKELKKLNEEK-KELEEKVKDLTKkiS 520
                          170       180
                   ....*....|....*....|.
gi 2015229467  600 FFDEEEDhwKLHP-ITRLENQ 619
Cdd:TIGR04523  521 SLKEKIE--KLESeKKEKESK 539
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
410-581 5.79e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  410 WREQQEKLEIEKRAIveDHSLVAEEKKRLLKEKEKKMEDLRREKDAaevLGAKIKAMESKLlvggknivDHTNEQQKILE 489
Cdd:COG4717    100 LEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEAELAE---LPERLEELEERL--------EELRELEEELE 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  490 QKRQEIAEQKRREREIQQQMESRDEETLE-LKETYSSLQQEVdiktkklkklfsklQAVKAEIHDLQEEHIKERQELEQT 568
Cdd:COG4717    167 ELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRL--------------AELEEELEEAQEELEELEEELEQL 232
                          170
                   ....*....|...
gi 2015229467  569 QNELTRELKLKHL 581
Cdd:COG4717    233 ENELEAAALEERL 245
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
479-584 3.10e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  479 DHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKA--------- 549
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNlkarlkvle 98
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2015229467  550 -EIHDLQEEH----------IKERQELEQTQNELTRELK----LKHLIIE 584
Cdd:pfam13851   99 kELKDLKWEHevleqrfekvERERDELYDKFEAAIQDVQqktgLKNLLLE 148
PRK12704 PRK12704
phosphodiesterase; Provisional
461-594 7.67e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  461 AKIKAMESKLlvggKNIVDHTNE------QQKILEQK------RQEI-AEQKRREREIQQQmESR---DEETLELK-ETY 523
Cdd:PRK12704    31 AKIKEAEEEA----KRILEEAKKeaeaikKEALLEAKeeihklRNEFeKELRERRNELQKL-EKRllqKEENLDRKlELL 105
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015229467  524 SSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHikeRQELEQTQNeLTRElKLKHLIIENfipLEEKSK 594
Cdd:PRK12704   106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQ---LQELERISG-LTAE-EAKEILLEK---VEEEAR 168
PHA03247 PHA03247
large tegument protein UL36; Provisional
1350-1631 8.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1350 PEPRGAPSAPGERASDLQRTQLLP-PCPLSGDHAQAETAVSRARREDLASLGKGKSCPLQkvldGPNSGLEDAFQLPVVP 1428
Cdd:PHA03247  2622 HAPDPPPPSPSPAANEPDPHPPPTvPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ----RPRRRAARPTVGSLTS 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1429 TRDPPcqalPPLPSRIPEPERLVEQLVLHPEGRTECGSGTTAWERGDEEPAPTIPSENSPVRALERPigleeGTGQAPDS 1508
Cdd:PHA03247  2698 LADPP----PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-----PTTAGPPA 2768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1509 SSNPtmKDLVNVTPSSIPESSLAScLQDRLFDDESELDDSGPPTRESASRQENLKTEAPVSPGAAPwrpglsndeAAGQP 1588
Cdd:PHA03247  2769 PAPP--AAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQP 2836
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015229467 1589 EPDSREEVPSAKSQVREKW------------EKAAPLIPASPAGLTAEEGLDPPV 1631
Cdd:PHA03247  2837 TAPPPPPGPPPPSLPLGGSvapggdvrrrppSRSPAAKPAAPARPPVRRLARPAV 2891
PHA03377 PHA03377
EBNA-3C; Provisional
1580-2001 1.17e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 44.27  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1580 SNDEAAGQPEPDSREEVPSAKSQVREKWEKAAPLIPASPAGlTAEEGLDPPVCLASLWTVPSGCVDSGGSDCKQLDGDKP 1659
Cdd:PHA03377   519 TTEEEESVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSD-RGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGP 597
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1660 RVNGDLEALSPHSESTDTASDceghlSEDSSEAEPSAALGLKRSLVAEQ--GEK------HNRNRCASLSKVNGNLSLVP 1731
Cdd:PHA03377   598 RQQAKCKDGPPASGPHEKQPP-----SSAPRDMAPSVVRMFLRERLLEQstGPKpksfweMRAGRDGSGIQQEPSSRRQP 672
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1732 RTDGMVAPQSWVSRVCAVPpKIPDSLLLASPEYQPRPVSLGRPTSSVE-------------------AANPLVMQLLQGH 1792
Cdd:PHA03377   673 ATQSTPPRPSWLPSVFVLP-SVDAGRAQPSEESHLSSMSPTQPISHEEqpryedpddpldlslhpdqAPPPSHQAPYSGH 751
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1793 LPLKKVLPPAHGGSKPEPPRLPLTAEQSPGGSlGVGSLQDPGEnrcgvgkSSPESLLPESCEASTGFARLeaSQAPGAPL 1872
Cdd:PHA03377   752 EEPQAQQAPYPGYWEPRPPQAPYLGYQEPQAQ-GVQVSSYPGY-------AGPWGLRAQHPRYRHSWAYW--SQYPGHGH 821
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1873 KMSKNAPSLDSLYPVTNPVAASGKAEVDFKEQL-----PPFSFEDQKEARDLSQCSISTAAPGVSlgnLTTSRAPLFSSP 1947
Cdd:PHA03377   822 PQGPWAPRPPHLPPQWDGSAGHGQDQVSQFPHLqsetgPPRLQLSQVPQLPYSQTLVSSSAPSWS---SPQPRAPIRPIP 898
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2015229467 1948 NAV--SSGPDQAGRALGDQNSAGGQGKKLFGSKNTAAALqcprlvepTPLPADAPH 2001
Cdd:PHA03377   899 TRFppPPMPLQDSMAVGCDSSGTACPSMPFASDYSQGAF--------TPLDINAQT 946
 
Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-340 0e+00

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


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 710.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:cd01371      1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   88 FNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd01371     81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQnNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01371    161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd01371    241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                          330
                   ....*....|....
gi 2015229467  327 TLTTLRYANRAKNI 340
Cdd:cd01371    321 TLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
15-340 8.54e-165

