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Conserved domains on  [gi|755494468|ref|XP_011246342|]
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kinesin-like protein KIF14 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
392-743 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 596.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDM---------KQVYSFIYDVSFWSFDECHPGYASQTTVYETL 462
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatrEVPKSFSFDYSYWSHDSEDPNYASQEQVYEDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  463 AAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLV 542
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  543 CKGEngQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVE 622
Cdd:cd01365   161 PKPK--KNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  623 GeeHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQAN----GKRVFIPYRESTLTWLLK 698
Cdd:cd01365   239 N--LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskKKSSFIPYRDSVLTWLLK 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 755494468  699 ESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVN 743
Cdd:cd01365   317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
829-936 6.15e-71

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


:

Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 232.16  E-value: 6.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  829 FQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNG 908
Cdd:cd22707     1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 755494468  909 THISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
Kinesin_assoc super family cl24686
Kinesin-associated;
740-859 5.58e-14

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 71.80  E-value: 5.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   740 AKVNEDMNAKLIRELKAEIEKLKAAQRS----------------NRNIDPERYRLCRQEITSLRMK-------------- 789
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAqglgdiidtiahptkkRANTPAANASAATAAMAGASPSpslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   790 ------------------LHQQERDMAEIQRVWKEKFEQAEKRKLQETKELQKAGVTFQMDN---------HLPNLVNLN 842
Cdd:pfam16183   81 slherimftpgseeaierLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGgtlgvfspkKTPHLVNLN 160
                          170
                   ....*....|....*..
gi 755494468   843 EDPQLSEMLLYMVKEGV 859
Cdd:pfam16183  161 EDPLMSECLLYYIKDGI 177
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
937-1109 1.15e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   937 VEVQKGKKLSSRNNLTtsegpKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKI 1016
Cdd:TIGR02168  300 LEQQKQILRERLANLE-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1017 QALEAELreESQRKRLEELNNQKASH---------KIEELERAKQHLEQEV--------YVNKRRLEMETLATKQALEDH 1079
Cdd:TIGR02168  375 EELEEQL--ETLRSKVAQLELQIASLnneierleaRLERLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEEL 452
                          170       180       190
                   ....*....|....*....|....*....|
gi 755494468  1080 RIRHARILEALEIEKQKIAEEVQMLQENRG 1109
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAER 482
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
392-743 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 596.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDM---------KQVYSFIYDVSFWSFDECHPGYASQTTVYETL 462
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatrEVPKSFSFDYSYWSHDSEDPNYASQEQVYEDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  463 AAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLV 542
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  543 CKGEngQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVE 622
Cdd:cd01365   161 PKPK--KNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  623 GeeHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQAN----GKRVFIPYRESTLTWLLK 698
Cdd:cd01365   239 N--LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskKKSSFIPYRDSVLTWLLK 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 755494468  699 ESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVN 743
Cdd:cd01365   317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
393-743 5.99e-150

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: 463.20  E-value: 5.99e-150
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    393 QVTVAVRVRPFSKREKTEKASQVVFTNGE---EITVEHPDMKQVYSFiydvsfWSFDECHPGYASQTTVYETLAAPLLDR 469
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGEKK------FTFDKVFDATASQEDVFEETAAPLVDS 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    470 AFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIaKKQTSEVSYHLEMSFFEVYNEKIHDLLVCkgengq 549
Cdd:smart00129   75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP------ 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    550 RKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEvvegEEHDHR 629
Cdd:smart00129  148 SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN----SSSGSG 223
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    630 ITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEqaNGKRVFIPYRESTLTWLLKESLGGNSKTAM 709
Cdd:smart00129  224 KASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQ--HSKSRHIPYRDSKLTRLLQDSLGGNSKTLM 301
                           330       340       350
                    ....*....|....*....|....*....|....
gi 755494468    710 IATVSPAASNIEETLSTLRYATQARLIVNIAKVN 743
Cdd:smart00129  302 IANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
399-736 1.80e-144

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 448.18  E-value: 1.80e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   399 RVRPFSKREKTEKASQVVFTNG----EEITVEHPDMKQVYSFIYDVSFWSFdechpgyASQTTVYETLAAPLLDRAFEGY 474
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESvdseTVESSHLTNKNRTKTFTFDKVFDPE-------ATQEDVYEETAKPLVESVLEGY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   475 NTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQtSEVSYHLEMSFFEVYNEKIHDLLVCKGENgqrKQPL 554
Cdd:pfam00225   74 NVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKN---KRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   555 RAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTevvEGEEHDHRITSRI 634
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR---STGGEESVKTGKL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   635 NLVDLAGSERCS-TAHSSGQRLKEGVSINKSLLTLGKVISALSEqanGKRVFIPYRESTLTWLLKESLGGNSKTAMIATV 713
Cdd:pfam00225  227 NLVDLAGSERASkTGAAGGQRLKEAANINKSLSALGNVISALAD---KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANI 303
                          330       340
                   ....*....|....*....|...
gi 755494468   714 SPAASNIEETLSTLRYATQARLI 736
Cdd:pfam00225  304 SPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
444-824 3.34e-82

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 282.40  E-value: 3.34e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  444 SFDECHPGYASQTTVYETLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIaKKQTSEVSY 523
Cdd:COG5059    59 AFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL-EDLSMTKDF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  524 HLEMSFFEVYNEKIHDLLVCKgengqrKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSS 603
Cdd:COG5059   138 AVSISYLEIYNEKIYDLLSPN------EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  604 RSHSVFTLVMTQTKTEVvegeehDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSeqANGKR 683
Cdd:COG5059   212 RSHSIFQIELASKNKVS------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALG--DKKKS 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  684 VFIPYRESTLTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMNaklireLKAEIEKLKa 763
Cdd:COG5059   284 GHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSD------SSREIEEIK- 356
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494468  764 aqrSNRNIDPERYRLCRQEITSLRMKLHQQERDmAEIQRVWKEKFEQAEKRKLQETKELQK 824
Cdd:COG5059   357 ---FDLSEDRSEIEILVFREQSQLSQSSLSGIF-AYMQSLKKETETLKSRIDLIMKSIISG 413
PLN03188 PLN03188
kinesin-12 family protein; Provisional
330-763 2.76e-71

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 263.72  E-value: 2.76e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  330 PPKSPALSTLKNRIASPRVK-------PRPKSSLFANKRESSRESTL---------PPEENSLVQKTFTE--PDSlKVEN 391
Cdd:PLN03188   19 EEQSPNPSSHKSKPSSRKLKsskenapPPDLNSLTSDLKPDHRSASAklksplpprPPSSNPLKRKLSAEtaPEN-GVSD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHpdmkqvysfiydvsfWSFDECHPGYASQTTVYETLAAPLLDRAF 471
Cdd:PLN03188   98 SGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQT---------------FTFDSIADPESTQEDIFQLVGAPLVENCL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  472 EGYNTCLFAYGQTGSGKSYTMMG----------LNEEPGIIPRFCEDLFAQIAKKQTS----EVSYHLEMSFFEVYNEKI 537
Cdd:PLN03188  163 AGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEEQIKhadrQLKYQCRCSFLEIYNEQI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  538 HDLLvckgENGQRKqpLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTK 617
Cdd:PLN03188  243 TDLL----DPSQKN--LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRC 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  618 TEVVEGEEHDHriTSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSE-QANGKRVFIPYRESTLTWL 696
Cdd:PLN03188  317 KSVADGLSSFK--TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKQRHIPYRDSRLTFL 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755494468  697 LKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMN------AKLIRELKAEIEKLKA 763
Cdd:PLN03188  395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQddvnflREVIRQLRDELQRVKA 467
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
829-936 6.15e-71

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


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 232.16  E-value: 6.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  829 FQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNG 908
Cdd:cd22707     1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 755494468  909 THISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
Kinesin_assoc pfam16183
Kinesin-associated;
740-859 5.58e-14

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 71.80  E-value: 5.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   740 AKVNEDMNAKLIRELKAEIEKLKAAQRS----------------NRNIDPERYRLCRQEITSLRMK-------------- 789
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAqglgdiidtiahptkkRANTPAANASAATAAMAGASPSpslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   790 ------------------LHQQERDMAEIQRVWKEKFEQAEKRKLQETKELQKAGVTFQMDN---------HLPNLVNLN 842
Cdd:pfam16183   81 slherimftpgseeaierLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGgtlgvfspkKTPHLVNLN 160
                          170
                   ....*....|....*..
gi 755494468   843 EDPQLSEMLLYMVKEGV 859
Cdd:pfam16183  161 EDPLMSECLLYYIKDGI 177
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
855-933 1.90e-09

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 56.12  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  855 VKEGVTTVGKHTPSsshDIQLSGVLIADDHCTIRNFGGTVSIVPAGEA-KTYVNGTHISEPTVLHHGDRVVLgGDHYFRF 933
Cdd:COG1716    18 LDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDLGSTnGTFVNGQRVTEPAPLRDGDVIRL-GKTELRF 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
937-1109 1.15e-08

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: 60.46  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   937 VEVQKGKKLSSRNNLTtsegpKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKI 1016
Cdd:TIGR02168  300 LEQQKQILRERLANLE-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1017 QALEAELreESQRKRLEELNNQKASH---------KIEELERAKQHLEQEV--------YVNKRRLEMETLATKQALEDH 1079
Cdd:TIGR02168  375 EELEEQL--ETLRSKVAQLELQIASLnneierleaRLERLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEEL 452
                          170       180       190
                   ....*....|....*....|....*....|
gi 755494468  1080 RIRHARILEALEIEKQKIAEEVQMLQENRG 1109
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAER 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
963-1113 2.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  963 AKNELLTAQRSRLEAEIKDAQ------LKAKEEMMQGIQIAKEMaQQELSSQKAVYERKIQALEAELREESQRKRLEELN 1036
Cdd:COG1196   267 AELEELRLELEELELELEEAQaeeyelLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEE 345
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468 1037 NQKASHKIEELERAKQHLEQEVyvnkRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDK 1113
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEAL----LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
860-925 5.83e-08

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 51.04  E-value: 5.83e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494468   860 TTVGKHtpsSSHDIQLSGVLIADDHCTI-RNFGGTVSIVPAGE-AKTYVNGTHIS-EPTVLHHGDRVVL 925
Cdd:pfam00498    1 VTIGRS---PDCDIVLDDPSVSRRHAEIrYDGGGRFYLEDLGStNGTFVNGQRLGpEPVRLKDGDVIRL 66
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
974-1106 8.99e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 52.23  E-value: 8.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   974 RLEAEIKDAQLkakEEMMQGIQIAKEMAQQELSSQkavyERKIQALEAELREesqrkrleelnnqkASHKIEELERAKQH 1053
Cdd:pfam20492    1 REEAEREKQEL---EERLKQYEEETKKAQEELEES----EETAEELEEERRQ--------------AEEEAERLEQKRQE 59
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468  1054 LEQEvyvnKRRLE---METLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:pfam20492   60 AEEE----KERLEesaEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQE 111
PRK12704 PRK12704
phosphodiesterase; Provisional
971-1081 4.31e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  971 QRSRLEAEI--KDAQLKAKEEMMQgiqiAKEMAQQELSSQkavyERKIQALEAEL--REESQRKRLEELNnqKASHKIEE 1046
Cdd:PRK12704   45 EEAKKEAEAikKEALLEAKEEIHK----LRNEFEKELRER----RNELQKLEKRLlqKEENLDRKLELLE--KREEELEK 114
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755494468 1047 LERAKQHLEQEvyVNKRRLEMETLATKQALEDHRI 1081
Cdd:PRK12704  115 KEKELEQKQQE--LEKKEEELEELIEEQLQELERI 147
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
860-911 2.93e-04

