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Conserved domains on  [gi|767984841|ref|XP_011520138|]
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stAR-related lipid transfer protein 9 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
1-337 6.50e-155

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.


The actual alignment was detected with superfamily member cd01365:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 361  Bit Score: 485.32  E-value: 6.50e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    1 MAFGFDYCYWSVNPEDPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVRE 80
Cdd:cd01365    52 KSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   81 KDCASLPSSCRIKVSFLEIYNERVRDLLKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAA 160
Cdd:cd01365   132 ADTTNQNMSYSVEVSYMEIYNEKVRDLLNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAA 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  161 THVHEASSRSHAIFTIHYTQAILE--NNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQ 237
Cdd:cd01365   212 TNMNDTSSRSHAVFTIVLTQKRHDaeTNLTTEKVSKISLVDLAGSERASSTgATGDRLKEGANINKSLTTLGKVISALAD 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  238 NSQvfsscqslnssvsnggdsgilsspsgtssgGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSET 317
Cdd:cd01365   292 MSS------------------------------GKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEET 341
                         330       340
                  ....*....|....*....|
gi 767984841  318 MSTLRYASSAKNIINKPRVN 337
Cdd:cd01365   342 LSTLRYADRAKKIVNRAVVN 361
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
4442-4651 5.79e-120

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


:

Pssm-ID: 176883  Cd Length: 205  Bit Score: 378.10  E-value: 5.79e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4442 MADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTA 4521
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4522 RLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEvpalvGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQ 4601
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKE-----GELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984841 4602 PITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR 4651
Cdd:cd08874   156 PVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
417-535 1.94e-76

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: 249.69  E-value: 1.94e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  417 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 496
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767984841  497 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRR 535
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
Kinesin_assoc super family cl24686
Kinesin-associated;
336-447 5.00e-04

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 44.06  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   336 VNEDANLKLIRELREEIERLKALLLSFELRN------------------------------------------------- 366
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYAQGLGDiidtiahptkkrantpaanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   367 -----FSSLSDENLKELvLQNELKIDQLTKDWTQKWN-------DWQALMEHYSVDI--NRRRAGVVIDSSLPHLMALED 432
Cdd:pfam16183   83 herimFTPGSEEAIERL-KETEKIIAELNETWEEKLRkteairmEREALLAEMGVAIreDGGTLGVFSPKKTPHLVNLNE 161
                          170
                   ....*....|....*
gi 767984841   433 DVLSTGVVLYHLKEG 447
Cdd:pfam16183  162 DPLMSECLLYYIKDG 176
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
526-732 4.23e-03

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  526 AEAAVLRQRRQVG--EAAAGRGSlEWLDLDGDLAASRLGLSPL-LWKERRALE------EQCDEDHQTPRDGETSHRAQI 596
Cdd:COG4913   240 AHEALEDAREQIEllEPIRELAE-RYAAARERLAELEYLRAALrLWFAQRRLElleaelEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  597 QQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASL--QQQQQEDQVAEKELEASVALDAWLQ 674
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEE 398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984841  675 TDPEIQpspfvqsqkrvvhlqlLRRHTLRAAERNVRRkkvsfQLERIIKKQRLLEAQK 732
Cdd:COG4913   399 ELEALE----------------EALAEAEAALRDLRR-----ELRELEAEIASLERRK 435
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
1-337 6.50e-155

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: 485.32  E-value: 6.50e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    1 MAFGFDYCYWSVNPEDPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVRE 80
Cdd:cd01365    52 KSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   81 KDCASLPSSCRIKVSFLEIYNERVRDLLKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAA 160
Cdd:cd01365   132 ADTTNQNMSYSVEVSYMEIYNEKVRDLLNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAA 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  161 THVHEASSRSHAIFTIHYTQAILE--NNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQ 237
Cdd:cd01365   212 TNMNDTSSRSHAVFTIVLTQKRHDaeTNLTTEKVSKISLVDLAGSERASSTgATGDRLKEGANINKSLTTLGKVISALAD 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  238 NSQvfsscqslnssvsnggdsgilsspsgtssgGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSET 317
Cdd:cd01365   292 MSS------------------------------GKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEET 341
                         330       340
                  ....*....|....*....|
gi 767984841  318 MSTLRYASSAKNIINKPRVN 337
Cdd:cd01365   342 LSTLRYADRAKKIVNRAVVN 361
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
4442-4651 5.79e-120

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 378.10  E-value: 5.79e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4442 MADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTA 4521
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4522 RLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEvpalvGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQ 4601
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKE-----GELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984841 4602 PITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR 4651
Cdd:cd08874   156 PVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-337 4.29e-116

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: 372.68  E-value: 4.29e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841      3 FGFDYCYwsvnpedPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKD 82
Cdd:smart00129   48 FTFDKVF-------DATASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDK 120
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841     83 CASLPSsCRIKVSFLEIYNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATH 162
Cdd:smart00129  121 REEGWQ-FSVKVSYLEIYNEKIRDLLNPSSKK----LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATK 195
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    163 VHEASSRSHAIFTIHYTQAILENNLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqv 241
Cdd:smart00129  196 MNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVDLAGSERAKKTGAEgDRLKEAGNINKSLSALGNVINALAQHS-- 273
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    242 fsscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTL 321
Cdd:smart00129  274 ----------------------------------KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTL 319
                           330
                    ....*....|....*.
gi 767984841    322 RYASSAKNIINKPRVN 337
Cdd:smart00129  320 RFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
2-330 6.54e-114

