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Conserved domains on  [gi|118572664|sp|Q02241|]
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RecName: Full=Kinesin-like protein KIF23; AltName: Full=Kinesin-like protein 5; AltName: Full=Mitotic kinesin-like protein 1

Protein Classification

kinesin-like protein KIF23( domain architecture ID 10842314)

kinesin-like protein KIF23 is essential for cytokinesis in Rho-mediated signaling; it has an N-terminal motor domain and is a (+) end-directed motor

CATH:  3.40.850.10
Gene Symbol:  KIF23
SCOP:  4004055

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
24-434 0e+00

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: 605.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  24 DPVGVYCRVRPLGFP----DQECCIEVINNTTVQLHTPEGYRLN---RNGDYKETQYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01368    1 DPVKVYLRVRPLSKDelesEDEGCIEVINSTTVVLHPPKGSAANkseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkr 176
Cdd:cd01368   81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 177 eampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEVPFDPikPKPPQSKLLREDK 256
Cdd:cd01368  130 ---------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSP--TKKRQSLRLREDH 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKEQITISQLSLV 336
Cdd:cd01368  169 NGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD-VDQDKDQITVSQLSLV 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01368  248 DLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPC 327
                        410
                 ....*....|....*...
gi 118572664 417 AEDYEENLQVMRFAEVTQ 434
Cdd:cd01368  328 ASDYDETLHVMKFSAIAQ 345
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
803-906 2.37e-57

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


:

Pssm-ID: 465166  Cd Length: 107  Bit Score: 192.14  E-value: 2.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  803 PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVP---HAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGD 879
Cdd:pfam16540   1 PVVNPRHRRSRSAGERWLDHKPPSNVPTGTILQPRIPnrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 118572664  880 IYKTRGGGQSVQFTDIETLKQESPNGS 906
Cdd:pfam16540  81 VIPTRGGGAQVQFNDIETLKQESPTGS 107
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
484-677 1.22e-06

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 484 EILDINDEqtLPRLIEALEKrhnlrqmmIDEFNKQSNAFKALLQEFDNAVLSKENHMQG---KLNEKEKMISGQKLEIER 560
Cdd:PRK03918 208 EINEISSE--LPELREELEK--------LEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKEIEE 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 561 LEKKNKTLE------YKIEILEKTTTIYEEDKRNLQQELETQNQK---LQRQFSDKRRLEARLqgmvtETTMKWEKECER 631
Cdd:PRK03918 278 LEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERL-----EELKKKLKELEK 352
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 118572664 632 RVAA--KQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREK 677
Cdd:PRK03918 353 RLEEleERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
24-434 0e+00

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: 605.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  24 DPVGVYCRVRPLGFP----DQECCIEVINNTTVQLHTPEGYRLN---RNGDYKETQYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01368    1 DPVKVYLRVRPLSKDelesEDEGCIEVINSTTVVLHPPKGSAANkseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkr 176
Cdd:cd01368   81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 177 eampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEVPFDPikPKPPQSKLLREDK 256
Cdd:cd01368  130 ---------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSP--TKKRQSLRLREDH 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKEQITISQLSLV 336
Cdd:cd01368  169 NGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD-VDQDKDQITVSQLSLV 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01368  248 DLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPC 327
                        410
                 ....*....|....*...
gi 118572664 417 AEDYEENLQVMRFAEVTQ 434
Cdd:cd01368  328 ASDYDETLHVMKFSAIAQ 345
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
25-442 8.19e-119

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: 366.13  E-value: 8.19e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664    25 PVGVYCRVRPLGfpDQE------CCIEVINNTTVQLhtpegyRLNRNGDYKETQ-YSFKQVFGTHTTQKELFDVVANPLV 97
Cdd:smart00129   1 NIRVVVRVRPLN--KREksrkspSVVPFPDKVGKTL------TVRSPKNRQGEKkFTFDKVFDATASQEDVFEETAAPLV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664    98 NDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQakryvfksndrnsmdiqcevdallerqkre 177
Cdd:smart00129  73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE------------------------------ 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   178 ampnpktssskrqvdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDK 256
Cdd:smart00129 123 ----------------------------------EGWQFSVKVSYLEIYNEKIRDLLN----------PSSKKLeIREDE 158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDAdgdnvlqEKEQITISQLSLV 336
Cdd:smart00129 159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-------SSGSGKASKLNLV 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS---KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
                          410       420
                   ....*....|....*....|....*.
gi 118572664   417 AEDYEENLQVMRFAEVTQEVEVARPV 442
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEIKNKPIV 334
Kinesin pfam00225
Kinesin motor domain;
31-431 1.45e-117

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 362.66  E-value: 1.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   31 RVRPLgFPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFT 110
Cdd:pfam00225   1 RVRPL-NEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  111 YGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQakryvfksndrnsmdiqcevdallerqkreampnpktssskrq 190
Cdd:pfam00225  80 YGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  191 vdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEEvpfdpiKPKPPQSKLLREDKNHNMYVAGCTEVEV 270
Cdd:pfam00225 117 ---------------------ERSEFSVKVSYLEIYNEKIRDLLSP------SNKNKRKLRIREDPKKGVYVKGLTEVEV 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  271 KSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGdnvlqeKEQITISQLSLVDLAGSERTNRT-RA 349
Cdd:pfam00225 170 SSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG------EESVKTGKLNLVDLAGSERASKTgAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  350 EGNRLREAGNINQSLMTLRTCMDVLRENQmygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRF 429
Cdd:pfam00225 244 GGQRLKEAANINKSLSALGNVISALADKK----SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRF 319

                  ..
gi 118572664  430 AE 431
Cdd:pfam00225 320 AS 321
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
69-437 1.94e-57

