|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
492-819 |
0e+00 |
|
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: 542.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 492 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFN 570
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 571 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 647
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 648 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 727
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 728 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 807
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 767989898 808 LKFAERVRSVEL 819
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
500-817 |
1.64e-151 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 448.18 E-value: 1.64e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 500 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVCIFAY 576
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 577 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 656
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 657 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 733
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 734 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 811
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 767989898 812 ERVRSV 817
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
494-821 |
4.39e-145 |
|
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: 432.00 E-value: 4.39e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDVFQEVQA-LVTSCIDGF 569
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 570 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 649
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 650 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 727
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 728 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 805
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 767989898 806 YSLKFAERVRSVELGP 821
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
494-815 |
1.83e-125 |
|
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: 380.83 E-value: 1.83e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPvtKEDGEGPEATNAVTFDADDDSIIHL--LHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFN 570
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 571 VCIFAYGQTGAGKTYTMEGTAEN-PGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 648
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 649 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 726
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 727 SERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 805
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 767989898 806 YSLKFAERVR 815
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
494-817 |
3.95e-106 |
|
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: 330.96 E-value: 3.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVT-KEDGEGpeATNAVTFDADDDSIIhlLHKGK------PVSFELDKVFSPQASQQDVFQE-VQALVTSC 565
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 566 IDGFNVCIFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEK 642
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 643 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 718
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 719 LNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 797
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 767989898 798 EKNTSETLYSLKFAERVRSV 817
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
495-818 |
2.26e-104 |
|
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: 326.60 E-value: 2.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 495 IRVIARVRPVT-KEDGEGPEatNAVTFDADDDSIIhllhKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 572
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 573 IFAYGQTGAGKTYTMEGTA------ENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIR 646
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 647 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 716
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 717 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 793
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 767989898 794 VSPVEKNTSETLYSLKFAERVRSVE 818
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
494-817 |
5.84e-95 |
|
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: 301.96 E-value: 5.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDADDDSIIHLL----------HKGKPVSFELDKVFSPQASQQDVFQ 556
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 557 E-VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLL 635
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 636 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 714
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 715 --TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 789
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 767989898 790 MVVQVSPVEKNTSETLYSLKFAERVRSV 817
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
494-817 |
1.11e-92 |
|
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: 295.01 E-value: 1.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVTKEDgegPEATNAVTFDADDDSIIHllHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFNVC 572
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 573 IFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkASDWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 652
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 653 GQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 728
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 729 RVGKSGAEGSRLREAQHINKSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 806
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 767989898 807 SLKFAERVRSV 817
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
494-817 |
3.53e-92 |
|
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: 293.85 E-value: 3.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVTKEDGEGPeatNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 572
Cdd:cd01369 3 NIKVVCRFRPLNELEVLQG---SKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFaAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 573 IFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGkepQEKLEIRLCP 649
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 650 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSER 729
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 730 VGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSL 808
Cdd:cd01369 237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316
|
....*....
gi 767989898 809 KFAERVRSV 817
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
494-817 |
7.44e-89 |
|
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: 286.14 E-value: 7.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVTKEDgegPEATNAVTFDADDDS----IIHLLHKGKPV--SFELDKVFSPQASQQDVFQEVQA-LVTSCI 566
Cdd:cd01364 3 NIQVVVRCRPFNLRE---RKASSHSVVEVDPVRkevsVRTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 567 DGFNVCIFAYGQTGAGKTYTMEG--------TAENP---GINQRALQLLFSEVQEkaSDWEYTITVSAAEIYNEVLRDLL 635
Cdd:cd01364 80 MGYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDplaGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 636 GKEPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG- 712
Cdd:cd01364 158 SPSSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 713 --LRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLM 790
Cdd:cd01364 238 eeLVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340
....*....|....*....|....*..
gi 767989898 791 VVQVSPVEKNTSETLYSLKFAERVRSV 817
Cdd:cd01364 318 IATISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
493-817 |
2.44e-87 |
|
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: 282.32 E-value: 2.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 493 GNIRVIARVRPVTK-EDGEGpeATNAVTFDADDDSIIHL--------LHKGKPVSFELDKVF-------SPQASQQDVFQ 556
Cdd:cd01365 1 ANVKVAVRVRPFNSrEKERN--SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 557 EVQA-LVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASD-WEYTITVSAAEIYNEVLRDL 634
Cdd:cd01365 79 DLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 635 LGKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHAL--LIVTVRGVDC 709
Cdd:cd01365 159 LNPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 710 STGLRT--TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQ 779
Cdd:cd01365 237 ETNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLK 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 767989898 780 DSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 817
Cdd:cd01365 317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
478-818 |
2.27e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 278.55 E-value: 2.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 478 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE 557
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 558 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 636
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 637 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 716
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 717 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 794
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 767989898 795 SPVEKNTSETLYSLKFAERVRSVE 818
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
494-815 |
1.27e-78 |
|
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: 258.59 E-value: 1.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVTKEDGEGpEATNAVTFDADDDSIihlLHKGKPVSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVC 572
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 573 IFAYGQTGAGKTYTMEGTAENP--------GINQRALQLLFSEVQ---EKASD-WEYTITVSAAEIYNEVLRDLLgkEP- 639
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 640 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 716
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 717 gKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 792
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 767989898 793 QVSPVEKNTSETLYSLKFAERVR 815
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
495-812 |
1.47e-78 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 258.48 E-value: 1.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 495 IRVIARVRPVTKEDGEGPEA-------TNAVTFDADDDSIIHLLHKG---KPVSFELDKVFSPQASQQDVFQEV-QALVT 563
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 564 SCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkasdweYTITVSAAEIYNEVLRDLL----GKEP 639
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 640 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 714
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 715 ---TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 786
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 767989898 787 KTLMVVQVSPVEKNTSETLYSLKFAE 812
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
495-815 |
1.87e-73 |
|
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: 244.41 E-value: 1.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 495 IRVIARVRPVTKEDGEGpeatnaVTFDADDDSI-IHLL---------HKGKPVSFELDKVFSpQASQQDVFQEV-QALVT 563
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLH-NASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 564 SCIDGFNVCIFAYGQTGAGKTYTMEGTAEN---PGINQRALQLLFSEVQEKASDwEYTITVSAAEIYNEVLRDLLGKEPQ 640
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 641 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 715
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 716 TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 794