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 509.04  E-value: 8.54e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   15 RCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVaHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFA 94
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTN-KNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   95 YGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQTK--RLELKERPD 171
Cdd:pfam00225   80 YGQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIqKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrKLRIREDPK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  172 TGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSER 251
Cdd:pfam00225  157 KGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSER 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  252 QAKTG-AQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTT 330
Cdd:pfam00225  237 ASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLST 316
                          330
                   ....*....|
gi 2015229467  331 LRYANRAKNI 340
Cdd:pfam00225  317 LRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
9-338 1.37e-161

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: 499.86  E-value: 1.37e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKEkAASYDKVVDVDVKlGQVSVKNPKGVaHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGF 88
Cdd:cd00106      1 NVRVAVRVRPLNGRE-ARSAKSVISVDGG-KSVVLDPPKNR-VAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   89 NGTIFAYGQTGTGKTYTMEGVrgDPEKRGVIPNSFDHIFTHIS--RSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLEL 166
Cdd:cd00106     78 NGTIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDkrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGEnHIRVGKLNLVDL 246
Cdd:cd00106    156 REDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE-SVTSSKLNLVDL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEE 326
Cdd:cd00106    235 AGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEE 314
                          330
                   ....*....|..
gi 2015229467  327 TLTTLRYANRAK 338
Cdd:cd00106    315 TLSTLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-347 1.30e-160

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: 497.48  E-value: 1.30e-160
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467     9 SVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQ-VSVKNPKGVAHEmpKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKtLTVRSPKNRQGE--KKFTFDKVFDATASQEDVFEETAAPLVDSVLEG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    88 FNGTIFAYGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIRDLLSKDQtKRLEL 166
Cdd:smart00129   79 YNATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIdKREEGWQFSVKVSYLEIYNEKIRDLLNPSS-KKLEI 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGlDGENHIRVGKLNLVDL 246
Cdd:smart00129  155 REDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDL 233
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:smart00129  234 AGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLE 313
                           330       340
                    ....*....|....*....|..
gi 2015229467   326 ETLTTLRYANRAKNIKNKPRVN 347
Cdd:smart00129  314 ETLSTLRFASRAKEIKNKPIVN 335
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
9-341 1.91e-125

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: 398.63  E-value: 1.91e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVknpkgvahEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGF 88
Cdd:cd01372      2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTV--------GTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   89 NGTIFAYGQTGTGKTYTMEG----VRGDPEKrGVIPNSFDHIFTHISRSQNQ-QYLVRASYLEIYQEEIRDLLSK--DQT 161
Cdd:cd01372     74 NATVLAYGQTGSGKTYTMGTaytaEEDEEQV-GIIPRAIQHIFKKIEKKKDTfEFQLKVSFLEIYNEEIRDLLDPetDKK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  162 KRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIE-------CSEVGLDGEN 234
Cdd:cd01372    153 PTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpIAPMSADDKN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  235 HIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNAKTV 312
Cdd:cd01372    233 STFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDEskKGAHVPYRDSKLTRLLQDSLGGNSHTL 312
                          330       340
                   ....*....|....*....|....*....
gi 2015229467  313 MVANVGPASYNVEETLTTLRYANRAKNIK 341
Cdd:cd01372    313 MIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
10-349 9.49e-125

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: 397.47  E-value: 9.49e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFN 89
Cdd:cd01364      4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   90 GTIFAYGQTGTGKTYTMEGVRGD--------PEKRGVIPNSFDHIFTHISrSQNQQYLVRASYLEIYQEEIRDLLS--KD 159
Cdd:cd01364     84 CTIFAYGQTGTGKTYTMEGDRSPneeytwelDPLAGIIPRTLHQLFEKLE-DNGTEYSVKVSYLEIYNEELFDLLSpsSD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  160 QTKRLELKERPDT--GVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIR 237
Cdd:cd01364    163 VSERLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  238 VGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDgKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANV 317
Cdd:cd01364    243 IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIATI 321
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2015229467  318 GPASYNVEETLTTLRYANRAKNIKNKPRVNED 349
Cdd:cd01364    322 SPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
9-340 6.45e-123

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: 390.92  E-value: 6.45e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKEKAASyDKVVdvdvklgqVSVKNPKGV---AHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVL 85
Cdd:cd01369      3 NIKVVCRFRPLNELEVLQG-SKSI--------VKFDPEDTVviaTSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   86 QGFNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRS-QNQQYLVRASYLEIYQEEIRDLLSKdQTKRL 164
Cdd:cd01369     74 NGYNGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMdENLEFHVKVSYFEIYMEKIRDLLDV-SKTNL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  165 ELKERPDTGVYVKDLSS-FVTkSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVgLDGEnhIRVGKLNL 243
Cdd:cd01369    153 SVHEDKNRGPYVKGATErFVS-SPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENV-ETEK--KKSGKLYL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  244 VDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYN 323
Cdd:cd01369    229 VDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYN 308
                          330
                   ....*....|....*..
gi 2015229467  324 VEETLTTLRYANRAKNI 340
Cdd:cd01369    309 ESETLSTLRFGQRAKTI 325
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
10-342 4.53e-121

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: 385.79  E-value: 4.53e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGVAHEmpktFTFDAVYDWNAKQFELYDETfRPLVDSVLQGFN 89
Cdd:cd01366      4 IRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAKQKE----FSFDKVFDPEASQEDVFEEV-SPLVQSALDGYN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   90 GTIFAYGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHISRSQNQ--QYLVRASYLEIYQEEIRDLLSKD--QTKRLE 165
Cdd:cd01366     79 VCIFAYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgwSYTIKASMLEIYNETIRDLLAPGnaPQKKLE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  166 LKERPDTG-VYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEcsevgldGEN----HIRVGK 240
Cdd:cd01366    156 IRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS-------GRNlqtgEISVGK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  241 LNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKStHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPA 320
Cdd:cd01366    229 LNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS-HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPA 307
                          330       340
                   ....*....|....*....|..
gi 2015229467  321 SYNVEETLTTLRYANRAKNIKN 342
Cdd:cd01366    308 ESNLNETLNSLRFASKVNSCEL 329
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
8-347 7.24e-120