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 40.24  E-value: 2.93e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 755494468    860 TTVGKHtpSSSHDIQLSGVLIADDHCTIRNFGGT-VSIVPAG-EAKTYVNGTHI 911
Cdd:smart00240    1 VTIGRS--SEDCDIQLDGPSISRRHAVIVYDGGGrFYLIDLGsTNGTFVNGKRI 52
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
965-1078 6.58e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  965 NELLTAQRSRLEAEIKDAQLKAKEEmmqgiqiAKEMAQQELSSQKAVYERKIQALEAELREesQRKRLEELNNQKASHKI 1044
Cdd:cd16269   184 EAILQADQALTEKEKEIEAERAKAE-------AAEQERKLLEEQQRELEQKLEDQERSYEE--HLRQLKEKMEEERENLL 254
                          90       100       110
                  ....*....|....*....|....*....|....
gi 755494468 1045 EELERAKQHLEQEvyvNKRRLEMETLATKQALED 1078
Cdd:cd16269   255 KEQERALESKLKE---QEALLEEGFKEQAELLQE 285
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
392-743 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 596.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDM---------KQVYSFIYDVSFWSFDECHPGYASQTTVYETL 462
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatrEVPKSFSFDYSYWSHDSEDPNYASQEQVYEDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  463 AAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLV 542
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  543 CKGEngQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVE 622
Cdd:cd01365   161 PKPK--KNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  623 GeeHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQAN----GKRVFIPYRESTLTWLLK 698
Cdd:cd01365   239 N--LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskKKSSFIPYRDSVLTWLLK 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 755494468  699 ESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVN 743
Cdd:cd01365   317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
393-743 5.99e-150

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: 463.20  E-value: 5.99e-150
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    393 QVTVAVRVRPFSKREKTEKASQVVFTNGE---EITVEHPDMKQVYSFiydvsfWSFDECHPGYASQTTVYETLAAPLLDR 469
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGEKK------FTFDKVFDATASQEDVFEETAAPLVDS 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    470 AFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIaKKQTSEVSYHLEMSFFEVYNEKIHDLLVCkgengq 549
Cdd:smart00129   75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP------ 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    550 RKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEvvegEEHDHR 629
Cdd:smart00129  148 SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN----SSSGSG 223
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468    630 ITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEqaNGKRVFIPYRESTLTWLLKESLGGNSKTAM 709
Cdd:smart00129  224 KASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQ--HSKSRHIPYRDSKLTRLLQDSLGGNSKTLM 301
                           330       340       350
                    ....*....|....*....|....*....|....
gi 755494468    710 IATVSPAASNIEETLSTLRYATQARLIVNIAKVN 743
Cdd:smart00129  302 IANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
399-736 1.80e-144

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 448.18  E-value: 1.80e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   399 RVRPFSKREKTEKASQVVFTNG----EEITVEHPDMKQVYSFIYDVSFWSFdechpgyASQTTVYETLAAPLLDRAFEGY 474
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESvdseTVESSHLTNKNRTKTFTFDKVFDPE-------ATQEDVYEETAKPLVESVLEGY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   475 NTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQtSEVSYHLEMSFFEVYNEKIHDLLVCKGENgqrKQPL 554
Cdd:pfam00225   74 NVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKN---KRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   555 RAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTevvEGEEHDHRITSRI 634
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR---STGGEESVKTGKL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   635 NLVDLAGSERCS-TAHSSGQRLKEGVSINKSLLTLGKVISALSEqanGKRVFIPYRESTLTWLLKESLGGNSKTAMIATV 713
Cdd:pfam00225  227 NLVDLAGSERASkTGAAGGQRLKEAANINKSLSALGNVISALAD---KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANI 303
                          330       340
                   ....*....|....*....|...
gi 755494468   714 SPAASNIEETLSTLRYATQARLI 736
Cdd:pfam00225  304 SPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
393-734 1.00e-125

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: 396.63  E-value: 1.00e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  393 QVTVAVRVRPFSKREKTEKASQVVFTNGEEITVeHPDMKQVYSfiyDVSFwSFDECHPGYASQTTVYETLAAPLLDRAFE 472
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVL-DPPKNRVAP---PKTF-AFDAVFDSTSTQEEVYEGTAKPLVDSALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  473 GYNTCLFAYGQTGSGKSYTMMGLN-EEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLvckgeNGQRK 551
Cdd:cd00106    76 GYNGTIFAYGQTGSGKTYTMLGPDpEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL-----SPVPK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  552 QPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEvvegEEHDHRIT 631
Cdd:cd00106   151 KPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNRE----KSGESVTS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  632 SRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALseqANGKRVFIPYRESTLTWLLKESLGGNSKTAMIA 711
Cdd:cd00106   227 SKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISAL---ADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIA 303
                         330       340
                  ....*....|....*....|...
gi 755494468  712 TVSPAASNIEETLSTLRYATQAR 734
Cdd:cd00106   304 CISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
394-736 8.90e-105

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: 338.67  E-value: 8.90e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  394 VTVAVRVRPFSKREKTEKASQVVFTNGE--EITVEHPD-----MKQVYSFiydvsfwsfDECHPGYASQTTVYETLAAPL 466
Cdd:cd01371     3 VKVVVRCRPLNGKEKAAGALQIVDVDEKrgQVSVRNPKatanePPKTFTF---------DAVFDPNSKQLDVYDETARPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  467 LDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEP---GIIPRFCEDLFAQIAKKQtSEVSYHLEMSFFEVYNEKIHDLLvc 543
Cdd:cd01371    74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ-NNQQFLVRVSYLEIYNEEIRDLL-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  544 kGENGQRKQPLRarEHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLvmTQTKTEVVEG 623
Cdd:cd01371   151 -GKDQTKRLELK--ERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTI--TIECSEKGED 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  624 EEhDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALseqANGKRVFIPYRESTLTWLLKESLGG 703
Cdd:cd01371   226 GE-NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISAL---VDGKSTHIPYRDSKLTRLLQDSLGG 301
                         330       340       350
                  ....*....|....*....|....*....|...
gi 755494468  704 NSKTAMIATVSPAASNIEETLSTLRYATQARLI 736
Cdd:cd01371   302 NSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
392-736 1.85e-103

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: 335.07  E-value: 1.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEkasqvvftnGEEITVEH-PDMKQVysFIYDVSFWSFDECHPGYASQTTVYETLAAPLLDRA 470
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIE---------GCRICVSFvPGEPQV--TVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  471 FEGYNTCLFAYGQTGSGKSYTMMG------LNEEPGIIPRFCEDLFAQIAKKQtSEVSYHLEMSFFEVYNEKIHDLLVCK 544
Cdd:cd01372    70 FEGYNATVLAYGQTGSGKTYTMGTaytaeeDEEQVGIIPRAIQHIFKKIEKKK-DTFEFQLKVSFLEIYNEEIRDLLDPE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  545 GEngqRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTK----TEV 620
Cdd:cd01372   149 TD---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKkngpIAP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  621 VEGEEHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISAL-SEQANGKrvFIPYRESTLTWLLKE 699
Cdd:cd01372   226 MSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALgDESKKGA--HVPYRDSKLTRLLQD 303
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 755494468  700 SLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLI 736
Cdd:cd01372   304 SLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
399-738 1.54e-101

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: 329.17  E-value: 1.54e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  399 RVRPFSKREKTEKASQVVFT--NGEEITVEHPDMKQvYSFIYDvsfWSFDEChpgyASQTTVYETLAaPLLDRAFEGYNT 476
Cdd:cd01366     9 RVRPLLPSEENEDTSHITFPdeDGQTIELTSIGAKQ-KEFSFD---KVFDPE----ASQEDVFEEVS-PLVQSALDGYNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  477 CLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLvckGENGQRKQPLRA 556
Cdd:cd01366    80 CIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLL---APGNAPQKKLEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  557 REHPVSGP-YVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLvmtqtkteVVEGE--EHDHRITSR 633
Cdd:cd01366   157 RHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFIL--------HISGRnlQTGEISVGK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  634 INLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEqangKRVFIPYRESTLTWLLKESLGGNSKTAMIATV 713
Cdd:cd01366   229 LNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQ----KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNI 304
                         330       340
                  ....*....|....*....|....*
gi 755494468  714 SPAASNIEETLSTLRYATQARLIVN 738
Cdd:cd01366   305 SPAESNLNETLNSLRFASKVNSCEL 329
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
394-736 3.07e-101

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: 327.75  E-value: 3.07e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  394 VTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDMKqvySFIYDVSFwsfdechPGYASQTTVYETLAAPLLDRAFEG 473
Cdd:cd01374     2 ITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPPST---SFTFDHVF-------GGDSTNREVYELIAKPVVKSALEG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  474 YNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIakKQTSEVSYHLEMSFFEVYNEKIHDLLVCKGengqrkQP 553
Cdd:cd01374    72 YNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKI--QDTPDREFLLRVSYLEIYNEKINDLLSPTS------QN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  554 LRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTlvMTQTKTEVVEGEEHDHRItSR 633
Cdd:cd01374   144 LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFR--ITIESSERGELEEGTVRV-ST 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  634 INLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANGKrvFIPYRESTLTWLLKESLGGNSKTAMIATV 713
Cdd:cd01374   221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG--HIPYRDSKLTRILQPSLGGNSRTAIICTI 298
                         330       340
                  ....*....|....*....|...
gi 755494468  714 SPAASNIEETLSTLRYATQARLI 736
Cdd:cd01374   299 TPAESHVEETLNTLKFASRAKKI 321
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
393-736 2.39e-96

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: 315.05  E-value: 2.39e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  393 QVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDMKQVYSFIYDVSF------------WSFDECHPGYASQTTVYE 460
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNrdrrkrrnkelkYVFDRVFDETSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  461 TLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIaKKQTSEVSYHLEMSFFEVYNEKIHDL 540
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI-ESLKDEKEFEVSMSYLEIYNETIRDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  541 LVCKGEngqrkqPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTktEV 620
Cdd:cd01370   160 LNPSSG------PLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ--DK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  621 VEGEEHDHRItSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANGKRvFIPYRESTLTWLLKES 700
Cdd:cd01370   232 TASINQQVRQ-GKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNK-HIPYRDSKLTRLLKDS 309
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 755494468  701 LGGNSKTAMIATVSPAASNIEETLSTLRYATQARLI 736
Cdd:cd01370   310 LGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
391-745 1.82e-95

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: 312.72  E-value: 1.82e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  391 NSQVTVAVRVRPFSKREKTEKASQVVFTNG--EEITVEH---PDMKQVYSFIYDVSFWSFdechpgyASQTTVYETLAAP 465
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPvrKEVSVRTgglADKSSTKTYTFDMVFGPE-------AKQIDVYRSVVCP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  466 LLDRAFEGYNTCLFAYGQTGSGKSYTMMG-----------LNEEPGIIPRFCEDLFAQIakkQTSEVSYHLEMSFFEVYN 534
Cdd:cd01364    74 ILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKL---EDNGTEYSVKVSYLEIYN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  535 EKIHDLLVCkgeNGQRKQPLRAREHP--VSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTlV 612
Cdd:cd01364   151 EELFDLLSP---SSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS-I 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  613 MTQTKTEVVEGEEHdHRItSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANgkrvFIPYREST 692
Cdd:cd01364   227 TIHIKETTIDGEEL-VKI-GKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP----HVPYRESK 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755494468  693 LTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNED 745
Cdd:cd01364   301 LTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
392-736 9.84e-95

