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Conserved domains on  [gi|2128100422|ref|XP_044771211|]
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kinesin-like protein KIF22 [Neomonachus schauinslandi]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 39-362 0e+00

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: 572.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNAS 118
Cdd:cd01376      1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  119 VLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGgegrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCR 198
Cdd:cd01376     81 VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA-----WALSFTMSYLEIYQEKILDLLEPASKELVIREDKD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  199 GNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNR 278
Cdd:cd01376    156 GNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLAGSEDNR 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  279 RTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFA 358
Cdd:cd01376    236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                   ....
gi 2128100422  359 ARSK 362
Cdd:cd01376    316 ARSR 319
ComEA super family cl43451
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 595-635 9.18e-06

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG1555:

Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 44.47  E-value: 9.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2128100422  595 LNEGSARDLRSLQRIGQKKAQLIVGWRELHGPFSQP-----VLGLD 635
Cdd:COG1555     15 INTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVedlleVKGIG 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
910-935 3.28e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.28e-05
                           10        20
                   ....*....|....*....|....*.
gi 2128100422  910 HLNRHKLSHSDEKPYQCPVCQQRFKR 935
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
894-947 1.12e-04

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2128100422  894 KNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSY--HVRSHD 947
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHH 87
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 920-977 1.44e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 1.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2128100422  920 DEKPYQCPV--CQQRFKRKDRMSYHVR---------------SHDG--AVHKPYNCSHCGKSFSRPDHLNSHVRQVH 977
Cdd:COG5189    346 DGKPYKCPVegCNKKYKNQNGLKYHMLhghqnqklhenpspeKMNIfsAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
COG5236 super family cl28715
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
924-1081 2.32e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5236:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.93  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  924 YQCP--VCQQRFKRKDRMSYHVRSHdgavHKPYNCSHCG---KSFS------RPDHLNSHvRQVHSTERPFK----CEKC 988
Cdd:COG5236    152 FKCPksKCHRRCGSLKELKKHYKAQ----HGFVLCSECIgnkKDFWneirlfRSSTLRDH-KNGGLEEEGFKghplCIFC 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  989 EAAFATKDRLRAH-TVRHEEkvpCHVCGKM--LSSAYISDH--MKVHSQGPHHVC--ELCNKG----FTTAAYLRIHAVK 1057
Cdd:COG5236    227 KIYFYDDDELRRHcRLRHEA---CHICDMVgpIRYQYFKSYedLEAHFRNAHYCCtfQTCRVGkcyvFPYHTELLEHLTR 303

                          170       180
                   ....*....|....*....|....
gi 2128100422 1058 DHGLQAPRADRILCKLCSVHCKTP 1081
Cdd:COG5236    304 FHKVNARLSEIPRPGRCSIPVMDP 327
 
Name Accession Description Interval E-value
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 39-362 0e+00

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: 572.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNAS 118
Cdd:cd01376      1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  119 VLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGgegrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCR 198
Cdd:cd01376     81 VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA-----WALSFTMSYLEIYQEKILDLLEPASKELVIREDKD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  199 GNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNR 278
Cdd:cd01376    156 GNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLAGSEDNR 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  279 RTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFA 358
Cdd:cd01376    236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                   ....
gi 2128100422  359 ARSK 362
Cdd:cd01376    316 ARSR 319
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 39-371 4.16e-144

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: 435.85  E-value: 4.16e-144
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422    39 RVRVAVRLRPFVDGTDGAGDPPCVRGLD--SCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQN 116
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   117 ASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGGEgrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIRED 196
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEG---WQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   197 CRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRER-LAPFRQREGKLYLIDLAGSE 275
Cdd:smart00129  158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKnSSSGSGKASKLNLVDLAGSE 237

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   276 DNRRTGNKGLRLKESGAINSSLFVLGKVVDAL--NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVS 353
Cdd:smart00129  238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALaqHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                           330
                    ....*....|....*...
gi 2128100422   354 ALNFAARSKEVINRPFTN 371
Cdd:smart00129  318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
45-364 6.37e-120