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: 383.63  E-value: 7.24e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    8 ESVRVVVRCRPMNGKEKAASYDKVVDVDVKlgQVSVKNPKGVAHEM------PKTFTFDAVYdWN--------AKQFELY 73
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGK--ETTLKNPKQADKNNkatrevPKSFSFDYSY-WShdsedpnyASQEQVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   74 DETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMegvRGDPEKRGVIPNSFDHIFTHISRSQNQ--QYLVRASYLEIYQEE 151
Cdd:cd01365     78 EDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTM---MGTQEQPGIIPRLCEDLFSRIADTTNQnmSYSVEVSYMEIYNEK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  152 IRDLLSKDQTKR---LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEC--- 225
Cdd:cd01365    155 VRDLLNPKPKKNkgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQkrh 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  226 -SEVGLDGEnhiRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-------GKSTHIPYRDSKL 297
Cdd:cd01365    235 dAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVL 311
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2015229467  298 TRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVN 347
Cdd:cd01365    312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
9-340 3.05e-117

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: 375.53  E-value: 3.05e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKEKAASYDKVVDV--------------DVKLGQVSVKNPKGVAHEMPKTFTFDAVYDWNAKQFELYD 74
Cdd:cd01370      1 SLTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdpkdeeDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   75 ETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGVRGDPekrGVIPNSFDHIFTHI-SRSQNQQYLVRASYLEIYQEEIR 153
Cdd:cd01370     81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIeSLKDEKEFEVSMSYLEIYNETIR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  154 DLLSKdQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGE 233
Cdd:cd01370    158 DLLNP-SSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASIN 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  234 NHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNAKT 311
Cdd:cd01370    237 QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPgkKNKHIPYRDSKLTRLLKDSLGGNCRT 316
                          330       340
                   ....*....|....*....|....*....
gi 2015229467  312 VMVANVGPASYNVEETLTTLRYANRAKNI 340
Cdd:cd01370    317 VMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
9-340 2.80e-116

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: 371.67  E-value: 2.80e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKEKAASYDKVVDVDvklgqvsvknPKGVAHE--MPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQ 86
Cdd:cd01374      1 KITVTVRVRPLNSREIGINEQVAWEID----------NDTIYLVepPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   87 GFNGTIFAYGQTGTGKTYTMegvRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKdQTKRLEL 166
Cdd:cd01374     71 GYNGTIFAYGQTSSGKTFTM---SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSP-TSQNLKI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDL 246
Cdd:cd01374    147 RDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGK-STHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:cd01374    227 AGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVE 306
                          330
                   ....*....|....*
gi 2015229467  326 ETLTTLRYANRAKNI 340
Cdd:cd01374    307 ETLNTLKFASRAKKI 321
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
10-349 1.30e-106

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: 344.88  E-value: 1.30e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPkgvahemPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFN 89
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKP-------PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   90 GTIFAYGQTGTGKTYTMEGVRGDPEK-----RGVIPNSFDHIFTHISRSQ-----NQQYLVRASYLEIYQEEIRDLLskD 159
Cdd:cd01373     76 GTIFAYGQTGSGKTYTMWGPSESDNEsphglRGVIPRIFEYLFSLIQREKekageGKSFLCKCSFLEIYNEQIYDLL--D 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  160 QTKR-LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGlDGENHIRV 238
Cdd:cd01373    154 PASRnLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKK-ACFVNIRT 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  239 GKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVA 315
Cdd:cd01373    233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
                          330       340       350
                   ....*....|....*....|....*....|....
gi 2015229467  316 NVGPASYNVEETLTTLRYANRAKNIKNKPRVNED 349
Cdd:cd01373    313 NVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
14-374 4.52e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 320.15  E-value: 4.52e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   14 VRCRPMNGKEKAASYDKVVDVDV--KLGQVSVK--NPKGVAHEM--PKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQG 87
Cdd:COG5059      9 LKSRLSSRNEKSVSDIKSTIRIIpgELGERLINtsKKSHVSLEKskEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   88 FNGTIFAYGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHIS-RSQNQQYLVRASYLEIYQEEIRDLLSKDqTKRLEL 166
Cdd:COG5059     89 YNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEdLSMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  167 KERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEcSEVGLDGENHIrvGKLNLVDL 246
Cdd:COG5059    165 REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELA-SKNKVSGTSET--SKLSLVDL 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  247 AGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD-GKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVE 325
Cdd:COG5059    242 AGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFE 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2015229467  326 ETLTTLRYANRAKNIKNKPRVNE----DPKDALLR----EFQEEIARLKAQLEKRSI 374
Cdd:COG5059    322 ETINTLKFASRAKSIKNKIQVNSssdsSREIEEIKfdlsEDRSEIEILVFREQSQLS 378
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
9-338 8.88e-84

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


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 279.08  E-value: 8.88e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGK--------EKAASYDKVVDVDVKLGQVSVKNPKgvahempKTFTFDAVYDwNAKQFELYDETFRPL 80
Cdd:cd01375      1 KVQAFVRVRPTDDFahemikygEDGKSISIHLKKDLRRGVVNNQQED-------WSFKFDGVLH-NASQELVYETVAKDV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   81 VDSVLQGFNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSK-- 158
Cdd:cd01375     73 VSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTlp 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  159 ---DQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLdGENH 235
Cdd:cd01375    153 yvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTL-SSEK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  236 IRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVA 315
Cdd:cd01375    232 YITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVA 311
                          330       340
                   ....*....|....*....|...
gi 2015229467  316 NVGPASYNVEETLTTLRYANRAK 338
Cdd:cd01375    312 NIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
10-338 5.32e-80