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 309.65  E-value: 9.84e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEK-ASQVVFTNGEEITVEHPDMKQVYSFiydvsfwsfDECHPGYASQTTVYETLAAPLLDRA 470
Cdd:cd01369     2 CNIKVVCRFRPLNELEVLQGsKSIVKFDPEDTVVIATSETGKTFSF---------DRVFDPNTTQEDVYNFAAKPIVDDV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  471 FEGYNTCLFAYGQTGSGKSYTMMGLNEEP---GIIPRFCEDLFAQIaKKQTSEVSYHLEMSFFEVYNEKIHDLLVckgen 547
Cdd:cd01369    73 LNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETI-YSMDENLEFHVKVSYFEIYMEKIRDLLD----- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  548 gQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVvegeehD 627
Cdd:cd01369   147 -VSKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVET------E 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  628 HRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEqanGKRVFIPYRESTLTWLLKESLGGNSKT 707
Cdd:cd01369   220 KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD---GKKTHIPYRDSKLTRILQDSLGGNSRT 296
                         330       340
                  ....*....|....*....|....*....
gi 755494468  708 AMIATVSPAASNIEETLSTLRYATQARLI 736
Cdd:cd01369   297 TLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
394-745 1.76e-87

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: 289.79  E-value: 1.76e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  394 VTVAVRVRPFSKREKTEKASQVVftngeeiTVEHPDMKQVYSfIYDVSFwSFDECHPGYASQTTVYETLAAPLLDRAFEG 473
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCL-------KKLSSDTLVLHS-KPPKTF-TFDHVADSNTNQESVFQSVGKPIVESCLSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  474 YNTCLFAYGQTGSGKSYTMMG--------LNEEPGIIPRFCEDLFAQIAKKQT---SEVSYHLEMSFFEVYNEKIHDLLv 542
Cdd:cd01373    74 YNGTIFAYGQTGSGKTYTMWGpsesdnesPHGLRGVIPRIFEYLFSLIQREKEkagEGKSFLCKCSFLEIYNEQIYDLL- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  543 ckgENGQRKqpLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMtqtktEVVE 622
Cdd:cd01373   153 ---DPASRN--LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-----ESWE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  623 GEEHDHRI-TSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANGKRVFIPYRESTLTWLLKESL 701
Cdd:cd01373   223 KKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSL 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 755494468  702 GGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNED 745
Cdd:cd01373   303 GGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
444-824 3.34e-82

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 282.40  E-value: 3.34e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  444 SFDECHPGYASQTTVYETLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIaKKQTSEVSY 523
Cdd:COG5059    59 AFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL-EDLSMTKDF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  524 HLEMSFFEVYNEKIHDLLVCKgengqrKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSS 603
Cdd:COG5059   138 AVSISYLEIYNEKIYDLLSPN------EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  604 RSHSVFTLVMTQTKTEVvegeehDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSeqANGKR 683
Cdd:COG5059   212 RSHSIFQIELASKNKVS------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALG--DKKKS 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  684 VFIPYRESTLTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMNaklireLKAEIEKLKa 763
Cdd:COG5059   284 GHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSD------SSREIEEIK- 356
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494468  764 aqrSNRNIDPERYRLCRQEITSLRMKLHQQERDmAEIQRVWKEKFEQAEKRKLQETKELQK 824
Cdd:COG5059   357 ---FDLSEDRSEIEILVFREQSQLSQSSLSGIF-AYMQSLKKETETLKSRIDLIMKSIISG 413
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
393-730 1.19e-76

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: 257.61  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  393 QVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDMKQV--YSFIYDVSFwSFDECHPGYASQTTVYETLAAPLLDRA 470
Cdd:cd01367     1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVdlTKYIENHTF-RFDYVFDESSSNETVYRSTVKPLVPHI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  471 FEG-YNTClFAYGQTGSGKSYTMMG----LNEEPGIIPRFCEDLFAQIAKKQTSEvSYHLEMSFFEVYNEKIHDLLvckg 545
Cdd:cd01367    80 FEGgKATC-FAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKD-NLGVTVSFFEIYGGKVFDLL---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  546 engQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVEGee 625
Cdd:cd01367   154 ---NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLHG-- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  626 hdhritsRINLVDLAGSERCS-TAHSSGQRLKEGVSINKSLLTLGKVISALSEQangkRVFIPYRESTLTWLLKESL-GG 703
Cdd:cd01367   229 -------KLSFVDLAGSERGAdTSSADRQTRMEGAEINKSLLALKECIRALGQN----KAHIPFRGSKLTQVLKDSFiGE 297
                         330       340
                  ....*....|....*....|....*..
gi 755494468  704 NSKTAMIATVSPAASNIEETLSTLRYA 730
Cdd:cd01367   298 NSKTCMIATISPGASSCEHTLNTLRYA 324
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
393-734 1.24e-74

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: 252.70  E-value: 1.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  393 QVTVAVRVRPFSKREKTEKASQ-VVFTNGEEITVEHPD----MKQVYSFIYDVSFWSFDECHPGYASQTTVYETLAAPLL 467
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGcIEVINSTTVVLHPPKgsaaNKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  468 DRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAkkqtsevSYHLEMSFFEVYNEKIHDLL-VCKGE 546
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIG-------GYSVFVSYIEIYNEYIYDLLePSPSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  547 NGQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVvEGEEH 626
Cdd:cd01368   155 PTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDS-DGDVD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  627 DHRI---TSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSE-QANGKRVFIPYRESTLTWLLKESLG 702
Cdd:cd01368   234 QDKDqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnQLQGTNKMVPFRDSKLTHLFQNYFD 313
                         330       340       350
                  ....*....|....*....|....*....|..
gi 755494468  703 GNSKTAMIATVSPAASNIEETLSTLRYATQAR 734
Cdd:cd01368   314 GEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
453-734 4.29e-73

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: 247.88  E-value: 4.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  453 ASQTTVYETLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNE---EPGIIPRFCEDLFAQIAKKQTSEVSYHLemSF 529
Cdd:cd01375    59 ASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFRMIEERPTKAYTVHV--SY 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  530 FEVYNEKIHDLLVCKGENGQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVF 609
Cdd:cd01375   137 LEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIF 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  610 TLVMTQTKTEVVEgeehDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQangKRVFIPYR 689
Cdd:cd01375   217 TIHLEAHSRTLSS----EKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK---DRTHVPFR 289
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 755494468  690 ESTLTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQAR 734
Cdd:cd01375   290 QSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
330-763 2.76e-71

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 263.72  E-value: 2.76e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  330 PPKSPALSTLKNRIASPRVK-------PRPKSSLFANKRESSRESTL---------PPEENSLVQKTFTE--PDSlKVEN 391
Cdd:PLN03188   19 EEQSPNPSSHKSKPSSRKLKsskenapPPDLNSLTSDLKPDHRSASAklksplpprPPSSNPLKRKLSAEtaPEN-GVSD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  392 SQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHpdmkqvysfiydvsfWSFDECHPGYASQTTVYETLAAPLLDRAF 471
Cdd:PLN03188   98 SGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQT---------------FTFDSIADPESTQEDIFQLVGAPLVENCL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  472 EGYNTCLFAYGQTGSGKSYTMMG----------LNEEPGIIPRFCEDLFAQIAKKQTS----EVSYHLEMSFFEVYNEKI 537
Cdd:PLN03188  163 AGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEEQIKhadrQLKYQCRCSFLEIYNEQI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  538 HDLLvckgENGQRKqpLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTK 617
Cdd:PLN03188  243 TDLL----DPSQKN--LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRC 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  618 TEVVEGEEHDHriTSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSE-QANGKRVFIPYRESTLTWL 696
Cdd:PLN03188  317 KSVADGLSSFK--TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKQRHIPYRDSRLTFL 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755494468  697 LKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMN------AKLIRELKAEIEKLKA 763
Cdd:PLN03188  395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQddvnflREVIRQLRDELQRVKA 467
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
829-936 6.15e-71

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


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 232.16  E-value: 6.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  829 FQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNG 908
Cdd:cd22707     1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 755494468  909 THISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
394-734 3.56e-66

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: 227.39  E-value: 3.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  394 VTVAVRVRPFSKREKTEKASQVV-FTNGEEITVEHPDMKQvysfiyDVSFWSFDECHPGYASQTTVYETLAAPLLDRAFE 472
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVsGIDSCSVELADPRNHG------ETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  473 GYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFaQIAKKQTSevSYHLEMSFFEVYNEKIHDLLVCKGENgqrkq 552
Cdd:cd01376    76 GQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW--ALSFTMSYLEIYQEKILDLLEPASKE----- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  553 pLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVvegeeHDHRITS 632
Cdd:cd01376   148 -LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA-----PFRQRTG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  633 RINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEqaNGKRvfIPYRESTLTWLLKESLGGNSKTAMIAT 712
Cdd:cd01376   222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNK--NLPR--IPYRDSKLTRLLQDSLGGGSRCIMVAN 297
                         330       340
                  ....*....|....*....|..
gi 755494468  713 VSPAASNIEETLSTLRYATQAR 734
Cdd:cd01376   298 IAPERTFYQDTLSTLNFAARSR 319
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
835-935 1.23e-43

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


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 153.93  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  835 LPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHISEP 914
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
                          90       100
                  ....*....|....*....|.
gi 755494468  915 TVLHHGDRVVLGGDHYFRFNH 935
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
836-936 2.08e-37

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


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 136.19  E-value: 2.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  836 PNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGE-AKTYVNGTHISEP 914
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSPgAKVIVNGVPVTGE 80
                          90       100
                  ....*....|....*....|..
gi 755494468  915 TVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22709    81 TELHHLDRVILGSNHLYVFVGP 102
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
836-941 9.59e-32

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


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 120.42  E-value: 9.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  836 PNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGT-----VSIVPAGEAKTYVNGTH 910
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 755494468  911 ISEPTVLHHGDRVVLGGDHYFRFNHPVEVQK 941
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQ 112
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
838-936 6.07e-31

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


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 117.78  E-value: 6.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  838 LVNLNEDPQLSEMLLYMVKEgVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHISEPTVL 917
Cdd:cd22706     4 LVNLNADPSLNELLVYYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQL 82
                          90
                  ....*....|....*....
gi 755494468  918 HHGDRVVLGGDHYFRFNHP 936
Cdd:cd22706    83 RHGDRILWGNNHFFRLNCP 101
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
836-936 1.71e-30

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


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 116.67  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  836 PNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIR-----NFGGTVSIVPAGEAKTYVNGTH 910
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRsernnNGEVIVTLEPCERSETYVNGKR 82
                          90       100
                  ....*....|....*....|....*.
gi 755494468  911 ISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHP 108
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
832-936 1.42e-26

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


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 105.43  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  832 DNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHI 911
Cdd:cd22708     5 DSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVNGQVI 84
                          90       100
                  ....*....|....*....|....*
gi 755494468  912 SEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22708    85 TQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
836-935 1.60e-26

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


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 105.34  E-value: 1.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  836 PNLVNLNEDPQLSEMLLYMVKEGVTTVGKhtpsSSHDIQLSGVLIADDHCTIR---NFGG--TVSIVPAGEAKTYVNGTH 910
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQ----VDVDIKLSGQFIREQHCLFRsipNPSGevVVTLEPCEGAETYVNGKQ 77
                          90       100
                  ....*....|....*....|....*
gi 755494468  911 ISEPTVLHHGDRVVLGGDHYFRFNH 935
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
396-674 3.55e-26

