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Conserved domains on  [gi|1034659761|ref|XP_016868746|]
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kinesin-like protein KIF13B isoform X5 [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 ...
 4-360 0e+00

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


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 600.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365     80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365    160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365    240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1034659761  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365    320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 447-545 3.39e-68

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: 224.02  E-value: 3.39e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730      1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                           90
                   ....*....|....*....
gi 1034659761  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730     81 HHGDRILWGNNHFFRINLP 99
Kinesin_assoc super family cl24686
Kinesin-associated;
357-469 2.24e-25

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 104.54  E-value: 2.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 1034659761  455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 756-802 2.86e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 65.32  E-value: 2.86e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034659761  756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
DUF3694 super family cl13857
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1221-1278 8.58e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


The actual alignment was detected with superfamily member pfam12473:

Pssm-ID: 463599  Cd Length: 149  Bit Score: 49.89  E-value: 8.58e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034659761 1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
bMERB_dom super family cl48129
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 1099-1143 3.80e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


The actual alignment was detected with superfamily member pfam12130:

Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 42.12  E-value: 3.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034659761 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 4-360 0e+00

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


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 600.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365     80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365    160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365    240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1034659761  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365    320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-360 6.11e-157

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: 478.22  E-value: 6.11e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761     6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129   70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129  148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129  225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300

                           330       340       350
                    ....*....|....*....|....*....|....*
gi 1034659761   326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129  301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 4.11e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 457.03  E-value: 4.11e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225   69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225  148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301

                          330       340
                   ....*....|....*....|....*
gi 1034659761  329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225  302 NISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
50-439 1.87e-91

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 308.59  E-value: 1.87e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059     52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059    124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059    201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059    277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059    353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432


                   ...
gi 1034659761  437 QSS 439
Cdd:COG5059    433 QFL 435
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 3-379 1.01e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 283.36  E-value: 1.01e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188    97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188   153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188   233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188   311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659761  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188   390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 447-545 3.39e-68

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: 224.02  E-value: 3.39e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730      1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                           90
                   ....*....|....*....
gi 1034659761  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730     81 HHGDRILWGNNHFFRINLP 99
Kinesin_assoc pfam16183
Kinesin-associated;
357-469 2.24e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 104.54  E-value: 2.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 1034659761  455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 756-802 2.86e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 65.32  E-value: 2.86e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034659761  756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 471-534 7.85e-11

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 59.13  E-value: 7.85e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034659761  471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1221-1278 8.58e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 49.89  E-value: 8.58e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034659761 1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
468-542 9.26e-06

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 45.72  E-value: 9.26e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659761  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716     20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 1099-1143 3.80e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 42.12  E-value: 3.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034659761 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
 368-444 3.55e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 40.74  E-value: 3.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034659761  368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493     36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-432 4.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659761  368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918   216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 4-360 0e+00

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


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 600.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365     80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365    160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365    240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1034659761  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365    320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-360 6.11e-157

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: 478.22  E-value: 6.11e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761     6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129   70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129  148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129  225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300

                           330       340       350
                    ....*....|....*....|....*....|....*
gi 1034659761   326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129  301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 4.11e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 457.03  E-value: 4.11e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225   69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225  148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301

                          330       340
                   ....*....|....*....|....*
gi 1034659761  329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225  302 NISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 5-351 1.05e-142

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: 439.77  E-value: 1.05e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRRETDLhTKCVVDVDANK-VILNPvntnlsKGDARGQPKVFAYDHCFWSMdesvkekyAGQDIVFKCL 83
Cdd:cd00106      1 NVRVAVRVRPLNGREARS-AKSVISVDGGKsVVLDP------PKNRVAPPKTFAFDAVFDST--------STQEEVYEGT 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD-QPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd00106     66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPeQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  163 DPKgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHtlYDVKSGTS 242
Cdd:cd00106    146 SPV-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd00106    223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNS 297

                          330       340
                   ....*....|....*....|....*....
gi 1034659761  323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd00106    298 KTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 6-353 3.14e-120