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: 267.45  E-value: 5.32e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   10 VRVVVRCRP-MNGKEKAASYDKVVDVDVKlgQVSVKNPKGvaHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGF 88
Cdd:cd01376      2 VRVAVRVRPfVDGTAGASDPSCVSGIDSC--SVELADPRN--HGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   89 NGTIFAYGQTGTGKTYTMEGvrgDPEKRGVIPNSFDHIFTHiSRSQNQQYLVRASYLEIYQEEIRDLLSKdQTKRLELKE 168
Cdd:cd01376     78 NATVFAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQM-TRKEAWALSFTMSYLEIYQEKILDLLEP-ASKELVIRE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  169 RPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIecSEVGLDGENHIRVGKLNLVDLAG 248
Cdd:cd01376    153 DKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--DQRERLAPFRQRTGKLNLIDLAG 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  249 SERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKStHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETL 328
Cdd:cd01376    231 SEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTL 309
                          330
                   ....*....|
gi 2015229467  329 TTLRYANRAK 338
Cdd:cd01376    310 STLNFAARSR 319
PLN03188 PLN03188
kinesin-12 family protein; Provisional
6-367 5.36e-79

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 289.14  E-value: 5.36e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    6 SSESVRVVVRCRPMNGKEKaasydkvvdvdvklGQVSVKNPKGVAHEM-PKTFTFDAVYDWNAKQFELYDETFRPLVDSV 84
Cdd:PLN03188    96 SDSGVKVIVRMKPLNKGEE--------------GEMIVQKMSNDSLTInGQTFTFDSIADPESTQEDIFQLVGAPLVENC 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   85 LQGFNGTIFAYGQTGTGKTYTM---------EGVRGDpeKRGVIPNSFDHIFTHISRSQNQ------QYLVRASYLEIYQ 149
Cdd:PLN03188   162 LAGFNSSVFAYGQTGSGKTYTMwgpanglleEHLSGD--QQGLTPRVFERLFARINEEQIKhadrqlKYQCRCSFLEIYN 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  150 EEIRDLLSKDQtKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIE--CSE 227
Cdd:PLN03188   240 EQITDLLDPSQ-KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrCKS 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  228 VGlDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVD----GKSTHIPYRDSKLTRLLQD 303
Cdd:PLN03188   319 VA-DGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQE 397
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  304 SLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKD------ALLREFQEEIARLKA 367
Cdd:PLN03188   398 SLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
10-338 1.56e-78

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: 263.39  E-value: 1.56e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   10 VRVVVRCRPMNGKEKAASYDKVVDVDVKLgQVSVKNPKGVAHEMPK----TFTFDAVYDWNAKQFELYDETFRPLVDSVL 85
Cdd:cd01367      2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKL-TLIVHEPKLKVDLTKYienhTFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   86 QGFNGTIFAYGQTGTGKTYTMEG-VRGDPEKRGVIPNSFDHIFTHISRSQ-NQQYLVRASYLEIYQEEIRDLLSKDqtKR 163
Cdd:cd01367     81 EGGKATCFAYGQTGSGKTYTMGGdFSGQEESKGIYALAARDVFRLLNKLPyKDNLGVTVSFFEIYGGKVFDLLNRK--KR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  164 LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIEcsevglDGENHIRVGKLNL 243
Cdd:cd01367    159 VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR------DRGTNKLHGKLSF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  244 VDLAGSERQAKTGAQG-ERLKEATKINLSLSALGNVISALVDGKStHIPYRDSKLTRLLQDSL-GGNAKTVMVANVGPAS 321
Cdd:cd01367    233 VDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA-HIPFRGSKLTQVLKDSFiGENSKTCMIATISPGA 311
                          330
                   ....*....|....*..
gi 2015229467  322 YNVEETLTTLRYANRAK 338
Cdd:cd01367    312 SSCEHTLNTLRYADRVK 328
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
8-338 7.83e-78

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: 262.33  E-value: 7.83e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    8 ESVRVVVRCRPMNGKEKAASYDKVVDVdVKLGQVSVKNPKGV-AHEMPKT-------FTFDAVYDWNAKQFELYDETFRP 79
Cdd:cd01368      1 DPVKVYLRVRPLSKDELESEDEGCIEV-INSTTVVLHPPKGSaANKSERNggqketkFSFSKVFGPNTTQKEFFQGTALP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   80 LVDSVLQGFNGTIFAYGQTGTGKTYTMEGVRGDPekrGVIPNSFDHIFTHIsrsqnQQYLVRASYLEIYQEEIRDLL--- 156
Cdd:cd01368     80 LVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSI-----GGYSVFVSYIEIYNEYIYDLLeps 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  157 SKDQTKR---LELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGE 233
Cdd:cd01368    152 PSSPTKKrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  234 -----NHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISAL----VDGKSTHIPYRDSKLTRLLQDS 304
Cdd:cd01368    232 vdqdkDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLFQNY 311
                          330       340       350
                   ....*....|....*....|....*....|....
gi 2015229467  305 LGGNAKTVMVANVGPASYNVEETLTTLRYANRAK 338
Cdd:cd01368    312 FDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
912-1037 1.18e-34

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 129.72  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  912 KPATGQMKRNRGEEIDFETPGSILVNTNLRALINSRTFHALPSHFQQQLLFLLPEVDRQVGTDGLLRLS--SSALNNEFF 989
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTDDSRPalPSLRNNEFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2015229467  990 THAAQSWRERLADGEFTHEMQVRIRQEMEKEK-KVEQWKEKFFEDYYGQ 1037
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
9-156 4.62e-23

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 97.29  E-value: 4.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKEKAASYDkvvDVDVKLGQVSVKNpkgvahempKTFTFDAVYDWNAKQFELYDEtFRPLVDSVLQGF 88
Cdd:pfam16796   21 NIRVFARVRPELLSEAQIDYP---DETSSDGKIGSKN---------KSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGY 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015229467   89 NGTIFAYGQTGTGKTytmegvrgdpekRGVIPNSFDHIFTHISRSQNQ-QYLVRASYLEIYQEEIRDLL 156
Cdd:pfam16796   88 NVCIFAYGQTGSGSN------------DGMIPRAREQIFRFISSLKKGwKYTIELQFVEIYNESSQDLL 144
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
12-281 8.13e-22