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 371.91  E-value: 6.37e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   45 RLRPFVDGTDGAGDPPCVR--GLDSCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASVLAY 122
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSveSVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  123 GPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGGEgrpWALSVTMSYLEIYQEKVLDLLDPA---SGDLVIREDCRG 199
Cdd:pfam00225   81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKER---SEFSVKVSYLEIYNEKIRDLLSPSnknKRKLRIREDPKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  200 NILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDN 277
Cdd:pfam00225  158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEEsvKTGKLNLVDLAGSERA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  278 RRTGN-KGLRLKESGAINSSLFVLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSAL 355
Cdd:pfam00225  238 SKTGAaGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                   ....*....
gi 2128100422  356 NFAARSKEV 364
Cdd:pfam00225  318 RFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
75-376 5.79e-79

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 270.07  E-value: 5.79e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   75 WRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLT 154
Cdd:COG5059     49 SLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  155 REEGGEGRpwaLSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATR 234
Cdd:COG5059    129 EDLSMTKD---FAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  235 LNQRSSRSHAVLLVKVDQRERLAPFRqREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDAL--NQGLP 312
Cdd:COG5059    206 INDESSRSHSIFQIELASKNKVSGTS-ETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALgdKKKSG 284

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2128100422  313 RVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQL 376
Cdd:COG5059    285 HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDS 348
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 40-375 1.90e-52

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 201.70  E-value: 1.90e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAgdpPCVRGLDSCSLEIanwrNHQetlKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASV 119
Cdd:PLN03188   100 VKVIVRMKPLNKGEEGE---MIVQKMSNDSLTI----NGQ---TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSV 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  120 LAYGPTGAGKTHTMLG----------SPEQPGVIPRALMDLLQLTREEGGE--GRPWALSVTMSYLEIYQEKVLDLLDPA 187
Cdd:PLN03188   170 FAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEEQIKhaDRQLKYQCRCSFLEIYNEQITDLLDPS 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  188 SGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQR-----ERLAPFRQr 262
Cdd:PLN03188   250 QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRcksvaDGLSSFKT- 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  263 eGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQ----GLPR-VPYRDSKLTRLLQDSLGGSAHSIL 337
Cdd:PLN03188   329 -SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRhIPYRDSRLTFLLQESLGGNAKLAM 407

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2128100422  338 IANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQ 375
Cdd:PLN03188   408 VCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQ 445
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 595-635 9.18e-06

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 44.47  E-value: 9.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2128100422  595 LNEGSARDLRSLQRIGQKKAQLIVGWRELHGPFSQP-----VLGLD 635
Cdd:COG1555     15 INTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVedlleVKGIG 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
910-935 3.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.28e-05
                           10        20
                   ....*....|....*....|....*.
gi 2128100422  910 HLNRHKLSHSDEKPYQCPVCQQRFKR 935
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
894-947 1.12e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2128100422  894 KNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSY--HVRSHD 947
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHH 87
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 920-977 1.44e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 1.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2128100422  920 DEKPYQCPV--CQQRFKRKDRMSYHVR---------------SHDG--AVHKPYNCSHCGKSFSRPDHLNSHVRQVH 977
Cdd:COG5189    346 DGKPYKCPVegCNKKYKNQNGLKYHMLhghqnqklhenpspeKMNIfsAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 954-977 4.26e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 4.26e-04
                           10        20
                   ....*....|....*....|....
gi 2128100422  954 YNCSHCGKSFSRPDHLNSHVRqVH 977
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
924-1081 2.32e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.93  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  924 YQCP--VCQQRFKRKDRMSYHVRSHdgavHKPYNCSHCG---KSFS------RPDHLNSHvRQVHSTERPFK----CEKC 988
Cdd:COG5236    152 FKCPksKCHRRCGSLKELKKHYKAQ----HGFVLCSECIgnkKDFWneirlfRSSTLRDH-KNGGLEEEGFKghplCIFC 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  989 EAAFATKDRLRAH-TVRHEEkvpCHVCGKM--LSSAYISDH--MKVHSQGPHHVC--ELCNKG----FTTAAYLRIHAVK 1057
Cdd:COG5236    227 KIYFYDDDELRRHcRLRHEA---CHICDMVgpIRYQYFKSYedLEAHFRNAHYCCtfQTCRVGkcyvFPYHTELLEHLTR 303

