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Conserved domains on  [gi|767984833|ref|XP_011520134|]
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stAR-related lipid transfer protein 9 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-390 6.59e-172

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: 534.24  E-value: 6.59e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    2 ANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPDGfgDSREKVMAFGFDYCYWSVNPEDPQYASQ-DVFQ 80
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNK--ATREVPKSFSFDYSYWSHDSEDPNYASQeQVYE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   81 DLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDL 160
Cdd:cd01365    79 DLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  161 LKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILE--N 238
Cdd:cd01365   159 LNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaeT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  239 NLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslnssvsnggdsgilssp 317
Cdd:cd01365   239 NLTTEKVSKISLVDLAGSERASSTgATGDRLKEGANINKSLTTLGKVISALADMSS------------------------ 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984833  318 sgtssgGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVN 390
Cdd:cd01365   295 ------GKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
4495-4704 5.53e-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: 5.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4495 MADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTA 4574
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4575 RLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEvpalvGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQ 4654
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKE-----GELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984833 4655 PITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR 4704
Cdd:cd08874   156 PVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
470-588 2.06e-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: 2.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  470 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 549
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767984833  550 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRR 588
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
Kinesin_assoc super family cl24686
Kinesin-associated;
389-500 5.21e-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: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   389 VNEDANLKLIRELREEIERLKALLLSFELRN------------------------------------------------- 419
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYAQGLGDiidtiahptkkrantpaanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   420 -----FSSLSDENLKELvLQNELKIDQLTKDWTQKWN-------DWQALMEHYSVDI--NRRRAGVVIDSSLPHLMALED 485
Cdd:pfam16183   83 herimFTPGSEEAIERL-KETEKIIAELNETWEEKLRkteairmEREALLAEMGVAIreDGGTLGVFSPKKTPHLVNLNE 161
                          170
                   ....*....|....*
gi 767984833   486 DVLSTGVVLYHLKEG 500
Cdd:pfam16183  162 DPLMSECLLYYIKDG 176
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
579-785 4.50e-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: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  579 AEAAVLRQRRQVG--EAAAGRGSlEWLDLDGDLAASRLGLSPL-LWKERRALE------EQCDEDHQTPRDGETSHRAQI 649
Cdd:COG4913   240 AHEALEDAREQIEllEPIRELAE-RYAAARERLAELEYLRAALrLWFAQRRLElleaelEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  650 QQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASL--QQQQQEDQVAEKELEASVALDAWLQ 727
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEE 398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833  728 TDPEIQpspfvqsqkrvvhlqlLRRHTLRAAERNVRRkkvsfQLERIIKKQRLLEAQK 785
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 ...
2-390 6.59e-172

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: 534.24  E-value: 6.59e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    2 ANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPDGfgDSREKVMAFGFDYCYWSVNPEDPQYASQ-DVFQ 80
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNK--ATREVPKSFSFDYSYWSHDSEDPNYASQeQVYE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   81 DLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDL 160
Cdd:cd01365    79 DLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  161 LKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILE--N 238
Cdd:cd01365   159 LNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaeT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  239 NLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslnssvsnggdsgilssp 317
Cdd:cd01365   239 NLTTEKVSKISLVDLAGSERASSTgATGDRLKEGANINKSLTTLGKVISALADMSS------------------------ 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984833  318 sgtssgGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVN 390
Cdd:cd01365   295 ------GKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-390 2.84e-126

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: 401.95  E-value: 2.84e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833      3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLkvdNRPDGFGDSREkvmaFGFDYCYwsvnpedPQYASQ-DVFQD 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTV---RSPKNRQGEKK----FTFDKVF-------DATASQeDVFEE 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833     82 LGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSsCRIKVSFLEIYNERVRDLL 161
Cdd:smart00129   67 TAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQ-FSVKVSYLEIYNEKIRDLL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    162 KQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLP 241
Cdd:smart00129  146 NPSSKK----LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG 221
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    242 SEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqvfsscqslnssvsnggdsgilsspsgt 320
Cdd:smart00129  222 SGKASKLNLVDLAGSERAKKTGAEgDRLKEAGNINKSLSALGNVINALAQHS---------------------------- 273
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    321 ssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVN 390
Cdd:smart00129  274 --------KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-383 1.23e-122

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 391.17  E-value: 1.23e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833     9 RVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRpdgfgdsREKVMAFGFDYCYWsvnPEDPQyasQDVFQDLGMEVLS 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTN-------KNRTKTFTFDKVFD---PEATQ---EDVYEETAKPLVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    89 GVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREKDCASLPSSCRIKVSFLEIYNERVRDLLkQSGQKK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLF-DRIQKTKERSEFSVKVSYLEIYNEKIRDLL-SPSNKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   169 SYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLPSE-MASK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   248 INLVDLAGSERAD--PSYCKDRIAEGANINKSLVTLGIVISTLAQNsqvfsscqslnssvsnggdsgilsspsgtssgga 325
Cdd:pfam00225  226 LNLVDLAGSERASktGAAGGQRLKEAANINKSLSALGNVISALADK---------------------------------- 271
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833   326 psrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:pfam00225  272 ---KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
4495-4704 5.53e-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: 5.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4495 MADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTA 4574
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4575 RLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEvpalvGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQ 4654
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKE-----GELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984833 4655 PITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR 4704
Cdd:cd08874   156 PVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
470-588 2.06e-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: 2.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  470 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 549
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767984833  550 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRR 588
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
57-442 1.12e-72