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 767989898 795 SPVEKNTSETLYSLKFAERVR 815
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
494-815 |
1.60e-72 |
|
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: 241.25 E-value: 1.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVtkEDGEGPEATNAVTFDADDDSII--HLLHKGKPVSFELDKVFSPQASQQDVF-QEVQALVTSCIDGFN 570
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 571 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKAsdWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 650
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 651 GSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 729
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 730 VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 809
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 767989898 810 FAERVR 815
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
494-814 |
3.72e-67 |
|
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: 226.79 E-value: 3.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 494 NIRVIARVRPVTKEDgEGPEATNAVTFDADDDSIIH-------LLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSC 565
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 566 IDGFNVCIFAYGQTGAGKTYTMEG----TAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLgkepQE 641
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 642 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 721
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 722 VDLAGSER-VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 799
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 767989898 800 NTSETLYSLKFAERV 814
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
495-818 |
1.23e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 215.57 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 495 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVCI 573
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 574 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLgkE 638
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL--D 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 639 P-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT 715
Cdd:PLN03188 248 PsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 716 --TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKT 788
Cdd:PLN03188 326 fkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350
....*....|....*....|....*....|
gi 767989898 789 LMVVQVSPVEKNTSETLYSLKFAERVRSVE 818
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
474-635 |
3.45e-44 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 156.23 E-value: 3.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 474 YRRELQLRKKCHNELVRLKGNIRVIARVRPvtkedgegpEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQD 553
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRP---------ELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 554 VFQEVQALVTSCIDGFNVCIFAYGQTGAGktytmegtaENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRD 633
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 767989898 634 LL 635
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
542-761 |
2.05e-23 |
|
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: 97.80 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 542 DKVFSPQASQQDVFQEVQALVTSCIDGFNV-CIFAYGQTGAGKTYTMEgtaenpGINQRALQLLFSEVQEKASDWEYTIT 620
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 621 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfghTNRTTEfTNLNEHSSRSHALL 700
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767989898 701 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegsrlreaqhINKSLSALGDVIAALR 761
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-462 |
2.26e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 151 LTLQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLR 230
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 231 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLS----------RRLRDSHETIASLRAQs 300
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltllnEEAANLRERLESLERR- 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 301 ppVKYVIKTVEvESSKTKQALSESQARNQHLQEQvamQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErahgQMLEE 380
Cdd:TIGR02168 833 --IAATERRLE-DLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELE----ELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 381 MQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND-YNGLKRQVRGFPLLLQEALRSVKaEIGQA 459
Cdd:TIGR02168 903 LRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLK-RLENK 980
|
...
gi 767989898 460 IEE 462
Cdd:TIGR02168 981 IKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-478 |
3.74e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKlISQAQEVSRLRSELGgtdlEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaqlrDKL 233
Cdd:TIGR02168 201 QLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE--------------------EEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 234 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA---QEEERLSRRLRDSHETIASLRAQsppvkyvIKTV 310
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 311 EVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT--------------ARLRAQIAMYESELER--AH 374
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 375 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 454
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330 340
....*....|....*....|....*.
gi 767989898 455 EIGQAIEEVNS--NNQELLRKYRREL 478
Cdd:TIGR02168 483 ELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-463 |
3.30e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 151 LTLQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQE-SAQL 229
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 230 RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIaslraqsppvkyvikt 309
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---------------- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 310 vevessktkQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKN 389
Cdd:COG1196 379 ---------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767989898 390 RA--IEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 463
Cdd:COG1196 450 EEaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-483 |
1.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 195 LRQEMRRCEAELQELRTKpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdclaE 274
Cdd:COG1196 218 LKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 275 KAQEEER-LSRRLRDSHETIASLRAQsppvkyviktveveSSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSH 353
Cdd:COG1196 285 EAQAEEYeLLAELARLEQDIARLEER--------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 354 QLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEafARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNG 433
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767989898 434 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 483
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
476-760 |
4.38e-11 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 66.30 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 476 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDADDDSIihllhKGKPV------------SFELDK 543
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 544 VFSPQASQQDVFQEVQALVTSCIDGfnvcIFAYGQTGAGKTYTMEgtAENPGINQRALQLLFSEVQ-EKASDWEYTITVS 622
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 623 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvddinkvfEFGHTNRTTEFTNLNEHSSRS 696
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--------EKASKLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767989898 697 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGSRLREAQHINKSLSALGDVIAAL 760
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-438 |
4.41e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 166 AQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaESKG 245
Cdd:TIGR02169 729 EQEEEKLKERL--EELEEDLSSLEQEIENVKSELKELEARIEELEEDLH------KLEEALNDLEARLSHSRIP--EIQA 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 246 MLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALS 322
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 323 ESQARNQHLQEQVAMQRQVLKEMEQQLQS---------SHQLTARLRAQIAMYE-SELERAHGQMLE------------- 379
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEEleaqiekkrKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqa 958
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767989898 380 -------EMQSLEEDKNRAIE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 438
Cdd:TIGR02169 959 elqrveeEIRALEPVNMLAIQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-495 |
5.57e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 196 RQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELRLkdclAEK 275
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL----ARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 276 AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQL 355
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 356 TARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK 435
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 436 RQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 495
Cdd:TIGR02168 887 EAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
150-386 |
3.25e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 150 YLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMvenerlrQEMRRCEAELQELRTkpagpcpgcehsqESAQL 229
Cdd:COG3206 179 FLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-------QQLSELESQLAEARA-------------ELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 230 RDKLSQLQLEMAESKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSHETIASLRAQsppvkyvI 307
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNHPDVIALRAQ-------I 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 308 KTVEVE-SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSshqlTARLRAQIAMYESELERAHGQMLEEMQSLEE 386
Cdd:COG3206 301 AALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-502 |
8.37e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 228 QLRDKLSQLQLEMAESKgmLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIaslraqsppvkyvi 307
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEEL-------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 308 ktvEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEED 387
Cdd:COG1196 280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 388 KN--RAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNS 465
Cdd:COG1196 357 EAelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAE 432
|
250 260 270
....*....|....*....|....*....|....*..
gi 767989898 466 NNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVR 502
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
154-476 |
1.25e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRSELGGT-----DLEKHRDLLMVENERLRQEMRRCEAELQELRTK--------PAGPCPGC 220
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDApvdlgNAEDFLEELREERDELREREAELEATLRTARERveeaeallEAGKCPEC 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 221 -------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDrLAEVELRLKDcLAEKAqeeERLSRRLRDSHETI 293
Cdd:PRK02224 458 gqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIER-LEERR---EDLEELIAERRETI 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 294 ASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLrAQIAMYESELERA 373
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERL 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 374 HGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPL 443
Cdd:PRK02224 612 REK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
330 340 350
....*....|....*....|....*....|....*...