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 208.05  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  69 KETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLdmifnsigsfqa 148
Cdd:COG5059   54 KEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSL------------ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 149 kRYVFKSNDRNSMDiqcevdallerqkreampnpktssskrqvdpefadmitvqefckaeevdedSVYGVFVSYIEIYNN 228
Cdd:COG5059  122 -KELFSKLEDLSMT---------------------------------------------------KDFAVSISYLEIYNE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 229 YIYDLLEevpfdpikpKPPQSKLLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIK 308
Cdd:COG5059  150 KIYDLLS---------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 309 LVQApldadgDNVLQEKEQitiSQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqmyGTNKMVPY 388
Cdd:COG5059  221 LASK------NKVSGTSET---SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDK---KKSGHIPY 288
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 118572664 389 RDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAEVTQEVE 437
Cdd:COG5059  289 RESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIK 337
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
803-906 2.37e-57

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


Pssm-ID: 465166  Cd Length: 107  Bit Score: 192.14  E-value: 2.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  803 PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVP---HAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGD 879
Cdd:pfam16540   1 PVVNPRHRRSRSAGERWLDHKPPSNVPTGTILQPRIPnrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 118572664  880 IYKTRGGGQSVQFTDIETLKQESPNGS 906
Cdd:pfam16540  81 VIPTRGGGAQVQFNDIETLKQESPTGS 107
PLN03188 PLN03188
kinesin-12 family protein; Provisional
70-431 1.13e-39

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 159.72  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   70 ETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTG----------SPGEGGLLPRCLDMI 139
Cdd:PLN03188  131 GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  140 FNSIGSFQAKRyvfksndrnsmdiqcevdalLERQKReampnpktssskrqvdpefadmitvqefckaeevdedsvYGVF 219
Cdd:PLN03188  211 FARINEEQIKH--------------------ADRQLK---------------------------------------YQCR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  220 VSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRES 298
Cdd:PLN03188  232 CSFLEIYNEQITDLLD----------PSQKNLqIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAES 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  299 SRSHSVFNIkLVQAPLD--ADGDNVLQekeqitISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRE 376
Cdd:PLN03188  302 SRSHSVFTC-VVESRCKsvADGLSSFK------TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAE 374
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118572664  377 NQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAE 431
Cdd:PLN03188  375 ISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQ 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
484-677 1.22e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 484 EILDINDEqtLPRLIEALEKrhnlrqmmIDEFNKQSNAFKALLQEFDNAVLSKENHMQG---KLNEKEKMISGQKLEIER 560
Cdd:PRK03918 208 EINEISSE--LPELREELEK--------LEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKEIEE 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 561 LEKKNKTLE------YKIEILEKTTTIYEEDKRNLQQELETQNQK---LQRQFSDKRRLEARLqgmvtETTMKWEKECER 631
Cdd:PRK03918 278 LEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERL-----EELKKKLKELEK 352
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 118572664 632 RVAA--KQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREK 677
Cdd:PRK03918 353 RLEEleERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
487-675 1.91e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.03  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  487 DIND----EQTLPRLIEAL-EKRHNLR---QMMIDEFNKQSNAFKALL-------QEFDNAVLSKENHM---QGKLNEKE 548
Cdd:pfam05483 521 DIINckkqEERMLKQIENLeEKEMNLRdelESVREEFIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMkilENKCNNLK 600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  549 KMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKL-------QRQFSDKRRLEARLQGMV--- 618
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeeiidnyQKEIEDKKISEEKLLEEVeka 680
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572664  619 ---TETTMKWEKECERRVAAKQLEMQNKLwvkdEKLK-QLKAIVTEPKTEKPERPSRERDR 675
Cdd:pfam05483 681 kaiADEAVKLQKEIDKRCQHKIAEMVALM----EKHKhQYDKIIEERDSELGLYKNKEQEQ 737
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
484-680 4.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   484 EILDINDE-QTLPRLIEALEKRhnlrQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKEKMISGQKLEIERLE 562
Cdd:TIGR02168  282 EIEELQKElYALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   563 KKNKTLEYKIEILEKTTTIYEEDKRN-------LQQELETQNQKLQRQFSDKRRLEARLQGMVTETtmkwEKECERRVAA 635
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEA 433
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 118572664   636 KQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPE-RPSRERDREKVTQ 680
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERLEEALEElREELEEAEQALDA 479
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
484-615 1.28e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 484 EILDINDEqtlprlIEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKE-----KMISGQKLEI 558
Cdd:COG1579   32 ELAELEDE------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqKEIESLKRRI 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572664 559 ERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQ 615
Cdd:COG1579  106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
24-434 0e+00

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: 605.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  24 DPVGVYCRVRPLGFP----DQECCIEVINNTTVQLHTPEGYRLN---RNGDYKETQYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01368    1 DPVKVYLRVRPLSKDelesEDEGCIEVINSTTVVLHPPKGSAANkseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkr 176
Cdd:cd01368   81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 177 eampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEVPFDPikPKPPQSKLLREDK 256
Cdd:cd01368  130 ---------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSP--TKKRQSLRLREDH 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKEQITISQLSLV 336
Cdd:cd01368  169 NGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD-VDQDKDQITVSQLSLV 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01368  248 DLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPC 327
                        410
                 ....*....|....*...
gi 118572664 417 AEDYEENLQVMRFAEVTQ 434
Cdd:cd01368  328 ASDYDETLHVMKFSAIAQ 345
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
25-434 1.24e-129