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 256.20  E-value: 1.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   57 FGFDYCYwsvNPEDPQYasqDVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREKDC 136
Cdd:COG5059    58 YAFDKVF---GPSATQE---DVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELF-SKLED 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  137 ASLPSSCRIKVSFLEIYNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHV 216
Cdd:COG5059   131 LSMTKDFAVSISYLEIYNEKIYDLLSPNEES----LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEI 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  217 HEASSRSHAIFTIHYTQAIlENNLPSEmASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqvf 295
Cdd:COG5059   207 NDESSRSHSIFQIELASKN-KVSGTSE-TSKLSLVDLAGSERAARTGNRgTRLKEGASINKSLLTLGNVINALGDKK--- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  296 sscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLR 375
Cdd:COG5059   282 ---------------------------------KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984833  376 YASSAKNIINKPRVNEDANLKL--------IRELREEIERLKALLLSFELRNFSSLSDENLKELVLQNELKIDQL 442
Cdd:COG5059   329 FASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRI 403
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-410 6.04e-64

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 242.92  E-value: 6.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    4 VQVAVRVRPLSKREtkEGGRIIVEVDGKVAKIRNlkvdnrpdgfgdsrekvMAFGFDycywsvNPEDPQYASQDVFQDLG 83
Cdd:PLN03188  100 VKVIVRMKPLNKGE--EGEMIVQKMSNDSLTING-----------------QTFTFD------SIADPESTQEDIFQLVG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   84 MEVLSGVAKGYNICLFAYGQTGSGKTYTMLGtPASV-----------GLTPRICEGLFVREKDCA------SLPSSCRik 146
Cdd:PLN03188  155 APLVENCLAGFNSSVFAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFARINEEQikhadrQLKYQCR-- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  147 VSFLEIYNERVRDLLKQSgQKksyTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAI 226
Cdd:PLN03188  232 CSFLEIYNEQITDLLDPS-QK---NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSV 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  227 FT--IHYTQAILENNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslns 303
Cdd:PLN03188  308 FTcvVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTgAAGDRLKEAGNINRSLSQLGNLINILAEISQ---------- 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  304 svsnggdsgilsspsgtssggapSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:PLN03188  378 -----------------------TGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
                         410       420       430
                  ....*....|....*....|....*....|...
gi 767984833  384 INKPRVNE----DANL--KLIRELREEIERLKA 410
Cdd:PLN03188  435 KNKAVVNEvmqdDVNFlrEVIRQLRDELQRVKA 467
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
495-575 8.93e-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: 8.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  495 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCT-VNGREVTASCRLTQGAVITLGKaQKF 573
Cdd:COG1716    16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTfVNGQRVTEPAPLRDGDVIRLGK-TEL 91

                  ..
gi 767984833  574 RF 575
Cdd:COG1716    92 RF 93
START pfam01852
START domain;
4550-4704 3.55e-06

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 50.86  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  4550 PLSRVWAAVSDPTV---------------WPLYYKPIQTarlHQRVTNSISLVYLVCNTTLCALKQPRDFccvcVEAKEV 4614
Cdd:pfam01852   43 EASRASGVVPMVAAllvaellkdmeyraqWDKDVRSAET---LEVISSGGDLQYYVAALVAPSPLSPRDF----VFLRYW 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  4615 PALVGHLSVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQPitvEGKEVTRVIYLAQVELGApGFPPQLLSSFIKR-QPL 4693
Cdd:pfam01852  116 RRLGGGVYVIVDRSVTHPQFP-PSSGYVRAERLPSGYLIQP---CGNGPSKVTWVSHADLKG-WLPSWLLRSLYKSgMPE 190
                          170
                   ....*....|.
gi 767984833  4694 VIARLASFLGR 4704
Cdd:pfam01852  191 GAKTWVATLQR 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
4516-4697 1.05e-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: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   4516 AGW--NYQGEEQavQLYYKVFSPTR---HGFLGAGVVSQPLSRVWA-AVSDPTVWPLYYKPIQTARLHQRVTNSISLVYL 4589
Cdd:smart00234   18 EGWvlSSENENG--DEVRSIFSPGRkpgEAFRLVGVVPMVCADLVEeLMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHY 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   4590 VCNTTLCALKqPRDFCCVCVEAKevpaLVGHLSVMAAQSVyDTSMPRPSRKMVRGEILPSAWILQPitvEGKEVTRVIYL 4669
Cdd:smart00234   96 VSKFAAGPVS-PRDFVFVRYWRE----DEDGSYAVVDVSV-THPTSPPESGYVRAENLPSGLLIEP---LGNGPSKVTWV 166
                           170       180
                    ....*....|....*....|....*...
gi 767984833   4670 AQVELGAPGfPPQLLSSFIKRQPLVIAR 4697
Cdd:smart00234  167 SHADLKGWL-PHWLVRSLIKSGLAEFAK 193
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
502-567 2.44e-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: 2.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984833   502 TKIGRidsDQEQDIVLQGQWIERDHCTIT-SACGVVVLRPARGARCT-VNGREVT-ASCRLTQGAVITL 567
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNGTfVNGQRLGpEPVRLKDGDVIRL 66
Kinesin_assoc pfam16183
Kinesin-associated;
389-500 5.21e-04

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 44.06  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   389 VNEDANLKLIRELREEIERLKALLLSFELRN------------------------------------------------- 419
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYAQGLGDiidtiahptkkrantpaanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   420 -----FSSLSDENLKELvLQNELKIDQLTKDWTQKWN-------DWQALMEHYSVDI--NRRRAGVVIDSSLPHLMALED 485
Cdd:pfam16183   83 herimFTPGSEEAIERL-KETEKIIAELNETWEEKLRkteairmEREALLAEMGVAIreDGGTLGVFSPKKTPHLVNLNE 161
                          170
                   ....*....|....*
gi 767984833   486 DVLSTGVVLYHLKEG 500
Cdd:pfam16183  162 DPLMSECLLYYIKDG 176
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
579-785 4.50e-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: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  579 AEAAVLRQRRQVG--EAAAGRGSlEWLDLDGDLAASRLGLSPL-LWKERRALE------EQCDEDHQTPRDGETSHRAQI 649
Cdd:COG4913   240 AHEALEDAREQIEllEPIRELAE-RYAAARERLAELEYLRAALrLWFAQRRLElleaelEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  650 QQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASL--QQQQQEDQVAEKELEASVALDAWLQ 727
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEE 398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833  728 TDPEIQpspfvqsqkrvvhlqlLRRHTLRAAERNVRRkkvsfQLERIIKKQRLLEAQK 785
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 ...
2-390 6.59e-172