gi 767989898 444 LLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 476
Cdd:PRK02224 689 ELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
191-406 |
2.13e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 191 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 270
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 271 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPP---------VKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 336
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 337 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 406
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
157-470 |
3.56e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 157 HLKEKLISQAQEVS-RLRSELGGTDLEKhrDLLMVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESA-----QLR 230
Cdd:pfam15921 387 HKREKELSLEKEQNkRLWDRDTGNSITI--DHLRRELDDRNMEVQRLEALLKAMKSE----CQGQMERQMAAiqgknESL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 231 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTV 310
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 311 EVESSKTK-QALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTA---RLRAQIAMYESELERAHGQM---LEEMQS 383
Cdd:pfam15921 532 ELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKI 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 384 LEEDKNRAIEEAFAR-AQVEMKAVH------ENLAGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQ 446
Cdd:pfam15921 612 LKDKKDAKIRELEARvSDLELEKVKlvnagsERLRAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
330 340
....*....|....*....|....
gi 767989898 447 EALRSVKAEIGQAIEEVNSNNQEL 470
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
181-462 |
3.58e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.49 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 181 LEKHRDLLMVENERLRQEMR--------------RCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGM 246
Cdd:pfam01576 375 LEKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQARLS------ESERQRAELAEKLSKLQSELESVSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 247 LSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALS 322
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 323 ESQARnqhlQEQVAMQRQVLKEMEQQLQS-SHQLTARLRAQIAMYEsELERAHGQMLEEMQSL--EEDKNRAIEEAFARA 399
Cdd:pfam01576 528 DMKKK----LEEDAGTLEALEEGKKRLQReLEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDHQRQLVSNLEKK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 400 Q-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKAEIGQAIE 461
Cdd:pfam01576 603 QkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQLRAEM-EDLVSSKDDVGKNVH 681
|
.
gi 767989898 462 E 462
Cdd:pfam01576 682 E 682
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-373 |
7.31e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKL 233
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKEL--AALKKEEKALLKQLAALERRIAALARRIRALEQELA------ALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 234 SQLQLEMAESKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLRAQSPPVKYV 306
Cdd:COG4942 93 AELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767989898 307 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERA 373
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-463 |
8.07e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 189 MVEN----ERLRQEMRRCEAELQELRtkpagpcPGCEHSQESAQLRDKLSQLQLemaeskgMLSELNLEVQQKTDRLAEV 264
Cdd:COG4913 230 LVEHfddlERAHEALEDAREQIELLE-------PIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 265 EL-RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqALSESQARNQHLQEQVAMQRQVLK 343
Cdd:COG4913 296 ELeELRAELARLEAELERLEARLDALREELDELEAQ--------------------IRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 344 EMEQQLQSSHQLTARLRAQIAMYESELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 423
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767989898 424 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 463
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-500 |
1.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 159 KEKLISQAQEVSRLRSELGG--TDLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaQLRDKLSQL 236
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKelEEVLREINEISSELPELREELEKLEKEVKELE-----------------ELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 237 QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEKAQEEERLSR-------RLRDSHETIASLRAQS 300
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 301 PPVKYVIKtvevESSKTKQALSESQARNQHLQEQVAmqrqVLKEMEQQLQSSHQLTA---RLRAQIAMYESE-------- 369
Cdd:PRK03918 324 NGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHELYEEAKAKKEeleRLKKRLTGLTPEklekelee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 370 LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----------------MKAVHENLAGVRTNLLTLQPA 423
Cdd:PRK03918 396 LEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767989898 424 LRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 500
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
156-479 |
3.66e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 156 EHLKEKLISQAQEVSRLRSELGgTDLEKHRDLL--MVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQES-AQLRDK 232
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLE-QDYQAASDHLnlVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQqEENEAR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 233 LSQLQLEMAESKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKDCLAE-KAQEEERLSRRLR---- 287
Cdd:PRK04863 385 AEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAEDWLEEfQAKEQEATEELLSleqk 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 288 -DSHETIASLRAQSppVKYVIKTV-EVESSKTKQALSE--SQARNQ-HLQEQVAMQRQVLKEMEQQLQSSHQLTARLR-- 360
Cdd:PRK04863 465 lSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRMRLSELEQRLRQQQRAERLLAef 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 361 --AQIAMY--ESELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLAGVRTNLLTLQPA---LRTLTNDY 431
Cdd:PRK04863 543 ckRLGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLAARAPAWLAAQDAlarLREQSGEE 622
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767989898 432 NGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 479
Cdd:PRK04863 623 FEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
234-456 |
3.74e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 234 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK-----AQEEERLSRRLRDSHETIASLRAQSPPVKYVIK 308
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 309 TVEVESSKTKQALSESQA--RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSlEE 386
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA-EL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 387 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpLLLQEALRSVKAEI 456
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVRV 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-496 |
5.32e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 159 KEKLISQAQEVSRLRSELggtdlEKHRDLLMVENERLRQEMRRCEAELQELRtKPAGPCPGC------EH---------- 222
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCgrelteEHrkelleeyta 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 223 -----SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKT--DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIAS 295
Cdd:PRK03918 460 elkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 296 LRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQ-LQSSHQLTARLRaqiamyesELERAH 374
Cdd:PRK03918 537 LKGE-------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLK--------ELEPFY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 375 GQMLEEMQSleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVK 453
Cdd:PRK03918 602 NEYLELKDA--EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLR 679
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767989898 454 AEIGQA---IEEVNSNNQEL------LRKYRRELQLRKKCHNELVRLKGNIR 496
Cdd:PRK03918 680 AELEELekrREEIKKTLEKLkeeleeREKAKKELEKLEKALERVEELREKVK 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-387 |
2.30e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLK------EKLISQAQEVSRLRSELGGTDLEKHR---DLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsQ 224
Cdd:COG4913 250 QIELLEpirelaERYAAARERLAELEYLRAALRLWFAQrrlELLEAELEELRAELARLEAELERLE-------------A 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 225 ESAQLRDKLSQLQLEMAESKG-MLSELNLEVQQKTDRLAEVELRLKDcLAEKAQeeeRLSRRLRDSHETIASLRAQSPpv 303
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRAR-LEALLA---ALGLPLPASAEEFAALRAEAA-- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 304 kyviktvevessKTKQALSESQARnqhLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQS 383
Cdd:COG4913 391 ------------ALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGL 455
|
....
gi 767989898 384 LEED 387
Cdd:COG4913 456 DEAE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-504 |
2.30e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 227 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyv 306
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 307 iktvevessktKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEE 386
Cdd:COG4913 677 -----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 387 DKNRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAI 460
Cdd:COG4913 746 ELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYL 818
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767989898 461 EEVNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 504
Cdd:COG4913 819 ALLDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-299 |
4.27e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 152 TLQVEHLKEKLISQAQEVSRLRSELGGTD-----LEKHRDLLMVENERLRQEMR--------RCEAELQELRTKPAgpcp 218
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEaelerLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELE---- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 219 gcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRA 298
Cdd:COG4913 356 --ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
.