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 366.13  E-value: 6.54e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841     2 AFGFDYCYWSVnpedpqyASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREK 81
Cdd:pfam00225   41 TFTFDKVFDPE-------ATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLF-DRI 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    82 DCASLPSSCRIKVSFLEIYNERVRDLLkQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAAT 161
Cdd:pfam00225  113 QKTKERSEFSVKVSYLEIYNEKIRDLL-SPSNKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAAT 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   162 HVHEASSRSHAIFTIHYTQAILENNLPSE-MASKINLVDLAGSERAD--PSYCKDRIAEGANINKSLVTLGIVISTLAQN 238
Cdd:pfam00225  192 KMNEESSRSHAIFTITVEQRNRSTGGEESvKTGKLNLVDLAGSERASktGAAGGQRLKEAANINKSLSALGNVISALADK 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   239 sqvfsscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETM 318
Cdd:pfam00225  272 -------------------------------------KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETL 314
                          330
                   ....*....|..
gi 767984841   319 STLRYASSAKNI 330
Cdd:pfam00225  315 STLRFASRAKNI 326
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
417-535 1.94e-76

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: 249.69  E-value: 1.94e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  417 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 496
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767984841  497 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRR 535
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
20-389 5.11e-73

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 257.36  E-value: 5.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREKDCASLPSSCRIKVSFLEI 99
Cdd:COG5059    68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELF-SKLEDLSMTKDFAVSISYLEI 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  100 YNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYT 179
Cdd:COG5059   147 YNEKIYDLLSPNEES----LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELA 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  180 QAIlENNLPSEmASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqvfsscqslnssvsnggds 258
Cdd:COG5059   223 SKN-KVSGTSE-TSKLSLVDLAGSERAARTGNRgTRLKEGASINKSLLTLGNVINALGDKK------------------- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  259 gilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVNE 338
Cdd:COG5059   282 -----------------KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNS 344
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767984841  339 DANLKL--------IRELREEIERLKALLLSFELRNFSSLSDENLKELVLQNELKIDQL 389
Cdd:COG5059   345 SSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRI 403
PLN03188 PLN03188
kinesin-12 family protein; Provisional
20-357 1.19e-61

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 235.21  E-value: 1.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGtPASV-----------GLTPRICEGLFVREKDCA---- 84
Cdd:PLN03188  144 STQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFARINEEQikha 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   85 --SLPSSCRikVSFLEIYNERVRDLLKQSgQKksyTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATH 162
Cdd:PLN03188  223 drQLKYQCR--CSFLEIYNEQITDLLDPS-QK---NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATS 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  163 VHEASSRSHAIFT--IHYTQAILENNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNS 239
Cdd:PLN03188  297 INAESSRSHSVFTcvVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTgAAGDRLKEAGNINRSLSQLGNLINILAEIS 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  240 QvfsscqslnssvsnggdsgilsspsgtssggapSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMS 319
Cdd:PLN03188  377 Q---------------------------------TGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFS 423
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 767984841  320 TLRYASSAKNIINKPRVNE----DANL--KLIRELREEIERLKA 357
Cdd:PLN03188  424 TLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVKA 467
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
442-522 8.83e-08

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 52.65  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  442 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCT-VNGREVTASCRLTQGAVITLGKaQKF 520
Cdd:COG1716    16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTfVNGQRVTEPAPLRDGDVIRLGK-TEL 91

                  ..
gi 767984841  521 RF 522
Cdd:COG1716    92 RF 93
START pfam01852
START domain;
4497-4651 3.44e-06

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 50.86  E-value: 3.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  4497 PLSRVWAAVSDPTV---------------WPLYYKPIQTarlHQRVTNSISLVYLVCNTTLCALKQPRDFccvcVEAKEV 4561
Cdd:pfam01852   43 EASRASGVVPMVAAllvaellkdmeyraqWDKDVRSAET---LEVISSGGDLQYYVAALVAPSPLSPRDF----VFLRYW 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  4562 PALVGHLSVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQPitvEGKEVTRVIYLAQVELGApGFPPQLLSSFIKR-QPL 4640
Cdd:pfam01852  116 RRLGGGVYVIVDRSVTHPQFP-PSSGYVRAERLPSGYLIQP---CGNGPSKVTWVSHADLKG-WLPSWLLRSLYKSgMPE 190
                          170
                   ....*....|.
gi 767984841  4641 VIARLASFLGR 4651
Cdd:pfam01852  191 GAKTWVATLQR 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
4463-4644 1.04e-05

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 49.74  E-value: 1.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   4463 AGW--NYQGEEQavQLYYKVFSPTR---HGFLGAGVVSQPLSRVWA-AVSDPTVWPLYYKPIQTARLHQRVTNSISLVYL 4536
Cdd:smart00234   18 EGWvlSSENENG--DEVRSIFSPGRkpgEAFRLVGVVPMVCADLVEeLMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHY 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   4537 VCNTTLCALKqPRDFCCVCVEAKevpaLVGHLSVMAAQSVyDTSMPRPSRKMVRGEILPSAWILQPitvEGKEVTRVIYL 4616
Cdd:smart00234   96 VSKFAAGPVS-PRDFVFVRYWRE----DEDGSYAVVDVSV-THPTSPPESGYVRAENLPSGLLIEP---LGNGPSKVTWV 166
                           170       180
                    ....*....|....*....|....*...
gi 767984841   4617 AQVELGAPGfPPQLLSSFIKRQPLVIAR 4644
Cdd:smart00234  167 SHADLKGWL-PHWLVRSLIKSGLAEFAK 193
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
449-514 2.41e-04

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 42.18  E-value: 2.41e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984841   449 TKIGRidsDQEQDIVLQGQWIERDHCTIT-SACGVVVLRPARGARCT-VNGREVT-ASCRLTQGAVITL 514
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNGTfVNGQRLGpEPVRLKDGDVIRL 66
Kinesin_assoc pfam16183
Kinesin-associated;
336-447 5.00e-04