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: 534.24  E-value: 6.59e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    2 ANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPDGfgDSREKVMAFGFDYCYWSVNPEDPQYASQ-DVFQ 80
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNK--ATREVPKSFSFDYSYWSHDSEDPNYASQeQVYE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   81 DLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDL 160
Cdd:cd01365    79 DLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  161 LKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILE--N 238
Cdd:cd01365   159 LNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaeT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  239 NLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslnssvsnggdsgilssp 317
Cdd:cd01365   239 NLTTEKVSKISLVDLAGSERASSTgATGDRLKEGANINKSLTTLGKVISALADMSS------------------------ 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984833  318 sgtssgGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVN 390
Cdd:cd01365   295 ------GKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-390 2.84e-126

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: 401.95  E-value: 2.84e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833      3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLkvdNRPDGFGDSREkvmaFGFDYCYwsvnpedPQYASQ-DVFQD 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTV---RSPKNRQGEKK----FTFDKVF-------DATASQeDVFEE 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833     82 LGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSsCRIKVSFLEIYNERVRDLL 161
Cdd:smart00129   67 TAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQ-FSVKVSYLEIYNEKIRDLL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    162 KQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLP 241
Cdd:smart00129  146 NPSSKK----LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG 221
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    242 SEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqvfsscqslnssvsnggdsgilsspsgt 320
Cdd:smart00129  222 SGKASKLNLVDLAGSERAKKTGAEgDRLKEAGNINKSLSALGNVINALAQHS---------------------------- 273
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    321 ssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVN 390
Cdd:smart00129  274 --------KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-383 1.23e-122

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 391.17  E-value: 1.23e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833     9 RVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRpdgfgdsREKVMAFGFDYCYWsvnPEDPQyasQDVFQDLGMEVLS 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTN-------KNRTKTFTFDKVFD---PEATQ---EDVYEETAKPLVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    89 GVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREKDCASLPSSCRIKVSFLEIYNERVRDLLkQSGQKK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLF-DRIQKTKERSEFSVKVSYLEIYNEKIRDLL-SPSNKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   169 SYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLPSE-MASK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   248 INLVDLAGSERAD--PSYCKDRIAEGANINKSLVTLGIVISTLAQNsqvfsscqslnssvsnggdsgilsspsgtssgga 325
Cdd:pfam00225  226 LNLVDLAGSERASktGAAGGQRLKEAANINKSLSALGNVISALADK---------------------------------- 271
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833   326 psrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:pfam00225  272 ---KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
4495-4704 5.53e-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: 5.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4495 MADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTA 4574
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4575 RLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEvpalvGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQ 4654
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKE-----GELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984833 4655 PITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR 4704
Cdd:cd08874   156 PVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
3-381 8.85e-116

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: 371.59  E-value: 8.85e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPDgfgdsrekvMAFGFDYCYWSVnpedpqyASQ-DVFQD 81
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP---------KTFAFDAVFDST-------STQeEVYEG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   82 LGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPAS-VGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDL 160
Cdd:cd00106    65 TAKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  161 LKQSgqkKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNL 240
Cdd:cd00106   145 LSPV---PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  241 PSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSQVfsscqslnssvsnggdsgilsspsg 319
Cdd:cd00106   222 ESVTSSKLNLVDLAGSERAKKTGAEgDRLKEGGNINKSLSALGKVISALADGQNK------------------------- 276
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767984833  320 tssggapsrrqsYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 381
Cdd:cd00106   277 ------------HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
4-383 2.79e-95

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: 313.11  E-value: 2.79e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    4 VQVAVRVRPLSKRETKEGGRIIVEVdgkvakirnlkVDNRPDGFGDSREkvmAFGFDYCYwsvNPEDPQyasQDVFQDLG 83
Cdd:cd01372     3 VRVAVRVRPLLPKEIIEGCRICVSF-----------VPGEPQVTVGTDK---SFTFDYVF---DPSTEQ---EEVYNTCV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   84 MEVLSGVAKGYNICLFAYGQTGSGKTYTMlGTPAS-------VGLTPRICEGLFvreKDCASLPSSCR--IKVSFLEIYN 154
Cdd:cd01372    63 APLVDGLFEGYNATVLAYGQTGSGKTYTM-GTAYTaeedeeqVGIIPRAIQHIF---KKIEKKKDTFEfqLKVSFLEIYN 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  155 ERVRDLLKQSGQKKSyTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQA 234
Cdd:cd01372   139 EEIRDLLDPETDKKP-TISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  235 ILEN--------NLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLaqnsqvfsscqslnssv 305
Cdd:cd01372   218 KKNGpiapmsadDKNSTFTSKFHFVDLAGSERLKRTGATgDRLKEGISINSGLLALGNVISAL----------------- 280
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833  306 sngGDsgilsspsgtssggaPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:cd01372   281 ---GD---------------ESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
3-383 1.66e-94

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: 311.20  E-value: 1.66e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEV--------DGKVAKIRNLKVDNRPDGFGDSREKVMAFGFDYCYwsvnpeDPQYA 74
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfDPKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVF------DETST 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   75 SQDVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDcASLPSSCRIKVSFLEIYN 154
Cdd:cd01370    75 QEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES-LKDEKEFEVSMSYLEIYN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  155 ERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQA 234
Cdd:cd01370   154 ETIRDLLNPSSGP----LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  235 ILENNLPSE-MASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQnsqvfsscqslnssvsnggdsg 312
Cdd:cd01370   230 DKTASINQQvRQGKLSLIDLAGSERASATNNRgQRLKEGANINRSLLALGNCINALAD---------------------- 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984833  313 ilsspsgtssggaPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:cd01370   288 -------------PGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
3-383 9.28e-94