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: 379.50  E-value: 3.14e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    6 VKVAVRIRPMNRRETDLHTKCVVDVDankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmDESVKEkYAGQDIVFKCLGE 85
Cdd:cd01371      3 VKVVVRCRPLNGKEKAAGALQIVDVD---EKRGQVSVRNPKATANEPPKTFTFDAVF---DPNSKQ-LDVYDETARPLVD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   86 NILQnafdGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01371     76 SVLE----GYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ-FLVRVSYLEIYNEEIRDLL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  163 DpKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlYDVKSGTS 242
Cdd:cd01371    151 G-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS-EKGEDGEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01371    229 HIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNS 303

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1034659761  323 KTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01371    304 KTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 5-355 1.22e-111

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: 355.75  E-value: 1.22e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNpvntnLSKGDARgqPKVFAYDHCFwSMDESvkekyagQDIVFKCLg 84
Cdd:cd01366      3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIE-----LTSIGAK--QKEFSFDKVF-DPEAS-------QEDVFEEV- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDP 164
Cdd:cd01366     67 SPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAP 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  165 KGSRQT-LKVREHSVLGP-YVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKItlthTLYDVKSGTS 242
Cdd:cd01366    147 GNAPQKkLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFIL----HISGRNLQTG 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01366    223 EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSLGGNS 296

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1034659761  323 KTAMVATVSPAADNYDETLSTLRYADRAKHIVN 355
Cdd:cd01366    297 KTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 6-353 1.14e-110

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: 353.96  E-value: 1.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    6 VKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNP----------VNTNLSKGDARGQPKVFAYDHCFwsmDEsvkekYA 74
Cdd:cd01370      2 LTVAVRVRPFSEKEKNEGFRRIVKVmDNHMLVFDPkdeedgffhgGSNNRDRRKRRNKELKYVFDRVF---DE-----TS 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   75 GQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIY 154
Cdd:cd01370     74 TQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK-DEKEFEVSMSYLEIY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  155 NEKVRDLLDPKGSRqtLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTl 234
Cdd:cd01370    153 NETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  235 YDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsaGKNKNKFVPYRDSVLTWLL 314
Cdd:cd01370    230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLL 306

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1034659761  315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01370    307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 4-353 2.18e-110

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: 352.79  E-value: 2.18e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANK--VILnpvntnlskgdarGQPKVFAYDHCFWSMDEsvkekyagQDIVFK 81
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEpqVTV-------------GTDKSFTFDYVFDPSTE--------QEEVYN 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA------DQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYN 155
Cdd:cd01372     60 TCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKVSFLEIYN 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  156 EKVRDLLDPKG-SRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTL 234
Cdd:cd01372    139 EEIRDLLDPETdKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTK 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  235 YDVKSGTSGEK------VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgknKNKFVPYRDS 308
Cdd:cd01372    219 KNGPIAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK---KGAHVPYRDS 295

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034659761  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01372    296 KLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 3-353 4.25e-110

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: 351.63  E-value: 4.25e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    3 DSKVKVAVRIRPMNRRETDLHTKCVVDVDankvilnPVNTNLSKGDARGqpKVFAYDHCFwSMDesvkekyAGQDIVFKC 82
Cdd:cd01369      1 ECNIKVVCRFRPLNELEVLQGSKSIVKFD-------PEDTVVIATSETG--KTFSFDRVF-DPN-------TTQEDVYNF 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEIYNEKVR 159
Cdd:cd01369     64 AAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSM-DENLEFHVKVSYFEIYMEKIR 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  160 DLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlyDVKS 239
Cdd:cd01369    143 DLLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVET 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  240 GTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLG 319
Cdd:cd01369    219 EKK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLG 291

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1034659761  320 GNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01369    292 GNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 5-353 8.62e-109

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: 347.78  E-value: 8.62e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNlskgdargqpkvFAYDHCFwSMDESVKEkyagqdiVFKCL 83
Cdd:cd01374      1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLvEPPSTS------------FTFDHVF-GGDSTNRE-------VYELI 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQkeENEEQSFKVEVSYMEIYNEKVRDLLD 163
Cdd:cd01374     61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKINDLLS 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  164 PKGsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGtSG 243
Cdd:cd01374    139 PTS--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GT 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  244 EKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqSAGKnKNKFVPYRDSVLTWLLKDSLGGNSK 323
Cdd:cd01374    216 VRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGK-VGGHIPYRDSKLTRILQPSLGGNSR 291