                          170       180
                   ....*....|....*....|....
gi 2128100422 1058 DHGLQAPRADRILCKLCSVHCKTP 1081
Cdd:COG5236    304 FHKVNARLSEIPRPGRCSIPVMDP 327
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 896-918 2.35e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 2.35e-03
                           10        20
                   ....*....|....*....|...
gi 2128100422  896 HACEMCGKAFRDVYHLNRHKLSH 918
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 595-627 2.38e-03

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 37.46  E-value: 2.38e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2128100422  595 LNEGSARDLRSLQRIGQKKAQLIVGWRELHGPF 627
Cdd:pfam12836    6 INTASAELLSRVPGLGPKLAKNIVEYREENGPF 38
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 595-627 5.39e-03

competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model. [Cellular processes, DNA transformation]


Pssm-ID: 129520 [Multi-domain]  Cd Length: 69  Bit Score: 36.83  E-value: 5.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2128100422  595 LNEGSARDL-RSLQRIGQKKAQLIVGWRELHGPF 627
Cdd:TIGR00426   10 INTATAEELqRAMNGVGLKKAEAIVSYREEYGPF 43
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 1017-1068 5.41e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 40.62  E-value: 5.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2128100422 1017 MLSSAYISDHMKVHSQGPHHVCELCNKGFTTAAYLRIHAVKDHGLQAPRADR 1068
Cdd:cd23959    227 SAASFPAAPVANGEAATPTHACTICGKAFSTHEGLRMHSKAKHGVELEKAKT 278
ZnF_C2H2 smart00355
zinc finger;
924-946 5.87e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 5.87e-03
                            10        20
                    ....*....|....*....|...
gi 2128100422   924 YQCPVCQQRFKRKDRMSYHVRSH 946
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 39-362 0e+00

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: 572.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNAS 118
Cdd:cd01376      1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  119 VLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGgegrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCR 198
Cdd:cd01376     81 VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA-----WALSFTMSYLEIYQEKILDLLEPASKELVIREDKD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  199 GNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNR 278
Cdd:cd01376    156 GNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLAGSEDNR 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  279 RTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFA 358
Cdd:cd01376    236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                   ....
gi 2128100422  359 ARSK 362
Cdd:cd01376    316 ARSR 319
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 39-371 4.16e-144

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: 435.85  E-value: 4.16e-144
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422    39 RVRVAVRLRPFVDGTDGAGDPPCVRGLD--SCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQN 116
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   117 ASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGGEgrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIRED 196
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEG---WQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   197 CRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRER-LAPFRQREGKLYLIDLAGSE 275
Cdd:smart00129  158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKnSSSGSGKASKLNLVDLAGSE 237

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   276 DNRRTGNKGLRLKESGAINSSLFVLGKVVDAL--NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVS 353
Cdd:smart00129  238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALaqHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                           330
                    ....*....|....*...
gi 2128100422   354 ALNFAARSKEVINRPFTN 371
Cdd:smart00129  318 TLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 39-362 1.48e-134

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: 410.49  E-value: 1.48e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVdGTDGAGDPPCVRGLDSCSLEIANWRN-HQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNA 117
Cdd:cd00106      1 NVRVAVRVRPLN-GREARSAKSVISVDGGKSVVLDPPKNrVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  118 SVLAYGPTGAGKTHTMLGS-PEQPGVIPRALMDLLQLTREEGGEGrpWALSVTMSYLEIYQEKVLDLLDPA-SGDLVIRE 195
Cdd:cd00106     80 TIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETK--SSFSVSASYLEIYNEKIYDLLSPVpKKPLSLRE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  196 DCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLA-PFRQREGKLYLIDLAGS 274
Cdd:cd00106    158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsGESVTSSKLNLVDLAGS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  275 EDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVS 353
Cdd:cd00106    238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGqNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317


                   ....*....
gi 2128100422  354 ALNFAARSK 362
Cdd:cd00106    318 TLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
45-364 6.37e-120