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 44.06  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   336 VNEDANLKLIRELREEIERLKALLLSFELRN------------------------------------------------- 366
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYAQGLGDiidtiahptkkrantpaanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   367 -----FSSLSDENLKELvLQNELKIDQLTKDWTQKWN-------DWQALMEHYSVDI--NRRRAGVVIDSSLPHLMALED 432
Cdd:pfam16183   83 herimFTPGSEEAIERL-KETEKIIAELNETWEEKLRkteairmEREALLAEMGVAIreDGGTLGVFSPKKTPHLVNLNE 161
                          170
                   ....*....|....*
gi 767984841   433 DVLSTGVVLYHLKEG 447
Cdd:pfam16183  162 DPLMSECLLYYIKDG 176
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
526-732 4.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  526 AEAAVLRQRRQVG--EAAAGRGSlEWLDLDGDLAASRLGLSPL-LWKERRALE------EQCDEDHQTPRDGETSHRAQI 596
Cdd:COG4913   240 AHEALEDAREQIEllEPIRELAE-RYAAARERLAELEYLRAALrLWFAQRRLElleaelEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  597 QQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASL--QQQQQEDQVAEKELEASVALDAWLQ 674
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEE 398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984841  675 TDPEIQpspfvqsqkrvvhlqlLRRHTLRAAERNVRRkkvsfQLERIIKKQRLLEAQK 732
Cdd:COG4913   399 ELEALE----------------EALAEAEAALRDLRR-----ELRELEAEIASLERRK 435
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
1-337 6.50e-155

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: 485.32  E-value: 6.50e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    1 MAFGFDYCYWSVNPEDPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVRE 80
Cdd:cd01365    52 KSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   81 KDCASLPSSCRIKVSFLEIYNERVRDLLKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAA 160
Cdd:cd01365   132 ADTTNQNMSYSVEVSYMEIYNEKVRDLLNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAA 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  161 THVHEASSRSHAIFTIHYTQAILE--NNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQ 237
Cdd:cd01365   212 TNMNDTSSRSHAVFTIVLTQKRHDaeTNLTTEKVSKISLVDLAGSERASSTgATGDRLKEGANINKSLTTLGKVISALAD 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  238 NSQvfsscqslnssvsnggdsgilsspsgtssgGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSET 317
Cdd:cd01365   292 MSS------------------------------GKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEET 341
                         330       340
                  ....*....|....*....|
gi 767984841  318 MSTLRYASSAKNIINKPRVN 337
Cdd:cd01365   342 LSTLRYADRAKKIVNRAVVN 361
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
4442-4651 5.79e-120

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 378.10  E-value: 5.79e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4442 MADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTA 4521
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4522 RLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEvpalvGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQ 4601
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKE-----GELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984841 4602 PITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR 4651
Cdd:cd08874   156 PVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-337 4.29e-116

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: 372.68  E-value: 4.29e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841      3 FGFDYCYwsvnpedPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKD 82
Cdd:smart00129   48 FTFDKVF-------DATASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDK 120
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841     83 CASLPSsCRIKVSFLEIYNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATH 162
Cdd:smart00129  121 REEGWQ-FSVKVSYLEIYNEKIRDLLNPSSKK----LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATK 195
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    163 VHEASSRSHAIFTIHYTQAILENNLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqv 241
Cdd:smart00129  196 MNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVDLAGSERAKKTGAEgDRLKEAGNINKSLSALGNVINALAQHS-- 273
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    242 fsscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTL 321
Cdd:smart00129  274 ----------------------------------KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTL 319
                           330
                    ....*....|....*.
gi 767984841    322 RYASSAKNIINKPRVN 337
Cdd:smart00129  320 RFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
2-330 6.54e-114

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 366.13  E-value: 6.54e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841     2 AFGFDYCYWSVnpedpqyASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREK 81
Cdd:pfam00225   41 TFTFDKVFDPE-------ATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLF-DRI 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    82 DCASLPSSCRIKVSFLEIYNERVRDLLkQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAAT 161
Cdd:pfam00225  113 QKTKERSEFSVKVSYLEIYNEKIRDLL-SPSNKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAAT 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   162 HVHEASSRSHAIFTIHYTQAILENNLPSE-MASKINLVDLAGSERAD--PSYCKDRIAEGANINKSLVTLGIVISTLAQN 238
Cdd:pfam00225  192 KMNEESSRSHAIFTITVEQRNRSTGGEESvKTGKLNLVDLAGSERASktGAAGGQRLKEAANINKSLSALGNVISALADK 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   239 sqvfsscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETM 318
Cdd:pfam00225  272 -------------------------------------KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETL 314
                          330
                   ....*....|..
gi 767984841   319 STLRYASSAKNI 330
Cdd:pfam00225  315 STLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
3-328 5.71e-108

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: 348.86  E-value: 5.71e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    3 FGFDYCYWSVnpedpqyASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPAS-VGLTPRICEGLFVREK 81
Cdd:cd00106    46 FAFDAVFDST-------STQEEVYEGTAKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERID 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   82 DCASLPSSCRIKVSFLEIYNERVRDLLKQSgqkKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAAT 161
Cdd:cd00106   119 KRKETKSSFSVSASYLEIYNEKIYDLLSPV---PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTAST 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  162 HVHEASSRSHAIFTIHYTQAILENNLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSQ 240
Cdd:cd00106   196 NMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLVDLAGSERAKKTGAEgDRLKEGGNINKSLSALGKVISALADGQN 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  241 VfsscqslnssvsnggdsgilsspsgtssggapsrrqsYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMST 320
Cdd:cd00106   276 K-------------------------------------HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLST 318

                  ....*...
gi 767984841  321 LRYASSAK 328
Cdd:cd00106   319 LRFASRAK 326
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
2-330 9.63e-86