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: 106.66  E-value: 3.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  396 VAVRVRPFSKREKtekasqvvftNGEEITvehpdmkqvysfiydvsfWSFDECHPGYASQTTVYEtLAAPLLDRAFEGYN 475
Cdd:cd01363     1 VLVRVNPFKELPI----------YRDSKI------------------IVFYRGFRRSESQPHVFA-IADPAYQSMLDGYN 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  476 -TCLFAYGQTGSGKSYTMMglneepGIIPRFCEDLFAQIAKKQTSEVSYHLEMSffevynekihdllvckgengqrkqpl 554
Cdd:cd01363    52 nQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLTEIT-------------------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  555 rarehpvsgpyveglsmnvVSSYSDIQSWLELGNKQRaTAATGMNDKSSRSHSVFTLVmtqtktevvegeehdhritsri 634
Cdd:cd01363   100 -------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEIL---------------------- 137
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 755494468  635 nlVDLAGSERcstahssgqrlkegvsINKSLLTLGKVISA 674
Cdd:cd01363   138 --LDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
831-941 5.07e-25

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


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 101.55  E-value: 5.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  831 MDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTH 910
Cdd:cd22732     4 LDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVNGVQ 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 755494468  911 ISEPTVLHHGDRVVLGGDHYFRFNHPVEVQK 941
Cdd:cd22732    84 ITEATQLNQGAVILLGRTNMFRFNHPKEAAK 114
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
838-936 7.69e-24

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


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 97.29  E-value: 7.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  838 LVNLNEDPQLSEMLLYMVKEGvTTVGKHtpsSSHDIQLSGVLIADDHCTIR-NFGGTVSIVPAGEAKTYVNGTHISEPTV 916
Cdd:cd22730     4 LVNLNADPALNELLVYYLKEH-TLIGSA---DSQDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
                          90       100
                  ....*....|....*....|
gi 755494468  917 LHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
826-938 1.55e-22

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


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 94.46  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  826 GVTfqMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTY 905
Cdd:cd22731     1 GVT--IDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 755494468  906 VNGTHISEPTVLHHGDRVVLGGDHYFRFNHPVE 938
Cdd:cd22731    79 VNGREVTESCRLSQGAVIVLGKTHKFRFNHPAE 111
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
838-936 4.07e-21

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


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 89.95  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  838 LVNLNEDPQLSEMLLYMVKeGVTTVGKHTpssSHDIQLSGVLIADDHCTIR-NFGGTVSIVPAGEAKTYVNGTHISEPTV 916
Cdd:cd22729     4 LVNLNADPALNELLVYYLK-DHTRVGADT---SQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
                          90       100
                  ....*....|....*....|
gi 755494468  917 LHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLP 99
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
835-936 5.52e-21

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


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 89.69  E-value: 5.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  835 LPNLVNLNEDPQLSEML-LYMVKEGVTTVG--KHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPA-GEAKTYVNGTH 910
Cdd:cd22711     1 LPYLLELSPDGSDRDKPrRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPAsQDAETYVNGQR 80
                          90       100
                  ....*....|....*....|....*.
gi 755494468  911 ISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22711    81 IYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
821-943 2.89e-18

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


Pssm-ID: 438765  Cd Length: 120  Bit Score: 82.37  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  821 ELQKAGVTFQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKhtpSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAG 900
Cdd:cd22713     2 ELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGT---AASDIISLQGPGVEPEHCYIENINGTVTLYPCG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 755494468  901 EAKTyVNGTHISEPTVLHHGDRVVLGGDHYFRFNHPVEVQKGK 943
Cdd:cd22713    79 NLCS-VDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
388-541 3.71e-18

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 82.65  E-value: 3.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   388 KVENS------QVTVAVRVRPFSKREKtekasQVVFTNGEEITVEHPDMKQVYSFiydvsfwsfDECHPGYASQTTVYET 461
Cdd:pfam16796   10 KLENSiqelkgNIRVFARVRPELLSEA-----QIDYPDETSSDGKIGSKNKSFSF---------DRVFPPESEQEDVFQE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   462 LAApLLDRAFEGYNTCLFAYGQTGSGksytmmglnEEPGIIPRFCEDLFAQIAKKQTSEvSYHLEMSFFEVYNEKIHDLL 541
Cdd:pfam16796   76 ISQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGW-KYTIELQFVEIYNESSQDLL 144
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
838-933 1.16e-14

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


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 71.15  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  838 LVNLNEDPQLSEmllYMVKEGVTTVGKhtpSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAG-EAKTYVNGTHISEPTV 916
Cdd:cd00060     2 LIVLDGDGGGRE---FPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGsTNGTFVNGKRITPPVP 75
                          90
                  ....*....|....*..
gi 755494468  917 LHHGDRVVLgGDHYFRF 933
Cdd:cd00060    76 LQDGDVIRL-GDTTFRF 91
Kinesin_assoc pfam16183
Kinesin-associated;
740-859 5.58e-14

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 71.80  E-value: 5.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   740 AKVNEDMNAKLIRELKAEIEKLKAAQRS----------------NRNIDPERYRLCRQEITSLRMK-------------- 789
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAqglgdiidtiahptkkRANTPAANASAATAAMAGASPSpslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   790 ------------------LHQQERDMAEIQRVWKEKFEQAEKRKLQETKELQKAGVTFQMDN---------HLPNLVNLN 842
Cdd:pfam16183   81 slherimftpgseeaierLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGgtlgvfspkKTPHLVNLN 160
                          170
                   ....*....|....*..
gi 755494468   843 EDPQLSEMLLYMVKEGV 859
Cdd:pfam16183  161 EDPLMSECLLYYIKDGI 177
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
834-936 3.20e-10

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


Pssm-ID: 438785  Cd Length: 113  Bit Score: 59.04  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  834 HLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIR-------NFGGTVSIVPAGEAKTYV 906
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvrlpkhRSEEKLVLEPIPGAHVSV 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 755494468  907 NGTHISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
855-933 5.35e-10

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


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 57.99  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  855 VKEGVTTVGKhtpSSSHDIQLSGVLIADDHCTIR-NFGGTVSIVPAGEAK-TYVNGTHISEPTVLHHGDRVVLgGDHYFR 932
Cdd:cd22673    18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENLSTTNpTLVNGKAIEKSAELKDGDVITI-GGRSFR 93

                  .
gi 755494468  933 F 933
Cdd:cd22673    94 F 94
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
855-933 1.90e-09

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 56.12  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  855 VKEGVTTVGKHTPSsshDIQLSGVLIADDHCTIRNFGGTVSIVPAGEA-KTYVNGTHISEPTVLHHGDRVVLgGDHYFRF 933
Cdd:COG1716    18 LDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDLGSTnGTFVNGQRVTEPAPLRDGDVIRL-GKTELRF 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
937-1109 1.15e-08

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: 60.46  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   937 VEVQKGKKLSSRNNLTtsegpKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKI 1016
Cdd:TIGR02168  300 LEQQKQILRERLANLE-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1017 QALEAELreESQRKRLEELNNQKASH---------KIEELERAKQHLEQEV--------YVNKRRLEMETLATKQALEDH 1079
Cdd:TIGR02168  375 EELEEQL--ETLRSKVAQLELQIASLnneierleaRLERLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEEL 452
                          170       180       190
                   ....*....|....*....|....*....|
gi 755494468  1080 RIRHARILEALEIEKQKIAEEVQMLQENRG 1109
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAER 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
963-1113 2.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  963 AKNELLTAQRSRLEAEIKDAQ------LKAKEEMMQGIQIAKEMaQQELSSQKAVYERKIQALEAELREESQRKRLEELN 1036
Cdd:COG1196   267 AELEELRLELEELELELEEAQaeeyelLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEE 345
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468 1037 NQKASHKIEELERAKQHLEQEVyvnkRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDK 1113
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEAL----LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
968-1108 2.35e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  968 LTAQRSRLEAEI---KDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREEsqRKRLEELNNQ--KASH 1042
Cdd:COG1196   218 LKEELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL--ELELEEAQAEeyELLA 295
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468 1043 KIEELERAKQHLEQEVYVNKRRLEmETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENR 1108
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
963-1108 2.78e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  963 AKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEmaQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKASH 1042
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEE--LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468 1043 KIEELERAKQHLEQEVyVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENR 1108
Cdd:COG1196   366 ALLEAEAELAEAEEEL-EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
966-1114 4.66e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  966 ELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAvyERKIQALEAELREESQRKRLEELNNQKASHKIE 1045
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA--EEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494468 1046 ELERAKQHLEQEVYVNKRRLEmETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDKT 1114
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
860-925 5.83e-08

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 51.04  E-value: 5.83e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494468   860 TTVGKHtpsSSHDIQLSGVLIADDHCTI-RNFGGTVSIVPAGE-AKTYVNGTHIS-EPTVLHHGDRVVL 925
Cdd:pfam00498    1 VTIGRS---PDCDIVLDDPSVSRRHAEIrYDGGGRFYLEDLGStNGTFVNGQRLGpEPVRLKDGDVIRL 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
968-1114 8.94e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 8.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  968 LTAQRSRLEAEIKDAQLKAKEemmqgiqIAKEMAQQELSSQKAVYERKIQALEAELREESQRkrLEELNNQKAShkIEEL 1047
Cdd:COG4717    93 LQEELEELEEELEELEAELEE-------LREELEKLEKLLQLLPLYQELEALEAELAELPER--LEELEERLEE--LREL 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494468 1048 ERAKQHLEQEVYVNKRRLEME----TLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDKT 1114
Cdd:COG4717   162 EEELEELEAELAELQEELEELleqlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
974-1106 8.99e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 52.23  E-value: 8.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   974 RLEAEIKDAQLkakEEMMQGIQIAKEMAQQELSSQkavyERKIQALEAELREesqrkrleelnnqkASHKIEELERAKQH 1053
Cdd:pfam20492    1 REEAEREKQEL---EERLKQYEEETKKAQEELEES----EETAEELEEERRQ--------------AEEEAERLEQKRQE 59
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468  1054 LEQEvyvnKRRLE---METLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:pfam20492   60 AEEE----KERLEesaEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQE 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
968-1106 2.10e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  968 LTAQRSRLEAEIKD--AQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKR--LEELNNQ-KASH 1042
Cdd:COG1196   321 LEEELAELEEELEEleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEelLEALRAAaELAA 400
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755494468 1043 KIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:COG1196   401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
968-1182 2.42e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.95  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   968 LTAQRSRLEAEIKD--AQLKAKEEMMQGIQ--IAKEMAQQElSSQKAVyeRKIQALEAELRE------------ESQRKR 1031
Cdd:pfam01576  220 LQEQIAELQAQIAElrAQLAKKEEELQAALarLEEETAQKN-NALKKI--RELEAQISELQEdleseraarnkaEKQRRD 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1032 L-EELNNQKAshkieELE------RAKQHL----EQEVYVNKRRLEMETLATKQALEDHRIRHARILEALeiekqkiAEE 1100
Cdd:pfam01576  297 LgEELEALKT-----ELEdtldttAAQQELrskrEQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------TEQ 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1101 VQMLQENRGNRDKT-FTIQPNWNSMK--LSTMIQEANAISDKFKKC-----YIFGRHDASDKGRSDTSVRVRNLQLGI-S 1171
Cdd:pfam01576  365 LEQAKRNKANLEKAkQALESENAELQaeLRTLQQAKQDSEHKRKKLegqlqELQARLSESERQRAELAEKLSKLQSELeS 444
                          250
                   ....*....|.
gi 755494468  1172 TFWSLEKFESK 1182
Cdd:pfam01576  445 VSSLLNEAEGK 455
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
836-936 8.23e-07