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 371.91  E-value: 6.37e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   45 RLRPFVDGTDGAGDPPCVR--GLDSCSLEIANWRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASVLAY 122
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSveSVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  123 GPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGGEgrpWALSVTMSYLEIYQEKVLDLLDPA---SGDLVIREDCRG 199
Cdd:pfam00225   81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKER---SEFSVKVSYLEIYNEKIRDLLSPSnknKRKLRIREDPKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  200 NILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDN 277
Cdd:pfam00225  158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEEsvKTGKLNLVDLAGSERA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  278 RRTGN-KGLRLKESGAINSSLFVLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSAL 355
Cdd:pfam00225  238 SKTGAaGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                   ....*....
gi 2128100422  356 NFAARSKEV 364
Cdd:pfam00225  318 RFASRAKNI 326
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 39-364 7.07e-98

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: 314.28  E-value: 7.07e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVDGTDGAGDPPCVRGLDSCSL-----------------EIANWRNHQETLKYQFDAFYGEKSSQQDIYA 101
Cdd:cd01370      1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  102 GSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDL---LQLTREEGgegrpwALSVTMSYLEIYQE 178
Cdd:cd01370     81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELfkrIESLKDEK------EFEVSMSYLEIYNE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  179 KVLDLLDPASGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAP 258
Cdd:cd01370    155 TIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTAS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  259 FRQ--REGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPR---VPYRDSKLTRLLQDSLGGSA 333
Cdd:cd01370    235 INQqvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKnkhIPYRDSKLTRLLKDSLGGNC 314

                          330       340       350
                   ....*....|....*....|....*....|.
gi 2128100422  334 HSILIANIAPERRFYLDTVSALNFAARSKEV 364
Cdd:cd01370    315 RTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 40-360 3.58e-87

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: 284.99  E-value: 3.58e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANwRNHQetlkYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASV 119
Cdd:cd01372      3 VRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVG-TDKS----FTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  120 LAYGPTGAGKTHTMLGS------PEQPGVIPRALMDLLQLTREEGGEgrpWALSVTMSYLEIYQEKVLDLLDPAS---GD 190
Cdd:cd01372     78 LAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDT---FEFQLKVSFLEIYNEEIRDLLDPETdkkPT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  191 LVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREG------ 264
Cdd:cd01372    155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSAddknst 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  265 ---KLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPR---VPYRDSKLTRLLQDSLGGSAHSILI 338
Cdd:cd01372    235 ftsKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKgahVPYRDSKLTRLLQDSLGGNSHTLMI 314

                          330       340
                   ....*....|....*....|..
gi 2128100422  339 ANIAPERRFYLDTVSALNFAAR 360
Cdd:cd01372    315 ACVSPADSNFEETLNTLKYANR 336
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 40-364 1.65e-85

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: 279.60  E-value: 1.65e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDppcvrgldSCSLEIAN---WRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQN 116
Cdd:cd01374      2 ITVTVRVRPLNSREIGINE--------QVAWEIDNdtiYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  117 ASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQltREEGGEGRPWALSVtmSYLEIYQEKVLDLLDPASGDLVIRED 196
Cdd:cd01374     74 GTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFS--KIQDTPDREFLLRV--SYLEIYNEKINDLLSPTSQNLKIRDD 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  197 CRGNILIPGLTQKPITSFADFeRHFLPA-SRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAG 273
Cdd:cd01374    150 VEKGVYVAGLTEEIVSSPEHA-LSLIARgEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtvRVSTLNLIDLAG 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  274 SEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPR--VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDT 351
Cdd:cd01374    229 SERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGghIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEET 308

                          330
                   ....*....|...
gi 2128100422  352 VSALNFAARSKEV 364
Cdd:cd01374    309 LNTLKFASRAKKI 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 40-360 1.12e-83