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: 285.76  E-value: 9.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    2 AFGFDYCYwsvNPEDPQyasqDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMlGTPAS-------VGLTPRICE 74
Cdd:cd01372    41 SFTFDYVF---DPSTEQ----EEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTM-GTAYTaeedeeqVGIIPRAIQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   75 GLFvreKDCASLPSSCR--IKVSFLEIYNERVRDLLKQSGQKKSyTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEG 152
Cdd:cd01372   113 HIF---KKIEKKKDTFEfqLKVSFLEIYNEEIRDLLDPETDKKP-TISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  153 IANRITAATHVHEASSRSHAIFTIHYTQAILEN--------NLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINK 223
Cdd:cd01372   189 SLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGpiapmsadDKNSTFTSKFHFVDLAGSERLKRTGATgDRLKEGISINS 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  224 SLVTLGIVISTLaqnsqvfsscqslnssvsngGDsgilsspsgtssggaPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIM 303
Cdd:cd01372   269 GLLALGNVISAL--------------------GD---------------ESKKGAHVPYRDSKLTRLLQDSLGGNSHTLM 313
                         330       340
                  ....*....|....*....|....*..
gi 767984841  304 VATVSPAHTSYSETMSTLRYASSAKNI 330
Cdd:cd01372   314 IACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
18-330 1.29e-85

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: 285.78  E-value: 1.29e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   18 QYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDcASLPSSCRIKVSFL 97
Cdd:cd01370    71 ETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES-LKDEKEFEVSMSYL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   98 EIYNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIH 177
Cdd:cd01370   150 EIYNETIRDLLNPSSGP----LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQIT 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  178 YTQAILENNLPSE-MASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQnsqvfsscqslnssvsng 255
Cdd:cd01370   226 VRQQDKTASINQQvRQGKLSLIDLAGSERASATNNRgQRLKEGANINRSLLALGNCINALAD------------------ 287
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984841  256 gdsgilsspsgtssggaPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 330
Cdd:cd01370   288 -----------------PGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
3-332 2.30e-84

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: 281.40  E-value: 2.30e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    3 FGFDYCYwsvnpeDPQyASQDVVFQDLGMEVLSGVaKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKD 82
Cdd:cd01366    47 FSFDKVF------DPE-ASQEDVFEEVSPLVQSAL-DGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   83 CASLPSSCRIKVSFLEIYNERVRDLL-KQSGQKKSYTLRvREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAAT 161
Cdd:cd01366   119 LKEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTAST 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  162 HVHEASSRSHAIFTIHytqaILENNLPSEMA--SKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQn 238
Cdd:cd01366   198 AMNEHSSRSHSVFILH----ISGRNLQTGEIsvGKLNLVDLAGSERLNKSGATgDRLKETQAINKSLSALGDVISALRQ- 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  239 sqvfsscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETM 318
Cdd:cd01366   273 -------------------------------------KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETL 315
                         330
                  ....*....|....
gi 767984841  319 STLRYASSAKNIIN 332
Cdd:cd01366   316 NSLRFASKVNSCEL 329
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
2-330 1.58e-81

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: 273.57  E-value: 1.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    2 AFGFDYCYwsvnpedPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASV---GLTPRICEGLFv 78
Cdd:cd01371    49 TFTFDAVF-------DPNSKQLDVYDETARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIF- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   79 reKDCASLPSSCR--IKVSFLEIYNERVRDLLKQSGQKKsytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANR 156
Cdd:cd01371   121 --GHIARSQNNQQflVRVSYLEIYNEEIRDLLGKDQTKR---LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNR 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  157 ITAATHVHEASSRSHAIFTIHYTQA-ILENNLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVIST 234
Cdd:cd01371   196 SVGATNMNEDSSRSHAIFTITIECSeKGEDGENHIRVGKLNLVDLAGSERQSKTGATgERLKEATKINLSLSALGNVISA 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  235 LAQNsqvfsscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSY 314
Cdd:cd01371   276 LVDG-------------------------------------KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNY 318
                         330
                  ....*....|....*.
gi 767984841  315 SETMSTLRYASSAKNI 330
Cdd:cd01371   319 DETLSTLRYANRAKNI 334
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
21-339 2.83e-80

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: 270.15  E-value: 2.83e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   21 SQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASV--------GLTPRICEGLFV---REKDCASLPSS 89
Cdd:cd01373    54 NQESVFQSVGKPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSliqREKEKAGEGKS 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   90 CRIKVSFLEIYNERVRDLLKQSgqkkSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSR 169
Cdd:cd01373   134 FLCKCSFLEIYNEQIYDLLDPA----SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSR 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  170 SHAIFTIHYTQAILENNLPSEMASKINLVDLAGSERADPSYC-KDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqsl 248
Cdd:cd01373   210 SHAVFTCTIESWEKKACFVNIRTSRLNLVDLAGSERQKDTHAeGVRLKEAGNINKSLSCLGHVINALVDVAH-------- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  249 nssvsnggdsgilsspsgtssggapsRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 328
Cdd:cd01373   282 --------------------------GKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAK 335
                         330
                  ....*....|.
gi 767984841  329 NIINKPRVNED 339
Cdd:cd01373   336 LIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
25-330 1.93e-76

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: 258.42  E-value: 1.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   25 VFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSscRIKVSFLEIYNERV 104
Cdd:cd01374    56 VYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREF--LLRVSYLEIYNEKI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  105 RDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILE 184
Cdd:cd01374   134 NDLLSPTSQN----LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  185 NNLPS-EMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLaqnsqvfsscqslnssvSNGgdsgils 262
Cdd:cd01374   210 ELEEGtVRVSTLNLIDLAGSERAAQTGAAgVRRKEGSHINKSLLTLGTVISKL-----------------SEG------- 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984841  263 spsgtssggapsRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 330
Cdd:cd01374   266 ------------KVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
417-535 1.94e-76