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: 393.93  E-value: 1.24e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  25 PVGVYCRVRPLGF---PDQECCIEVINNTTVQLHTPEgyrlnrNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLI 101
Cdd:cd00106    1 NVRVAVRVRPLNGreaRSAKSVISVDGGKSVVLDPPK------NRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 102 HGKNGLLFTYGVTGSGKTHTMTGSPGEG-GLLPRCLDMIFNSIGSFQAKryvfksndrnsmdiqcevdallerqkreamp 180
Cdd:cd00106   75 EGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKRKET------------------------------- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 181 npktssskrqvdpefadmitvqefckaeevdeDSVYGVFVSYIEIYNNYIYDLLEevpfdpikPKPPQSKLLREDKNHNM 260
Cdd:cd00106  124 --------------------------------KSSFSVSASYLEIYNEKIYDLLS--------PVPKKPLSLREDPKRGV 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 261 YVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGdnvlqekEQITISQLSLVDLAG 340
Cdd:cd00106  164 YVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG-------ESVTSSKLNLVDLAG 236
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 341 SERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDY 420
Cdd:cd00106  237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQ----NKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENF 312
                        410
                 ....*....|....
gi 118572664 421 EENLQVMRFAEVTQ 434
Cdd:cd00106  313 EETLSTLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
25-442 8.19e-119

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: 366.13  E-value: 8.19e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664    25 PVGVYCRVRPLGfpDQE------CCIEVINNTTVQLhtpegyRLNRNGDYKETQ-YSFKQVFGTHTTQKELFDVVANPLV 97
Cdd:smart00129   1 NIRVVVRVRPLN--KREksrkspSVVPFPDKVGKTL------TVRSPKNRQGEKkFTFDKVFDATASQEDVFEETAAPLV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664    98 NDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQakryvfksndrnsmdiqcevdallerqkre 177
Cdd:smart00129  73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE------------------------------ 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   178 ampnpktssskrqvdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDK 256
Cdd:smart00129 123 ----------------------------------EGWQFSVKVSYLEIYNEKIRDLLN----------PSSKKLeIREDE 158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDAdgdnvlqEKEQITISQLSLV 336
Cdd:smart00129 159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-------SSGSGKASKLNLV 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS---KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
                          410       420
                   ....*....|....*....|....*.
gi 118572664   417 AEDYEENLQVMRFAEVTQEVEVARPV 442
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEIKNKPIV 334
Kinesin pfam00225
Kinesin motor domain;
31-431 1.45e-117

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 362.66  E-value: 1.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   31 RVRPLgFPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFT 110
Cdd:pfam00225   1 RVRPL-NEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  111 YGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQakryvfksndrnsmdiqcevdallerqkreampnpktssskrq 190
Cdd:pfam00225  80 YGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  191 vdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEEvpfdpiKPKPPQSKLLREDKNHNMYVAGCTEVEV 270
Cdd:pfam00225 117 ---------------------ERSEFSVKVSYLEIYNEKIRDLLSP------SNKNKRKLRIREDPKKGVYVKGLTEVEV 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  271 KSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGdnvlqeKEQITISQLSLVDLAGSERTNRT-RA 349
Cdd:pfam00225 170 SSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG------EESVKTGKLNLVDLAGSERASKTgAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  350 EGNRLREAGNINQSLMTLRTCMDVLRENQmygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRF 429
Cdd:pfam00225 244 GGQRLKEAANINKSLSALGNVISALADKK----SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRF 319

                  ..
gi 118572664  430 AE 431
Cdd:pfam00225 320 AS 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
28-431 1.07e-72

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: 243.27  E-value: 1.07e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  28 VYCRVRPLgFPDQE----CCIEVINNTTVQLHTPegyrlnrNGDYKETQYSFKQVFGTHTTQKELFDVVAnPLVNDLIHG 103
Cdd:cd01366    6 VFCRVRPL-LPSEEnedtSHITFPDEDGQTIELT-------SIGAKQKEFSFDKVFDPEASQEDVFEEVS-PLVQSALDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 104 KNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQAKRYVFksndrnsmDIQCevdallerqkreampnpk 183
Cdd:cd01366   77 YNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSY--------TIKA------------------ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 184 tssskrqvdpefadmitvqefckaeevdedsvygvfvSYIEIYNNYIYDLLeevpfdpIKPKPPQSKL-LREDKNHNM-Y 261
Cdd:cd01366  131 -------------------------------------SMLEIYNETIRDLL-------APGNAPQKKLeIRHDSEKGDtT 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 262 VAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLvqapldaDGDNvlQEKEQITISQLSLVDLAGS 341
Cdd:cd01366  167 VTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-------SGRN--LQTGEISVGKLNLVDLAGS 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 342 ERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYgtnkmVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYE 421
Cdd:cd01366  238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSH-----IPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLN 312
                        410
                 ....*....|
gi 118572664 422 ENLQVMRFAE 431
Cdd:cd01366  313 ETLNSLRFAS 322
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
28-429 1.24e-69

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: 234.53  E-value: 1.24e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  28 VYCRVRPLgfPDQEC------CIEVINNTTVQLHTPEgyrlnrngdyKETQYSFKQVFGTHTTQKELFDVVANPLVNDLI 101
Cdd:cd01369    6 VVCRFRPL--NELEVlqgsksIVKFDPEDTVVIATSE----------TGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 102 HGKNGLLFTYGVTGSGKTHTMTGSPGEG---GLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkrea 178
Cdd:cd01369   74 NGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYS--------------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 179 mpnpktssskrqvdpefadmitvqefckaeeVDEDSVYGVFVSYIEIYNNYIYDLLEEVPfDPIKpkppqsklLREDKNH 258
Cdd:cd01369  121 -------------------------------MDENLEFHVKVSYFEIYMEKIRDLLDVSK-TNLS--------VHEDKNR 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 259 NMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQapldadgDNVlqEKEQITISQLSLVDL 338
Cdd:cd01369  161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------ENV--ETEKKKSGKLYLVDL 231
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 339 AGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLREnqmyGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAE 418
Cdd:cd01369  232 AGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD----GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSY 307
                        410
                 ....*....|.
gi 118572664 419 DYEENLQVMRF 429
Cdd:cd01369  308 NESETLSTLRF 318
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
25-430 1.96e-67