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: 308.62  E-value: 9.28e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIrnlKVDNrPDGfgDSREKVMAFGFDYCYwsvnpeDPQYASQDVFQDL 82
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQV---SVRN-PKA--TANEPPKTFTFDAVF------DPNSKQLDVYDET 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   83 GMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASV---GLTPRICEGLFvreKDCASLPSSCR--IKVSFLEIYNERV 157
Cdd:cd01371    70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIF---GHIARSQNNQQflVRVSYLEIYNEEI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  158 RDLLKQSGQKKsytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQA-IL 236
Cdd:cd01371   147 RDLLGKDQTKR---LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSeKG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  237 ENNLPSEMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNsqvfsscqslnssvsnggdsgils 315
Cdd:cd01371   224 EDGENHIRVGKLNLVDLAGSERQSKTGATgERLKEATKINLSLSALGNVISALVDG------------------------ 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833  316 spsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:cd01371   280 -------------KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
3-385 2.32e-88

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: 292.96  E-value: 2.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDnrpdgfgdsrEKVMAFGFDYCYwsvnpeDPQyASQ-DVFQD 81
Cdd:cd01366     3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIG----------AKQKEFSFDKVF------DPE-ASQeDVFEE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   82 LGMEVLSGVaKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDLL 161
Cdd:cd01366    66 VSPLVQSAL-DGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  162 -KQSGQKKSYTLRvREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHytqaILENNL 240
Cdd:cd01366   145 aPGNAPQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILH----ISGRNL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  241 PSEMA--SKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQnsqvfsscqslnssvsnggdsgilssp 317
Cdd:cd01366   220 QTGEIsvGKLNLVDLAGSERLNKSGATgDRLKETQAINKSLSALGDVISALRQ--------------------------- 272
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833  318 sgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIIN 385
Cdd:cd01366   273 -----------KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
3-383 1.42e-84

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: 281.53  E-value: 1.42e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDgkvakirnlkvdnrPDGFGDSREKVMAFGFDYCYwsvnpeDPQYASQDVFQDL 82
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEID--------------NDTIYLVEPPSTSFTFDHVF------GGDSTNREVYELI 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   83 GMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSscRIKVSFLEIYNERVRDLLK 162
Cdd:cd01374    61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREF--LLRVSYLEIYNEKINDLLS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  163 QSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLPS 242
Cdd:cd01374   139 PTSQN----LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  243 -EMASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLaqnsqvfsscqslnssvSNGgdsgilsspsgt 320
Cdd:cd01374   215 tVRVSTLNLIDLAGSERAAQTGAAgVRRKEGSHINKSLLTLGTVISKL-----------------SEG------------ 265
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984833  321 ssggapsRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:cd01374   266 -------KVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
1-392 2.88e-83

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: 279.21  E-value: 2.88e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    1 MANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIrnlKVDNRPDGFGDSREKvmaFGFDYCYwsvNPEDPQyasQDVFQ 80
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEV---SVRTGGLADKSSTKT---YTFDMVF---GPEAKQ---IDVYR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   81 DLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLG-----------TPASVGLTPRICEGLFvreKDCASLPSSCRIKVSF 149
Cdd:cd01364    69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLF---EKLEDNGTEYSVKVSY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  150 LEIYNERVRDLLKQSGQKKSyTLRVREHPEM--GPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIF 227
Cdd:cd01364   146 LEIYNEELFDLLSPSSDVSE-RLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  228 TIhyTQAILENNLPSE---MASKINLVDLAGSERADPSYCKDRIA-EGANINKSLVTLGIVISTLAQNSqvfsscqslns 303
Cdd:cd01364   225 SI--TIHIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRArEAGNINQSLLTLGRVITALVERA----------- 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  304 svsnggdsgilsspsgtssggapsrrqSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:cd01364   292 ---------------------------PHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNI 344

                  ....*....
gi 767984833  384 INKPRVNED 392
Cdd:cd01364   345 KNKPEVNQK 353
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
1-383 1.38e-82

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: 276.13  E-value: 1.38e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    1 MANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPdgfgdsrekvmaFGFDYcywsVNPEDpqyASQ-DVF 79
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSETGKT------------FSFDR----VFDPN---TTQeDVY 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   80 QDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGT---PASVGLTPRICEGLFVR-EKDCASLPSScrIKVSFLEIYNE 155
Cdd:cd01369    62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETiYSMDENLEFH--VKVSYFEIYME 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  156 RVRDLLKQSgqKKSytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAI 235
Cdd:cd01369   140 KIRDLLDVS--KTN--LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQEN 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  236 LENNlpSEMASKINLVDLAGSERADpsyckDRIAEGA------NINKSLVTLGIVISTLAQNSqvfsscqslnssvsngg 309
Cdd:cd01369   216 VETE--KKKSGKLYLVDLAGSEKVS-----KTGAEGAvldeakKINKSLSALGNVINALTDGK----------------- 271
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984833  310 dsgilsspsgtssggapsrrQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:cd01369   272 --------------------KTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
3-392 2.26e-82

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: 276.31  E-value: 2.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRpdgfgdsrekvmaFGFDYCYwsvnpeDPQYASQDVFQDL 82
Cdd:cd01373     2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPKT-------------FTFDHVA------DSNTNQESVFQSV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   83 GMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASV--------GLTPRICEGLFV---REKDCASLPSSCRIKVSFLE 151
Cdd:cd01373    63 GKPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSliqREKEKAGEGKSFLCKCSFLE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  152 IYNERVRDLLKQSgqkkSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHY 231
Cdd:cd01373   143 IYNEQIYDLLDPA----SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  232 TQAILENNLPSEMASKINLVDLAGSERADPSYC-KDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslnssvsnggd 310
Cdd:cd01373   219 ESWEKKACFVNIRTSRLNLVDLAGSERQKDTHAeGVRLKEAGNINKSLSCLGHVINALVDVAH----------------- 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  311 sgilsspsgtssggapsRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVN 390
Cdd:cd01373   282 -----------------GKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344

