|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
556-883 |
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: 539.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 556 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFN 634
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 635 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 711
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 712 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 791
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 792 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 871
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 2462548931 872 LKFAERVRSVEL 883
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
564-881 |
5.11e-150 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 446.25 E-value: 5.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 564 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVCIFAY 640
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 641 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 720
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 721 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 797
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 798 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 875
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 2462548931 876 ERVRSV 881
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
558-885 |
1.46e-143 |
|
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: 430.07 E-value: 1.46e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDVFQEVQA-LVTSCIDGF 633
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 634 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 713
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 714 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 791
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 792 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 869
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 2462548931 870 YSLKFAERVRSVELGP 885
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
558-879 |
4.88e-124 |
|
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: 378.91 E-value: 4.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPvtKEDGEGPEATNAVTFDADDDSIIHL--LHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFN 634
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 635 VCIFAYGQTGAGKTYTMEGTAEN-PGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 712
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 713 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 790
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 791 SERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 869
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 2462548931 870 YSLKFAERVR 879
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
558-881 |
4.61e-105 |
|
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: 329.81 E-value: 4.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVT-KEDGEGpeATNAVTFDADDDSIIhlLHKGK------PVSFELDKVFSPQASQQDVFQE-VQALVTSC 629
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 630 IDGFNVCIFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEK 706
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 707 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 782
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 783 LNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 861
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 2462548931 862 EKNTSETLYSLKFAERVRSV 881
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
559-882 |
3.32e-103 |
|
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: 325.05 E-value: 3.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 559 IRVIARVRPVT-KEDGEGPEatNAVTFDADDDSIIhllhKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 636
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 637 IFAYGQTGAGKTYTMEGTA------ENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIR 710
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 711 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 780
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 781 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 857
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 2462548931 858 VSPVEKNTSETLYSLKFAERVRSVE 882
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
558-881 |
7.71e-94 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 300.42 E-value: 7.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDADDDSIIHLL----------HKGKPVSFELDKVFSPQASQQDVFQ 620
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 621 E-VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLL 699
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 700 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 778
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 779 --TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 853
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 2462548931 854 MVVQVSPVEKNTSETLYSLKFAERVRSV 881
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
558-881 |
4.05e-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: 4.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVTKEDgegPEATNAVTFDADDDSIIHllHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFNVC 636
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 637 IFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkASDWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 716
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 717 GQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 792
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 793 RVGKSGAEGSRLREAQHINKSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 870
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 2462548931 871 SLKFAERVRSV 881
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
558-881 |
1.23e-91 |
|
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: 1.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVTKEDGEGPeatNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 636
Cdd:cd01369 3 NIKVVCRFRPLNELEVLQG---SKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFaAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 637 IFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGkepQEKLEIRLCP 713
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 714 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSER 793
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 794 VGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSL 872
Cdd:cd01369 237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316
|
....*....
gi 2462548931 873 KFAERVRSV 881
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
558-881 |
5.95e-88 |
|
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: 284.99 E-value: 5.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVTKEDgegPEATNAVTFDADDDS----IIHLLHKGKPV--SFELDKVFSPQASQQDVFQEVQA-LVTSCI 630
Cdd:cd01364 3 NIQVVVRCRPFNLRE---RKASSHSVVEVDPVRkevsVRTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 631 DGFNVCIFAYGQTGAGKTYTMEG--------TAENP---GINQRALQLLFSEVQEkaSDWEYTITVSAAEIYNEVLRDLL 699
Cdd:cd01364 80 MGYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDplaGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 700 GKEPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG- 776
Cdd:cd01364 158 SPSSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 777 --LRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLM 854
Cdd:cd01364 238 eeLVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340
....*....|....*....|....*..