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: 229.14  E-value: 1.96e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  25 PVGVYCRVRPLGFPDQ----ECCIEVINNTT-VQLHTPEGYrlnrngdyketqySFKQVFGTHTTQKELFDVVANPLVND 99
Cdd:cd01372    2 SVRVAVRVRPLLPKEIiegcRICVSFVPGEPqVTVGTDKSF-------------TFDYVFDPSTEQEEVYNTCVAPLVDG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 100 LIHGKNGLLFTYGVTGSGKTHTM-TGSPGEG-----GLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdaller 173
Cdd:cd01372   69 LFEGYNATVLAYGQTGSGKTYTMgTAYTAEEdeeqvGIIPRAIQHIFKKI------------------------------ 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 174 qkreampnpktssSKRQVDPEFAdmitvqefckaeevdedsvygVFVSYIEIYNNYIYDLLEevPFDPIKPKPPqsklLR 253
Cdd:cd01372  119 -------------EKKKDTFEFQ---------------------LKVSFLEIYNEEIRDLLD--PETDKKPTIS----IR 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 254 EDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGD-NVLQEKEQITISQ 332
Cdd:cd01372  159 EDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIApMSADDKNSTFTSK 238
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 333 LSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNkmVPYRDSKLTHLFKNYFDGEGKVRMIVC 412
Cdd:cd01372  239 FHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAH--VPYRDSKLTRLLQDSLGGNSHTLMIAC 316
                        410
                 ....*....|....*...
gi 118572664 413 VNPKAEDYEENLQVMRFA 430
Cdd:cd01372  317 VSPADSNFEETLNTLKYA 334
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
26-430 2.83e-67

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: 227.99  E-value: 2.83e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  26 VGVYCRVRPL---GFPDQECCIEVINNTTVQLHTPEGyrlnrngdykeTQYSFKQVFGTHTTQKELFDVVANPLVNDLIH 102
Cdd:cd01374    2 ITVTVRVRPLnsrEIGINEQVAWEIDNDTIYLVEPPS-----------TSFTFDHVFGGDSTNREVYELIAKPVVKSALE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 103 GKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvFKSNDRNsmdiqcevdallerqkreampnp 182
Cdd:cd01374   71 GYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKI---------QDTPDRE----------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 183 ktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikpkpPQSKLL--REDKNHNM 260
Cdd:cd01374  119 ---------------------------------FLLRVSYLEIYNEKINDLLS-----------PTSQNLkiRDDVEKGV 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 261 YVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADgdnvlqEKEQITISQLSLVDLAG 340
Cdd:cd01374  155 YVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGEL------EEGTVRVSTLNLIDLAG 228
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 341 SERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDY 420
Cdd:cd01374  229 SERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKV---GGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHV 305
                        410
                 ....*....|
gi 118572664 421 EENLQVMRFA 430
Cdd:cd01374  306 EETLNTLKFA 315
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
26-430 1.40e-66

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: 227.62  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  26 VGVYCRVRPLG----FPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHT-------TQKELFDVVAN 94
Cdd:cd01365    3 VKVAVRVRPFNsrekERNSKCIVQMSGKETTLKNPKQADKNNKATREVPKSFSFDYSYWSHDsedpnyaSQEQVYEDLGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  95 PLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdallerq 174
Cdd:cd01365   83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI------------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 175 krEAMPNPKTSsskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLeevpfDPIKPKPPQSKLLRE 254
Cdd:cd01365  132 --ADTTNQNMS------------------------------YSVEVSYMEIYNEKVRDLL-----NPKPKKNKGNLKVRE 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 255 DKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKeqitISQLS 334
Cdd:cd01365  175 HPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN-LTTEK----VSKIS 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 335 LVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQ---MYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIV 411
Cdd:cd01365  250 LVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSsgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329
                        410
                 ....*....|....*....
gi 118572664 412 CVNPKAEDYEENLQVMRFA 430
Cdd:cd01365  330 AISPADINYEETLSTLRYA 348
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
28-430 5.68e-65

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: 222.60  E-value: 5.68e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  28 VYCRVRPLGFPD----QECCIEVINN----------TTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVA 93
Cdd:cd01370    4 VAVRVRPFSEKEknegFRRIVKVMDNhmlvfdpkdeEDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYEETT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  94 NPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdaller 173
Cdd:cd01370   84 KPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI------------------------------ 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 174 qkreampnpktssskrqvdpefadmitvqefckaEEVDEDSVYGVFVSYIEIYNNYIYDLLEevpfdpikpkpPQSKLL- 252
Cdd:cd01370  134 ----------------------------------ESLKDEKEFEVSMSYLEIYNETIRDLLN-----------PSSGPLe 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 253 -REDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADgdnvlqEKEQITIS 331
Cdd:cd01370  169 lREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTAS------INQQVRQG 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 332 QLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmyGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIV 411
Cdd:cd01370  243 KLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPG--KKNKHIPYRDSKLTRLLKDSLGGNCRTVMIA 320
                        410
                 ....*....|....*....
gi 118572664 412 CVNPKAEDYEENLQVMRFA 430
Cdd:cd01370  321 NISPSSSSYEETHNTLKYA 339
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
24-431 3.44e-62