                  ..
gi 767984833  391 ED 392
Cdd:cd01373   345 ED 346
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
470-588 2.06e-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: 2.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  470 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 549
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767984833  550 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRR 588
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
57-442 1.12e-72

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 256.20  E-value: 1.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   57 FGFDYCYwsvNPEDPQYasqDVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvREKDC 136
Cdd:COG5059    58 YAFDKVF---GPSATQE---DVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELF-SKLED 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  137 ASLPSSCRIKVSFLEIYNERVRDLLKQSGQKksytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHV 216
Cdd:COG5059   131 LSMTKDFAVSISYLEIYNEKIYDLLSPNEES----LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEI 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  217 HEASSRSHAIFTIHYTQAIlENNLPSEmASKINLVDLAGSERADPSYCK-DRIAEGANINKSLVTLGIVISTLAQNSqvf 295
Cdd:COG5059   207 NDESSRSHSIFQIELASKN-KVSGTSE-TSKLSLVDLAGSERAARTGNRgTRLKEGASINKSLLTLGNVINALGDKK--- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  296 sscqslnssvsnggdsgilsspsgtssggapsrRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLR 375
Cdd:COG5059   282 ---------------------------------KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984833  376 YASSAKNIINKPRVNEDANLKL--------IRELREEIERLKALLLSFELRNFSSLSDENLKELVLQNELKIDQL 442
Cdd:COG5059   329 FASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRI 403
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-410 6.04e-64

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 242.92  E-value: 6.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    4 VQVAVRVRPLSKREtkEGGRIIVEVDGKVAKIRNlkvdnrpdgfgdsrekvMAFGFDycywsvNPEDPQYASQDVFQDLG 83
Cdd:PLN03188  100 VKVIVRMKPLNKGE--EGEMIVQKMSNDSLTING-----------------QTFTFD------SIADPESTQEDIFQLVG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   84 MEVLSGVAKGYNICLFAYGQTGSGKTYTMLGtPASV-----------GLTPRICEGLFVREKDCA------SLPSSCRik 146
Cdd:PLN03188  155 APLVENCLAGFNSSVFAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFARINEEQikhadrQLKYQCR-- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  147 VSFLEIYNERVRDLLKQSgQKksyTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAI 226
Cdd:PLN03188  232 CSFLEIYNEQITDLLDPS-QK---NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSV 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  227 FT--IHYTQAILENNLPSEMASKINLVDLAGSERADPS-YCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslns 303
Cdd:PLN03188  308 FTcvVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTgAAGDRLKEAGNINRSLSQLGNLINILAEISQ---------- 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  304 svsnggdsgilsspsgtssggapSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNI 383
Cdd:PLN03188  378 -----------------------TGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
                         410       420       430
                  ....*....|....*....|....*....|...
gi 767984833  384 INKPRVNE----DANL--KLIRELREEIERLKA 410
Cdd:PLN03188  435 KNKAVVNEvmqdDVNFlrEVIRQLRDELQRVKA 467
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
3-381 5.39e-61

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: 214.08  E-value: 5.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRN---LKVDNRPDGfgdsreKVMAFGFDYCYwsvnpeDPQYASQDVF 79
Cdd:cd01367     1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHepkLKVDLTKYI------ENHTFRFDYVF------DESSSNETVY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   80 QDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEG----LFvREKDCASLPSSCRIKVSFLEIYNE 155
Cdd:cd01367    69 RSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVF-RLLNKLPYKDNLGVTVSFFEIYGG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  156 RVRDLLkqSGQKKsytLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIhytqaI 235
Cdd:cd01367   148 KVFDLL--NRKKR---VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI-----I 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  236 LENNLPSEMASKINLVDLAGSERADPSYCKDRI--AEGANINKSLVTLGIVISTLAQNsqvfsscqslnssvsnggdsgi 313
Cdd:cd01367   218 LRDRGTNKLHGKLSFVDLAGSERGADTSSADRQtrMEGAEINKSLLALKECIRALGQN---------------------- 275
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984833  314 lsspsgtssggapsrrQSYIPYRDSVLTWLLKDSL-GGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 381
Cdd:cd01367   276 ----------------KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
470-578 5.49e-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: 5.49e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  470 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 549
Cdd:cd22708     1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
                          90       100
                  ....*....|....*....|....*....
gi 767984833  550 GREVTASCRLTQGAVITLGKAQKFRFNHP 578
Cdd:cd22708    81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
4-381 7.65e-59

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: 208.40  E-value: 7.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    4 VQVAVRVRPLSKRETKEGGRIIVEVdgkvakIRNLKVD-NRPDG-FGDSREKVMAF-GFDYCYWSVNPedPQYASQDVFQ 80
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEV------INSTTVVlHPPKGsAANKSERNGGQkETKFSFSKVFG--PNTTQKEFFQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   81 DLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFvrekdcASLPSScRIKVSFLEIYNERVRDL 160
Cdd:cd01368    75 GTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF------NSIGGY-SVFVSYIEIYNEYIYDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  161 LKQSGQ---KKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILE 237
Cdd:cd01368   148 LEPSPSsptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  238 NNLPSEM------ASKINLVDLAGSERA-DPSYCKDRIAEGANINKSLVTLGIVISTLAQNSQvfsscqslnssvsnggd 310
Cdd:cd01368   228 SDGDVDQdkdqitVSQLSLVDLAGSERTsRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQL----------------- 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984833  311 sgilsspsgtssggapSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 381
Cdd:cd01368   291 ----------------QGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
4-381 1.31e-57