gi 767989898 299 Q 299
Cdd:COG4913 434 R 434
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
179-300 |
5.05e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 179 TDLEKHRDLLMVENERLRQEMRRC--------------EAELQELR--TKPAGPCPgcehSQESAQLRDKLSQLQLEMAE 242
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLnsikpklrdrkdalEEELRQLKqlEDELEDCD----PTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767989898 243 SKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 300
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-481 |
7.48e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 227 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYV 306
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 307 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQsleE 386
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE---A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 387 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSN 466
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*
gi 767989898 467 NQELLRKYRRELQLR 481
Cdd:COG4372 260 IEELELAILVEKDTE 274
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
159-358 |
9.60e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 159 KEKLISQAQEVSRLRSELGGT-------DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpagpcpgcEHSQESAQLRD 231
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEA---------QQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 232 KLSQLQLEMAESKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 311
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767989898 312 VESSKTKQALSESQARNQHLQEQVAMQRQV----LKEMEQQLQSSHQLTAR 358
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQGEGSN 216
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
153-480 |
1.97e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 153 LQVEHLKEKLISQaqevSRLRSELGGTDLEKHRDL---------LMVENERLRQEMRRCEAELQEL-RTKPAGPCPGCEH 222
Cdd:pfam05483 279 LQDENLKELIEKK----DHLTKELEDIKMSLQRSMstqkaleedLQIATKTICQLTEEKEAQMEELnKAKAAHSFVVTEF 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 223 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRL---------AEVELR-LKDCLAEKA------QEEERLSRRL 286
Cdd:pfam05483 355 EATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELeemtkfknnKEVELEeLKKILAEDEklldekKQFEKIAEEL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 287 RDS-HETIASLRAQSPPVK------YVIKTVEVESSKTKQALsESQARNQHLQ--EQVAMQRQVLKEMEQQLQSSHQLTA 357
Cdd:pfam05483 435 KGKeQELIFLLQAREKEIHdleiqlTAIKTSEEHYLKEVEDL-KTELEKEKLKniELTAHCDKLLLENKELTQEASDMTL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 358 RLRAQ---IAMYESELERahgqMLEEMQSLEE------DKNRAIEEAFARAQVEMKA----VHENLAGVRTNLLTLQPAL 424
Cdd:pfam05483 514 ELKKHqedIINCKKQEER----MLKQIENLEEkemnlrDELESVREEFIQKGDEVKCkldkSEENARSIEYEVLKKEKQM 589
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 767989898 425 RTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 480
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
154-394 |
2.83e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRSElggtdlEKHRDLLMVENERLRQEMRRCEAELQELR------TKPAGpcpgcEHSQESA 227
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNE------GDHLRNVQTECEALKLQMAEKDKVIEILRqqienmTQLVG-----QHGRTAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 228 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSH 290
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSR 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 291 ETIASLRAQSPPVK--YVIKTVEVESSKTKQALSESQArnqhlQEQVAMQRQVLKEMEQQ--------LQSSHQLTARlR 360
Cdd:pfam15921 667 NELNSLSEDYEVLKrnFRNKSEEMETTTNKLKMQLKSA-----QSELEQTRNTLKSMEGSdghamkvaMGMQKQITAK-R 740
|
250 260 270
....*....|....*....|....*....|....*..
gi 767989898 361 AQIAMYESE---LERAHGQMLEEMQSLEEDKNRAIEE 394
Cdd:pfam15921 741 GQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQE 777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-481 |
3.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 273 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALsesqarnqhLQEQVAMQRQVLKEMEQQLQSS 352
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 353 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 418
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767989898 419 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 481
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-487 |
4.01e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 223 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 300
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 301 PPVKYVIKTVEVESS-------KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERa 373
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 374 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 450
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767989898 451 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 487
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-490 |
4.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 197 QEMRRCEAELQELRTKPAgpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 274
Cdd:COG4717 71 KELKELEEELKEAEEKEE----------EYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 275 KAQEEERLsRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQARNQhlQEQVAMQRQVLKEMEQQLQSSHQ 354
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE------------------LEELEAELAELQ--EELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 355 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGL 434
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767989898 435 KRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 490
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
193-464 |
5.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 193 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ--LEMAESKGMLSELNLEVQQKTDRLAEVEL---- 266
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE------ALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 267 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQARNQHLQEQV--AM 337
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 338 QRQVLKEMEQQLQSShqlTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 417
Cdd:COG4913 760 GDAVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767989898 418 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 464
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
224-400 |
6.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 224 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 296
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 297 RAQSpPVKYV--IKTVEVESSKTKQALSE---SQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 371
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 767989898 372 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 400
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
187-507 |
8.13e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 187 LLMVENERLRQEMRRcEAELQELRTKPAGPCPGCEH-SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 265
Cdd:pfam05557 11 LSQLQNEKKQMELEH-KRARIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 266 LRLKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQARNQHLQEQVAMQRQVLKEM 345
Cdd:pfam05557 90 KKLN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 346 EQ---QLQSSHQLTA-------RLRAQIAMYES----------------ELERAHGQMLEE---MQSLEEDKNRAIEEAF 396
Cdd:pfam05557 152 EQlrqNLEKQQSSLAeaeqrikELEFEIQSQEQdseivknskselaripELEKELERLREHnkhLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 397 araqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL 470
Cdd:pfam05557 232 -----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767989898 471 --LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 507
Cdd:pfam05557 307 rqLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-497 |
9.19e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRSELGG------------TDLEKHRDLLMVE-------NERLRQEMRRCEAELQELRTKpa 214
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKlnnkyndlkkqkEELENELNLLEKEklniqknIDKIKNKLLKLELLLSNLKKK-- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 215 gpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHE 291
Cdd:TIGR04523 210 --------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 292 TIASLRAQsppvkyvIKTVEVESSKTKQalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 371
Cdd:TIGR04523 282 KIKELEKQ-------LNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 372 RAHGQMLEEMQSLEEdKNRAIEeafaraqvemKAVHENlagvRTNLLTLQpalrTLTNDYNGLKRQvrgfpllLQEAlRS 451
Cdd:TIGR04523 353 NSESENSEKQRELEE-KQNEIE----------KLKKEN----QSYKQEIK----NLESQINDLESK-------IQNQ-EK 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 767989898 452 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRV 497
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
285-492 |
1.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 285 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQAR--------NQHLQEQVAMQRQVLK-EMEQQLQS 351
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 352 SH-----QLTARLRAQIAMYESELErahgqMLEE-------MQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVR 414