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: 214.68  E-value: 3.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  24 DPVGVYCRVRPLGFPDQEC----CIEVINNTTVQLHTpegyrlnrngdYKETQYSFKQVFGTHTTQKELFDVVANPLVND 99
Cdd:cd01373    1 DAVKVFVRIRPPAEREGDGeygqCLKKLSSDTLVLHS-----------KPPKTFTFDHVADSNTNQESVFQSVGKPIVES 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 100 LIHGKNGLLFTYGVTGSGKTHTMTGSPGEG--------GLLPRCLDMIFNSIgsfqaKRYVFKSNDRNSMDIQCevdall 171
Cdd:cd01373   70 CLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLI-----QREKEKAGEGKSFLCKC------ 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 172 erqkreampnpktssskrqvdpefadmitvqefckaeevdedsvygvfvSYIEIYNNYIYDLLEevpfdpikpkPPQSKL 251
Cdd:cd01373  139 -------------------------------------------------SFLEIYNEQIYDLLD----------PASRNL 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 252 -LREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNvlqekeqITI 330
Cdd:cd01373  160 kLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN-------IRT 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 331 SQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMI 410
Cdd:cd01373  233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDV-AHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
                        410       420
                 ....*....|....*....|.
gi 118572664 411 VCVNPKAEDYEENLQVMRFAE 431
Cdd:cd01373  312 ANVHPSSKCFGETLSTLRFAQ 332
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
28-430 9.12e-60

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: 208.33  E-value: 9.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  28 VYCRVRPlgFPDQECCIeviNNTTVQLHTPEGYRL-----NRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIH 102
Cdd:cd01364    6 VVVRCRP--FNLRERKA---SSHSVVEVDPVRKEVsvrtgGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 103 GKNGLLFTYGVTGSGKTHTMTG--SPGEG---------GLLPRCLDMIFNSigsfqakryvfksndrnsmdiqcevdalL 171
Cdd:cd01364   81 GYNCTIFAYGQTGTGKTYTMEGdrSPNEEytweldplaGIIPRTLHQLFEK----------------------------L 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 172 ERQKREampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikPKPPQSKL 251
Cdd:cd01364  133 EDNGTE--------------------------------------YSVKVSYLEIYNEELFDLLS--------PSSDVSER 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 252 LR----EDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNVLQekeq 327
Cdd:cd01364  167 LRmfddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVK---- 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 328 itISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqmygtNKMVPYRDSKLTHLFKNYFDGEGKV 407
Cdd:cd01364  243 --IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVER-----APHVPYRESKLTRLLQDSLGGRTKT 315
                        410       420
                 ....*....|....*....|...
gi 118572664 408 RMIVCVNPKAEDYEENLQVMRFA 430
Cdd:cd01364  316 SIIATISPASVNLEETLSTLEYA 338
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
24-430 1.04e-58

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: 204.62  E-value: 1.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  24 DPVGVYCRVRPL-GFPDQECCIEVIN----NTTVQLHTPegyrlnrNGDYKET--QYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01371    1 ENVKVVVRCRPLnGKEKAAGALQIVDvdekRGQVSVRNP-------KATANEPpkTFTFDAVFDPNSKQLDVYDETARPL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTG---SPGEGGLLPRCLDMIFNSIGsfqakryvfksndrnsmdiqcevdaller 173
Cdd:cd01371   74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIA----------------------------- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 174 qkreampnpKTSSSKRqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikpKPPQSKL-L 252
Cdd:cd01371  125 ---------RSQNNQQ--------------------------FLVRVSYLEIYNEEIRDLLG---------KDQTKRLeL 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 253 REDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNVlqekeqITISQ 332
Cdd:cd01371  161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENH------IRVGK 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 333 LSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLREnqmyGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVC 412
Cdd:cd01371  235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD----GKSTHIPYRDSKLTRLLQDSLGGNSKTVMCAN 310
                        410
                 ....*....|....*...
gi 118572664 413 VNPKAEDYEENLQVMRFA 430
Cdd:cd01371  311 IGPADYNYDETLSTLRYA 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
25-430 1.85e-58

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: 203.50  E-value: 1.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  25 PVGVYCRVRPLGFPDQEC----CIEVINNTTVQLHTPEGYRLNRngdyketQYSFKQVFGTHTTQKELFDVVANPLVNDL 100
Cdd:cd01376    1 NVRVAVRVRPFVDGTAGAsdpsCVSGIDSCSVELADPRNHGETL-------KYQFDAFYGEESTQEDIYAREVQPIVPHL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 101 IHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCldmifnsigsfqakryvfksndrnsmdiqceVDALLERQKREAMP 180
Cdd:cd01376   74 LEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLT-------------------------------VMDLLQMTRKEAWA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 181 npktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDKNHN 259
Cdd:cd01376  123 -----------------------------------LSFTMSYLEIYQEKILDLLE----------PASKELvIREDKDGN 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 260 MYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIklvqapldadgdNVLQEKEQITISQ----LSL 335
Cdd:cd01376  158 ILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLI------------KVDQRERLAPFRQrtgkLNL 225
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 336 VDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygtnKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNP 415
Cdd:cd01376  226 IDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNL-----PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
                        410
                 ....*....|....*
gi 118572664 416 KAEDYEENLQVMRFA 430
Cdd:cd01376  301 ERTFYQDTLSTLNFA 315
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
69-437 1.94e-57

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 208.05  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  69 KETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLdmifnsigsfqa 148
Cdd:COG5059   54 KEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSL------------ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 149 kRYVFKSNDRNSMDiqcevdallerqkreampnpktssskrqvdpefadmitvqefckaeevdedSVYGVFVSYIEIYNN 228
Cdd:COG5059  122 -KELFSKLEDLSMT---------------------------------------------------KDFAVSISYLEIYNE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 229 YIYDLLEevpfdpikpKPPQSKLLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIK 308
Cdd:COG5059  150 KIYDLLS---------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 309 LVQApldadgDNVLQEKEQitiSQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqmyGTNKMVPY 388
Cdd:COG5059  221 LASK------NKVSGTSET---SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDK---KKSGHIPY 288
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 118572664 389 RDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAEVTQEVE 437
Cdd:COG5059  289 RESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIK 337
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
803-906 2.37e-57