                          330       340       350
                   ....*....|....*....|....*....|
gi 1034659761  324 TAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01374    292 TAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 6-362 2.53e-100

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: 325.23  E-value: 2.53e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    6 VKVAVRIRPMNRRETDL-HTKCVVDVDANKVILNPVntnlskgdargQPKVFAYDHcfwsmdesVKEKYAGQDIVFKCLG 84
Cdd:cd01373      3 VKVFVRIRPPAEREGDGeYGQCLKKLSSDTLVLHSK-----------PPKTFTFDH--------VADSNTNQESVFQSVG 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP--------GLIPRLCSGLFERTQKEEN---EEQSFKVEVSYMEI 153
Cdd:cd01373     64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEkagEGKSFLCKCSFLEI 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  154 YNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 233
Cdd:cd01373    144 YNEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES- 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  234 lYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNkfVPYRDSVLTWL 313
Cdd:cd01373    221 -WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRH--VCYRDSKLTFL 297

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1034659761  314 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01373    298 LRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 3-362 3.77e-94

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: 308.10  E-value: 3.77e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    3 DSKVKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNPVNTNLSKGDArgqpKVFAYDHCFWSmdesvkekYAGQDIVFK 81
Cdd:cd01364      1 GKNIQVVVRCRPFNLRERKASSHSVVEVdPVRKEVSVRTGGLADKSST----KTYTFDMVFGP--------EAKQIDVYR 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMG-----------TADQPGLIPRLCSGLFErtqKEENEEQSFKVEVSY 150
Cdd:cd01364     69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFE---KLEDNGTEYSVKVSY 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  151 MEIYNEKVRDLLDPKGS-RQTLKVREHS--VLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFK 227
Cdd:cd01364    146 LEIYNEELFDLLSPSSDvSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  228 ITLthtlYDVKSGTSGE---KVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagknKNKFVP 304
Cdd:cd01364    226 ITI----HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVP 295

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034659761  305 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01364    296 YRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
50-439 1.87e-91

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 308.59  E-value: 1.87e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059     52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059    124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059    201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059    277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059    353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432


                   ...
gi 1034659761  437 QSS 439
Cdd:COG5059    433 QFL 435
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 5-351 1.74e-78

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 263.49  E-value: 1.74e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRRETDLHTK-CVVDVDANKVILNPVNTNLSKGDARG---QPKVFAYDHCFwSMDESVKEKYAGqdiVF 80
Cdd:cd01368      2 PVKVYLRVRPLSKDELESEDEgCIEVINSTTVVLHPPKGSAANKSERNggqKETKFSFSKVF-GPNTTQKEFFQG---TA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   81 KCLGENILQnafdGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFertqkeeNEEQSFKVEVSYMEIYNEKVRD 160
Cdd:cd01368     78 LPLVQDLLH----GKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF-------NSIGGYSVFVSYIEIYNEYIYD 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  161 LLDPKGS-----RQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL----T 231
Cdd:cd01368    147 LLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapG 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  232 HTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdQSAGKNKNKFVPYRDSVLT 311
Cdd:cd01368    227 DSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLR-ENQLQGTNKMVPFRDSKLT 305

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1034659761  312 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01368    306 HLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 3-379 1.01e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 283.36  E-value: 1.01e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188    97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188   153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188   233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188   311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659761  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188   390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 5-351 1.26e-74

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: 252.12  E-value: 1.26e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRREtdlHTKCVVDVDaNKVILNPVNTNLSKGDARGQPKVFAYdhcfwSMDESVKEkyAGQDIVFKCLG 84
Cdd:cd01375      1 KVQAFVRVRPTDDFA---HEMIKYGED-GKSISIHLKKDLRRGVVNNQQEDWSF-----KFDGVLHN--ASQELVYETVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD---QPGLIPRLCSGLFErtQKEENEEQSFKVEVSYMEIYNEKVRDL 161
Cdd:cd01375     70 KDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFR--MIEERPTKAYTVHVSYLEIYNEQLYDL 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  162 LDPK----GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL---THTL 234
Cdd:cd01375    148 LSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeahSRTL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  235 YDVKSGTSgekvgKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQsagknKNKFVPYRDSVLTWLL 314
Cdd:cd01375    228 SSEKYITS-----KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHVPFRQSKLTHVL 297