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFQKVIK-----MYEKggvcptcTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIM 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767989898 415 TNLLTLQPALRTLTNDYNGLKRQVrgfpLLLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 492
Cdd:PHA02562 330 DEFNEQSKKLLELKNKISTNKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
152-495 |
1.63e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 152 TLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLL--------------------MVENE----RLRQEMRRCEAELQ 207
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelkselknqekkleeiqnqISQNNkiisQLNEQISQLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 208 ELRTkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGML----------SELNLEVQQKTDRLAEVELRLKDCLAEK-- 275
Cdd:TIGR04523 353 NSES---------ENSEKQRELEEKQNEIEKLKKENQSYKqeiknlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKel 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 276 -AQEEERLSRRLRDSHETIASLRAQSPPVKYVIKtvEVESSKTKQ-----ALSESQARNQHLQEQvamQRQVLKEMEQQL 349
Cdd:TIGR04523 424 lEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK--NLDNTRESLetqlkVLSRSINKIKQNLEQ---KQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 350 QSSHQLTARLRAQIamyeSELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENL--AGVRTNLLTLQPALRTL 427
Cdd:TIGR04523 499 KKLNEEKKELEEKV----KDLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEEL 573
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767989898 428 TNDYNGLKRQVRGFPLLLQEaLRSVKAEIGQAIEEvnsnNQELLRKYRRELQLRKKCHNELVRLKGNI 495
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQ-KEKEKKDLIKEIEE----KEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-438 |
1.65e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 197 QEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELN-LEVQQKTDRLAEVELRLKDCLAEK 275
Cdd:PRK04863 837 AELRQLNRRRVELERALA------DHESQEQQQRSQLEQAKEGLSALNRLLPRLNlLADETLADRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 276 A-----------------------QEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE-------VESSKTKQALSES- 324
Cdd:PRK04863 911 RfvqqhgnalaqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKNSDLNEKl 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 325 QARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyeseleRAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEM 403
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAEERARARR 1062
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767989898 404 KAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 438
Cdd:PRK04863 1063 DELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
196-483 |
1.91e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 196 RQEMRRCEAELQELRTKPAGPCpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE------LRLK 269
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKAC----------EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlskiMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 270 D---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEME 346
Cdd:TIGR00606 269 NeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 347 QQL---QSSHQLTA-RLRAQIAMYESelERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMKAVHENLAGVRTN 416
Cdd:TIGR00606 343 TELlveQGRLQLQAdRHQEHIRARDS--LIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767989898 417 LLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQLRKK 483
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEK 492
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
125-361 |
1.92e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 125 AARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKE---KLISQAQEVSRLRSELGGTDLEK---HRDLLMVENERLRQE 198
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLDAELQLSAHLIQQEVGRAREQgeaERQQLSEVAQQLEQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 199 MRRCEAELQELRTKPAGPCPGCEHS-QESAQLRDKLSQLQlemaeskgmlselNLEVQQKTDRLAEVELRLKDCLAEKaq 277
Cdd:pfam07111 533 LQRAQESLASVGQQLEVARQGQQEStEEAASLRQELTQQQ-------------EIYGQALQEKVAEVETRLREQLSDT-- 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 278 eEERLSRRLRDSHETIASLRA-QSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT 356
Cdd:pfam07111 598 -KRRLNEARREQAKAVVSLRQiQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQ 676
|
....*
gi 767989898 357 ARLRA 361
Cdd:pfam07111 677 QRLLA 681
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
229-423 |
2.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 229 LRDKLSQLQLEMAESKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 307
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 308 KTVEV--ESSKTKQALSESQARNQHLQEQVamqrQVLKEMEQQLQsshqltaRLRAQIAMYESELERAHGQ----MLEEM 381
Cdd:COG4717 126 QLLPLyqELEALEAELAELPERLEELEERL----EELRELEEELE-------ELEAELAELQEELEELLEQlslaTEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767989898 382 QSLEEDKNRA------IEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 423
Cdd:COG4717 195 QDLAEELEELqqrlaeLEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
188-475 |
2.11e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 188 LMVENERLRQEMRRCEAELQELRTKPAgpcpgcehSQESAQLRDKL----SQLQLEMAESKgmlselnlEVQQKTDRLAE 263
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEA--------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 264 VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVesskTKQALSESQARNQHLQEQVAMQRQVLK 343
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDE----ITERIAEQEIAYSELQEELEEILKQLE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 344 EME-QQLQSSHQLtarlraqIAMYESELErAHgQMLEEMQS-LEEDKnRAIE------------EAFARAQVEMKAVHEN 409
Cdd:PRK04778 394 EIEkEQEKLSEML-------QGLRKDELE-AR-EKLERYRNkLHEIK-RYLEksnlpglpedylEMFFEVSDEIEALAEE 463
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767989898 410 LAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRKYR 475
Cdd:PRK04778 464 LEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFREYD 534
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
153-420 |
2.42e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 153 LQVEHLKEKLISQAQEVSRLRSELG-----GTDLEKHRDLLMVENERLR----QEMRRCEAELQELRtkpagpcpgcEHS 223
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVliqkfGRSLKAKKRFSLLKKETIYlqsaQRVELAERQLQELK----------IDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 224 QESAQLRDKLSQLQLEMAE-SKGMLSELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLRAQS 300
Cdd:COG5022 892 KSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETS 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 301 PPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV----AMQRQV--LKEMEQQLQSSHQLTARLRA-----QIAMYESE 369
Cdd:COG5022 971 EEYEDLLKKSTILVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQK 1050
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767989898 370 LERAHgqMLEEMQSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 420
Cdd:COG5022 1051 LKGLL--LLENNQLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
226-413 |
2.63e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 43.06 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 226 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 299
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 300 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 379
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 767989898 380 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 413
Cdd:cd07627 181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
190-402 |
3.28e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 190 VENERLRQEMRRCEAELQELRTkpagpcpgCEHSQESAQLR-DKLSQLQLEMaESKGMLSELNLEVQQKTDRLAEVELRL 268
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRK--------LEEAEKARQAEmDRQAAIYAEQ-ERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 269 KDCLA---EKAQEEERL-------SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARN-QHLQEQVA- 336
Cdd:pfam17380 367 QEEIAmeiSRMRELERLqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAr 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767989898 337 -MQRQVLKEMEQQLQSS---HQLTARLRAQIAMYESELERAHGQMLEEM---QSLEEDKNRAIEEAFARAQVE 402
Cdd:pfam17380 447 eMERVRLEEQERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
158-417 |
3.34e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 158 LKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehsqeSAQLRDKLSQLQ 237
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESEL--KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK-------------LQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 238 LEMAESKGMLSELNLEVQQKTDRLAEVEL--RLKDCLAEKAQEEERLSRRLR--DSHETIASLRAQSPPVKYVIKTVEVE 313
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTImeRFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 314 SSKTKQALSESQARNQHLQE---QVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR 390
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
250 260
....*....|....*....|....*..