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: 274.86  E-value: 1.12e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGtDGAGDPPCVRGLDSCSLEIAnwRNHQETLKYQF--DAFYGEKSSQQDIYAgSVQPILRHLLEGQNA 117
Cdd:cd01366      4 IRVFCRVRPLLPS-EENEDTSHITFPDEDGQTIE--LTSIGAKQKEFsfDKVFDPEASQEDVFE-EVSPLVQSALDGYNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  118 SVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGGEGrpWALSVTMSYLEIYQEKVLDLLDPASGD---LVIR 194
Cdd:cd01366     80 CIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKG--WSYTIKASMLEIYNETIRDLLAPGNAPqkkLEIR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  195 ED-CRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVdQRERLAPFRQREGKLYLIDLAG 273
Cdd:cd01366    158 HDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRNLQTGEISVGKLNLVDLAG 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  274 SEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVS 353
Cdd:cd01366    237 SERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLN 316


                   ....*..
gi 2128100422  354 ALNFAAR 360
Cdd:cd01366    317 SLRFASK 323
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 40-372 1.71e-81

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: 269.76  E-value: 1.71e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEianWRNHQETlKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASV 119
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLV---LHSKPPK-TFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  120 LAYGPTGAGKTHTMLGSPEQP--------GVIPRA---LMDLLQLTREEGGEGRPWalSVTMSYLEIYQEKVLDLLDPAS 188
Cdd:cd01373     79 FAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIfeyLFSLIQREKEKAGEGKSF--LCKCSFLEIYNEQIYDLLDPAS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  189 GDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPF-RQREGKLY 267
Cdd:cd01373    157 RNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFvNIRTSRLN 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  268 LIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDAL----NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAP 343
Cdd:cd01373    237 LVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 316

                          330       340
                   ....*....|....*....|....*....
gi 2128100422  344 ERRFYLDTVSALNFAARSKEVINRPFTNE 372
Cdd:cd01373    317 SSKCFGETLSTLRFAQRAKLIKNKAVVNE 345
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
75-376 5.79e-79

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 270.07  E-value: 5.79e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   75 WRNHQETLKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLT 154
Cdd:COG5059     49 SLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  155 REEGGEGRpwaLSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATR 234
Cdd:COG5059    129 EDLSMTKD---FAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  235 LNQRSSRSHAVLLVKVDQRERLAPFRqREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDAL--NQGLP 312
Cdd:COG5059    206 INDESSRSHSIFQIELASKNKVSGTS-ETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALgdKKKSG 284

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2128100422  313 RVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQL 376
Cdd:COG5059    285 HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDS 348
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 40-373 3.66e-77

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: 258.02  E-value: 3.66e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANWRNHQETL---KYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQN 116
Cdd:cd01364      4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSstkTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  117 ASVLAYGPTGAGKTHTMLGS-----------PEQPGVIPRALMDLLQLTREEGGEgrpwaLSVTMSYLEIYQEKVLDLLD 185
Cdd:cd01364     84 CTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDNGTE-----YSVKVSYLEIYNEELFDLLS 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  186 PASGD---LVIREDCR--GNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFR 260
Cdd:cd01364    159 PSSDVserLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  261 Q--REGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILI 338
Cdd:cd01364    239 ElvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSII 318

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2128100422  339 ANIAPERRFYLDTVSALNFAARSKEVINRPFTNES 373
Cdd:cd01364    319 ATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 40-364 1.11e-76

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: 255.85  E-value: 1.11e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDPPCVRgLDSCSLEIAnWRNHQETLK-----YQFDAFYGEKSSQQDIYAGSVQPILRHLLEG 114
Cdd:cd01371      3 VKVVVRCRPLNGKEKAAGALQIVD-VDEKRGQVS-VRNPKATANeppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  115 QNASVLAYGPTGAGKTHTMLGSPEQP---GVIPRALMDLLQLTREEGGEGRpwaLSVTMSYLEIYQEKVLDLL-DPASGD 190
Cdd:cd01371     81 YNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ---FLVRVSYLEIYNEEIRDLLgKDQTKR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  191 LVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYL 268
Cdd:cd01371    158 LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENhiRVGKLNL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  269 IDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRF 347
Cdd:cd01371    238 VDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGkSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYN 317

                          330
                   ....*....|....*..
gi 2128100422  348 YLDTVSALNFAARSKEV 364
Cdd:cd01371    318 YDETLSTLRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 40-364 3.80e-76