gi 2462548931 855 VVQVSPVEKNTSETLYSLKFAERVRSV 881
Cdd:cd01364 318 IATISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
557-881 |
1.50e-86 |
|
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: 281.55 E-value: 1.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 557 GNIRVIARVRPVTK-EDGEGpeATNAVTFDADDDSIIHL--------LHKGKPVSFELDKVF-------SPQASQQDVFQ 620
Cdd:cd01365 1 ANVKVAVRVRPFNSrEKERN--SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 621 EVQA-LVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASD-WEYTITVSAAEIYNEVLRDL 698
Cdd:cd01365 79 DLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 699 LGKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHAL--LIVTVRGVDC 773
Cdd:cd01365 159 LNPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 774 STGLRT--TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQ 843
Cdd:cd01365 237 ETNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLK 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462548931 844 DSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 881
Cdd:cd01365 317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
542-882 |
4.83e-82 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 276.23 E-value: 4.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 542 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE 621
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 622 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 700
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 701 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 780
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 781 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 858
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 2462548931 859 SPVEKNTSETLYSLKFAERVRSVE 882
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
558-879 |
1.19e-77 |
|
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: 257.05 E-value: 1.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVTKEDGEGpEATNAVTFDADDDSIihlLHKGKPVSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVC 636
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 637 IFAYGQTGAGKTYTMEGTAENP--------GINQRALQLLFSEVQ---EKASD-WEYTITVSAAEIYNEVLRDLLgkEP- 703
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 704 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 780
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 781 gKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 856
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 2462548931 857 QVSPVEKNTSETLYSLKFAERVR 879
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
559-876 |
1.31e-77 |
|
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: 256.94 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 559 IRVIARVRPVTKEDGEGPEA-------TNAVTFDADDDSIIHLLHKG---KPVSFELDKVFSPQASQQDVFQEV-QALVT 627
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 628 SCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkasdweYTITVSAAEIYNEVLRDLL----GKEP 703
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 704 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 778
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 779 ---TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 850
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 2462548931 851 KTLMVVQVSPVEKNTSETLYSLKFAE 876
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
559-879 |
9.65e-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: 243.26 E-value: 9.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 559 IRVIARVRPVTKEDGEGpeatnaVTFDADDDSI-IHLL---------HKGKPVSFELDKVFSpQASQQDVFQEV-QALVT 627
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLH-NASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 628 SCIDGFNVCIFAYGQTGAGKTYTMEGTAEN---PGINQRALQLLFSEVQEKASDwEYTITVSAAEIYNEVLRDLLGKEPQ 704
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 705 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 779
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 780 TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 858
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 2462548931 859 SPVEKNTSETLYSLKFAERVR 879
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
558-879 |
1.60e-71 |
|
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: 239.33 E-value: 1.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVtkEDGEGPEATNAVTFDADDDSII--HLLHKGKPVSFELDKVFSPQASQQDVF-QEVQALVTSCIDGFN 634
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 635 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKAsdWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 714
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 715 GSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 793
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 794 VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 873
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 2462548931 874 FAERVR 879
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
558-878 |
1.43e-66 |
|
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: 226.02 E-value: 1.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 558 NIRVIARVRPVTKEDgEGPEATNAVTFDADDDSIIH-------LLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSC 629
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 630 IDGFNVCIFAYGQTGAGKTYTMEG----TAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLgkepQE 705
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 706 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 785
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 786 VDLAGSER-VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 863
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 2462548931 864 NTSETLYSLKFAERV 878
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
559-882 |
5.57e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 214.41 E-value: 5.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 559 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVCI 637
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 638 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLgkE 702
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL--D 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 703 P-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT 779
Cdd:PLN03188 248 PsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 780 --TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKT 852
Cdd:PLN03188 326 fkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350
....*....|....*....|....*....|
gi 2462548931 853 LMVVQVSPVEKNTSETLYSLKFAERVRSVE 882
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
538-699 |
4.41e-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: 4.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 538 YRRELQLRKKCHNELVRLKGNIRVIARVRPvtkedgegpEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQD 617
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRP---------ELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 618 VFQEVQALVTSCIDGFNVCIFAYGQTGAGktytmegtaENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRD 697
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 2462548931 698 LL 699
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
606-825 |
2.23e-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: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 606 DKVFSPQASQQDVFQEVQALVTSCIDGFNV-CIFAYGQTGAGKTYTMEgtaenpGINQRALQLLFSEVQEKASDWEYTIT 684
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 685 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfghTNRTTEfTNLNEHSSRSHALL 764
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 765 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegsrlreaqhINKSLSALGDVIAALR 825
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-527 |
6.80e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 189 QLQEELVVLQ-ERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCE 267
Cdd:COG1196 217 ELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 268 AELQELRTkpagpcpGCEHSQE-SAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERL 346
Cdd:COG1196 295 AELARLEQ-------DIARLEErRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 347 SRRLRDSHETIaslraqsppvkyviktvevessktkQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQ 426
Cdd:COG1196 368 LEAEAELAEAE-------------------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 427 IAMYESELERAHGQMLEEMQSLEEDKNRA--IEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 504
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340
....*....|....*....|...