gi 767989898 391 AiEEAFARAQVEMKAVHENLAGVRTNL 417
Cdd:TIGR00606 925 K-EELISSKETSNKKAQDKVNDIKEKV 950
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
232-394 |
3.61e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 232 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHETIASLRAQSPPVK---- 304
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 305 YVIKTVEVESSKTKQALSESQARNqhLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYESELERAHGQMLEEMQSL 384
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 767989898 385 EEDKNRAIEE 394
Cdd:COG1579 162 EAEREELAAK 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
155-496 |
4.51e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 155 VEHLKEKLISQAQEVSRLRSELggTDLEKHRDllmVENERLRQEMRRCE---AELQELRTKpAGPCPGCEH---SQESAQ 228
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSEL--RQARKRRD---QASEALRQASRRLEerqSALDELELQ-LFPQAGTLLhflRKEAPD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 229 LRDKLSQL-QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLA-EKAQEEERLSRR-------LRDSHETIASLRAQ 299
Cdd:pfam12128 547 WEQSIGKViSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVpEWAASEEELRERldkaeeaLQSAREKQAAAEEQ 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 300 SPPVKYVIKTVEVESSKTKQALSESQAR-----NQHLQEQVAMQRQV---LKEMEQQLQS-SHQLTARLRAQIAMYES-- 368
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKALaerKDSANERLNSlEAQLKQLDKKHQAWLEEqk 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 369 -ELERAHGQMLEEMQSLEEDKNRA---IEEAFARAQVEMKA--------VHENLAGV---RTNLLTLQPALRTLT---ND 430
Cdd:pfam12128 707 eQKREARTEKQAYWQVVEGALDAQlalLKAAIAARRSGAKAelkaletwYKRDLASLgvdPDVIAKLKREIRTLErkiER 786
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767989898 431 YNGLKRQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL----RKKCHNELVRLKGNIR 496
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
151-411 |
5.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 151 LTLQVEHLKEKLISQAQEVSRLRSELGGTDlEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQE-SAQL 229
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEErLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 230 RDKLSQLQLEMAESKGMLSELNLEVQQKTD--------------RLAEVELRLKDCLAEKAQEEERLS---RRLRDSHET 292
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelkeeledlraELEEVDKEFAETRDELKDYREKLEklkREINELKRE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 293 IASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELer 372
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL-- 485
|
250 260 270
....*....|....*....|....*....|....*....
gi 767989898 373 ahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 411
Cdd:TIGR02169 486 -------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
203-438 |
6.10e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 203 EAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESK--------------GMLSELNL---------------- 252
Cdd:COG3096 835 EAELAALR-------------QRRSELERELAQHRAQEQQLRqqldqlkeqlqllnKLLPQANLladetladrleelree 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 253 ---------EVQQKTDRLAEVElRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVES-SKTKQALS 322
Cdd:COG3096 902 ldaaqeaqaFIQQHGKALAQLE-PLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 323 ESQARNQHLQEQ-VAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESelERAHGQMLEE-MQSLEEDKNRAIEEAFARAQ 400
Cdd:COG3096 981 ENSDLNEKLRARlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS--RDAKQQTLQElEQELEELGVQADAEAEERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767989898 401 VEMKAVHENL---AGVRTNLLT-----------LQPALRTLTNDYNGLKRQV 438
Cdd:COG3096 1059 IRRDELHEELsqnRSRRSQLEKqltrceaemdsLQKRLRKAERDYKQEREQV 1110
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-418 |
6.49e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 151 LTLQVEHLKEKLISQAQEVSRLRsELGGTDLEKHRDLLmvenERLRQEMRrceaelqelrtkpagpcpgcEHSQESAQLR 230
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK--------------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 231 DKLSQLQLEMAESKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrlrdshetiaslraqsp 301
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK----------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 302 pvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML--- 378
Cdd:PHA02562 304 -----IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVdna 378
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767989898 379 EEMQSLEEDKNRAIEEafaRAQVEMKAVHEnlaGVRTNLL 418
Cdd:PHA02562 379 EELAKLQDELDKIVKT---KSELVKEKYHR---GIVTDLL 412
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
158-395 |
7.71e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 158 LKEKLISQAQEVSRLRSElggtdlekhRDLLMVENERLRqemrrCeAELQELRTKPAGPCPGCEHSQE--------SAQL 229
Cdd:pfam05622 216 LEEKLEALQKEKERLIIE---------RDTLRETNEELR-----C-AQLQQAELSQADALLSPSSDPGdnlaaeimPAEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 230 RDKLSQLQLEmaesKGMLSELnlEVQQKTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKT 309
Cdd:pfam05622 281 REKLIRLQHE----NKMLRLG--QEGSYRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 310 VEVESSKT------KQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTArlraqiamyeSELERAHGQMLEEMQS 383
Cdd:pfam05622 348 LQEQGSKAedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKA 417
|
250
....*....|..
gi 767989898 384 LEEDKNRAIEEA 395
Cdd:pfam05622 418 MEERYKKYVEKA 429
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
193-403 |
8.57e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 41.57 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 193 ERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQktdRLAEVELRLKDCL 272
Cdd:cd07596 7 EEAKDYILKLEEQLKKLSKQ----------AQRLVKRRRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 273 AEKAQEEERLSRR--------LRDSHETIASLRAqsppvkyVIKT-----VEVESSKtkQALSESQARNQHLQEQVAMQR 339
Cdd:cd07596 74 EELSSLSEAQANQelvkllepLKEYLRYCQAVKE-------TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767989898 340 QVLKEMEQQLQSSHQLTARLRAqiamyesELERAHGQMLEEMQSLEEDKNRAIEEA---FARAQVEM 403
Cdd:cd07596 145 AKVEELEEELEEAESALEEARK-------RYEEISERLKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
196-400 |
8.79e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 196 RQEMRRCEAELQElrtkpagpcpgcehsQESAQLRdKLSQLQLEMAESkgMLSELNLEVQQKTDRLAEVELRLKDclAEK 275
Cdd:pfam15709 342 RAEMRRLEVERKR---------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 276 AQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQA---RNQHLQEQVAMQRQVLKEMEQQlqss 352
Cdd:pfam15709 402 RQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAEE---- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767989898 353 hqltARLRAQIAMYESElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 400
Cdd:pfam15709 475 ----ERLEYQRQKQEAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-502 |
1.03e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 338 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVhENLAGVRTNl 417
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQ- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 418 ltLQPALRTLTNDYNGLKRQVRGFPLLLQEALR---SVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGN 494
Cdd:TIGR02168 752 --LSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
....*...
gi 767989898 495 IRVIARVR 502
Cdd:TIGR02168 830 ERRIAATE 837
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
194-371 |
1.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 194 RLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLA 273
Cdd:COG1579 21 RLEHRLKELPAELAELE-------------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 274 EK-----AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVamqRQVLKEMEQQ 348
Cdd:COG1579 88 NKeyealQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAE 157
|
170 180
....*....|....*....|...