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


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 49.61  E-value: 8.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  836 PNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSS-SHDIQLSGVLIADDHCTIR-----------NFGGT----VSIVPA 899
Cdd:cd22712     4 PYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEGArKVDISLRAPDILPQHCWIRrkpeplsddedSDKESadyrVVLSPL 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755494468  900 GEAKTYVNGTHISEPTVLHHGDRVVLGGDHYFRFNHP 936
Cdd:cd22712    84 RGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
966-1106 1.40e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  966 ELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAvyERKIQALEAELRE--------ESQRKRLEELNN 1037
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL--ELELEEAQAEEYEllaelarlEQDIARLEERRR 312
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494468 1038 QkASHKIEELERAKQHLEQEvyvnKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:COG1196   313 E-LEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
963-1102 1.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  963 AKNELLTAQRSRLEAEikDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKASH 1042
Cdd:COG1196   349 AEEELEEAEAELAEAE--EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755494468 1043 KIEELERAKQHLE-----QEVYVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQ 1102
Cdd:COG1196   427 EEALAELEEEEEEeeealEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
968-1106 2.22e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   968 LTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQE---LSSQKAVYERKIQALEAELREESQRKRLEELNNQKASHKI 1044
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEAEEEleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494468  1045 EELERAKQHLEQEVYVNKRRLEmETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLE-ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
961-1106 2.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  961 EFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKA 1040
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468 1041 SHKIEELERAKQHLEQEVYVNKRRLEmETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLE-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
964-1100 2.83e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.80  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  964 KNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQE-----LSSQKAVYERKIQALEAELRE-------ESQRKR 1031
Cdd:COG2268   182 ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREaeeaeLEQEREIETARIAEAEAELAKkkaeerrEAETAR 261
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494468 1032 LEelnnQKASHKIEElERAKQHLEQEVYVNKRRLEMEtLATKQALEDHRIRHARILEALEIEKQKIAEE 1100
Cdd:COG2268   262 AE----AEAAYEIAE-ANAEREVQRQLEIAEREREIE-LQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
677-1187 4.98e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 51.66  E-value: 4.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   677 EQANGKRVfipYRESTLTWLLKESLGGNSKTAM------IATVSPAASNIEETLSTLRYATQARLIVnIAKVNEDMNAKL 750
Cdd:pfam15921  197 EEASGKKI---YEHDSMSTMHFRSLGSAISKILreldteISYLKGRIFPVEDQLEALKSESQNKIEL-LLQQHQDRIEQL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   751 IRELKAEI----EKLKAAQ------RSNRNIDPERYR----LCRQEITSLRMKLHQQERDMAEIQRVWKEKFEQAEKRKL 816
Cdd:pfam15921  273 ISEHEVEItgltEKASSARsqansiQSQLEIIQEQARnqnsMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   817 QETKELQKAGVtfQMDNHLPNLVNLneDPQLSEMLLYMVK-EGVTTVGKHTPSSSHDiQLSGVLIADDHCTiRNFGGTVS 895
Cdd:pfam15921  353 LANSELTEART--ERDQFSQESGNL--DDQLQKLLADLHKrEKELSLEKEQNKRLWD-RDTGNSITIDHLR-RELDDRNM 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   896 IVPAGEA-----KTYVNGT----------------HISEPTVLHHGDRVVLggdhyfrfNHPVEVQKGKKLSSRN----- 949
Cdd:pfam15921  427 EVQRLEAllkamKSECQGQmerqmaaiqgknesleKVSSLTAQLESTKEML--------RKVVEELTAKKMTLESsertv 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   950 -NLTTSEGPKDFEF-AKNELLTAQRSRLEAEIKDAQ-LKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREE 1026
Cdd:pfam15921  499 sDLTASLQEKERAIeATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1027 SQRKRleelnnQKASHKIEeleraKQHLEQEVyvNKRRLEMETLATKQALEDHRIR--HARILEaLEIEKQKI----AEE 1100
Cdd:pfam15921  579 GQHGR------TAGAMQVE-----KAQLEKEI--NDRRLELQEFKILKDKKDAKIRelEARVSD-LELEKVKLvnagSER 644
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1101 VQMLQENRGNRDKTFtiqpnwNSMKLSTmiQEANAISDKFKkcyIFGRHDASDKGRSDTSVRVRNLQLGiSTFWSLEKFE 1180
Cdd:pfam15921  645 LRAVKDIKQERDQLL------NEVKTSR--NELNSLSEDYE---VLKRNFRNKSEEMETTTNKLKMQLK-SAQSELEQTR 712

                   ....*..
gi 755494468  1181 SKLAAMK 1187
Cdd:pfam15921  713 NTLKSME 719
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
964-1075 5.91e-06

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 47.68  E-value: 5.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   964 KNELLTAQRSRLEAEIKDAQLKAKEEmmqgiqiakemaqQELSSQKAVYERKIQALEAELrEESQrKRLEELNNQ--KAS 1041
Cdd:pfam12718   43 KNQQLEEEVEKLEEQLKEAKEKAEES-------------EKLKTNNENLTRKIQLLEEEL-EESD-KRLKETTEKlrETD 107
                           90       100       110
                   ....*....|....*....|....*....|....
gi 755494468  1042 HKIEELERAKQHLEQEVYVNKRRleMETLATKQA 1075
Cdd:pfam12718  108 VKAEHLERKVQALEQERDEWEKK--YEELEEKYK 139
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
971-1102 9.28e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.51  E-value: 9.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   971 QRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEE---------LNNQKAS 1041
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEqerqqqverLRQQEEE 471
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755494468  1042 HKIEELERAKQHLEQEVYVNKRR--LEMETLATKQA-LEDHRIRhaRILEALEIEKQK-IAEEVQ 1102
Cdd:pfam17380  472 RKRKKLELEKEKRDRKRAEEQRRkiLEKELEERKQAmIEEERKR--KLLEKEMEERQKaIYEEER 534
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
963-1108 1.72e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   963 AKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAEL--REESQRKRLEELNNQKA 1040
Cdd:TIGR02169  707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeLEEDLHKLEEALNDLEA 786
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494468  1041 S---HKIEELERAKQHLEQEVyvnkRRLEMetlatkqaledhRIRHA-RILEALEIEKQKIAEEVQMLQENR 1108
Cdd:TIGR02169  787 RlshSRIPEIQAELSKLEEEV----SRIEA------------RLREIeQKLNRLTLEKEYLEKEIQELQEQR 842
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
940-1108 1.88e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   940 QKGKKLSSRNNLTTSEGPKDFE-------FAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQ-QELSSQKAV 1011
Cdd:pfam17380  307 EKAREVERRRKLEEAEKARQAEmdrqaaiYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRmRELERLQME 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1012 YERKIQALEAELREESQRKRLEELNNQKASHKIEELERAKQhlEQEvyvNKRRLEMETLATKQALEDHRIRHArilealE 1091
Cdd:pfam17380  387 RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA--EQE---EARQREVRRLEEERAREMERVRLE------E 455
                          170
                   ....*....|....*..
gi 755494468  1092 IEKQKIAEEVQMLQENR 1108
Cdd:pfam17380  456 QERQQQVERLRQQEEER 472
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
955-1101 2.19e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.61  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  955 EGPKDFEFAKNEL--LTAQRSRLEAEIKDA--QLKAKEEMMQGIQIAKEMAQQELSSQKAvyERKIQALEAELreESQRK 1030
Cdd:COG1579    28 ELPAELAELEDELaaLEARLEAAKTELEDLekEIKRLELEIEEVEARIKKYEEQLGNVRN--NKEYEALQKEI--ESLKR 103
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755494468 1031 RLEELNNQ--KASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRhariLEALEIEKQKIAEEV 1101
Cdd:COG1579   104 RISDLEDEilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE----LEELEAEREELAAKI 172
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
336-675 2.85e-05