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


Pssm-ID: 465166  Cd Length: 107  Bit Score: 192.14  E-value: 2.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  803 PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVP---HAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGD 879
Cdd:pfam16540   1 PVVNPRHRRSRSAGERWLDHKPPSNVPTGTILQPRIPnrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 118572664  880 IYKTRGGGQSVQFTDIETLKQESPNGS 906
Cdd:pfam16540  81 VIPTRGGGAQVQFNDIETLKQESPTGS 107
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
26-431 2.14e-50

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: 181.24  E-value: 2.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  26 VGVYCRVRPLGFPDQECCIEVINNTTVQLHTPEGYR---LNRngdyKETQYSFKQVFGTHTTQKEL-FDVVANPLVNDLI 101
Cdd:cd01375    2 VQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRrgvVNN----QQEDWSFKFDGVLHNASQELvYETVAKDVVSSAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 102 HGKNGLLFTYGVTGSGKTHTMTGSpGEG----GLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdallerqkre 177
Cdd:cd01375   78 AGYNGTIFAYGQTGAGKTFTMTGG-TENykhrGIIPRALQQVFRMI---------------------------------- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 178 ampnpktssskrqvdpefadmitvqefckaeEVDEDSVYGVFVSYIEIYNNYIYDLLEEVPFdpIKPKPPQSKLLrEDKN 257
Cdd:cd01375  123 -------------------------------EERPTKAYTVHVSYLEIYNEQLYDLLSTLPY--VGPSVTPMTIL-EDSP 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 258 HNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDAdgdnvlqEKEQITISQLSLVD 337
Cdd:cd01375  169 QNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTL-------SSEKYITSKLNLVD 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 338 LAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVL-RENQMYgtnkmVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01375  242 LAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTH-----VPFRQSKLTHVLRDSLGGNCNTVMVANIYGE 316
                        410
                 ....*....|....*
gi 118572664 417 AEDYEENLQVMRFAE 431
Cdd:cd01375  317 AAQLEETLSTLRFAS 331
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
25-430 1.30e-47

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: 172.87  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  25 PVGVYCRVRPLgfPDQECC------IEVINNTTVQLHTPegyRLNRNGDYKETQYSFK--QVFGTHTTQKELFDVVANPL 96
Cdd:cd01367    1 KIKVCVRKRPL--NKKEVAkkeidvVSVPSKLTLIVHEP---KLKVDLTKYIENHTFRfdYVFDESSSNETVYRSTVKPL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMifnsigsfqAKRYVFksndrnsmdiqcevdalleRQKr 176
Cdd:cd01367   76 VPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYAL---------AARDVF-------------------RLL- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 177 eampnpKTSSSKRQvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEvpfdpikpkppQSKL-LRED 255
Cdd:cd01367  127 ------NKLPYKDN-------------------------LGVTVSFFEIYGGKVFDLLNR-----------KKRVrLRED 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 256 KNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQApldadgdnvlqeKEQITISQLSL 335
Cdd:cd01367  165 GKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDR------------GTNKLHGKLSF 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 336 VDLAGSERTNRTRAEG-NRLREAGNINQSLMTLRTCMDVLRENQMYgtnkmVPYRDSKLTHLFKNYFDGE-GKVRMIVCV 413
Cdd:cd01367  233 VDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKAH-----IPFRGSKLTQVLKDSFIGEnSKTCMIATI 307
                        410
                 ....*....|....*..
gi 118572664 414 NPKAEDYEENLQVMRFA 430
Cdd:cd01367  308 SPGASSCEHTLNTLRYA 324
PLN03188 PLN03188
kinesin-12 family protein; Provisional
70-431 1.13e-39

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 159.72  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   70 ETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTG----------SPGEGGLLPRCLDMI 139
Cdd:PLN03188  131 GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  140 FNSIGSFQAKRyvfksndrnsmdiqcevdalLERQKReampnpktssskrqvdpefadmitvqefckaeevdedsvYGVF 219
Cdd:PLN03188  211 FARINEEQIKH--------------------ADRQLK---------------------------------------YQCR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  220 VSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRES 298
Cdd:PLN03188  232 CSFLEIYNEQITDLLD----------PSQKNLqIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAES 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  299 SRSHSVFNIkLVQAPLD--ADGDNVLQekeqitISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRE 376
Cdd:PLN03188  302 SRSHSVFTC-VVESRCKsvADGLSSFK------TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAE 374
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118572664  377 NQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAE 431
Cdd:PLN03188  375 ISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQ 429
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
28-180 2.98e-08

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: 54.27  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  28 VYCRVRPLgfpdqeccievinnttvqlhtpegyrlNRNGDYKETQY-SFKQVFGTHTTQKELFDVvANPLVNDLIHGKNG 106
Cdd:cd01363    1 VLVRVNPF---------------------------KELPIYRDSKIiVFYRGFRRSESQPHVFAI-ADPAYQSMLDGYNN 52
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118572664 107 L-LFTYGVTGSGKTHTMTgspgegGLLPRCLDMIFNSIgsfqakryvfKSNDRNSMDIQCEVDALLERQKREAMP 180
Cdd:cd01363   53 QsIFAYGESGAGKTETMK------GVIPYLASVAFNGI----------NKGETEGWVYLTEITVTLEDQILQANP 111
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
484-677 1.22e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 484 EILDINDEqtLPRLIEALEKrhnlrqmmIDEFNKQSNAFKALLQEFDNAVLSKENHMQG---KLNEKEKMISGQKLEIER 560
Cdd:PRK03918 208 EINEISSE--LPELREELEK--------LEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKEIEE 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 561 LEKKNKTLE------YKIEILEKTTTIYEEDKRNLQQELETQNQK---LQRQFSDKRRLEARLqgmvtETTMKWEKECER 631
Cdd:PRK03918 278 LEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERL-----EELKKKLKELEK 352
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 118572664 632 RVAA--KQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREK 677
Cdd:PRK03918 353 RLEEleERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
28-157 1.31e-06