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: 94.33  E-value: 8.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   12 VVVRCRPMNGKEKaaSYDKVVDvdvklgqvsvknpkgvahempktfTFDAVYDWNAKQFELYDETfRPLVDSVLQGFNG- 90
Cdd:cd01363      1 VLVRVNPFKELPI--YRDSKII------------------------VFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNNq 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   91 TIFAYGQTGTGKTYTMEGVrgdpekrgvIPNSFDHIFTHISRSQNQqylvrasyLEIYQEEIRDLLSKdqtkrlelkerp 170
Cdd:cd01363     54 SIFAYGESGAGKTETMKGV---------IPYLASVAFNGINKGETE--------GWVYLTEITVTLED------------ 104
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  171 dtgvyvkdlssfvtksvkEIEHVMNVGNQNRsVGATNMNEHSSRSHAIFVItiecsevgldgenhirvgklnLVDLAGSE 250
Cdd:cd01363    105 ------------------QILQANPILEAFG-NAKTTRNENSSRFGKFIEI---------------------LLDIAGFE 144
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2015229467  251 RqaktgaqgerlkeatkINLSLSALGNVISA 281
Cdd:cd01363    145 I----------------INESLNTLMNVLRA 159
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
2177-2210 4.06e-20

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 86.11  E-value: 4.06e-20
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2015229467 2177 CACSLKAMIMCQGCGAFCHDDCIGPSKLCVLCLV 2210
Cdd:pfam13922   35 CACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
9-285 2.14e-08

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 59.37  E-value: 2.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467    9 SVRVVVRCRPMNGKE-------KAASYDKVVDVDVKLGQVSVKNPKgvAHEMPKTFTFDAvydwnAKQFELYDETFRPLV 81
Cdd:COG5059    306 NTRVICTISPSSNSFeetintlKFASRAKSIKNKIQVNSSSDSSRE--IEEIKFDLSEDR-----SEIEILVFREQSQLS 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467   82 DSVLQGfngtIFAYGQTGTGKTYTMEgvrgdpEKRGVIPNSFD-HIFTHISRSQNQQYLVRAS--YLEIYQEEIRDL--- 155
Cdd:COG5059    379 QSSLSG----IFAYMQSLKKETETLK------SRIDLIMKSIIsGTFERKKLLKEEGWKYKSTlqFLRIEIDRLLLLree 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  156 -LSKDQTKRLELKE-RpdtgvyvKDLSSFVTKSVKEIEH-VMNVGNQ-NRSVGATNMNEHSSRSHaifviTIECSEvgLD 231
Cdd:COG5059    449 eLSKKKTKIHKLNKlR-------HDLSSLLSSIPEETSDrVESEKASkLRSSASTKLNLRSSRSH-----SKFRDH--LN 514
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015229467  232 GENHIR-VGKLNLVDLAGSERQAKTgAQGERLKEATKINLSLSALGNVISALVDG 285
Cdd:COG5059    515 GSNSSTkELSLNQVDLAGSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHALGSK 568
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
447-619 4.42e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRRE----KDAAEVLGAKIKAMESKLLvggknivdhtnEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKET 522
Cdd:TIGR04523  373 EKLKKEnqsyKQEIKNLESQINDLESKIQ-----------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  523 YSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTR-ELKLKHLIIENfIPLEEKSKIMNR--S 599
Cdd:TIGR04523  442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkEKELKKLNEEK-KELEEKVKDLTKkiS 520
                          170       180
                   ....*....|....*....|.
gi 2015229467  600 FFDEEEDhwKLHP-ITRLENQ 619
Cdd:TIGR04523  521 SLKEKIE--KLESeKKEKESK 539
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
410-581 5.79e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  410 WREQQEKLEIEKRAIveDHSLVAEEKKRLLKEKEKKMEDLRREKDAaevLGAKIKAMESKLlvggknivDHTNEQQKILE 489
Cdd:COG4717    100 LEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEAELAE---LPERLEELEERL--------EELRELEEELE 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  490 QKRQEIAEQKRREREIQQQMESRDEETLE-LKETYSSLQQEVdiktkklkklfsklQAVKAEIHDLQEEHIKERQELEQT 568
Cdd:COG4717    167 ELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRL--------------AELEEELEEAQEELEELEEELEQL 232
                          170
                   ....*....|...
gi 2015229467  569 QNELTRELKLKHL 581
Cdd:COG4717    233 ENELEAAALEERL 245
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
447-611 1.08e-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: 47.74  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRREKDAAEVLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYS-- 524
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAei 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  525 -SLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRSFFDE 603
Cdd:TIGR02168  785 eELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                   ....*...
gi 2015229467  604 EEDHWKLH 611
Cdd:TIGR02168  865 EELIEELE 872
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
226-624 1.52e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  226 SEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGE--RLKEATKINLSLSALGNVISALV-DGKSTHIPYRDSKLTRLLQ 302
Cdd:pfam02463  584 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDdkRAKVVEGILKDTELTKLKESAKAkESGLRKGVSLEEGLAEKSE 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  303 DSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKP-RVNEDPKDALLREFQEEIARLKaQLEKRSIGRRKRRE 381
Cdd:pfam02463  664 VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEqREKEELKKLKLEAEELLADRVQ-EAQDKINEELKLLK 742
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  382 KRRGVGGGEEEEEEGEEGEEEGDDKDdywREQQEKLEIEKRAIVEDHSLVAEEKkrllkekekkmEDLRREKDAAEVLGA 461
Cdd:pfam02463  743 QKIDEEEEEEEKSRLKKEEKEEEKSE---LSLKEKELAEEREKTEKLKVEEEKE-----------EKLKAQEEELRALEE 808
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  462 KIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLF 541
Cdd:pfam02463  809 ELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  542 SKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRSFFDEEEDHwklHPITRLENQQM 621
Cdd:pfam02463  889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---KEEEEERNKRL 965