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 48.97  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  336 LSTLKNRIASPRVKPRPKSSLFankressRESTLppeenslvqkTFTEPDSLKvENSQVTVAVRVRP------------- 402
Cdd:COG5059   267 LLTLGNVINALGDKKKSGHIPY-------RESKL----------TRLLQDSLG-GNCNTRVICTISPssnsfeetintlk 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  403 FSKREKTEKASQVVftngeEITVEHPDmkQVYSFIYDVSFwsfdechpgYASQTTVYETLAAPLL-DRAFEGYntclFAY 481
Cdd:COG5059   329 FASRAKSIKNKIQV-----NSSSDSSR--EIEEIKFDLSE---------DRSEIEILVFREQSQLsQSSLSGI----FAY 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  482 GQTGSGKSYTMMglNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLVCK-GENGQRKQPLRAREHP 560
Cdd:COG5059   389 MQSLKKETETLK--SRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEElSKKKTKIHKLNKLRHD 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  561 VSGpyveglSMNVVSSY-SDIQSWLELGNKQRaTAATGMNDKSSRSHSVFTLVMTQ-TKTEVVEgeehdhritsRINLVD 638
Cdd:COG5059   467 LSS------LLSSIPEEtSDRVESEKASKLRS-SASTKLNLRSSRSHSKFRDHLNGsNSSTKEL----------SLNQVD 529
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 755494468  639 LAGSERCSTaHSSGQRLKEGVSINKSLLTLGKVISAL 675
Cdd:COG5059   530 LAGSERKVS-QSVGELLRETQSLNKSLSSLGDVIHAL 565
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
966-1107 4.11e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   966 ELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAvyERKIQALEAELREESQRKRLEELNNQKASHKIE 1045
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL--ESELEALLNERASLEEALALLRSELEELSEELR 904
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494468  1046 ELERAKQHLEQevyvnkrrlemETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQEN 1107
Cdd:TIGR02168  905 ELESKRSELRR-----------ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
PRK12704 PRK12704
phosphodiesterase; Provisional
971-1081 4.31e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  971 QRSRLEAEI--KDAQLKAKEEMMQgiqiAKEMAQQELSSQkavyERKIQALEAEL--REESQRKRLEELNnqKASHKIEE 1046
Cdd:PRK12704   45 EEAKKEAEAikKEALLEAKEEIHK----LRNEFEKELRER----RNELQKLEKRLlqKEENLDRKLELLE--KREEELEK 114
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755494468 1047 LERAKQHLEQEvyVNKRRLEMETLATKQALEDHRI 1081
Cdd:PRK12704  115 KEKELEQKQQE--LEKKEEELEELIEEQLQELERI 147
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
958-1112 4.82e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 4.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   958 KDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQI----------AKEMAQQELSSQKAVYERKIQALEAELREES 1027
Cdd:pfam13868   39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeqieereqKRQEEYEEKLQEREQMDEIVERIQEEDQAEA 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1028 QRKRLEELNNQKASHKIEELERAKQHLEQEvyvnKRRLE----METLATKQALEDHRIRH-ARILEALEIEKQKIAEEVQ 1102
Cdd:pfam13868  119 EEKLEKQRQLREEIDEFNEEQAEWKELEKE----EEREEderiLEYLKEKAEREEEREAErEEIEEEKEREIARLRAQQE 194
                          170
                   ....*....|
gi 755494468  1103 MLQENRGNRD 1112
Cdd:pfam13868  195 KAQDEKAERD 204
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
966-1108 5.79e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  966 ELLTAQRSRLEAEIKD--AQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELRE------------------ 1025
Cdd:COG4942    58 AALERRIAALARRIRAleQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedfldavrr 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1026 --------ESQRKRLEELNNQKashkiEELERAKQHLEQEVyVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKI 1097
Cdd:COG4942   138 lqylkylaPARREQAEELRADL-----AELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
                         170
                  ....*....|.
gi 755494468 1098 AEEVQMLQENR 1108
Cdd:COG4942   212 AAELAELQQEA 222
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
958-1119 6.22e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  958 KDFEFAKNEL--LTAQRSRLEAEIKDA---------QLKAKEEMMQGIQIAKEMAQQELSS---QKAVYERKIQALEAEL 1023
Cdd:COG4372    45 EELEQLREELeqAREELEQLEEELEQArseleqleeELEELNEQLQAAQAELAQAQEELESlqeEAEELQEELEELQKER 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1024 RE-ESQRKRLEElNNQKASHKIEELERAKQHLEQEVYVNKRRLEmETLATKQALEDHRIRHAriLEALEIEKQKIAEEVQ 1102
Cdd:COG4372   125 QDlEQQRKQLEA-QIAELQSEIAEREEELKELEEQLESLQEELA-ALEQELQALSEAEAEQA--LDELLKEANRNAEKEE 200
                         170
                  ....*....|....*..
gi 755494468 1103 MLQENRGNRDKTFTIQP 1119
Cdd:COG4372   201 ELAEAEKLIESLPRELA 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
954-1114 6.66e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   954 SEGPKDFEFAKN--ELLTAQRSRLEAEIKD--AQLKAKEEMMQGIQIAKEMAQQELSSQKAVYE----------RKIQAL 1019
Cdd:TIGR02168  729 SALRKDLARLEAevEQLEERIAQLSKELTEleAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeelkalrEALDEL 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1020 EAELREE-----SQRKRLEELNNQKASHK--IEEL-ERAKQHLEQEVYVNKRRLEMETLATKQALEdhrirhariLEALE 1091
Cdd:TIGR02168  809 RAELTLLneeaaNLRERLESLERRIAATErrLEDLeEQIEELSEDIESLAAEIEELEELIEELESE---------LEALL 879
                          170       180
                   ....*....|....*....|...
gi 755494468  1092 IEKQKIAEEVQMLQENRGNRDKT 1114
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEE 902
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
970-1141 6.96e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  970 AQRSRLEAEIKDA--QLKAKEEMMQGIQIAKEMAQQELSS-QKAVYERKIQALEAELREESQRKRLEELNNQ--KASHKI 1044
Cdd:COG4372    38 FELDKLQEELEQLreELEQAREELEQLEEELEQARSELEQlEEELEELNEQLQAAQAELAQAQEELESLQEEaeELQEEL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1045 EELERAKQHLEQEvyvnKRRLEmetlATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDKTFTIQpnwnsm 1124
Cdd:COG4372   118 EELQKERQDLEQQ----RKQLE----AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ------ 183
                         170
                  ....*....|....*..
gi 755494468 1125 KLSTMIQEANAISDKFK 1141
Cdd:COG4372   184 ALDELLKEANRNAEKEE 200
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
970-1106 7.58e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 7.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  970 AQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAvyERKIQALEAELREesQRKRLEELNNQkashkIEELER 1049
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAA--LEAELAELEKE-----IAELRA 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755494468 1050 AKQHLEQEV-------YVNKRRLEMETLATKQALEDHrIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:COG4942    98 ELEAQKEELaellralYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLA 160
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
960-1110 8.63e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  960 FEFAKNELLTAQRSRLEAEIK--DAQLKAKEEMMQGIQIAKEMAQQELSSQKAvyeRKIQALEAELREESQRKRLEELNN 1037
Cdd:COG4913   285 FAQRRLELLEAELEELRAELArlEAELERLEARLDALREELDELEAQIRGNGG---DRLEQLEREIERLERELEERERRR 361
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468 1038 QKASHKIEELErAKQHLEQEVYVNKRRLEMETLAT----KQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGN 1110
Cdd:COG4913   362 ARLEALLAALG-LPLPASAEEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
959-1056 9.29e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 43.75  E-value: 9.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   959 DFEFAKNELLTAQRS--RLEAEIKDAQLKAKEemMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQR-KRLEEL 1035
Cdd:pfam20492   21 ETKKAQEELEESEETaeELEEERRQAEEEAER--LEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEiARLEEE 98
                           90       100
                   ....*....|....*....|.
gi 755494468  1036 NNQKAshkiEELERAKQHLEQ 1056
Cdd:pfam20492   99 VERKE----EEARRLQEELEE 115
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
965-1108 9.79e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 9.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   965 NELLTAQRS--RLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKavyERKIQALEAELREESQRKR-LEELNNQKAS 1041
Cdd:pfam13868  136 NEEQAEWKEleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK---EREIARLRAQQEKAQDEKAeRDELRAKLYQ 212
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468  1042 HKIEELERAKQHLEQEvyvnkRRLEMEtLATKQALEDHrIRHARILEALEIEKQKiAEEVQMLQENR 1108
Cdd:pfam13868  213 EEQERKERQKEREEAE-----KKARQR-QELQQAREEQ-IELKERRLAEEAEREE-EEFERMLRKQA 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
963-1132 1.07e-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: 47.36  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   963 AKNELLTAQRSRLEAEIKDAQlkaKEEMMQGIQIAK-EMAQQELSSQKAVYERKIQALEAELREESQRK----------- 1030
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQ---KELYALANEISRlEQQKQILRERLANLERQLEELEAQLEELESKLdelaeelaele 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1031 -RLEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHARI-LEALEIEKQKIAEEVQML-QEN 1107
Cdd:TIGR02168  344 eKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeIERLEARLERLEDRRERLqQEI 423
                          170       180
                   ....*....|....*....|....*
gi 755494468  1108 RGNRDKTFTIQPNWNSMKLSTMIQE 1132
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEE 448
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
751-1102 1.50e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  751 IRELKAEIEKLKAAQRSNRNidpERYRLCRQEITSLRMKLHQQERDMAEIQRvwKEKFEQAEKRKLQETKELQKAgvtfQ 830
Cdd:COG4717   158 LRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEE----E 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  831 MDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTV--GKHTPSSSHDIQLSGVLIAddhctirnFGGTVSIVPAGEAKTYVNG 908
Cdd:COG4717   229 LEQLENELEAAALEERLKEARLLLLIAAALLAllGLGGSLLSLILTIAGVLFL--------VLGLLALLFLLLAREKASL 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  909 THISEPTVLHHGDRVVlggdhyfrfnhpvEVQKGKKLSSRNNLTTSEGPKDFEFAKNELLTAQRSRLEAEIKDAQL---- 984
Cdd:COG4717   301 GKEAEELQALPALEEL-------------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlee 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  985 --KAKEEMMQGIQIAKEMA----------QQELSSQKAVYERKIQALEAELREESQRKRLEELNN--QKASHKIEELERA 1050
Cdd:COG4717   368 leQEIAALLAEAGVEDEEElraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEE 447
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755494468 1051 KQHLEQEVyvNKRRLEMETLATKQALedhrirhARILEALEIEKQKIAEEVQ 1102
Cdd:COG4717   448 LEELREEL--AELEAELEQLEEDGEL-------AELLQELEELKAELRELAE 490
PTZ00121 PTZ00121
MAEBL; Provisional
972-1099 1.68e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  972 RSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKA-----VYERKIQALEAELREESQRKRLEELNNQKAshkiEE 1046
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEA----EE 1714
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755494468 1047 LERAKQhLEQEVYVNKRRLEMetlATKQALEDHriRHARILEALEIEKQKIAE 1099
Cdd:PTZ00121 1715 KKKAEE-LKKAEEENKIKAEE---AKKEAEEDK--KKAEEAKKDEEEKKKIAH 1761
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
969-1099 1.79e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   969 TAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQ---ELSSQKAVYERKiQALEAELREESQRKRLEELNNQKASHKIE 1045
Cdd:TIGR02794   49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQraaEQARQKELEQRA-AAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468  1046 ELERAKQHLEQEvyvNKRRLEMEtlATKQALEDHRIRHARI--LEALEIEKQKIAE 1099
Cdd:TIGR02794  128 QAAEAKAKAEAE---AERKAKEE--AAKQAEEEAKAKAAAEakKKAEEAKKKAEAE 178
PTZ00121 PTZ00121
MAEBL; Provisional
955-1199 1.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  955 EGPKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSS----QKAVYERKIQALEAELREESQRK 1030
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeelKKAEEENKIKAAEEAKKAEEDKK 1675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1031 RLEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQAL---EDHRIRHARILEALEIEKQKIAEEvqmLQEN 1107
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaEEENKIKAEEAKKEAEEDKKKAEE---AKKD 1752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1108 RGNRDKTFTIQPNWNSMKLSTMIQEANAISDKFKKcYIFGRHDASDKGRSDTSVRVRNLQLG--ISTFWSLEKFESKLAA 1185
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE-EDEKRRMEVDKKIKDIFDNFANIIEGgkEGNLVINDSKEMEDSA 1831
                         250
                  ....*....|....
gi 755494468 1186 MKELYESNGGDRDE 1199
Cdd:PTZ00121 1832 IKEVADSKNMQLEE 1845
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
972-1102 1.89e-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: 46.60  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   972 RSRLEAEIKDAQLKAKEEMMQ----GIQIAKEMAQQELSSQK-AVYERKIQALEAELREESQRKRLEELNNQ--KASHKI 1044
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRerleGLKRELSSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEeeKLKERL 739
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1045 EELERAKQHLEQEVYVNKR----------RLEMETLATKQALED--HRIRHARILEaLEIEKQKIAEEVQ 1102
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSelkelearieELEEDLHKLEEALNDleARLSHSRIPE-IQAELSKLEEEVS 808
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
972-1097 2.67e-04

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 43.12  E-value: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   972 RSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQkAVYERKIQALEAELREESQRKRLEELNNQkASHKIEELERAK 1051
Cdd:pfam15346   21 AKRVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEE-LEREREAELEEERRKEEEERKKREELERI-LEENNRKIEEAQ 98
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 755494468  1052 QHLEQEvyvnkrRLEMetLATKQALEDHRIRHARILEALEIEKQKI 1097
Cdd:pfam15346   99 RKEAEE------RLAM--LEEQRRMKEERQRREKEEEEREKREQQK 136
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
860-911 2.93e-04