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: 249.69  E-value: 1.94e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  417 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 496
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767984841  497 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRR 535
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
2-330 4.35e-76

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: 257.26  E-value: 4.35e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    2 AFGFDYcywsVNPEDpqyASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGT---PASVGLTPRICEGLFV 78
Cdd:cd01369    44 TFSFDR----VFDPN---TTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   79 R-EKDCASLPSScrIKVSFLEIYNERVRDLLKQSgqKKSytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRI 157
Cdd:cd01369   117 TiYSMDENLEFH--VKVSYFEIYMEKIRDLLDVS--KTN--LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRH 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  158 TAATHVHEASSRSHAIFTIHYTQAILENNlpSEMASKINLVDLAGSERADpsyckDRIAEGA------NINKSLVTLGIV 231
Cdd:cd01369   191 VAVTNMNEESSRSHSIFLINVKQENVETE--KKKSGKLYLVDLAGSEKVS-----KTGAEGAvldeakKINKSLSALGNV 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  232 ISTLAQNSqvfsscqslnssvsnggdsgilsspsgtssggapsrrQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAH 311
Cdd:cd01369   264 INALTDGK-------------------------------------KTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSS 306
                         330
                  ....*....|....*....
gi 767984841  312 TSYSETMSTLRYASSAKNI 330
Cdd:cd01369   307 YNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
20-339 9.48e-76

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: 257.64  E-value: 9.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLG-----------TPASVGLTPRICEGLFvreKDCASLPS 88
Cdd:cd01364    61 AKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLF---EKLEDNGT 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   89 SCRIKVSFLEIYNERVRDLLKQSGQKKSyTLRVREHPEM--GPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEA 166
Cdd:cd01364   138 EYSVKVSYLEIYNEELFDLLSPSSDVSE-RLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQ 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  167 SSRSHAIFTIhyTQAILENNLPSE---MASKINLVDLAGSERADPSYCKDRIA-EGANINKSLVTLGIVISTLAQNSqvf 242
Cdd:cd01364   217 SSRSHSVFSI--TIHIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRArEAGNINQSLLTLGRVITALVERA--- 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  243 sscqslnssvsnggdsgilsspsgtssggapsrrqSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLR 322
Cdd:cd01364   292 -----------------------------------PHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLE 336
                         330
                  ....*....|....*..
gi 767984841  323 YASSAKNIINKPRVNED 339
Cdd:cd01364   337 YAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
20-389 5.11e-73

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 257.36  E-value: 5.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREKDCASLPSSCRIKVSFLEI 99
Cdd:COG5059    68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELF-SKLEDLSMTKDFAVSISYLEI 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  100 YNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYT 179
Cdd:COG5059   147 YNEKIYDLLSPNEES----LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELA 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  180 QAIlENNLPSEmASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqvfsscqslnssvsnggds 258
Cdd:COG5059   223 SKN-KVSGTSE-TSKLSLVDLAGSERAARTGNRgTRLKEGASINKSLLTLGNVINALGDKK------------------- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  259 gilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVNE 338
Cdd:COG5059   282 -----------------KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNS 344
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767984841  339 DANLKL--------IRELREEIERLKALLLSFELRNFSSLSDENLKELVLQNELKIDQL 389
Cdd:COG5059   345 SSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRI 403
PLN03188 PLN03188
kinesin-12 family protein; Provisional
20-357 1.19e-61

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 235.21  E-value: 1.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGtPASV-----------GLTPRICEGLFVREKDCA---- 84
Cdd:PLN03188  144 STQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFARINEEQikha 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   85 --SLPSSCRikVSFLEIYNERVRDLLKQSgQKksyTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATH 162
Cdd:PLN03188  223 drQLKYQCR--CSFLEIYNEQITDLLDPS-QK---NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATS 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  163 VHEASSRSHAIFT--IHYTQAILENNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNS 239
Cdd:PLN03188  297 INAESSRSHSVFTcvVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTgAAGDRLKEAGNINRSLSQLGNLINILAEIS 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  240 QvfsscqslnssvsnggdsgilsspsgtssggapSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMS 319
Cdd:PLN03188  377 Q---------------------------------TGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFS 423
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 767984841  320 TLRYASSAKNIINKPRVNE----DANL--KLIRELREEIERLKA 357
Cdd:PLN03188  424 TLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVKA 467
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
417-525 5.43e-60

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: 202.12  E-value: 5.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  417 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 496
Cdd:cd22708     1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
                          90       100
                  ....*....|....*....|....*....
gi 767984841  497 GREVTASCRLTQGAVITLGKAQKFRFNHP 525
Cdd:cd22708    81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
20-328 5.38e-56

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: 200.31  E-value: 5.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvrekdcASLPSSCrIKVSFLEI 99
Cdd:cd01368    67 TTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF------NSIGGYS-VFVSYIEI 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  100 YNERVRDLLKQSGQ---KKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTI 176
Cdd:cd01368   140 YNEYIYDLLEPSPSsptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTI 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  177 HYTQAILENNLPSEM------ASKINLVDLAGSERA-DPSYCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqsln 249
Cdd:cd01368   220 KLVQAPGDSDGDVDQdkdqitVSQLSLVDLAGSERTsRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQL--------- 290
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984841  250 ssvsnggdsgilsspsgtssggapSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 328
Cdd:cd01368   291 ------------------------QGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
2-328 1.64e-55