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


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 254.18  E-value: 3.80e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANWRNHQetlKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASV 119
Cdd:cd01369      4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSETGK---TFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  120 LAYGPTGAGKTHTMLGSPEQP---GVIPRALMDLLQLTR--EEGGEgrpwaLSVTMSYLEIYQEKVLDLLDPASGDLVIR 194
Cdd:cd01369     81 FAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYsmDENLE-----FHVKVSYFEIYMEKIRDLLDVSKTNLSVH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  195 EDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPfRQREGKLYLIDLAGS 274
Cdd:cd01369    156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETE-KKKSGKLYLVDLAGS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  275 EDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVS 353
Cdd:cd01369    235 EKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLS 314

                          330
                   ....*....|.
gi 2128100422  354 ALNFAARSKEV 364
Cdd:cd01369    315 TLRFGQRAKTI 325
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 40-362 3.69e-72

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: 243.84  E-value: 3.69e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAGDPPCVRGLDS---------CSLEIANWRNH-QETLKYQFDAFYGEKSSQQDIYAGSVQPILR 109
Cdd:cd01368      3 VKVYLRVRPLSKDELESEDEGCIEVINSttvvlhppkGSAANKSERNGgQKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  110 HLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALmDLlqLTREEGGegrpwaLSVTMSYLEIYQEKVLDLLDPASG 189
Cdd:cd01368     83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSL-DV--IFNSIGG------YSVFVSYIEIYNEYIYDLLEPSPS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  190 D-------LVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFR-- 260
Cdd:cd01368    154 SptkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDvd 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  261 -----QREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDAL--NQGLPR---VPYRDSKLTRLLQDSLG 330
Cdd:cd01368    234 qdkdqITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTnkmVPFRDSKLTHLFQNYFD 313

                          330       340       350
                   ....*....|....*....|....*....|..
gi 2128100422  331 GSAHSILIANIAPERRFYLDTVSALNFAARSK 362
Cdd:cd01368    314 GEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 38-371 1.52e-71

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: 242.64  E-value: 1.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   38 ARVRVAVRLRPFVDGTDGAG-------DPPCVRGLDSCSLEIANWRNHQETLKYQFD-AFYGEKS------SQQDIYAGS 103
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNskcivqmSGKETTLKNPKQADKNNKATREVPKSFSFDySYWSHDSedpnyaSQEQVYEDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  104 VQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQltREEGGEGRPWALSVTMSYLEIYQEKVLDL 183
Cdd:cd01365     81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFS--RIADTTNQNMSYSVEVSYMEIYNEKVRDL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  184 LDP----ASGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQrERLAPF 259
Cdd:cd01365    159 LNPkpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ-KRHDAE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  260 RQREG----KLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQ--------GLPRVPYRDSKLTRLLQD 327
Cdd:cd01365    238 TNLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskkKSSFIPYRDSVLTWLLKE 317

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2128100422  328 SLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTN 371
Cdd:cd01365    318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 39-362 5.78e-59

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: 206.28  E-value: 5.78e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVDGTDG----AGDPPCVRGLDSCSLEIANWRNHQETLKYQFDAFYgEKSSQQDIYAGSVQPILRHLLEG 114
Cdd:cd01375      1 KVQAFVRVRPTDDFAHEmikyGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  115 QNASVLAYGPTGAGKTHTMLGSPE---QPGVIPRALMDLLQLTREEGGEgrpwALSVTMSYLEIYQEKVLDLLD------ 185
Cdd:cd01375     80 YNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFRMIEERPTK----AYTVHVSYLEIYNEQLYDLLStlpyvg 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  186 PASGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRER-LAPFRQREG 264
Cdd:cd01375    156 PSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRtLSSEKYITS 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  265 KLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDAL-NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAP 343
Cdd:cd01375    236 KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYG 315

                          330
                   ....*....|....*....
gi 2128100422  344 ERRFYLDTVSALNFAARSK 362
Cdd:cd01375    316 EAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 39-343 6.60e-59