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 40.24  E-value: 2.93e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 755494468    860 TTVGKHtpSSSHDIQLSGVLIADDHCTIRNFGGT-VSIVPAG-EAKTYVNGTHI 911
Cdd:smart00240    1 VTIGRS--SEDCDIQLDGPSISRRHAVIVYDGGGrFYLIDLGsTNGTFVNGKRI 52
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
970-1082 3.00e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   970 AQRSRLEAEIKDAQLKAKEEMMQgiQIAKEMAQQELSSQKAVyeRKIQALEAELREESQRKRLEELNNQKASHK-IEELE 1048
Cdd:pfam13868  228 EKKARQRQELQQAREEQIELKER--RLAEEAEREEEEFERML--RKQAEDEEIEQEEAEKRRMKRLEHRRELEKqIEERE 303
                           90       100       110
                   ....*....|....*....|....*....|....
gi 755494468  1049 RAKQHLEQEVYVNKRRLEMETLATKQALEDHRIR 1082
Cdd:pfam13868  304 EQRAAEREEELEEGERLREEEAERRERIEEERQK 337
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
963-1108 3.79e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   963 AKNELLTAQRSRLEAEIKDAQlKAKEEMMQGIQIAKEMAQQELSsqkavYERKIQALEAELREESQRKRLEElnnQKASH 1042
Cdd:pfam13868  128 LREEIDEFNEEQAEWKELEKE-EEREEDERILEYLKEKAEREEE-----REAEREEIEEEKEREIARLRAQQ---EKAQD 198
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468  1043 KIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHARiLEALEIEKQKIAEEVQMLQENR 1108
Cdd:pfam13868  199 EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR-EEQIELKERRLAEEAEREEEEF 263
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
972-1113 5.35e-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: 45.06  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   972 RSRLEAEIKDaqlKAKEEMmqgIQIAKEMAqqELSSQKAVYERKIQALEAELR--EESQRKRLEELNNQKASH-----KI 1044
Cdd:TIGR02169  274 LEELNKKIKD---LGEEEQ---LRVKEKIG--ELEAEIASLERSIAEKERELEdaEERLAKLEAEIDKLLAEIeelerEI 345
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494468  1045 EELERAKQHLEQEvyVNKRRLEMETLatKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDK 1113
Cdd:TIGR02169  346 EEERKRRDKLTEE--YAELKEELEDL--RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
964-1193 5.77e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   964 KNELltaQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELreESQRKRLEELNNQKASHK 1043
Cdd:pfam05483  547 RDEL---ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--ENKNKNIEELHQENKALK 621
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1044 IEELERAKQHLEQEVYVNKrrLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVqmlQENRGNRDKTFTIQPNWNs 1123
Cdd:pfam05483  622 KKGSAENKQLNAYEIKVNK--LELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV---EKAKAIADEAVKLQKEID- 695
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1124 MKLSTMIQEANAISDKFKKCYifgrhdasdkgrsDTSVRVRNLQLGIstFWSLEKFESKLAAMKELYESN 1193
Cdd:pfam05483  696 KRCQHKIAEMVALMEKHKHQY-------------DKIIEERDSELGL--YKNKEQEQSSAKAALEIELSN 750
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
947-1107 6.36e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  947 SRNNLTTSEGpkdfefaKNELLTAQRSRLEAEIKDAQ--LKAKEEMMQGIQIAKEMAQQEL-----SSQKAVYERKIQAL 1019
Cdd:COG3206   203 QKNGLVDLSE-------EAKLLLQQLSELESQLAEARaeLAEAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAEL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1020 EAELREESQR------------KRLEELNNQKAshkiEELERAKQHLEQEVYVNKRRLEmetlATKQALEDHRIRhARIL 1087
Cdd:COG3206   276 EAELAELSARytpnhpdvialrAQIAALRAQLQ----QEAQRILASLEAELEALQAREA----SLQAQLAQLEAR-LAEL 346
                         170       180
                  ....*....|....*....|
gi 755494468 1088 EALEIEKQKIAEEVQMLQEN 1107
Cdd:COG3206   347 PELEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
966-1106 6.67e-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: 44.66  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   966 ELLTAQRSRLEAEIKDA--QLKAKEEMMQGIQIAKEMAQQELSSQKAVYER---KIQALEAELREESqrKRLEELNNQ-- 1038
Cdd:TIGR02168  687 EELEEKIAELEKALAELrkELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEERIAQLS--KELTELEAEie 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1039 -------KASHKIEELERAKQHLEQEvyVNKRRLEMETL-----ATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:TIGR02168  765 eleerleEAEEELAEAEAEIEELEAQ--IEQLKEELKALrealdELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
963-1106 7.17e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   963 AKNELLTAQRSRLEAEIKDAQlKAKEEMMQGIQIAKEMAQQELssQKAVYERKIQALEAElREESQRKRLeeLNNQKASH 1042
Cdd:pfam13868  201 AERDELRAKLYQEEQERKERQ-KEREEAEKKARQRQELQQARE--EQIELKERRLAEEAE-REEEEFERM--LRKQAEDE 274
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755494468  1043 KIEELERAKQHLEQEVYvnkrRLEMEtlatKQALEDHRIRHARILEALEiEKQKIAEEVQMLQE 1106
Cdd:pfam13868  275 EIEQEEAEKRRMKRLEH----RRELE----KQIEEREEQRAAEREEELE-EGERLREEEAERRE 329
FHA_EmbR-like cd22669
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ...
852-933 8.45e-04

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


Pssm-ID: 438721 [Multi-domain]  Cd Length: 89  Bit Score: 40.09  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  852 LYMVKEGVTTVGKHtpsSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAK-TYVNGTHISEPTVLHHGDRVVLgGDHY 930
Cdd:cd22669    10 GYPLQAAATRIGRL---HDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNgVHVQHERIRSAVTLNDGDHIRI-CDHE 85

                  ...
gi 755494468  931 FRF 933
Cdd:cd22669    86 FTF 88
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
971-1099 8.52e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.64  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  971 QRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQ---KAVYERKIQALEAELREESQRKRLEELNNQKASHKIEEL 1047
Cdd:PRK09510   63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQerlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755494468 1048 ERAKQHLEQEvyvnKRRLEmetLATKQALEDhrirhARILEALEIEKQKIAE 1099
Cdd:PRK09510  143 AAAKAKAEAE----AKRAA---AAAKKAAAE-----AKKKAEAEAAKKAAAE 182
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
1020-1106 9.37e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.56  E-value: 9.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1020 EAELREESQRKRLEELNNQKASHKIEELERAkQHLEQEvyvnkRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAE 1099
Cdd:pfam05672   33 ERLEKEEEERLRKEELRRRAEEERARREEEA-RRLEEE-----RRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEA 106

                   ....*..
gi 755494468  1100 EVQMLQE 1106
Cdd:pfam05672  107 EAKAREE 113
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
966-1106 1.02e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  966 ELLTAQRSRLEAEIKDAQLKAKEEMMQGIQ---------IAKEM-AQQELSSQKAVYERKIQALEA---ELREESQRKRL 1032
Cdd:PRK04778  259 QDLKEQIDENLALLEELDLDEAEEKNEEIQeridqlydiLEREVkARKYVEKNSDTLPDFLEHAKEqnkELKEEIDRVKQ 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1033 E-ELNNqkashkiEELERAKQHLEQEvyvnkRRLEMETLATKQALEDHRIRHARILEALE--------IEKQ--KIAEEV 1101
Cdd:PRK04778  339 SyTLNE-------SELESVRQLEKQL-----ESLEKQYDEITERIAEQEIAYSELQEELEeilkqleeIEKEqeKLSEML 406

                  ....*
gi 755494468 1102 QMLQE 1106
Cdd:PRK04778  407 QGLRK 411
mukB PRK04863
chromosome partition protein MukB;
969-1108 1.11e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  969 TAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAvyerkiqalEAELREESQRKRLEELNNQkashkIEELE 1048
Cdd:PRK04863  534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS---------EARERRMALRQQLEQLQAR-----IQRLA 599
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755494468 1049 -RAKQHLEQEVYVNKRRlEM--ETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENR 1108
Cdd:PRK04863  600 aRAPAWLAAQDALARLR-EQsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1008-1111 1.39e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1008 QKAVYERKIQALEAELREESQRKRLEELNNQ-KASHKIEELERAKQ---------HLEQEVYVNKRRLEMETLATKQ-AL 1076
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREvERRRKLEEAEKARQaemdrqaaiYAEQERMAMERERELERIRQEErKR 360
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 755494468  1077 EDHRIRHARIleALEIEKQKIAEEVQMLQENRGNR 1111
Cdd:pfam17380  361 ELERIRQEEI--AMEISRMRELERLQMERQQKNER 393
PTZ00121 PTZ00121
MAEBL; Provisional
938-1108 1.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  938 EVQKGKKLSSRNNLTTSEGPKDFEFAKNELLtaqrsRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKavyERKIQ 1017
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMAL-----RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE---EAKIK 1621
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1018 ALEAElREESQRKRLEELNNQKAshkiEELERAKQhLEQEVYVNKRRLEMEtlaTKQALEDHriRHARILEALEIEKQKI 1097
Cdd:PTZ00121 1622 AEELK-KAEEEKKKVEQLKKKEA----EEKKKAEE-LKKAEEENKIKAAEE---AKKAEEDK--KKAEEAKKAEEDEKKA 1690
                         170
                  ....*....|.
gi 755494468 1098 AEEVQMLQENR 1108
Cdd:PTZ00121 1691 AEALKKEAEEA 1701
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
747-838 1.57e-03

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: 41.82  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   747 NAKLIRELKAEIEKLKAAQRSNRNIDPERyrlcRQEITSLRMKLHQQERDMAEIQRvwKEKFEQAEKRKLQETKELQKag 826
Cdd:pfam13851   24 NLELIKSLKEEIAELKKKEERNEKLMSEI----QQENKRLTEPLQKAQEEVEELRK--QLENYEKDKQSLKNLKARLK-- 95
                           90
                   ....*....|..
gi 755494468   827 vtfQMDNHLPNL 838
Cdd:pfam13851   96 ---VLEKELKDL 104
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
940-1075 1.78e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  940 QKGKKLSSRNNLTTSEGPKDF-----------EFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQ 1008
Cdd:COG3883    97 RSGGSVSYLDVLLGSESFSDFldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468 1009 KAVYERKIQALEAELREESQRKrlEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQA 1075
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQL--AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
968-1113 1.82e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  968 LTAQRSRLEAEIKDAQlKAKEemmqgIQIAKEMAQQELSSqkavyeRKIQALEAELREESQRKRLEELNNQKASHKIEEL 1047
Cdd:COG1196   198 LERQLEPLERQAEKAE-RYRE-----LKEELKELEAELLL------LKLRELEAELEELEAELEELEAELEELEAELAEL 265
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494468 1048 ERAKQHLEQEVYvnkrRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDK 1113
Cdd:COG1196   266 EAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
981-1105 2.04e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 42.27  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   981 DAQLKAKEEMMQGIQIAKEMAQQELssqkavyerkiQALEAELREESQRkrleeLNNQKASHK------IEELERAKQHL 1054
Cdd:pfam02841  196 DQALTAKEKAIEAERAKAEAAEAEQ-----------ELLREKQKEEEQM-----MEAQERSYQehvkqlIEKMEAEREQL 259
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755494468  1055 --EQEVYVNKRRLEMETLatkqaledhrirharILEALEIEKQKIAEEVQMLQ 1105
Cdd:pfam02841  260 laEQERMLEHKLQEQEEL---------------LKEGFKTEAESLQKEIQDLK 297
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
949-1099 2.12e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   949 NNLTTSEGPKDFEFAKNEL--LTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMaqQELSSQKAVYERKIQALEAELreE 1026
Cdd:TIGR02169  782 NDLEARLSHSRIPEIQAELskLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEI--E 857
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1027 SQRKRLEELNNQKASHK--IEELERAKQHLEQEvyVNKRRLEMETLATKQ-----ALEDHRIRHARILEALEIEKQKIAE 1099
Cdd:TIGR02169  858 NLNGKKEELEEELEELEaaLRDLESRLGDLKKE--RDELEAQLRELERKIeeleaQIEKKRKRLSELKAKLEALEEELSE 935
PTZ00121 PTZ00121
MAEBL; Provisional
938-1108 2.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  938 EVQKGKKLSSRNNLTTSEGPKDFEFAKNELLTAQRSRLEAEI-KDAQLKAKEEMMQGIQIAKEMAQQELSS--------- 1007
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeakikae 1623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1008 --QKAVYERKIQALEAELREESQRKRlEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHAR 1085
Cdd:PTZ00121 1624 elKKAEEEKKKVEQLKKKEAEEKKKA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
                         170       180
                  ....*....|....*....|....*.
gi 755494468 1086 ILEAL---EIEKQKIAEEVQMLQENR 1108
Cdd:PTZ00121 1703 KAEELkkkEAEEKKKAEELKKAEEEN 1728
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
961-1106 2.39e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   961 EFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQE----LSSQKAVYERKIQALEAE-------LR---EE 1026
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRevrrLEEERAREMERVRLEEQErqqqverLRqqeEE 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1027 SQRKRLEELNNQKASHKIEELERakQHLEQEVYVNKRRL------------EMETLATKQALEDHRirhaRILEAlEIEK 1094
Cdd:pfam17380  472 RKRKKLELEKEKRDRKRAEEQRR--KILEKELEERKQAMieeerkrkllekEMEERQKAIYEEERR----REAEE-ERRK 544
                          170
                   ....*....|..
gi 755494468  1095 QKIAEEVQMLQE 1106
Cdd:pfam17380  545 QQEMEERRRIQE 556
PTZ00121 PTZ00121
MAEBL; Provisional
970-1108 2.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  970 AQRSRLEAEIKDAQLKAKEEMMQGIQIAK--EMAQQELSSQKAVYERKIQaleaELREESQRKRLEELNNQKASHKIEEL 1047
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkaEEAKKADEAKKAEEAKKAD----EAKKAEEKKKADELKKAEELKKAEEK 1563
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755494468 1048 ERAKQhleqevyvNKRRLEMETLATKQALEDHRIRHARILEAL---EIEKQKIAEEVQMLQENR 1108
Cdd:PTZ00121 1564 KKAEE--------AKKAEEDKNMALRKAEEAKKAEEARIEEVMklyEEEKKMKAEEAKKAEEAK 1619
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
964-1100 2.61e-03