gi 2462548931 505 FPLLLQEALRSVKAEIGQAIEEV 527
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
147-502 |
2.38e-15 |
|
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: 80.88 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 147 VENTGGRLFGSRRCSSLSG-PPGAAPMVLRMVEAMSQLQDEKTQLQEELVVLQERL-ALRD--SDQQATSTQLQNQVEHL 222
Cdd:TIGR02169 649 FEKSGAMTGGSRAPRGGILfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdELSQelSDASRKIGEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 223 KEKLISQAQEVSRLRSELggtdlekhrDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQL 302
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDL---------SSLEQEIENVKSELKELEARIEELEEDLH------KLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 303 EmaESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESS 379
Cdd:TIGR02169 794 P--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 380 KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQS---------SHQLTARLRAQIAMYE-SELERAHGQMLE------ 443
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqiekkrKRLSELKAKLEALEEElSEIEDPKGEDEEipeeel 951
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462548931 444 --------------EMQSLEEDKNRAIE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 502
Cdd:TIGR02169 952 sledvqaelqrveeEIRALEPVNMLAIQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-526 |
1.62e-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: 75.09 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 214 QLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQL 293
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 294 RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLS----------RRLRDSHETIASLRAQ 363
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltllnEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 364 sppVKYVIKTVEvESSKTKQALSESQARNQHLQEQvamQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErahgQMLE 443
Cdd:TIGR02168 833 ---IAATERRLE-DLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELE----ELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 444 EMQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND-YNGLKRQVRGFPLLLQEALRSVKaEIGQ 522
Cdd:TIGR02168 902 ELRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLK-RLEN 979
|
....
gi 2462548931 523 AIEE 526
Cdd:TIGR02168 980 KIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-439 |
3.70e-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: 73.94 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 173 VLRMVEA---MSQLQDEKTQLQEELVVLQERLALRDSDQQAT---STQLQNQVEHLKEKLISQAQEVSRlrselggtdLE 246
Cdd:TIGR02168 231 VLRLEELreeLEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISR---------LE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 247 KHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 326
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLD------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 327 EVE---LRLKDCLAEKAQEE--------------ERLSRRLRDSHETIASLRAQSPPVKyvIKTVEVESSKTKQALSESQ 389
Cdd:TIGR02168 376 ELEeqlETLRSKVAQLELQIaslnneierlearlERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462548931 390 ARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHG 439
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-466 |
4.75e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 182 QLQDEKTQLQEELVVLQERLALRDSDQQ---ATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENER 258
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 259 LRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 338
Cdd:COG1196 314 LEERLEELEEELAELE-------------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 339 KAQEEERLSRRLRDSHETIASLRAQsppvKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQ 418
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462548931 419 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 466
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
215-542 |
5.67e-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: 73.17 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 215 LQNQVEHLKEKlISQAQEVSRLRSELGgtdlEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaqlr 294
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE-------------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 295 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA---QEEERLSRRLRDSHETIASLRAQsppvkyvI 371
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQ-------L 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 372 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT--------------ARLRAQIAMYESELER- 436
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERl 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 437 -AHGQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRS 515
Cdd:TIGR02168 406 eARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDA 479
|
330 340
....*....|....*....|....*....
gi 2462548931 516 VKAEIGQAIEEVNS--NNQELLRKYRREL 542
Cdd:TIGR02168 480 AERELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
197-450 |
1.59e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.59 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 197 LQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMvenerlrQEMRRCEAELQELRTk 276
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-------QQLSELESQLAEARA- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 277 pagpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 354
Cdd:COG3206 234 ------------ELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 355 ETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSshqlTARLRAQIAMYESE 433
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLERE 359
|
250
....*....|....*..