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: 204.35  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    4 VQVAVRVRPlskRETKEGGRIIVEVDGKVAKIrNLKVDNRpDGFGDSREKVMAFGFDYCYwsvnpedpQYASQD-VFQDL 82
Cdd:cd01375     2 VQAFVRVRP---TDDFAHEMIKYGEDGKSISI-HLKKDLR-RGVVNNQQEDWSFKFDGVL--------HNASQElVYETV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   83 GMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTP---ASVGLTPRICEGLFvREKDCASlPSSCRIKVSFLEIYNERVRD 159
Cdd:cd01375    69 AKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTenyKHRGIIPRALQQVF-RMIEERP-TKAYTVHVSYLEIYNEQLYD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  160 LL--KQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILE 237
Cdd:cd01375   147 LLstLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  238 NNLPSEMASKINLVDLAGSERADPSYCKDRI-AEGANINKSLVTLGIVISTLAQnsqvfsscqslnssvsnggdsgilss 316
Cdd:cd01375   227 LSSEKYITSKLNLVDLAGSERLSKTGVEGQVlKEATYINKSLSFLEQAIIALSD-------------------------- 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984833  317 psgtssggapsRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 381
Cdd:cd01375   281 -----------KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
3-381 1.58e-54

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: 195.03  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    3 NVQVAVRVRPLSKRETKEGGRIIVEVDGKVAkirnLKVDNRpdgfgDSREKVMAFGFDYCYwsvNPEDPQyasQDVFQDL 82
Cdd:cd01376     1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCS----VELADP-----RNHGETLKYQFDAFY---GEESTQ---EDIYARE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   83 GMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLfVREKDCASLPSscRIKVSFLEIYNERVRDLLk 162
Cdd:cd01376    66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDL-LQMTRKEAWAL--SFTMSYLEIYQEKILDLL- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  163 qsgQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLpS 242
Cdd:cd01376   142 ---EPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPF-R 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  243 EMASKINLVDLAGSERADPSYCKD-RIAEGANINKSLVTLGIVISTLAQNsqvfsscqslnssvsnggdsgilsspsgts 321
Cdd:cd01376   218 QRTGKLNLIDLAGSEDNRRTGNEGiRLKESGAINSSLFVLSKVVNALNKN------------------------------ 267
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  322 sggapsrrQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAK 381
Cdd:cd01376   268 --------LPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
470-586 1.36e-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: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  470 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVN 549
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767984833  550 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQ 586
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
470-585 6.22e-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: 6.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  470 GVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDqeqDIVLQGQWIERDHCTITSACGVVVLRPArGARCTVN 549
Cdd:cd22713     9 ALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASD---IISLQGPGVEPEHCYIENINGTVTLYPC-GNLCSVD 84
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767984833  550 GREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLR 585
Cdd:cd22713    85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
477-577 6.92e-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: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  477 LPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGREVTAS 556
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
                          90       100
                  ....*....|....*....|.
gi 767984833  557 CRLTQGAVITLGKAQKFRFNH 577
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
478-589 2.30e-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: 2.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  478 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITS---ACG--VVVLRPARGARCTVNGRE 552
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSdtrSGGeaVVTLEPCEGADTYVNGKK 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767984833  553 VTASCRLTQGAVITLGKAQKFRFNHPAEAavlRQRRQ 589
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQA---RQERE 115
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
473-578 1.78e-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: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  473 IDSSLPHLMAL-EDDVLStGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGR 551
Cdd:cd22707     3 VDNKLPNLVNLnEDPQLS-EMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGE 81
                          90       100
                  ....*....|....*....|....*..
gi 767984833  552 EVTASCRLTQGAVITLGKAQKFRFNHP 578
Cdd:cd22707    82 LISEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
478-580 1.39e-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: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  478 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACG-----VVVLRPARGARCTVNGRE 552
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNnngevIVTLEPCERSETYVNGKR 82
                          90       100
                  ....*....|....*....|....*...
gi 767984833  553 VTASCRLTQGAVITLGKAQKFRFNHPAE 580
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
478-578 5.56e-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: 5.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  478 PHLMAL-EDDVLStGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPAR-GARCTVNGREVTA 555
Cdd:cd22709     1 PHLLNLnEDPQLS-GVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTG 79
                          90       100
                  ....*....|....*....|...
gi 767984833  556 SCRLTQGAVITLGKAQKFRFNHP 578
Cdd:cd22709    80 ETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
478-577 6.28e-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: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  478 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDqeqdIVLQGQWIERDHC---TITSACG--VVVLRPARGARCTVNGRE 552
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVD----IKLSGQFIREQHClfrSIPNPSGevVVTLEPCEGAETYVNGKQ 77
                          90       100
                  ....*....|....*....|....*
gi 767984833  553 VTASCRLTQGAVITLGKAQKFRFNH 577
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
4512-4704 7.88e-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: 7.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4512 CQATAGWNYQGEEQAVQLYYK-VFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTARLHQRVTNSISLVYLV 4590
Cdd:cd00177    11 LEEPEGWKLVKEKDGVKIYTKpYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4591 cnTTLCALKQPRDFCCVCVEAKEVPALVghlsVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQPItveGKEVTRVIYLA 4670
Cdd:cd00177    91 --TKPPWPVSPRDFVYLRRRRKLDDGTY----VIVSKSVDHDSHP-KEKGYVRAEIKLSGWIIEPL---DPGKTKVTYVL 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767984833 4671 QVELGApGFPPQLLSSFIKRQPLVIARLASFLGR 4704
Cdd:cd00177   161 QVDPKG-SIPKSLVNSAAKKQLASFLKDLRKAKK 193
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
60-287 2.63e-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: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   60 DYCYWSVNPEDPQYASQ-DVFQDLGmEVLSGVAKGYNI-CLFAYGQTGSGKTYTMLGtpasvgLTPRICEGLFvrekdca 137
Cdd:cd01363    16 DSKIIVFYRGFRRSESQpHVFAIAD-PAYQSMLDGYNNqSIFAYGESGAGKTETMKG------VIPYLASVAF------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  138 slpsscrikvsfleiynervrdllkqSGQKKSYTLrvrehpemgpYVQGLSQHVVTNYKQVIQLLEEGIANRiTAATHVH 217
Cdd:cd01363    82 --------------------------NGINKGETE----------GWVYLTEITVTLEDQILQANPILEAFG-NAKTTRN 124
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  218 EASSRSHAIFTIhytqailennlpsemaskinLVDLAGSERadpsyckdriaeganINKSLVTLGIVIST 287
Cdd:cd01363   125 ENSSRFGKFIEI--------------------LLDIAGFEI---------------INESLNTLMNVLRA 159
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
495-578 2.14e-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: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  495 YHLKEgTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGREVTASCRLTQGAVITLGKAQKFR 574
Cdd:cd22706    19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97