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1034659761  315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01375    298 RDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 5-351 1.12e-73

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 249.14  E-value: 1.12e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIlnPVNTNLSKGDARGQPKV--FAYDHCFwsmDESVKekyagQDIVFKC 82
Cdd:cd01367      1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTL--IVHEPKLKVDLTKYIENhtFRFDYVF---DESSS-----NETVYRS 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMG----TADQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKV 158
Cdd:cd01367     71 TVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN-LGVTVSFFEIYGGKV 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  159 RDLLDPKgsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvK 238
Cdd:cd01367    150 FDLLNRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------R 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  239 SGTSGEKVGKLSLVDLAGSERATKTGAAG-DRLKEGSNINKSLTTLGLVISALADQSAgknknkFVPYRDSVLTWLLKDS 317
Cdd:cd01367    220 DRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA------HIPFRGSKLTQVLKDS 293

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1034659761  318 L-GGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01367    294 FiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 6-351 7.62e-69

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: 234.70  E-value: 7.62e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    6 VKVAVRIRPMNRRETDLHTKCVVDvdankvILNPVNTNLSKGDARGQPKVFAYDHcFWSMDESVKEKYAGQdivFKClge 85
Cdd:cd01376      2 VRVAVRVRPFVDGTAGASDPSCVS------GIDSCSVELADPRNHGETLKYQFDA-FYGEESTQEDIYARE---VQP--- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   86 nILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEneeQSFKVEVSYMEIYNEKVRDLLDPK 165
Cdd:cd01376     69 -IVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA---WALSFTMSYLEIYQEKILDLLEPA 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  166 GSRqtLKVRE---HSVLGPyvdGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVksgTS 242
Cdd:cd01376    145 SKE--LVIREdkdGNILIP---GLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---PF 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqsagKNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01376    217 RQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------NKNLPRIPYRDSKLTRLLQDSLGGGS 290

                          330       340
                   ....*....|....*....|....*....
gi 1034659761  323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01376    291 RCIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 447-545 3.39e-68

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: 224.02  E-value: 3.39e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730      1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                           90
                   ....*....|....*....
gi 1034659761  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730     81 HHGDRILWGNNHFFRINLP 99
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 447-545 1.98e-59

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: 199.06  E-value: 1.98e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANS---QDIQLCGMGILPEHCIIDItSEGQVMLTPQKNTRTFVNGSSVSSP 523
Cdd:cd22706      1 KYYLVNLNADPSLNELLVYYLKEHTLIGRSDAptqQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79

                           90       100
                   ....*....|....*....|..
gi 1034659761  524 IQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22706     80 TQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 447-550 1.16e-55

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: 188.56  E-value: 1.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22729      1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80

                           90       100
                   ....*....|....*....|....
gi 1034659761  527 HHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22729     81 WHGDRILWGNNHFFRINLPKRKRR 104
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 450-543 6.41e-34

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: 126.19  E-value: 6.41e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22705      4 LVNLNEDPLMSECLLYYIKPgITRVGRADAdvpQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPTR 82

                           90
                   ....*....|....*...
gi 1034659761  526 LHHGDRILWGNNHFFRLN 543
Cdd:cd22705     83 LKTGSRVILGKNHVFRFN 100
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 450-545 3.20e-31

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: 118.52  E-value: 3.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKE-HTLIGS--ANSQ-DIQLCGMGILPEHCIIdITSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22707     10 LVNLNEDPQLSEMLLYMLKEgQTRVGRskASSShDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88

                           90       100
                   ....*....|....*....|
gi 1034659761  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22707     89 LHHGDRVILGGDHYFRFNHP 108
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 448-545 1.28e-28

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: 110.77  E-value: 1.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  448 CFLVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIdITSEGQVMLTPQKNT-RTFVNGSSVSS 522
Cdd:cd22709      1 PHLLNLNEDPQLSGVIVHFLQEgETTIGRADAepePDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPGaKVIVNGVPVTG 79