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


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 41.18  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   964 KNELLT---AQRSRLEaeikDAQLKAKEEMMQGIQiakEMAQQELSSQKAvYERKIQALEaELREESQRKRLEELNNQKA 1040
Cdd:pfam15665   69 KRQALTefeQYKRRVE----ERELKAEAEHRQRVV---ELSREVEEAKRA-FEEKLESFE-QLQAQFEQEKRKALEELRA 139
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1041 SHKIEELERAKQHLEQEVYVNKRRLEMETLaTKQALEDHRIRhariLEALEIEKQKIAEE 1100
Cdd:pfam15665  140 KHRQEIQELLTTQRAQSASSLAEQEKLEEL-HKAELESLRKE----VEDLRKEKKKLAEE 194
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
981-1106 2.75e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.95  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   981 DAQLKAKEEMMQGiqiakemaQQELSSQKA--VYERKIQALEAELREESQRkrlEELNNQKASHKIEELERA-KQHLEQE 1057
Cdd:pfam15558  188 DCQAKAEELLRRL--------SLEQSLQRSqeNYEQLVEERHRELREKAQK---EEEQFQRAKWRAEEKEEErQEHKEAL 256
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755494468  1058 VYVNKRRLEMETLATKQALEDhRIRHARILEALE-----IEKQKIAEEVQMLQE 1106
Cdd:pfam15558  257 AELADRKIQQARQVAHKTVQD-KAQRARELNLEReknhhILKLKVEKEEKCHRE 309
PTZ00121 PTZ00121
MAEBL; Provisional
938-1108 2.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  938 EVQKGKKLSSRNNLTTSEGPKDFEFAK--------NELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQK 1009
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468 1010 AVYERKIQALEAELREESQRKRLEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEmetlATKQALEDHRIRHARILEA 1089
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKK 1669
                         170
                  ....*....|....*....
gi 755494468 1090 LEIEKQKiAEEVQMLQENR 1108
Cdd:PTZ00121 1670 AEEDKKK-AEEAKKAEEDE 1687
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
980-1108 2.97e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   980 KDAQLKAKEEMMQGIQIAKEMAQQELSSQKAV-------------------YERKIQALEAELREESQRKRLE--ELNNQ 1038
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKaqdekaerdelraklyqeeQERKERQKEREEAEKKARQRQElqQAREE 243
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755494468  1039 KASHKIEELERAKQHLEQEV-YVNKRRLEMETLATKQALEDHRIR--HARILEAL--EIEKQKIAEEVQMLQENR 1108
Cdd:pfam13868  244 QIELKERRLAEEAEREEEEFeRMLRKQAEDEEIEQEEAEKRRMKRleHRRELEKQieEREEQRAAEREEELEEGE 318
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
966-1106 3.33e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   966 ELLTAQRSRLEAEIKDAQ--LKAKEEMMQGIQI------AKEMAQQELSSQKAVYERKIQALEAEL--------REESQR 1029
Cdd:pfam01576   75 EILHELESRLEEEEERSQqlQNEKKKMQQHIQDleeqldEEEAARQKLQLEKVTTEAKIKKLEEDIllledqnsKLSKER 154
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468  1030 KRLEELNNQKASHKIEELERAKQhleqevyVNKRRLEMETLATKqaLEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:pfam01576  155 KLLEERISEFTSNLAEEEEKAKS-------LSKLKNKHEAMISD--LEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
972-1038 4.36e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 39.29  E-value: 4.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468  972 RSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRlEELNNQ 1038
Cdd:PRK08476   61 EHEIETILKNAREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELK-EQLLSQ 126
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
972-1099 4.40e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  972 RSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQElsSQKAVYERkIQALEAELREesQRKRLEELNNQKASHK--IEELER 1049
Cdd:COG0542   401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKE--QDEASFER-LAELRDELAE--LEEELEALKARWEAEKelIEEIQE 475
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755494468 1050 AKQHLEQEvYVNKRRLEMETLATKQALEDhrirhARILEALEIEKQKIAE 1099
Cdd:COG0542   476 LKEELEQR-YGKIPELEKELAELEEELAE-----LAPLLREEVTEEDIAE 519
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
868-927 4.50e-03

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 41.29  E-value: 4.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468  868 SSSHDIQL---SGVlIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHIS----EPTVLHHGDRVVLGG 927
Cdd:COG3456    33 SADCDWVLpdpDRS-VSRRHAEIRFRDGAFCLTDLSTNGTFLNGSDHPlgpgRPVRLRDGDRLRIGD 98
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
975-1109 5.27e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  975 LEAEIKDAQLKAKEEMMQGIQIAKEMAQQELssqkAVYERKIQALEAELreesqrKRLEELNnQKASHKIEELERAKQHL 1054
Cdd:COG2433   378 IEEALEELIEKELPEEEPEAEREKEHEEREL----TEEEEEIRRLEEQV------ERLEAEV-EELEAELEEKDERIERL 446
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755494468 1055 EQEVYVNKRRLEMEtlatkqALEDhriRHARILEAlEIE--KQKIAEEVQMLQENRG 1109
Cdd:COG2433   447 ERELSEARSEERRE------IRKD---REISRLDR-EIErlERELEEERERIEELKR 493
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
970-1109 6.27e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 6.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   970 AQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRK-----RLEELNNQKAS--H 1042
Cdd:pfam01576  424 SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlstRLRQLEDERNSlqE 503
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755494468  1043 KIEELERAKQHLEQEVYV-------NKRRLEmETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRG 1109
Cdd:pfam01576  504 QLEEEEEAKRNVERQLSTlqaqlsdMKKKLE-EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN 576
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
984-1106 6.33e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.67  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   984 LKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKASHKIEELERAKQHLEQEvyvnkr 1063
Cdd:pfam13868    8 LRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ------ 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 755494468  1064 rlemetlatkqaLEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:pfam13868   82 ------------IEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
937-1034 6.39e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  937 VEVQKGKKLSSRNNLTTSEGPKDFEFAKNEL--LTAQRSRLEAEIKDA--QLKAKEEMMQGIQIAKEMAQQELSSQKAVY 1012
Cdd:COG1579    68 IEEVEARIKKYEEQLGNVRNNKEYEALQKEIesLKRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEEKKAEL 147
                          90       100
                  ....*....|....*....|...
gi 755494468 1013 ERKIQALEAELRE-ESQRKRLEE 1034
Cdd:COG1579   148 DEELAELEAELEElEAEREELAA 170
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
965-1078 6.58e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  965 NELLTAQRSRLEAEIKDAQLKAKEEmmqgiqiAKEMAQQELSSQKAVYERKIQALEAELREesQRKRLEELNNQKASHKI 1044
Cdd:cd16269   184 EAILQADQALTEKEKEIEAERAKAE-------AAEQERKLLEEQQRELEQKLEDQERSYEE--HLRQLKEKMEEERENLL 254
                          90       100       110
                  ....*....|....*....|....*....|....
gi 755494468 1045 EELERAKQHLEQEvyvNKRRLEMETLATKQALED 1078
Cdd:cd16269   255 KEQERALESKLKE---QEALLEEGFKEQAELLQE 285
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
970-1106 6.93e-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: 39.91  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  970 AQRSRLEAEIKD--AQLKAKEEMMQGIQIAKEMAQQELSSqkavYERKIQALEAELREESQR-KRLEE-LNNQKASHKIE 1045
Cdd:COG1579    17 SELDRLEHRLKElpAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARiKKYEEqLGNVRNNKEYE 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494468 1046 ELERakqhleqevyvnkrrlEMETLATKQA-LEDHRIRHARILEALEIEKQKIAEEVQMLQE 1106
Cdd:COG1579    93 ALQK----------------EIESLKRRISdLEDEILELMERIEELEEELAELEAELAELEA 138
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
966-1113 8.07e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   966 ELLTAQRSRLEAEIKDAQLKAKEEM---MQGIQIAKEMAQQELSSQKAVYERKIQALEAELReesqrkrlEELNNQKASH 1042
Cdd:pfam12128  364 KALTGKHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESELR--------EQLEAGKLEF 435
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494468  1043 KIEELERAKQHLEQEVYVNKRRLEMETLaTKQALEDHRIRHARilEALEIEKQKIAEEVQMLQENRGNRDK 1113
Cdd:pfam12128  436 NEEEYRLKSRLGELKLRLNQATATPELL-LQLENFDERIERAR--EEQEAANAEVERLQSELRQARKRRDQ 503
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
966-1102 8.23e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 39.17  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  966 ELLTAQRSRLEAEIKDA---QLKAKEEMMQgiqiakemAQQELSSQKAVYERKIQalEAELREESQRKRLEelnnQKAsh 1042
Cdd:PRK07352   46 KILEERREAILQALKEAeerLRQAAQALAE--------AQQKLAQAQQEAERIRA--DAKARAEAIRAEIE----KQA-- 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494468 1043 kIEELERAKQHLEQEVYVNKRRL--EMETLATKQALedhrirhARILEALeieKQKIAEEVQ 1102
Cdd:PRK07352  110 -IEDMARLKQTAAADLSAEQERViaQLRREAAELAI-------AKAESQL---PGRLDEDAQ 160
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
958-1111 9.08e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.59  E-value: 9.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   958 KDFEFAKNELLTAQRSRLEAE-----IKDAQLKAKEeMMQgiQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRL 1032
Cdd:pfam12795   20 QDLQQALSLLDKIDASKQRAAayqkaLDDAPAELRE-LRQ--ELAALQAKAEAAPKEILASLSLEELEQRLLQTSAQLQE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1033 EELNNQKASHKIEELERAKQHLEQEVYVNKRRL-EMETLATKQALEDHRIRHARILeALEIEKQKIAEEVQML---QENR 1108
Cdd:pfam12795   97 LQNQLAQLNSQLIELQTRPERAQQQLSEARQRLqQIRNRLNGPAPPGEPLSEAQRW-ALQAELAALKAQIDMLeqeLLSN 175

                   ...
gi 755494468  1109 GNR 1111
Cdd:pfam12795  176 NNR 178
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
1013-1106 9.88e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.12  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468  1013 ERKIQALEAEL-REESQRKRLEELNNQKASHKIEELERAKQHLEQEVYVNKRRleMETLATKQALEDHRIRHArilEALE 1091
Cdd:pfam15619   87 ERKLKEKEAELlRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEK--IQDLERKLELENKSFRRQ---LAAE 161
                           90
                   ....*....|....*.
gi 755494468  1092 IEKQKIA-EEVQMLQE 1106
Cdd:pfam15619  162 KKKHKEAqEEVKILQE 177
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
985-1093 9.88e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 39.52  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494468   985 KAKEEMMQGIQIAKEmAQQ---ELSSQKAVYERKIQALEAEL------------REESQRKRLEELNNQKAShkIEELER 1049
Cdd:pfam11932   17 QALDLAEKAVAAAAQ-SQKkidKWDDEKQELLAEYRALKAELeslevynrqlerLVASQEQEIASLERQIEE--IERTER 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494468  1050 A------------KQHLEQEV--YVNKRRLEMETLatKQALEDHRI----RHARILEALEIE 1093
Cdd:pfam11932   94 ElvplmlkmldrlEQFVALDLpfLLEERQARLARL--RELMDDADVslaeKYRRILEAYQVE 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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