                   ...
gi 2015229467  622 MKR 624
Cdd:pfam02463  966 LLA 968
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
411-577 2.98e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  411 REQQEKLEIEKRAIVEDHSLVAEEKKRLLKEKEKKMEDLRREKDAAEVLGAKIKAMESKLLVGGKNIvdhtNEQQKILEQ 490
Cdd:COG1196    245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  491 KRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQN 570
Cdd:COG1196    321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                   ....*..
gi 2015229467  571 ELTRELK 577
Cdd:COG1196    401 QLEELEE 407
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
479-584 3.10e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  479 DHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKA--------- 549
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNlkarlkvle 98
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2015229467  550 -EIHDLQEEH----------IKERQELEQTQNELTRELK----LKHLIIE 584
Cdd:pfam13851   99 kELKDLKWEHevleqrfekvERERDELYDKFEAAIQDVQqktgLKNLLLE 148
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
411-607 3.63e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  411 REQQEKLEIEKraiveDHSLvaeekkrllkekekKMEDLRREKDAAE--VLGAKIKAMESKLLVGGKNIVDHTNEQQKI- 487
Cdd:TIGR02169  197 RQQLERLRRER-----EKAE--------------RYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLt 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  488 --LEQKRQEIAEQKRREREIQQQMESR-DEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQE 564
Cdd:TIGR02169  258 eeISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2015229467  565 LEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRSFFDEEEDH 607
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
446-592 4.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  446 MEDLRREKDAAE---VLGAKIKAMESKLLVggKNIVDHTNEQQKI---LEQKRQEIAEQKRREREIQQQMESRDEETLEL 519
Cdd:COG1196    202 LEPLERQAEKAEryrELKEELKELEAELLL--LKLRELEAELEELeaeLEELEAELEELEAELAELEAELEELRLELEEL 279
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015229467  520 KETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEK 592
Cdd:COG1196    280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
450-604 5.21e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  450 RREKDAAEVLGAKIKAMESKLlvggKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQE 529
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  530 VDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTREL---------KLKHLIIENFIPLEEKSKIMNRSF 600
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelsKLEEEVSRIEARLREIEQKLNRLT 825