gi 767989898 349 LqsshqltARLRAQIAMYESELE 371
Cdd:COG1579 158 L-------EELEAEREELAAKIP 173
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
229-464 |
1.36e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 229 LRDKLSQLQL---EMAESKGMLSELNL--EVQQKTDRLAEVELRLKDC-LAEKAQEEERLSRRLRDSHETIAslraqspp 302
Cdd:PRK04778 228 LPDQLQELKAgyrELVEEGYHLDHLDIekEIQDLKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDILE-------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 303 vKYVI--KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQ---- 376
Cdd:PRK04778 300 -REVKarKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQeiay 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 377 -MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTltndyngLKRQVR-----GFPLLLQEALR 450
Cdd:PRK04778 379 sELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHE-------IKRYLEksnlpGLPEDYLEMFF 451
|
250
....*....|....
gi 767989898 451 SVKAEIGQAIEEVN 464
Cdd:PRK04778 452 EVSDEIEALAEELE 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
151-481 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 151 LTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcPGCEHSQESAQLR 230
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE---ELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 231 DKLSQLQLEMAE--------SKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHE-------- 291
Cdd:COG4717 170 AELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEEELEEAqeeLEELEEELEQLENELEAAALeerlkear 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 292 -------TIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQ 350
Cdd:COG4717 250 lllliaaALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 351 SSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEmkavheNLAGVRtNLLTLQPALRTLTN 429
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVE------DEEELR-AALEQAEEYQELKE 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767989898 430 DYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 481
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
159-285 |
1.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 159 KEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQL-- 236
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE-------------EELEELREELAELea 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767989898 237 QLEMAESKGMLSELNLEVQQKTDRLAEVE-----LRLKDCLAEKAQEEERLSRR 285
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAeewaaLKLALELLEEAREEYREERL 514
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
167-403 |
1.70e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 167 QEVSRLRSELggtdLEKHRDllmvenerlrqemrRCEAELQELRtkpagpcpgcehSQESAQlRDKLSQLQLEMAEskgM 246
Cdd:PRK10929 203 QELARLRSEL----AKKRSQ--------------QLDAYLQALR------------NQLNSQ-RQREAERALESTE---L 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 247 LSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRdsheTIASlraQSPPVKYVIKTVEVESsktkQALSESQA 326
Cdd:PRK10929 249 LAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQR----QAAS---QTLQVRQALNTLREQS----QWLGVSNA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 327 RNQHLQEQVAMqrqvLKEME--QQLQSShqlTARLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRaIEEAFARAQV 401
Cdd:PRK10929 318 LGEALRAQVAR----LPEMPkpQQLDTE---MAQLRVQRLRYEDLLNKQPQLRqirQADGQPLTAEQNR-ILDAQLRTQR 389
|
..
gi 767989898 402 EM 403
Cdd:PRK10929 390 EL 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
180-483 |
1.80e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 180 DLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD 259
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELE------QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 260 RLAEVElrlkdclaekaQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAmqR 339
Cdd:COG4372 116 ELEELQ-----------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA--E 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 340 QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLT 419
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767989898 420 LQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 483
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
155-481 |
1.92e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 155 VEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESA-QLRDKL 233
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQL----------------AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiQYQQAV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 234 SQLQlemaESKGMLSELNLEVQQKTDRLAEVELRlkdclaEKAQEEERLS--RRLRDSHETIASLRAQSPPVKYVIKTVE 311
Cdd:COG3096 420 QALE----KARALCGLPDLTPENAEDYLAAFRAK------EQQATEEVLEleQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 312 VES--SKTKQALSesQARNQ-HLQEQVAMQRQVLKEMEQQLQSSH-------QLTARLRAQIAMYEsELERAHGQMLEEM 381
Cdd:COG3096 490 RSQawQTARELLR--RYRSQqALAQRLQQLRAQLAELEQRLRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQL 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 382 QSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNLLTLQPALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE 461
Cdd:COG3096 567 EELEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARAPAWLA------------------AQDALERLREQSGEALA 623
|
330 340
....*....|....*....|...
gi 767989898 462 ---EVNSNNQELLRKYRRELQLR 481
Cdd:COG3096 624 dsqEVTAAMQQLLEREREATVER 646
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-489 |
1.95e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRS-----ELGGTDLEKHRDLLMVENERLRQEMRRCEAEL----QELRTKpagpcpgcehSQ 224
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLeqkqKELKSK----------EK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 225 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVK 304
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN----------------LE 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 305 YVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyeSELERAHGQMLEEMQSL 384
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL----EKAKKENEKLSSIIKNI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 385 EEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQPALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIE 461
Cdd:TIGR04523 637 KSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKIKESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR 702
|
330 340 350
....*....|....*....|....*....|.
gi 767989898 462 evNSNNQELLRKYR---RELQLRKKCHNELV 489
Cdd:TIGR04523 703 --IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
154-417 |
2.13e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRSELGGTD---LEKHRDLLMVENERLRQEMRRCEaELQELRtkpagpcpgcehsQESAQLR 230
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEealSEKERIIERLKEQREREDRERLE-ELESLK-------------KENKDLK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 231 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAqSPPVKYVI 307
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRI 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 308 KTVEVESSKTKQALSESQARNQHLQE---QVAMQR----QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEE 380
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVERLLGilrEVENEKndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE 640
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767989898 381 MQSLEEDKNRA-----IEE---AFARAQVEMKAVHENLAGVRTNL 417
Cdd:pfam10174 641 ARRREDNLADNsqqlqLEElmgALEKTRQELDATKARLSSTQQSL 685
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-499 |
2.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 154 QVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKL 233
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEEL----------------EQARSELEQLEEELEELNEQLQ------AAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 234 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKtvEVE 313
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 314 SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIE 393
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 394 EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRK 473
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
330 340
....*....|....*....|....*.