                           90       100
                   ....*....|....*....|...
gi 1034659761  523 PIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22709     80 ETELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 58-289 3.07e-28

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: 112.44  E-value: 3.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   58 YDHCFWSMDeSVKEKYAGQDIVFKcLGENILQNAFDGYN-ACIFAYGQTGSGKSYTMMGtadqpgLIPRLCSGLFERTQK 136
Cdd:cd01363     15 RDSKIIVFY-RGFRRSESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  137 EENEEQsfkvevsymeiynekvrdlldpkgsrqtlkvrehsvlgpyvDGLSKLAVTSYKDIESLMSEGNKSRTvAATNMN 216
Cdd:cd01363     87 GETEGW-----------------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRN 124

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034659761  217 EESSRSHAVFKItlthtlydvksgtsgekvgklsLVDLAGSERatktgaagdrlkegsnINKSLTTLGLVISA 289
Cdd:cd01363    125 ENSSRFGKFIEI----------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
Kinesin_assoc pfam16183
Kinesin-associated;
357-469 2.24e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 104.54  E-value: 2.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 1034659761  455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 450-547 1.32e-23

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: 97.03  E-value: 1.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVS 521
Cdd:cd22727      5 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNNNGEVIVTlePCERSETYVNGKRVV 84

                           90       100
                   ....*....|....*....|....*.
gi 1034659761  522 SPIQLHHGDRILWGNNHFFRLNLPKK 547
Cdd:cd22727     85 QPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 450-554 4.19e-20

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: 87.29  E-value: 4.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQ--VMLTPQKNTRTFVNGSSVS 521
Cdd:cd22726      4 LVNLNEDPLMSECLLYYIKDGiTRVGREDAerrQDIVLSGHFIKEEHCIFrsDTRSGGEavVTLEPCEGADTYVNGKKVT 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034659761  522 SPIQLHHGDRILWGNNHFFRLNLPKKKKKaERE 554
Cdd:cd22726     84 EPSILRSGNRIIMGKSHVFRFNHPEQARQ-ERE 115
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 5-162 1.95e-18

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 83.42  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761    5 KVKVAVRIRPMNRREtdlhtkcvvdvdankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmdesvkEKYAGQDIVFKCLg 84
Cdd:pfam16796   21 NIRVFARVRPELLSE---------------AQIDYPDETSSDGKIGSKNKSFSFDRVF--------PPESEQEDVFQEI- 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034659761   85 ENILQNAFDGYNACIFAYGQTGSGKSytmmgtadqPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:pfam16796   77 SQLVQSCLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGWK-YTIELQFVEIYNESSQDLL 144
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 450-543 2.10e-17

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: 79.14  E-value: 2.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKEH-TLIGSANSqDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVSSPI 524
Cdd:cd22728      4 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLSGQFIREQHCLFrsIPNPSGEVVVTlePCEGAETYVNGKQVTEPL 82

                           90
                   ....*....|....*....
gi 1034659761  525 QLHHGDRILWGNNHFFRLN 543
Cdd:cd22728     83 VLKSGNRIVMGKNHVFRFN 101
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 450-545 3.14e-17

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: 78.85  E-value: 3.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22708     11 LIGIDDDLLSTGVVLYHLKEgKTRIGREDApqeQDIVLDGEDIEAEHCIIE-NVGGVVTLHPLPGALCAVNGQVITQPTR 89

                           90       100
                   ....*....|....*....|
gi 1034659761  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22708     90 LTQGDVILLGKTNMFRFNHP 109
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 448-545 2.27e-15

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: 73.51  E-value: 2.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  448 CFLVNLNADPALNellvYYLKEH------TLIGSANS-----QDIQLCGMGILPEHCIIDITsEGQVMLTP-QKNTRTFV 515
Cdd:cd22711      2 PYLLELSPDGSDR----DKPRRHrlqpnvTEVGSERSpansgQFIQLFGPDILPRHCVITHM-EGVVTVTPaSQDAETYV 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 1034659761  516 NGSSVSSPIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22711     77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 468-539 9.63e-14

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: 68.39  E-value: 9.63e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034659761  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTP-QKNTRTFVNGSSVSSPIQLHHGDRILWGNNHF 539
Cdd:cd22673     20 KKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGRSF 92
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 438-549 1.91e-13