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: 205.61  E-value: 6.60e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   39 RVRVAVRLRPFVDGTDGAGDPPCVRGLDSCSLEIANWRNHQETLKY------QFDAFYGEKSSQQDIYAGSVQPILRHLL 112
Cdd:cd01367      1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVDLTKYienhtfRFDYVFDESSSNETVYRSTVKPLVPHIF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  113 EGQNASVLAYGPTGAGKTHTMLGS----PEQPGVIPRALMDLLQLTREEGGEGRpwaLSVTMSYLEIYQEKVLDLLDPAS 188
Cdd:cd01367     81 EGGKATCFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLPYKDN---LGVTVSFFEIYGGKVFDLLNRKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  189 gDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVdqrERLAPFRQReGKLYL 268
Cdd:cd01367    158 -RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---RDRGTNKLH-GKLSF 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  269 IDLAGSE-------DNRRTgnkglrLKESGAINSSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSL-GGSAHSILIAN 340
Cdd:cd01367    233 VDLAGSErgadtssADRQT------RMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFiGENSKTCMIAT 306


                   ...
gi 2128100422  341 IAP 343
Cdd:cd01367    307 ISP 309
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 40-375 1.90e-52

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 201.70  E-value: 1.90e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFVDGTDGAgdpPCVRGLDSCSLEIanwrNHQetlKYQFDAFYGEKSSQQDIYAGSVQPILRHLLEGQNASV 119
Cdd:PLN03188   100 VKVIVRMKPLNKGEEGE---MIVQKMSNDSLTI----NGQ---TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSV 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  120 LAYGPTGAGKTHTMLG----------SPEQPGVIPRALMDLLQLTREEGGE--GRPWALSVTMSYLEIYQEKVLDLLDPA 187
Cdd:PLN03188   170 FAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEEQIKhaDRQLKYQCRCSFLEIYNEQITDLLDPS 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  188 SGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQR-----ERLAPFRQr 262
Cdd:PLN03188   250 QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRcksvaDGLSSFKT- 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  263 eGKLYLIDLAGSEDNRRTGNKGLRLKESGAINSSLFVLGKVVDALNQ----GLPR-VPYRDSKLTRLLQDSLGGSAHSIL 337
Cdd:PLN03188   329 -SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRhIPYRDSRLTFLLQESLGGNAKLAM 407

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2128100422  338 IANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQ 375
Cdd:PLN03188   408 VCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQ 445
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 87-306 2.86e-11

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: 63.13  E-value: 2.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   87 DAFYGEK---SSQQDIYAgSVQPILRHLLEGQN-ASVLAYGPTGAGKTHTMLgspeqpGVIPRALMDLlqLTREEGGEGR 162
Cdd:cd01363     20 IVFYRGFrrsESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVA--FNGINKGETE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  163 PWAlSVTMSYLEIYQEkVLDLLdpasgdlviredcrgnilipgltqkpitsfadferHFLPASRNrtvGATRLNQRSSRS 242
Cdd:cd01363     91 GWV-YLTEITVTLEDQ-ILQAN-----------------------------------PILEAFGN---AKTTRNENSSRF 130

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2128100422  243 HAVLLVkvdqrerlapfrqregklyLIDLAGSEdnrrtgnkglrlkesgAINSSLFVLGKVVDA 306
Cdd:cd01363    131 GKFIEI-------------------LLDIAGFE----------------IINESLNTLMNVLRA 159
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 40-184 5.20e-08

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 52.99  E-value: 5.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422   40 VRVAVRLRPFvdgtdgagdppcvrGLDSCSLE-----IANWRNHQETLKYQFDAFYGEKSSQQDIYagsvQPIlRHL--- 111
Cdd:pfam16796   22 IRVFARVRPE--------------LLSEAQIDypdetSSDGKIGSKNKSFSFDRVFPPESEQEDVF----QEI-SQLvqs 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2128100422  112 -LEGQNASVLAYGPTGAGKThtmlgspeqPGVIPRALMDLLQlTREEGGEGrpWALSVTMSYLEIYQEKVLDLL 184
Cdd:pfam16796   83 cLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFR-FISSLKKG--WKYTIELQFVEIYNESSQDLL 144
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 595-635 9.18e-06