                  ....
gi 767984833  575 FNHP 578
Cdd:cd22706    98 LNCP 101
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
3-161 1.79e-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: 67.63  E-value: 1.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833     3 NVQVAVRVRPLSKRETKeggriivevdgkvakirnLKVDNRPDGFGDSREKVMAFGFDYCywsVNPEDPQyasQDVFQDL 82
Cdd:pfam16796   21 NIRVFARVRPELLSEAQ------------------IDYPDETSSDGKIGSKNKSFSFDRV---FPPESEQ---EDVFQEI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    83 GMEVLSgVAKGYNICLFAYGQTGSGKTytmlgtpasVGLTPRICEGLF--VREKDCAslpSSCRIKVSFLEIYNERVRDL 160
Cdd:pfam16796   77 SQLVQS-CLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFrfISSLKKG---WKYTIELQFVEIYNESSQDL 143

                   .
gi 767984833   161 L 161
Cdd:pfam16796  144 L 144
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
495-575 3.84e-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: 3.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  495 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCT-VNGREVTASCRLTQGAVITLGKAQkF 573
Cdd:cd00060    14 FPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTfVNGKRITPPVPLQDGDVIRLGDTT-F 89

                  ..
gi 767984833  574 RF 575
Cdd:cd00060    90 RF 91
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
480-578 3.99e-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: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  480 LMALEDDVLSTGVVLYHLKEgTTKIGRIDSdqeQDIVLQGQWIERDHCTI-TSACGVVVLRPARGARCTVNGREVTASCR 558
Cdd:cd22730     4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIdITPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
                          90       100
                  ....*....|....*....|
gi 767984833  559 LTQGAVITLGKAQKFRFNHP 578
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
480-588 1.36e-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: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  480 LMALEDDVLSTGVVLYHLKEGTtkigRIDSDQEQDIVLQGQWIERDHCTITSAC-GVVVLRPARGARCTVNGREVTASCR 558
Cdd:cd22729     4 LVNLNADPALNELLVYYLKDHT----RVGADTSQDIQLFGIGIQPEHCVIDIAAdGDVTLTPKENARTCVNGTLVCSVTQ 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 767984833  559 LTQGAVITLGKAQKFRFNHPAeaavlRQRR 588
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLPK-----RKRR 104
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
477-578 1.45e-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: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  477 LPHLMALEDDVLSTG-VVLYHLKEGTTKIG--RIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARG-ARCTVNGRE 552
Cdd:cd22711     1 LPYLLELSPDGSDRDkPRRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYVNGQR 80
                          90       100
                  ....*....|....*....|....*.
gi 767984833  553 VTASCRLTQGAVITLGKAQKFRFNHP 578
Cdd:cd22711    81 IYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
475-578 5.38e-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: 5.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  475 SSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSD-QEQDIVLQGQWIERDHCTIT---------------SACGVVVL 538
Cdd:cd22712     1 SDYPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEGaRKVDISLRAPDILPQHCWIRrkpeplsddedsdkeSADYRVVL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767984833  539 RPARGARCTVNGREVTASCRLTQGAVITLGKAQKFRFNHP 578
Cdd:cd22712    81 SPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
495-575 8.93e-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: 8.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  495 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCT-VNGREVTASCRLTQGAVITLGKaQKF 573
Cdd:COG1716    16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTfVNGQRVTEPAPLRDGDVIRLGK-TEL 91

                  ..
gi 767984833  574 RF 575
Cdd:COG1716    92 RF 93
START pfam01852
START domain;
4550-4704 3.55e-06

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 50.86  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  4550 PLSRVWAAVSDPTV---------------WPLYYKPIQTarlHQRVTNSISLVYLVCNTTLCALKQPRDFccvcVEAKEV 4614
Cdd:pfam01852   43 EASRASGVVPMVAAllvaellkdmeyraqWDKDVRSAET---LEVISSGGDLQYYVAALVAPSPLSPRDF----VFLRYW 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  4615 PALVGHLSVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQPitvEGKEVTRVIYLAQVELGApGFPPQLLSSFIKR-QPL 4693
Cdd:pfam01852  116 RRLGGGVYVIVDRSVTHPQFP-PSSGYVRAERLPSGYLIQP---CGNGPSKVTWVSHADLKG-WLPSWLLRSLYKSgMPE 190
                          170
                   ....*....|.
gi 767984833  4694 VIARLASFLGR 4704
Cdd:pfam01852  191 GAKTWVATLQR 201
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
497-575 6.27e-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: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  497 LKEGTTKIGRidsDQEQDIVLQGQWIERDHCTIT-SACGVVVLRP-ARGARCTVNGREVTASCRLTQGAVITLGKAqKFR 574
Cdd:cd22673    18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGR-SFR 93