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 48.76  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   28 VYCRVRPLGfpDQECCIEVINNTTvqlHTPEGYRLNRngdyketQYSFKQVFGTHTTQKELFDVVANpLVNDLIHGKNGL 107
Cdd:pfam16796  24 VFARVRPEL--LSEAQIDYPDETS---SDGKIGSKNK-------SFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVC 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572664  108 LFTYGVTGSGKThtmtgspgeGGLLPRCLDMIFNSIGSFQAK-------RYVFKSND 157
Cdd:pfam16796  91 IFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGwkytielQFVEIYNE 138
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
487-675 1.91e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.03  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  487 DIND----EQTLPRLIEAL-EKRHNLR---QMMIDEFNKQSNAFKALL-------QEFDNAVLSKENHM---QGKLNEKE 548
Cdd:pfam05483 521 DIINckkqEERMLKQIENLeEKEMNLRdelESVREEFIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMkilENKCNNLK 600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  549 KMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKL-------QRQFSDKRRLEARLQGMV--- 618
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeeiidnyQKEIEDKKISEEKLLEEVeka 680
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572664  619 ---TETTMKWEKECERRVAAKQLEMQNKLwvkdEKLK-QLKAIVTEPKTEKPERPSRERDR 675
Cdd:pfam05483 681 kaiADEAVKLQKEIDKRCQHKIAEMVALM----EKHKhQYDKIIEERDSELGLYKNKEQEQ 737
PRK12704 PRK12704
phosphodiesterase; Provisional
497-602 4.10e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 497 LIEALEKRHNLRQmmidEFNKQSNAFKALLQEFDNAVLSKENHmqgkLNEKEkmisgqkleiERLEKKNKTLEYKIEILE 576
Cdd:PRK12704  59 LLEAKEEIHKLRN----EFEKELRERRNELQKLEKRLLQKEEN----LDRKL----------ELLEKREEELEKKEKELE 120
                         90       100
                 ....*....|....*....|....*.
gi 118572664 577 KTTTIYEEDKRNLQQELETQNQKLQR 602
Cdd:PRK12704 121 QKQQELEKKEEELEELIEEQLQELER 146
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
488-686 4.42e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.66  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   488 INDEQTLPRLIEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKEKMISGQKLEIERLEKKNKT 567
Cdd:pfam02463  267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   568 LEYKIEILEKTttiyEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQGMVTETTMKWEKECERRVAAKQLEMQNKLWVK 647
Cdd:pfam02463  347 LEIKREAEEEE----EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK 422
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 118572664   648 DEKLKQL-KAIVTEPKTEKPERPSRERDREKVTQRSVSPS 686
Cdd:pfam02463  423 EEKKEELeILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
503-643 2.39e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  503 KRHNLRQMMIDEFN---KQSNAFKALLQEFDNAVLS-----KENH---------MQGKLNEKEKMISGQKLEIERLEKKN 565
Cdd:pfam05483 177 EREETRQVYMDLNNnieKMILAFEELRVQAENARLEmhfklKEDHekiqhleeeYKKEINDKEKQVSLLLIQITEKENKM 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  566 KTLEY-------KIEILEKTTTIYEED-------KRNLQQELETQNQKLQRQFSDKRRLEARLQgMVTETTMKWEKECEr 631
Cdd:pfam05483 257 KDLTFlleesrdKANQLEEKTKLQDENlkeliekKDHLTKELEDIKMSLQRSMSTQKALEEDLQ-IATKTICQLTEEKE- 334
                         170
                  ....*....|..
gi 118572664  632 rvaaKQLEMQNK 643
Cdd:pfam05483 335 ----AQMEELNK 342
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
538-678 3.44e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 538 NHMQGKLNEKEKMISG-QKLEIErLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSD-----KRRLE 611
Cdd:PRK00409 509 KLIGEDKEKLNELIASlEELERE-LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaikeaKKEAD 587
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572664 612 ARLQGMVTEttmkwEKECERRVAAKQL-EMQNKLwvkDEKLKQLKAIVTEPKteKPERPSRERDREKV 678
Cdd:PRK00409 588 EIIKELRQL-----QKGGYASVKAHELiEARKRL---NKANEKKEKKKKKQK--EKQEELKVGDEVKY 645
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
484-680 4.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   484 EILDINDE-QTLPRLIEALEKRhnlrQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKEKMISGQKLEIERLE 562
Cdd:TIGR02168  282 EIEELQKElYALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   563 KKNKTLEYKIEILEKTTTIYEEDKRN-------LQQELETQNQKLQRQFSDKRRLEARLQGMVTETtmkwEKECERRVAA 635
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEA 433
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 118572664   636 KQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPE-RPSRERDREKVTQ 680
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERLEEALEElREELEEAEQALDA 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
496-664 7.36e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   496 RLIEALEKRHNLrQMMIDEFNKQSNAFKALLQEfdnavlskenhMQGKLNEKEKMISGQKLEIERLEKKNKTLEYKIEIL 575
Cdd:TIGR02168  233 RLEELREELEEL-QEELKEAEEELEELTAELQE-----------LEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   576 EKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQgmvtettmKWEKECErRVAAKQLEMQNKLWVKDEKLKQLK 655
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA--------ELEEKLE-ELKEELESLEAELEELEAELEELE 371