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 44.47  E-value: 9.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2128100422  595 LNEGSARDLRSLQRIGQKKAQLIVGWRELHGPFSQP-----VLGLD 635
Cdd:COG1555     15 INTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVedlleVKGIG 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
910-935 3.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.28e-05
                           10        20
                   ....*....|....*....|....*.
gi 2128100422  910 HLNRHKLSHSDEKPYQCPVCQQRFKR 935
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
894-947 1.12e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2128100422  894 KNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSY--HVRSHD 947
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHH 87
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 920-977 1.44e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 1.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2128100422  920 DEKPYQCPV--CQQRFKRKDRMSYHVR---------------SHDG--AVHKPYNCSHCGKSFSRPDHLNSHVRQVH 977
Cdd:COG5189    346 DGKPYKCPVegCNKKYKNQNGLKYHMLhghqnqklhenpspeKMNIfsAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 954-977 4.26e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 4.26e-04
                           10        20
                   ....*....|....*....|....
gi 2128100422  954 YNCSHCGKSFSRPDHLNSHVRqVH 977
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 954-977 1.23e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 37.24  E-value: 1.23e-03
                           10        20
                   ....*....|....*....|....
gi 2128100422  954 YNCSHCGKSFSRPDHLNSHVRQVH 977
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTHH 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
914-982 1.91e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128100422  914 HKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGavHKPYNCSH--CGKSFSRPDhlNSHVRQVHSTERP 982
Cdd:COG5048     24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTG--EKPSQCSYsgCDKSFSRPL--ELSRHLRTHHNNP 90
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
924-1081 2.32e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.93  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  924 YQCP--VCQQRFKRKDRMSYHVRSHdgavHKPYNCSHCG---KSFS------RPDHLNSHvRQVHSTERPFK----CEKC 988
Cdd:COG5236    152 FKCPksKCHRRCGSLKELKKHYKAQ----HGFVLCSECIgnkKDFWneirlfRSSTLRDH-KNGGLEEEGFKghplCIFC 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128100422  989 EAAFATKDRLRAH-TVRHEEkvpCHVCGKM--LSSAYISDH--MKVHSQGPHHVC--ELCNKG----FTTAAYLRIHAVK 1057
Cdd:COG5236    227 KIYFYDDDELRRHcRLRHEA---CHICDMVgpIRYQYFKSYedLEAHFRNAHYCCtfQTCRVGkcyvFPYHTELLEHLTR 303

                          170       180
                   ....*....|....*....|....
gi 2128100422 1058 DHGLQAPRADRILCKLCSVHCKTP 1081
Cdd:COG5236    304 FHKVNARLSEIPRPGRCSIPVMDP 327
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 896-918 2.35e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 2.35e-03
                           10        20
                   ....*....|....*....|...
gi 2128100422  896 HACEMCGKAFRDVYHLNRHKLSH 918
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 595-627 2.38e-03

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 37.46  E-value: 2.38e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2128100422  595 LNEGSARDLRSLQRIGQKKAQLIVGWRELHGPF 627
Cdd:pfam12836    6 INTASAELLSRVPGLGPKLAKNIVEYREENGPF 38
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 595-627 5.39e-03

competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model. [Cellular processes, DNA transformation]


Pssm-ID: 129520 [Multi-domain]  Cd Length: 69  Bit Score: 36.83  E-value: 5.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2128100422  595 LNEGSARDL-RSLQRIGQKKAQLIVGWRELHGPF 627
Cdd:TIGR00426   10 INTATAEELqRAMNGVGLKKAEAIVSYREEYGPF 43
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 1017-1068 5.41e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 40.62  E-value: 5.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2128100422 1017 MLSSAYISDHMKVHSQGPHHVCELCNKGFTTAAYLRIHAVKDHGLQAPRADR 1068
Cdd:cd23959    227 SAASFPAAPVANGEAATPTHACTICGKAFSTHEGLRMHSKAKHGVELEKAKT 278
ZnF_C2H2 smart00355
zinc finger;
924-946 5.87e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 5.87e-03
                            10        20
                    ....*....|....*....|...
gi 2128100422   924 YQCPVCQQRFKRKDRMSYHVRSH 946
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 924-946 9.46e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 9.46e-03
                           10        20
                   ....*....|....*....|...
gi 2128100422  924 YQCPVCQQRFKRKDRMSYHVRSH 946
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
 
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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