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: 198.29  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    2 AFGFDYCYwsvnPEDpqyASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEG----LF 77
Cdd:cd01367    51 TFRFDYVF----DES---SSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVF 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   78 vREKDCASLPSSCRIKVSFLEIYNERVRDLLkqSGQKKsytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRI 157
Cdd:cd01367   124 -RLLNKLPYKDNLGVTVSFFEIYGGKVFDLL--NRKKR---VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  158 TAATHVHEASSRSHAIFTIhytqaILENNLPSEMASKINLVDLAGSERADPSYCKDRI--AEGANINKSLVTLGIVISTL 235
Cdd:cd01367   198 TGQTSANSQSSRSHAILQI-----ILRDRGTNKLHGKLSFVDLAGSERGADTSSADRQtrMEGAEINKSLLALKECIRAL 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  236 AQNsqvfsscqslnssvsnggdsgilsspsgtssggapsrrQSYIPYRDSVLTWLLKDSL-GGNSKTIMVATVSPAHTSY 314
Cdd:cd01367   273 GQN--------------------------------------KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSC 314
                         330
                  ....*....|....
gi 767984841  315 SETMSTLRYASSAK 328
Cdd:cd01367   315 EHTLNTLRYADRVK 328
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
20-328 6.86e-54

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: 193.57  E-value: 6.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTP---ASVGLTPRICEGLFvREKDCASlPSSCRIKVSF 96
Cdd:cd01375    59 ASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTenyKHRGIIPRALQQVF-RMIEERP-TKAYTVHVSY 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   97 LEIYNERVRDLL--KQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIF 174
Cdd:cd01375   137 LEIYNEQLYDLLstLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIF 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  175 TIHYTQAILENNLPSEMASKINLVDLAGSERADPSYCKDRI-AEGANINKSLVTLGIVISTLAQnsqvfsscqslnssvs 253
Cdd:cd01375   217 TIHLEAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVlKEATYINKSLSFLEQAIIALSD---------------- 280
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984841  254 nggdsgilsspsgtssggapsRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 328
Cdd:cd01375   281 ---------------------KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
20-328 2.13e-47

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: 174.61  E-value: 2.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   20 ASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLfVREKDCASLPSscRIKVSFLEI 99
Cdd:cd01376    56 STQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDL-LQMTRKEAWAL--SFTMSYLEI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  100 YNERVRDLLkqsgQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYT 179
Cdd:cd01376   133 YQEKILDLL----EPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVD 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  180 QAILENNLpSEMASKINLVDLAGSERADPSYCKD-RIAEGANINKSLVTLGIVISTLAQNsqvfsscqslnssvsnggds 258
Cdd:cd01376   209 QRERLAPF-RQRTGKLNLIDLAGSEDNRRTGNEGiRLKESGAINSSLFVLSKVVNALNKN-------------------- 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  259 gilsspsgtssggapsrrQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 328
Cdd:cd01376   268 ------------------LPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
417-533 1.35e-43

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: 155.86  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  417 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 496
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767984841  497 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQ 533
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
417-532 6.27e-29

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: 113.96  E-value: 6.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  417 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDqeqDIVLQGQWIERDHCTITSACGVVVLRPArGARCTVN 496
Cdd:cd22713     9 ALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASD---IISLQGPGVEPEHCYIENINGTVTLYPC-GNLCSVD 84
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767984841  497 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLR 532
Cdd:cd22713    85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
424-524 6.84e-28

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: 110.40  E-value: 6.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  424 LPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGREVTAS 503
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
                          90       100
                  ....*....|....*....|.
gi 767984841  504 CRLTQGAVITLGKAQKFRFNH 524
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
425-536 2.27e-27

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: 109.25  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  425 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITS---ACG--VVVLRPARGARCTVNGRE 499
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSdtrSGGeaVVTLEPCEGADTYVNGKK 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767984841  500 VTASCRLTQGAVITLGKAQKFRFNHPAEAavlRQRRQ 536
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQA---RQERE 115
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
420-525 1.76e-23

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: 98.11  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  420 IDSSLPHLMAL-EDDVLStGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGR 498
Cdd:cd22707     3 VDNKLPNLVNLnEDPQLS-EMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGE 81
                          90       100
                  ....*....|....*....|....*..
gi 767984841  499 EVTASCRLTQGAVITLGKAQKFRFNHP 525
Cdd:cd22707    82 LISEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
425-527 1.37e-22

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: 95.49  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  425 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACG-----VVVLRPARGARCTVNGRE 499
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNnngevIVTLEPCERSETYVNGKR 82
                          90       100
                  ....*....|....*....|....*...
gi 767984841  500 VTASCRLTQGAVITLGKAQKFRFNHPAE 527
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
425-525 5.50e-22

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: 93.43  E-value: 5.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  425 PHLMAL-EDDVLStGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPAR-GARCTVNGREVTA 502
Cdd:cd22709     1 PHLLNLnEDPQLS-GVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTG 79
                          90       100
                  ....*....|....*....|...
gi 767984841  503 SCRLTQGAVITLGKAQKFRFNHP 525
Cdd:cd22709    80 ETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
425-524 6.21e-20

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: 87.62  E-value: 6.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  425 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDqeqdIVLQGQWIERDHC---TITSACG--VVVLRPARGARCTVNGRE 499
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVD----IKLSGQFIREQHClfrSIPNPSGevVVTLEPCEGAETYVNGKQ 77
                          90       100
                  ....*....|....*....|....*
gi 767984841  500 VTASCRLTQGAVITLGKAQKFRFNH 524
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
4459-4651 7.79e-19

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 87.78  E-value: 7.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4459 CQATAGWNYQGEEQAVQLYYK-VFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTARLHQRVTNSISLVYLV 4537
Cdd:cd00177    11 LEEPEGWKLVKEKDGVKIYTKpYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4538 cnTTLCALKQPRDFCCVCVEAKEVPALVghlsVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQPItveGKEVTRVIYLA 4617
Cdd:cd00177    91 --TKPPWPVSPRDFVYLRRRRKLDDGTY----VIVSKSVDHDSHP-KEKGYVRAEIKLSGWIIEPL---DPGKTKVTYVL 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767984841 4618 QVELGApGFPPQLLSSFIKRQPLVIARLASFLGR 4651
Cdd:cd00177   161 QVDPKG-SIPKSLVNSAAKKQLASFLKDLRKAKK 193
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
6-234 2.57e-17