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: 68.12  E-value: 1.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  438 SSGIKVGDDKCFLVNLNADPALNELLVYYLKE-HTLIGSANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNtRTFVN 516
Cdd:cd22713      7 GKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGN-LCSVD 84

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034659761  517 GSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKK 549
Cdd:cd22713     85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 756-802 2.86e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 65.32  E-value: 2.86e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034659761  756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 450-550 1.39e-12

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: 65.73  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKE-HTLIG---SANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22732     11 LIGIDDDLLSTGIILYHLKEgRTYVGrddATTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEATQ 89

                           90       100
                   ....*....|....*....|....*
gi 1034659761  526 LHHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22732     90 LNQGAVILLGRTNMFRFNHPKEAAK 114
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 449-539 4.21e-11

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: 60.75  E-value: 4.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  449 FLVNLNADPALNELLVYylKEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNT-RTFVNGSSVSSPIQLH 527
Cdd:cd00060      1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEVD-GGGVYLEDLGSTnGTFVNGKRITPPVPLQ 77

                           90
                   ....*....|..
gi 1034659761  528 HGDRILWGNNHF 539
Cdd:cd00060     78 DGDVIRLGDTTF 89
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 471-534 7.85e-11

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 59.13  E-value: 7.85e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034659761  471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
 450-545 4.18e-10

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: 58.63  E-value: 4.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  450 LVNLNADPALNELLVYYLKEHTL-IGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22731     11 LIAMDDDILSTGVVLYHLREGTTkIGRSDSeqeQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESCR 89

                           90       100
                   ....*....|....*....|
gi 1034659761  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22731     90 LSQGAVIVLGKTHKFRFNHP 109
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 446-540 7.72e-10

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: 58.08  E-value: 7.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  446 DKCFLVNLNADPALNELLVYYLKEHT-LIGS----ANSQDIQLCGMGILPEHCII--------------DITSEGQVMLT 506
Cdd:cd22712      2 DYPYLLTLRGFSPKQDLLVYPLLEQViLVGSrtegARKVDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1034659761  507 PQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFF 540
Cdd:cd22712     82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
79-290 3.78e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 54.74  E-value: 3.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761   79 VFKCLGENIlQNAFDGynacIFAYGQTGSGKSYTMMgtaDQPGLIPRLC-SGLFERTQKEENEEQSFKVEVSYMEIY-NE 156
Cdd:COG5059    370 VFREQSQLS-QSSLSG----IFAYMQSLKKETETLK---SRIDLIMKSIiSGTFERKKLLKEEGWKYKSTLQFLRIEiDR 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  157 KVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLA-VTSYKDIESLMSegnKSRTVAATNMNEESSRSHAVFKitlthtly 235
Cdd:COG5059    442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPeETSDRVESEKAS---KLRSSASTKLNLRSSRSHSKFR-------- 510

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034659761  236 DVKSG-TSGEKVGKLSLVDLAGSERaTKTGAAGDRLKEGSNINKSLTTLGLVISAL 290
Cdd:COG5059    511 DHLNGsNSSTKELSLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1221-1278 8.58e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 49.89  E-value: 8.58e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034659761 1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
468-542 9.26e-06

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 45.72  E-value: 9.26e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659761  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716     20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 1099-1143 3.80e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 42.12  E-value: 3.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034659761 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
 460-540 4.26e-04

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


Pssm-ID: 438785  Cd Length: 113  Bit Score: 41.32  E-value: 4.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659761  460 NELLVYYL-KEHTLIG---SANSQDIQLCGMGILPEHCII------DITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHG 529
Cdd:cd22733     18 HDCLVYLLnREQHTVGqetPSSKPNISLSAPDILPLHCTIrrvrlpKHRSEEKLVLEPIPGAHVSVNFSEVERTTLLRHG 97

                           90
                   ....*....|.
gi 1034659761  530 DRILWGNNHFF 540
Cdd:cd22733     98 DLLSFGAYYLF 108
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
 368-444 3.55e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 40.74  E-value: 3.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034659761  368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493     36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-432 4.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659761  368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918   216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
 
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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