                   ....*....
gi 118572664   656 AIVTEPKTE 664
Cdd:TIGR02168  372 SRLEELEEQ 380
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
484-615 1.28e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 484 EILDINDEqtlprlIEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKE-----KMISGQKLEI 558
Cdd:COG1579   32 ELAELEDE------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqKEIESLKRRI 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572664 559 ERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQ 615
Cdd:COG1579  106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
512-667 2.10e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  512 IDEFNKQSNAFKALLQEFDNAVLSKENHMQG---KLNEKEKMISgqklEIERLEKKNKTLEYKIEILEKTTTIYEEDKRN 588
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLS----NLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  589 LQQELETQNQKLQRQfsdkrrlearlQGMVTETTMKWEKEcERRVAAKQLEMQN---KLWVKDEKLKQLKAIVTEPKTEK 665
Cdd:TIGR04523 237 KQQEINEKTTEISNT-----------QTQLNQLKDEQNKI-KKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQK 304

                  ..
gi 118572664  666 PE 667
Cdd:TIGR04523 305 EQ 306
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
497-707 2.50e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 497 LIEALEKRHN-LRQMM-IDEFNKQSNAFKALLQEFDNAV------LSKENHMQGKLNEKEKMISGQKLEIERLEKKNKTL 568
Cdd:PRK03918 140 ILESDESREKvVRQILgLDDYENAYKNLGEVIKEIKRRIerlekfIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 569 EYKIEILEKTTTIYEEDKRNLqQELETQNQKLQRqfsDKRRLEARLqgmvtettmkweKECERRVAakqlEMQNKLWVKD 648
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEI-EELEKELESLEG---SKRKLEEKI------------RELEERIE----ELKKEIEELE 279
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118572664 649 EKLKQLKAIvtEPKTEKPERPSRERDREKVTQRSVSpspvPLSSNYIAQISNGQQLMSQ 707
Cdd:PRK03918 280 EKVKELKEL--KEKAEEYIKLSEFYEEYLDELREIE----KRLSRLEEEINGIEERIKE 332
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
512-665 2.65e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  512 IDEFNKQSNAFKALLQEFDNAVLSKENhmqgKLNEKEKMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQ 591
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118572664  592 ELETQNQklqrqfsDKRRLEARLQGMVTETTMKWE--KECERRVAAKQLEMQNKLWVKDEKLKQLKAIVTEPKTEK 665
Cdd:TIGR04523 413 QIKKLQQ-------EKELLEKEIERLKETIIKNNSeiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
549-637 2.68e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 549 KMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQGMVTETTMKWEKE 628
Cdd:COG3883  133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212

                 ....*....
gi 118572664 629 CERRVAAKQ 637
Cdd:COG3883  213 AAAAAAAAA 221
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
498-665 3.60e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  498 IEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKEKM----------ISGQKLEIERLEKKNKT 567
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLekeierlketIIKNNSEIKDLTNQDSV 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664  568 LEYKIEILEKTTTI-----------YEEDKRNL---QQELETQNQKLQRQFSDKRRLEARLQGMVTEttMKWEKECERRV 633
Cdd:TIGR04523 452 KELIIKNLDNTRESletqlkvlsrsINKIKQNLeqkQKELKSKEKELKKLNEEKKELEEKVKDLTKK--ISSLKEKIEKL 529
                         170       180       190
                  ....*....|....*....|....*....|..
gi 118572664  634 AAKQLEMQNKLWVKDEKLKQLKAIVTEPKTEK 665
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELKKENLEK 561
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
492-675 5.67e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   492 QTLPRLIEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKekmISGQKLEIERLEKKNKTLEYK 571
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERE 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   572 IEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQGmvtettmKWEKECERRVAAKQLEMQNKLWVkdEKL 651
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE-------LKEELEDLRAELEEVDKEFAETR--DEL 387
                          170       180
                   ....*....|....*....|....
gi 118572664   652 KQLKAIVTEPKTEKPERpSRERDR 675
Cdd:TIGR02169  388 KDYREKLEKLKREINEL-KRELDR 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
498-660 7.03e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 498 IEALEKRHNLRQMMIDEFNKQSNAFKALLQEfdnaVLSKENHMQGKLNEKEKMISGQKLEIERLEKKNKTLEYKIEILEK 577
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYE----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 578 TTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQGMVTEttmkwEKECERRVAAKQLEMQNKLWVKDEKLKQLKAI 657
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                 ...
gi 118572664 658 VTE 660
Cdd:COG1196  413 LER 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
542-681 7.44e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   542 GKLNEKEKMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELEtqnqKLQRQFSDKRRLEARLQGMVTET 621
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE----QLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664   622 TMKWEKeCERRVAAKQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREKVTQR 681
Cdd:TIGR02168  739 EAEVEQ-LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
531-709 9.72e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 531 NAVLSKENHMQGKLNEKEKMISGQKLEIERLEKKNKTLEYKIEILektttiyEEDKRNLQQELETQNQKLQRQFSDKRRL 610
Cdd:COG4372   90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-------EAQIAELQSEIAEREEELKELEEQLESL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572664 611 EARLQGMVTETTMKWEKECERRVAAKQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREKVTQRSVSPSPVPL 690
Cdd:COG4372  163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
                        170
                 ....*....|....*....
gi 118572664 691 SSNYIAQISNGQQLMSQPQ 709
Cdd:COG4372  243 ELEEDKEELLEEVILKEIE 261
 
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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