                   ....
gi 2015229467  601 FDEE 604
Cdd:TIGR02169  826 LEKE 829
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
483-574 6.30e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  483 EQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDiktkklkKLFSKLQAVKAEIHDLQEEHIKER 562
Cdd:COG4372     42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-------AAQAELAQAQEELESLQEEAEELQ 114
                           90
                   ....*....|..
gi 2015229467  563 QELEQTQNELTR 574
Cdd:COG4372    115 EELEELQKERQD 126
PRK12704 PRK12704
phosphodiesterase; Provisional
461-594 7.67e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  461 AKIKAMESKLlvggKNIVDHTNE------QQKILEQK------RQEI-AEQKRREREIQQQmESR---DEETLELK-ETY 523
Cdd:PRK12704    31 AKIKEAEEEA----KRILEEAKKeaeaikKEALLEAKeeihklRNEFeKELRERRNELQKL-EKRllqKEENLDRKlELL 105
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015229467  524 SSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHikeRQELEQTQNeLTRElKLKHLIIENfipLEEKSK 594
Cdd:PRK12704   106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQ---LQELERISG-LTAE-EAKEILLEK---VEEEAR 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
446-574 8.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 8.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  446 MEDLRREKDAAEvlgAKIKAMESKLLVGGKNIVDHTNEQQKI---LEQKRQEIAEQKRREREIQQQMESRDEETLELKET 522
Cdd:COG4372     40 LDKLQEELEQLR---EELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2015229467  523 YSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTR 574
Cdd:COG4372    117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
PHA03247 PHA03247
large tegument protein UL36; Provisional
1350-1631 8.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1350 PEPRGAPSAPGERASDLQRTQLLP-PCPLSGDHAQAETAVSRARREDLASLGKGKSCPLQkvldGPNSGLEDAFQLPVVP 1428
Cdd:PHA03247  2622 HAPDPPPPSPSPAANEPDPHPPPTvPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ----RPRRRAARPTVGSLTS 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1429 TRDPPcqalPPLPSRIPEPERLVEQLVLHPEGRTECGSGTTAWERGDEEPAPTIPSENSPVRALERPigleeGTGQAPDS 1508
Cdd:PHA03247  2698 LADPP----PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-----PTTAGPPA 2768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1509 SSNPtmKDLVNVTPSSIPESSLAScLQDRLFDDESELDDSGPPTRESASRQENLKTEAPVSPGAAPwrpglsndeAAGQP 1588
Cdd:PHA03247  2769 PAPP--AAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQP 2836
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015229467 1589 EPDSREEVPSAKSQVREKW------------EKAAPLIPASPAGLTAEEGLDPPV 1631
Cdd:PHA03247  2837 TAPPPPPGPPPPSLPLGGSvapggdvrrrppSRSPAAKPAAPARPPVRRLARPAV 2891
PHA03377 PHA03377
EBNA-3C; Provisional
1580-2001 1.17e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 44.27  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1580 SNDEAAGQPEPDSREEVPSAKSQVREKWEKAAPLIPASPAGlTAEEGLDPPVCLASLWTVPSGCVDSGGSDCKQLDGDKP 1659
Cdd:PHA03377   519 TTEEEESVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSD-RGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGP 597
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1660 RVNGDLEALSPHSESTDTASDceghlSEDSSEAEPSAALGLKRSLVAEQ--GEK------HNRNRCASLSKVNGNLSLVP 1731
Cdd:PHA03377   598 RQQAKCKDGPPASGPHEKQPP-----SSAPRDMAPSVVRMFLRERLLEQstGPKpksfweMRAGRDGSGIQQEPSSRRQP 672
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1732 RTDGMVAPQSWVSRVCAVPpKIPDSLLLASPEYQPRPVSLGRPTSSVE-------------------AANPLVMQLLQGH 1792
Cdd:PHA03377   673 ATQSTPPRPSWLPSVFVLP-SVDAGRAQPSEESHLSSMSPTQPISHEEqpryedpddpldlslhpdqAPPPSHQAPYSGH 751
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1793 LPLKKVLPPAHGGSKPEPPRLPLTAEQSPGGSlGVGSLQDPGEnrcgvgkSSPESLLPESCEASTGFARLeaSQAPGAPL 1872
Cdd:PHA03377   752 EEPQAQQAPYPGYWEPRPPQAPYLGYQEPQAQ-GVQVSSYPGY-------AGPWGLRAQHPRYRHSWAYW--SQYPGHGH 821
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1873 KMSKNAPSLDSLYPVTNPVAASGKAEVDFKEQL-----PPFSFEDQKEARDLSQCSISTAAPGVSlgnLTTSRAPLFSSP 1947
Cdd:PHA03377   822 PQGPWAPRPPHLPPQWDGSAGHGQDQVSQFPHLqsetgPPRLQLSQVPQLPYSQTLVSSSAPSWS---SPQPRAPIRPIP 898
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2015229467 1948 NAV--SSGPDQAGRALGDQNSAGGQGKKLFGSKNTAAALqcprlvepTPLPADAPH 2001
Cdd:PHA03377   899 TRFppPPMPLQDSMAVGCDSSGTACPSMPFASDYSQGAF--------TPLDINAQT 946
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
411-576 1.28e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  411 REQQEKLEIEKRAIVEDHSLVAEEKKRLLKEKEKKMEDLRREKDAAEV-----------LGAKIKAMESKL--LVGGKNI 477
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEelkeaeeeleeLTAELQELEEKLeeLRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  478 VDHT-NEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQE 556
Cdd:TIGR02168  279 LEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
                          170       180
                   ....*....|....*....|...
gi 2015229467  557 EHIK---ERQELEQTQNELTREL 576
Cdd:TIGR02168  359 ELEEleaELEELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
447-584 1.55e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRREKDAAEVLGAKIKAMESKLLvggKNIVDHTNEQQKIlEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSL 526
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2015229467  527 QQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIE 584
Cdd:COG1196    322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1355-1699 1.66e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1355 APSAPGERASDlqrtqllppcPLSGDhaQAETAVSRARREDLASLGKGKSCPLQKVLDGPNSGledafQLPVVPTRDPPC 1434
Cdd:PHA03307    24 PPATPGDAADD----------LLSGS--QGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPG-----PGTEAPANESRS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1435 QALPPLPSRIPEPERlveqlvlhPEGRTECGSGTTAWERGD----EEPAPTIPSENSPVRALERPIGLEEGTGQAPDSSS 1510
Cdd:PHA03307    87 TPTWSLSTLAPASPA--------REGSPTPPGPSSPDPPPPtpppASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1511 NPTmkdlvnvtpssiPESSLASCLQDRLFddeseLDDSGPPTRESASRQENLKTEAPvSPGAAPWRPGLSNDEAAGQPEP 1590
Cdd:PHA03307   159 PAA------------VASDAASSRQAALP-----LSSPEETARAPSSPPAEPPPSTP-PAAASPRPPRRSSPISASASSP 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1591 DSREEVPSAKSQVREKWEKAAPLIPASPAGLTAEEGLDPP--------VCLASLWTVPS---GCVDSGGSDCKQLDGDKP 1659
Cdd:PHA03307   221 APAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPapitlptrIWEASGWNGPSsrpGPASSSSSPRERSPSPSP 300
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2015229467 1660 RVNGDLEALSPHSESTDTASDCEGHLSEDSSEAEPSAALG 1699
Cdd:PHA03307   301 SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAA 340
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
484-576 1.73e-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: 43.21  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  484 QQKIlEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVdiktkklkklfsklQAVKAEIHDLQEEHIKERQ 563
Cdd:COG4942     33 QQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--------------AALEAELAELEKEIAELRA 97
                           90
                   ....*....|...
gi 2015229467  564 ELEQTQNELTREL 576
Cdd:COG4942     98 ELEAQKEELAELL 110
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
447-606 1.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRREKDAAEVLGAKIKAMESKLlvggknivdhtNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSL 526
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQL-----------QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  527 QQEVDIKTKKLKKLFSKLQAVKAEIHDLQEE--------HIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSKIMNR 598
Cdd:COG4372    135 EAQIAELQSEIAEREEELKELEEQLESLQEElaaleqelQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214