gi 767989898 474 YRRELQLRKKCHNELVRLKGNIRVIA 499
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
151-477 |
2.18e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 151 LTLQVEHLKEKLISQAQEVSRLRSELGGTDLE---KHRDLLMVENERLRQEMRRCEAelQELrtkpagpcpgcEHSQESA 227
Cdd:pfam07111 268 LQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkKCRSLLNRWREKVFALMVQLKA--QDL-----------EHRDSVK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 228 QLRDKLSQLQ-------------------------LEMAESKGMLSELNLEVQ---QKTDRLAEVELRLKDCLAEKAQEE 279
Cdd:pfam07111 335 QLRGQVAELQeqvtsqsqeqailqralqdkaaeveVERMSAKGLQMELSRAQEarrRQQQQTASAEEQLKFVVNAMSSTQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 280 ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQH---------LQEQVAMQRQVLKEMEQQLQ 350
Cdd:pfam07111 415 IWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScpppppappVDADLSLELEQLREERNRLD 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 351 SSHQLTARLRAQiamyesELERAHGQMLEEMQSLEEDKNRaIEEAFARAQvemkavhENLAGVRTNLLTLQPALRTLTND 430
Cdd:pfam07111 495 AELQLSAHLIQQ------EVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-------ESLASVGQQLEVARQGQQESTEE 560
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 767989898 431 YNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 477
Cdd:pfam07111 561 AASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-537 |
2.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 203 EAELQELRTKPAGPCPGCEHSQESAQLR---DKLSQLQLEMAESKGMLSELnlevqQKTDRLAEVELRLKdcLAEKAQEE 279
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADEL-----KKAEELKKAEEKKK--AEEAKKAE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 280 ERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVEVESS-KTKQALSESQARNQhlQEQVAMQRQVLKEMEQ----------- 347
Cdd:PTZ00121 1574 EDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQlkkkeaeekkk 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 348 --QLQSSHQLTARLRAQIAMYESELERAhgqmLEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagvrtnlltlqpaLR 425
Cdd:PTZ00121 1649 aeELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE---------------LK 1708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 426 TLTNDYNGLKRQVRGfplllQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE----LQLRKKCHNELVRLKGNIRVIARv 501
Cdd:PTZ00121 1709 KKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIE- 1782
|
330 340 350
....*....|....*....|....*....|....*...
gi 767989898 502 RPVTKEDGEGPEATNAVTFDADDDS--IIHLLHKGKPV 537
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIKDIFDNFanIIEGGKEGNLV 1820
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
234-502 |
4.03e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 234 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDShetiasLRAQ 299
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKN------LTVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 300 SPPVKYVIkTVEVESSKTKQA-------------------LSESQARNQHLQEQVAMQRQVLKEMEQQLQ---SSHQLTA 357
Cdd:COG3206 131 PVKGSNVI-EISYTSPDPELAaavanalaeayleqnlelrREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGLVD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 358 rLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHEN--LAGVRTNLLTLQPALRTLTNDYNG 433
Cdd:COG3206 210 -LSEEAKLLLQQLSELESQLAEARAELAEAEARlaALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767989898 434 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLrkyRRELQLRKkchnELVRLKGNIRVIARVR 502
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ---AREASLQA----QLAQLEARLAELPELE 350
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
159-287 |
4.40e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 159 KEKLISQAQEVSRLRSELggtdlekhRDLLMVENERLRQ------EMRRC-EAELQELRTKPAGPCpgcehsQESAQLRD 231
Cdd:smart00787 160 YKLLMKELELLNSIKPKL--------RDRKDALEEELRQlkqledELEDCdPTELDRAKEKLKKLL------QEIMIKVK 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767989898 232 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLR 287
Cdd:smart00787 226 KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLK 281
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
225-484 |
4.41e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 225 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSppvk 304
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 305 yviKTVEVESSKTKQALSESQARNQHL----------QEQVAMQRQVLKEMEQQLQSSHQlTARLRAQiaMYESELERAh 374
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE-ECRVAAQ--AHNEEAESL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 375 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 454
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422
|
250 260 270
....*....|....*....|....*....|..
gi 767989898 455 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 484
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
180-430 |
4.44e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 180 DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpaGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD 259
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLES---GDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 260 RLAEVELRLKDC--LAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktveVESSKTK-QALSESQARNQHLQEQVA 336
Cdd:pfam05622 95 EVLELQHRNEELtsLAEEAQALKDEMDILRESSDKVKKLEAT------------VETYKKKlEDLGDLRRQVKLLEERNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 337 MQRQVLKEMEQQLQSshqlTARLRAQIAMYESELERAHGQMLEEMQSLEedknraieeafaRAQVEMKAVHENLAGV--- 413
Cdd:pfam05622 163 EYMQRTLQLEEELKK----ANALRGQLETYKRQVQELHGKLSEESKKAD------------KLEFEYKKLEEKLEALqke 226
|
250
....*....|....*..
gi 767989898 414 RTNLLTLQPALRTlTND 430
Cdd:pfam05622 227 KERLIIERDTLRE-TNE 242
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
228-383 |
4.60e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 40.43 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 228 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 307
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQ-------VRTLREEKERSVSQVQELETSLAELKNQAAVPPAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 308 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVlkemeqQLQSSHQLTaRLRAQIAMYESELERA----------HGQM 377
Cdd:pfam15070 74 EQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQA------QVQDNEQLS-RLNQEQEQRLLELERAaerwgeqaedRKQI 146
|
....*.
gi 767989898 378 LEEMQS 383
Cdd:pfam15070 147 LEDMQS 152
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
247-371 |
4.72e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 247 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQA 326
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767989898 327 RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 371
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
230-382 |
5.15e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 230 RDK-LSQLQLEMAESKGMLS-------ELNLEVQQKTDRLAEVEL---RLKDCLAEKAQEEERLSRRLRDSHETIASLRA 298
Cdd:PRK09039 51 KDSaLDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 299 QSppvkyviktvevessktkqalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML 378
Cdd:PRK09039 131 VS---------------------ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....
gi 767989898 379 EEMQ 382
Cdd:PRK09039 190 QELN 193
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
238-395 |
9.19e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.74 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 238 LEMAESKGMLSELNLEVQQKTDRLAE----VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEV- 312
Cdd:pfam09731 280 LSNDDLNSLIAHAHREIDQLSKKLAElkkrEEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIr 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 313 ---ESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARlraqiAMYESELERAHGQmLEEMQSLEEDKN 389
Cdd:pfam09731 360 esyEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEER-----AGRLLKLNELLAN-LKGLEKATSSHS 433
|
....*.
gi 767989898 390 RAIEEA 395
Cdd:pfam09731 434 EVEDEN 439
|
|
| Vps5 |
pfam09325 |
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
230-402 |
9.69e-03 |
|
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.
Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 38.80 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 230 RDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---QSPPV 303
Cdd:pfam09325 54 RKELASATGEFAKSLASLASLELStgLSRALSQLAEVEERIKELLERQALQDVLtLGETIDEYLRLIGSVKAvfnQRVKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989898 304 KYVIKTVEVESSKTKQALSESQARNQHLQEQVAmqrQVLKEMEqqlqsshqlTARLRAQIAmyESELERAHGQMLEEMQS 383
Cdd:pfam09325 134 WQSWQNAEQELSKKKEQLEKLLRANKSQNDKLQ---QAKKEVE---------ELERRVQQA--EKEFEDISELIKKELER 199
|
170 180
....*....|....*....|..
gi 767989898 384 LEEDKN---RAIEEAFARAQVE 402
Cdd:pfam09325 200 FELERVddfKNSVEIYLESAIE 221
|
|
| |