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: 82.39  E-value: 2.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841    6 DYCYWSVNPEDPQYASQDVVFQDLGmEVLSGVAKGYNI-CLFAYGQTGSGKTYTMLGtpasvgLTPRICEGLFvrekdca 84
Cdd:cd01363    16 DSKIIVFYRGFRRSESQPHVFAIAD-PAYQSMLDGYNNqSIFAYGESGAGKTETMKG------VIPYLASVAF------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   85 slpsscrikvsfleiynervrdllkqSGQKKSYTLrvrehpemgpYVQGLSQHVVTNYKQVIQLLEEGIANRiTAATHVH 164
Cdd:cd01363    82 --------------------------NGINKGETE----------GWVYLTEITVTLEDQILQANPILEAFG-NAKTTRN 124
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  165 EASSRSHAIFTIhytqailennlpsemaskinLVDLAGSERadpsyckdriaeganINKSLVTLGIVIST 234
Cdd:cd01363   125 ENSSRFGKFIEI--------------------LLDIAGFEI---------------INESLNTLMNVLRA 159
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
442-525 2.11e-16

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: 77.33  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  442 YHLKEgTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGREVTASCRLTQGAVITLGKAQKFR 521
Cdd:cd22706    19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97

                  ....
gi 767984841  522 FNHP 525
Cdd:cd22706    98 LNCP 101
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
3-108 3.61e-12

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 66.86  E-value: 3.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841     3 FGFDYCywsVNPEdpqyASQDVVFQDLGMEVLSgVAKGYNICLFAYGQTGSGKTytmlgtpasVGLTPRICEGLF--VRE 80
Cdd:pfam16796   57 FSFDRV---FPPE----SEQEDVFQEISQLVQS-CLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFrfISS 119
                           90       100
                   ....*....|....*....|....*...
gi 767984841    81 KDCAslpSSCRIKVSFLEIYNERVRDLL 108
Cdd:pfam16796  120 LKKG---WKYTIELQFVEIYNESSQDLL 144
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
442-522 3.80e-10

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: 59.21  E-value: 3.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  442 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCT-VNGREVTASCRLTQGAVITLGKAQkF 520
Cdd:cd00060    14 FPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTfVNGKRITPPVPLQDGDVIRLGDTT-F 89

                  ..
gi 767984841  521 RF 522
Cdd:cd00060    90 RF 91
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
427-525 4.10e-09

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: 56.85  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  427 LMALEDDVLSTGVVLYHLKEgTTKIGRIDSdqeQDIVLQGQWIERDHCTI-TSACGVVVLRPARGARCTVNGREVTASCR 505
Cdd:cd22730     4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIdITPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
                          90       100
                  ....*....|....*....|
gi 767984841  506 LTQGAVITLGKAQKFRFNHP 525
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
427-535 1.34e-08

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: 55.67  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  427 LMALEDDVLSTGVVLYHLKEGTtkigRIDSDQEQDIVLQGQWIERDHCTITSAC-GVVVLRPARGARCTVNGREVTASCR 505
Cdd:cd22729     4 LVNLNADPALNELLVYYLKDHT----RVGADTSQDIQLFGIGIQPEHCVIDIAAdGDVTLTPKENARTCVNGTLVCSVTQ 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 767984841  506 LTQGAVITLGKAQKFRFNHPAeaavlRQRR 535
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLPK-----RKRR 104
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
424-525 1.47e-08

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: 55.41  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  424 LPHLMALEDDVLSTG-VVLYHLKEGTTKIG--RIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARG-ARCTVNGRE 499
Cdd:cd22711     1 LPYLLELSPDGSDRDkPRRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYVNGQR 80
                          90       100
                  ....*....|....*....|....*.
gi 767984841  500 VTASCRLTQGAVITLGKAQKFRFNHP 525
Cdd:cd22711    81 IYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
422-525 5.58e-08

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


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 54.23  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  422 SSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSD-QEQDIVLQGQWIERDHCTIT---------------SACGVVVL 485
Cdd:cd22712     1 SDYPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEGaRKVDISLRAPDILPQHCWIRrkpeplsddedsdkeSADYRVVL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767984841  486 RPARGARCTVNGREVTASCRLTQGAVITLGKAQKFRFNHP 525
Cdd:cd22712    81 SPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
442-522 8.83e-08

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 52.65  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  442 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCT-VNGREVTASCRLTQGAVITLGKaQKF 520
Cdd:COG1716    16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTfVNGQRVTEPAPLRDGDVIRLGK-TEL 91

                  ..
gi 767984841  521 RF 522
Cdd:COG1716    92 RF 93
START pfam01852
START domain;
4497-4651 3.44e-06

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 50.86  E-value: 3.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  4497 PLSRVWAAVSDPTV---------------WPLYYKPIQTarlHQRVTNSISLVYLVCNTTLCALKQPRDFccvcVEAKEV 4561
Cdd:pfam01852   43 EASRASGVVPMVAAllvaellkdmeyraqWDKDVRSAET---LEVISSGGDLQYYVAALVAPSPLSPRDF----VFLRYW 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  4562 PALVGHLSVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQPitvEGKEVTRVIYLAQVELGApGFPPQLLSSFIKR-QPL 4640
Cdd:pfam01852  116 RRLGGGVYVIVDRSVTHPQFP-PSSGYVRAERLPSGYLIQP---CGNGPSKVTWVSHADLKG-WLPSWLLRSLYKSgMPE 190
                          170
                   ....*....|.
gi 767984841  4641 VIARLASFLGR 4651
Cdd:pfam01852  191 GAKTWVATLQR 201
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
444-522 6.20e-06