                  .
gi 767984833  575 F 575
Cdd:cd22673    94 F 94
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
4516-4697 1.05e-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: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   4516 AGW--NYQGEEQavQLYYKVFSPTR---HGFLGAGVVSQPLSRVWA-AVSDPTVWPLYYKPIQTARLHQRVTNSISLVYL 4589
Cdd:smart00234   18 EGWvlSSENENG--DEVRSIFSPGRkpgEAFRLVGVVPMVCADLVEeLMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHY 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   4590 VCNTTLCALKqPRDFCCVCVEAKevpaLVGHLSVMAAQSVyDTSMPRPSRKMVRGEILPSAWILQPitvEGKEVTRVIYL 4669
Cdd:smart00234   96 VSKFAAGPVS-PRDFVFVRYWRE----DEDGSYAVVDVSV-THPTSPPESGYVRAENLPSGLLIEP---LGNGPSKVTWV 166
                           170       180
                    ....*....|....*....|....*...
gi 767984833   4670 AQVELGAPGfPPQLLSSFIKRQPLVIAR 4697
Cdd:smart00234  167 SHADLKGWL-PHWLVRSLIKSGLAEFAK 193
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
502-567 2.44e-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: 2.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984833   502 TKIGRidsDQEQDIVLQGQWIERDHCTIT-SACGVVVLRPARGARCT-VNGREVT-ASCRLTQGAVITL 567
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNGTfVNGQRLGpEPVRLKDGDVIRL 66
Kinesin_assoc pfam16183
Kinesin-associated;
389-500 5.21e-04

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 44.06  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   389 VNEDANLKLIRELREEIERLKALLLSFELRN------------------------------------------------- 419
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYAQGLGDiidtiahptkkrantpaanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   420 -----FSSLSDENLKELvLQNELKIDQLTKDWTQKWN-------DWQALMEHYSVDI--NRRRAGVVIDSSLPHLMALED 485
Cdd:pfam16183   83 herimFTPGSEEAIERL-KETEKIIAELNETWEEKLRkteairmEREALLAEMGVAIreDGGTLGVFSPKKTPHLVNLNE 161
                          170
                   ....*....|....*
gi 767984833   486 DVLSTGVVLYHLKEG 500
Cdd:pfam16183  162 DPLMSECLLYYIKDG 176
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
495-578 6.10e-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: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   495 YHLKEGTTKIGridSDQEQDIVLQGQWIERDHCTITSACGVVVLRPArGARC--TVNGREVT-ASCRLTQGAVITLGKAq 571
Cdd:pfam16697   12 FPLEGGRYRIG---SDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDL-GSGNgtLVNGQRVTeLGIALRPGDRIELGQT- 86

                   ....*..
gi 767984833   572 KFRFNHP 578
Cdd:pfam16697   87 EFCLVPA 93
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
4506-4658 3.62e-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: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4506 LHNLFSCQATAGWNYQGEE--------QAVQLYYKVFSPTrhgflgaGVVSQPLSRVWAA-VSDPTVWPLYYKPIQTARL 4576
Cdd:cd08868    14 LARAWSILTDPGWKLEKNTtwgdvvysRNVPGVGKVFRLT-------GVLDCPAEFLYNElVLNVESLPSWNPTVLECKI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833 4577 HQRVTNSISLVYLVCNTTLCALKQPRDFCCV-CVEAKEvpalvgHLSVMAAQSVYDTSMPrPSRKMVRGEILPSAWILQP 4655
Cdd:cd08868    87 IQVIDDNTDISYQVAAEAGGGLVSPRDFVSLrHWGIRE------NCYLSSGVSVEHPAMP-PTKNYVRGENGPGCWILRP 159

                  ...
gi 767984833 4656 ITV 4658
Cdd:cd08868   160 LPN 162
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-285 3.94e-03

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 43.57  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833    1 MANVQVAVRVRPLS-KRETKEGGRIIVEVDgkvAKIRNLKVDNrpdGFGDSREKVMAFGFDYCywsvnpEDPQYASQDVF 79
Cdd:COG5059   304 NCNTRVICTISPSSnSFEETINTLKFASRA---KSIKNKIQVN---SSSDSSREIEEIKFDLS------EDRSEIEILVF 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833   80 QDLGMEVLSgvaKGYNIclFAYGQTGSGKTYTMLgtPASVGLTPRICEGLFvreKDCASLPSSCRIKVS---FLEIYNER 156
Cdd:COG5059   372 REQSQLSQS---SLSGI--FAYMQSLKKETETLK--SRIDLIMKSIISGTF---ERKKLLKEEGWKYKStlqFLRIEIDR 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  157 VRDLLKQSGQKKSYTLRVREHpemgpyvqgLSQHVVTNYKQV----IQLLEEGIA--NRITAATHVHEASSRSHAIFTIH 230
Cdd:COG5059   442 LLLLREEELSKKKTKIHKLNK---------LRHDLSSLLSSIpeetSDRVESEKAskLRSSASTKLNLRSSRSHSKFRDH 512
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767984833  231 ytqaiLENNLPSEMASKINLVDLAGSERADPSYCKDRIAEGANINKSLVTLGIVI 285
Cdd:COG5059   513 -----LNGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSLNKSLSSLGDVI 562
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
579-785 4.50e-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: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  579 AEAAVLRQRRQVG--EAAAGRGSlEWLDLDGDLAASRLGLSPL-LWKERRALE------EQCDEDHQTPRDGETSHRAQI 649
Cdd:COG4913   240 AHEALEDAREQIEllEPIRELAE-RYAAARERLAELEYLRAALrLWFAQRRLElleaelEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  650 QQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASL--QQQQQEDQVAEKELEASVALDAWLQ 727
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEE 398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984833  728 TDPEIQpspfvqsqkrvvhlqlLRRHTLRAAERNVRRkkvsfQLERIIKKQRLLEAQK 785
Cdd:COG4913   399 ELEALE----------------EALAEAEAALRDLRR-----ELRELEAEIASLERRK 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
579-790 8.17e-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: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  579 AEAAVLRQRRQVGEAAAGRGSLEWLDLDGDLAASRLglspllwkERRALEEQcDEDHQTPRDGETSHRAQIQQQQSYVED 658
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRL--------ELEELELE-LEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984833  659 LRHQILAEEIRAAKELEfdqAWISQQIKENQQcllrEETWLASLQQQQQEDQVAEKELEASVALdawlqtdpeiqpspfV 738
Cdd:COG1196   310 RRRELEERLEELEEELA---ELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEA---------------L 367
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767984833  739 QSQKRVVHLQLLRRHTLRAAERNVRRKKVSFQLERIIKKQRLLEAQKRLEKL 790
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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