                   ....*...
gi 2015229467  599 SFFDEEED 606
Cdd:COG4372    215 ELAEELLE 222
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
446-595 2.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  446 MEDLRR-EKDAAEV---LGAKIKAMEsKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKE 521
Cdd:PRK03918   157 LDDYENaYKNLGEVikeIKRRIERLE-KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015229467  522 TYSSLqQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELT--RELKLKHLIIENFIP--LEEKSKI 595
Cdd:PRK03918   236 LKEEI-EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEeyLDELREI 312
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
447-568 2.21e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  447 EDLRREKDAAE----VLGAKIKAMESKLLVGGKNivdhtneqqKILEQKRQEIAEQKRR----EREIQQQMESRDeetlE 518
Cdd:COG1579     55 EDLEKEIKRLEleieEVEARIKKYEEQLGNVRNN---------KEYEALQKEIESLKRRisdlEDEILELMERIE----E 121
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2015229467  519 LKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQT 568
Cdd:COG1579    122 LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
PHA03247 PHA03247
large tegument protein UL36; Provisional
1129-1699 2.22e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1129 AKTDATGVGSPHPPGTSSAASNPESPefpaetvSSRLQPSPNDPARVS--ASPDRIPsllQETVDQEPKDQKRKSFEQAT 1206
Cdd:PHA03247  2544 ASDDAGDPPPPLPPAAPPAAPDRSVP-------PPRPAPRPSEPAVTSraRRPDAPP---QSARPRAPVDDRGDPRGPAP 2613
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1207 SASFPEKKPRLEDRQSFRNTIESVHPEKPQPTKEEPKVPPIRIQLSRIKPPWVVKGQPTyqicpriVPITESSCRGWTga 1286
Cdd:PHA03247  2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR-------AAQASSPPQRPR-- 2684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1287 rtladikARALqvRGARGHHCHREAATTAIGGGGGPGGGGGGATDEGGGRGGGSGDGGEACGHPEPRGAPSAP----GER 1362
Cdd:PHA03247  2685 -------RRAA--RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpgGPA 2755
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1363 ASDLQRTQLLPPCPlSGDHAQAETAVSRARREDLASLGKGK-SCPLQKVLDGPNSGLEDAfqLPVVPTRDPPCQALPPLP 1441
Cdd:PHA03247  2756 RPARPPTTAGPPAP-APPAAPAAGPPRRLTRPAVASLSESReSLPSPWDPADPPAAVLAP--AAALPPAASPAGPLPPPT 2832
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1442 SRIPEPERLVEQLVlhPEGRTECGS---GTTAWERGDEEPAPTIPSENS--PVRALERPigleeGTGQAPDSSSNPTMKD 1516
Cdd:PHA03247  2833 SAQPTAPPPPPGPP--PPSLPLGGSvapGGDVRRRPPSRSPAAKPAAPArpPVRRLARP-----AVSRSTESFALPPDQP 2905
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1517 LVNVTPSSIPESSLASCLQdrlfddeselddsgPPTRESASRQENLKTEAPVSPGAAPwrpglsndeaAGQPEPDSREE- 1595
Cdd:PHA03247  2906 ERPPQPQAPPPPQPQPQPP--------------PPPQPQPPPPPPPRPQPPLAPTTDP----------AGAGEPSGAVPq 2961
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1596 ------VPSAKSQVREKWEKAAPLIPA---SPAGLTA----------------EEGLDPPVCLASLWTVPSGCVDSggSD 1650
Cdd:PHA03247  2962 pwlgalVPGRVAVPRFRVPQPAPSREApasSTPPLTGhslsrvsswasslalhEETDPPPVSLKQTLWPPDDTEDS--DA 3039
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2015229467 1651 CKQLDGDKPRVngDLEALSPHS--ESTDTASDCEGHLSEDSSEAEPSAALG 1699
Cdd:PHA03247  3040 DSLFDSDSERS--DLEALDPLPpePHDPFAHEPDPATPEAGARESPSSQFG 3088
PHA03247 PHA03247
large tegument protein UL36; Provisional
1467-2032 3.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1467 GTTAWERGDEEPAPTIPsenspvRALERPIGLEEGTGQAPDSSSNPTmkdlvnvtPSSIPESSLASCLQDRLFD-----D 1541
Cdd:PHA03247  2476 GAPVYRRPAEARFPFAA------GAAPDPGGGGPPDPDAPPAPSRLA--------PAILPDEPVGEPVHPRMLTwirglE 2541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1542 ESELDDSGPPTresasrqenlkteAPVSPGAAPWRPglsnDEAAGQPEPDSREEVPSAKSQVREKwekAAPLIPASPAGL 1621
Cdd:PHA03247  2542 ELASDDAGDPP-------------PPLPPAAPPAAP----DRSVPPPRPAPRPSEPAVTSRARRP---DAPPQSARPRAP 2601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1622 TAEEGlDPPVCLASLWTVPsgcvdsggsdckqldgDKPRVNGDLEALSPHSEStdtasdceghlsedSSEAEPSAALGLK 1701
Cdd:PHA03247  2602 VDDRG-DPRGPAPPSPLPP----------------DTHAPDPPPPSPSPAANE--------------PDPHPPPTVPPPE 2650
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1702 RSLVAEQGEKHNRNRCASlskvngnlSLVPRTDGMVAPQSWVSRvcAVPPKIPDSLLLASPEYQPRPVSlGRPTSSVEAa 1781
Cdd:PHA03247  2651 RPRDDPAPGRVSRPRRAR--------RLGRAAQASSPPQRPRRR--AARPTVGSLTSLADPPPPPPTPE-PAPHALVSA- 2718
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1782 nplvmqllqghLPLKKVlPPAHGGSKPEPPRLPL-----TAEQSPGGSLGVGSLQDPgenrcgvgkSSPESLLPESCEAS 1856
Cdd:PHA03247  2719 -----------TPLPPG-PAAARQASPALPAAPAppavpAGPATPGGPARPARPPTT---------AGPPAPAPPAAPAA 2777
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1857 TGFARLEAsqAPGAPLKMSKNA-PSLDSLYPVTNPVAASGKAEVDFKEQ---LPPFSFEDQKEARDLSQCSISTAAPG-- 1930
Cdd:PHA03247  2778 GPPRRLTR--PAVASLSESRESlPSPWDPADPPAAVLAPAAALPPAASPagpLPPPTSAQPTAPPPPPGPPPPSLPLGgs 2855
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467 1931 VSLGNLTTSRAPLFSSPNAVSSGPDQAGRALgdqnsaggqgkklfgskntaAALQCPRLVEPTPLPADAPHAFPNRKSGP 2010
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSPAAKPAAPARPPVRRL--------------------ARPAVSRSTESFALPPDQPERPPQPQAPP 2915
                          570       580
                   ....*....|....*....|..
gi 2015229467 2011 GKTSLSGGVQTAREDWVPKPPP 2032
Cdd:PHA03247  2916 PPQPQPQPPPPPQPQPPPPPPP 2937
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
325-624 5.26e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  325 EETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKAQLEKrsigrrkrrekrrgvgggeeeeeegeegeeegd 404
Cdd:pfam02463  220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK--------------------------------- 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  405 dkddywREQQEKLEIEKRAIVEDHSLVAEEKKRLLKEKEKKMEDLRREKDAAEvlgAKIKAMESKLlvggKNIVDHTNEQ 484
Cdd:pfam02463  267 ------LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE---EKLKESEKEK----KKAEKELKKE 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  485 QKILEQKRQEIAEQKRRereiQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQE 564
Cdd:pfam02463  334 KEEIEELEKELKELEIK----REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015229467  565 LEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRSFFDEEEDHWKLHPITRLENQQMMKR 624
Cdd:pfam02463  410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
 
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