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: 47.59  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  444 LKEGTTKIGRidsDQEQDIVLQGQWIERDHCTIT-SACGVVVLRP-ARGARCTVNGREVTASCRLTQGAVITLGKAqKFR 521
Cdd:cd22673    18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGR-SFR 93

                  .
gi 767984841  522 F 522
Cdd:cd22673    94 F 94
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
4463-4644 1.04e-05

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 49.74  E-value: 1.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   4463 AGW--NYQGEEQavQLYYKVFSPTR---HGFLGAGVVSQPLSRVWA-AVSDPTVWPLYYKPIQTARLHQRVTNSISLVYL 4536
Cdd:smart00234   18 EGWvlSSENENG--DEVRSIFSPGRkpgEAFRLVGVVPMVCADLVEeLMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHY 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   4537 VCNTTLCALKqPRDFCCVCVEAKevpaLVGHLSVMAAQSVyDTSMPRPSRKMVRGEILPSAWILQPitvEGKEVTRVIYL 4616
Cdd:smart00234   96 VSKFAAGPVS-PRDFVFVRYWRE----DEDGSYAVVDVSV-THPTSPPESGYVRAENLPSGLLIEP---LGNGPSKVTWV 166
                           170       180
                    ....*....|....*....|....*...
gi 767984841   4617 AQVELGAPGfPPQLLSSFIKRQPLVIAR 4644
Cdd:smart00234  167 SHADLKGWL-PHWLVRSLIKSGLAEFAK 193
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
449-514 2.41e-04

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 42.18  E-value: 2.41e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984841   449 TKIGRidsDQEQDIVLQGQWIERDHCTIT-SACGVVVLRPARGARCT-VNGREVT-ASCRLTQGAVITL 514
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNGTfVNGQRLGpEPVRLKDGDVIRL 66
Kinesin_assoc pfam16183
Kinesin-associated;
336-447 5.00e-04

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 44.06  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   336 VNEDANLKLIRELREEIERLKALLLSFELRN------------------------------------------------- 366
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYAQGLGDiidtiahptkkrantpaanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   367 -----FSSLSDENLKELvLQNELKIDQLTKDWTQKWN-------DWQALMEHYSVDI--NRRRAGVVIDSSLPHLMALED 432
Cdd:pfam16183   83 herimFTPGSEEAIERL-KETEKIIAELNETWEEKLRkteairmEREALLAEMGVAIreDGGTLGVFSPKKTPHLVNLNE 161
                          170
                   ....*....|....*
gi 767984841   433 DVLSTGVVLYHLKEG 447
Cdd:pfam16183  162 DPLMSECLLYYIKDG 176
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
442-525 5.91e-04

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 41.86  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841   442 YHLKEGTTKIGridSDQEQDIVLQGQWIERDHCTITSACGVVVLRPArGARC--TVNGREVT-ASCRLTQGAVITLGKAq 518
Cdd:pfam16697   12 FPLEGGRYRIG---SDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDL-GSGNgtLVNGQRVTeLGIALRPGDRIELGQT- 86

                   ....*..
gi 767984841   519 KFRFNHP 525
Cdd:pfam16697   87 EFCLVPA 93
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
4453-4605 3.57e-03

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 41.96  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4453 LHNLFSCQATAGWNYQGEE--------QAVQLYYKVFSPTrhgflgaGVVSQPLSRVWAA-VSDPTVWPLYYKPIQTARL 4523
Cdd:cd08868    14 LARAWSILTDPGWKLEKNTtwgdvvysRNVPGVGKVFRLT-------GVLDCPAEFLYNElVLNVESLPSWNPTVLECKI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841 4524 HQRVTNSISLVYLVCNTTLCALKQPRDFCCV-CVEAKEvpalvgHLSVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQP 4602
Cdd:cd08868    87 IQVIDDNTDISYQVAAEAGGGLVSPRDFVSLrHWGIRE------NCYLSSGVSVEHPAMP-PTKNYVRGENGPGCWILRP 159

                  ...
gi 767984841 4603 ITV 4605
Cdd:cd08868   160 LPN 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
526-732 4.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  526 AEAAVLRQRRQVG--EAAAGRGSlEWLDLDGDLAASRLGLSPL-LWKERRALE------EQCDEDHQTPRDGETSHRAQI 596
Cdd:COG4913   240 AHEALEDAREQIEllEPIRELAE-RYAAARERLAELEYLRAALrLWFAQRRLElleaelEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  597 QQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASL--QQQQQEDQVAEKELEASVALDAWLQ 674
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEE 398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984841  675 TDPEIQpspfvqsqkrvvhlqlLRRHTLRAAERNVRRkkvsfQLERIIKKQRLLEAQK 732
Cdd:COG4913   399 ELEALE----------------EALAEAEAALRDLRR-----ELRELEAEIASLERRK 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
526-737 7.75e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  526 AEAAVLRQRRQVGEAAAGRGSLEWLDLDGDLAASRLglspllwkERRALEEQcDEDHQTPRDGETSHRAQIQQQQSYVED 605
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRL--------ELEELELE-LEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984841  606 LRHQILAEEIRAAKELEfdqAWISQQIKENQQcllrEETWLASLQQQQQEDQVAEKELEASVALdawlqtdpeiqpspfV 685
Cdd:COG1196   310 RRRELEERLEELEEELA---ELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEA---------------L 367
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767984841  686 QSQKRVVHLQLLRRHTLRAAERNVRRKKVSFQLERIIKKQRLLEAQKRLEKL 737
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
 
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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