gi 2462548931 434 LERAHGQMLEEMQSLEE 450
Cdd:COG3206 360 VEVARELYESLLQRLEE 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-464 |
2.04e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQ---ERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 254
Cdd:COG1196 246 AELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 255 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELN---LEVQQKTDRLAEVELR 331
Cdd:COG1196 324 ELAELEEELEELEEELEELE-------------EELEEAEEELEEAEAELAEAEEALLEAEaelAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 332 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQ 411
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462548931 412 QLQSSHQLTARLRAQIAMYESELERAHGQ--MLEEMQSLEEDKNRAIEEAFARAQ 464
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-540 |
7.62e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 183 LQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLMVENERL 259
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDLG--NAEDFLEELREERDEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 260 RQEMRRCEAELQELRTK--------PAGPCPGC-------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDr 324
Cdd:PRK02224 425 REREAELEATLRTARERveeaeallEAGKCPECgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 325 LAEVELRLKDcLAEKAqeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQ 404
Cdd:PRK02224 504 LVEAEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 405 VLKEMEQQLQSSHQLTARLrAQIAMYESELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENL 474
Cdd:PRK02224 580 KLAELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDK 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 475 AGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 540
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-559 |
8.31e-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: 66.23 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 260 RQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELRLkdclAEK 339
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL----ARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 340 AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQL 419
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 420 TARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK 499
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 500 RQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 559
Cdd:TIGR02168 887 EAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
540-824 |
1.04e-10 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 65.53 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 540 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDADDDSIihllhKGKPV------------SFELDK 607
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 608 VFSPQASQQDVFQEVQALVTSCIDGfnvcIFAYGQTGAGKTYTMEgtAENPGINQRALQLLFSEVQ-EKASDWEYTITVS 686
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 687 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvddinkvfEFGHTNRTTEFTNLNEHSSRS 760
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--------EKASKLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548931 761 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGSRLREAQHINKSLSALGDVIAAL 824
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-537 |
2.63e-10 |
|
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: 64.70 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 181 SQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLR 260
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL--EKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 261 QEMRRCEAELQELRtkpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdclaeka 340
Cdd:TIGR02169 272 QLLEELNKKIKDLG------------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI-------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 341 qeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT 420
Cdd:TIGR02169 332 ---DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 421 ARLRAQIAMYESELERAHgqmlEEMQSLEEDKNrAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR 500
Cdd:TIGR02169 409 DRLQEELQRLSEELADLN----AAIAGIEAKIN-ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350
....*....|....*....|....*....|....*....
gi 2462548931 501 QVRGfpllLQEALRSVKAEIGQAIEEVNSN--NQELLRK 537
Cdd:TIGR02169 484 ELSK----LQRELAEAEAQARASEERVRGGraVEEVLKA 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-534 |
6.25e-10 |
|
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: 63.21 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERL--ALRDSDQ-QATSTQLQNQVE------HLKEKLISQAQEVS-RLRSELGGTDLEK 247
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELteARTERDQfSQESGNLDDQLQklladlHKREKELSLEKEQNkRLWDRDTGNSITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 248 hrDLLMVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESA-----QLRDKLSQLQLEMAESKGMLSELNLEVQQKT 322
Cdd:pfam15921 415 --DHLRRELDDRNMEVQRLEALLKAMKSE----CQGQMERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 323 DRLAEVELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQARNQHLQEQVAM 401
Cdd:pfam15921 489 MTLESSERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 402 QRQVLKEMEQQLQSSHQLTA---RLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH--- 471
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvn 639
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548931 472 ---ENLAGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 534
Cdd:pfam15921 640 agsERLRAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-560 |
2.32e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 176 MVEAMSQLQDEKTQLQEELVVLQERLALRDsdqqaTSTQLQNQVEHLKEKLisQAQEVSRLRSELggTDLEKHRDLLMVE 255
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYE-----EAKAKKEELERLKKRL--TGLTPEKLEKEL--EELEKAKEEIEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 256 NERLRQEMRRCEAELQELRT------KPAGPCPGC------EH---------------SQESAQLRDKLSQLQLEMAESK 308
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKaieelkKAKGKCPVCgrelteEHrkelleeytaelkriEKELKEIEEKERKLRKELRELE 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 309 GMLSELNLEVQQKT--DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIASLRAQsppvkyvIKTVEVESSKTKQALS 386
Cdd:PRK03918 487 KVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIKLKGE-------IKSLKKELEKLEELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 387 ESQARNQHLQEQVAMQRQVLKEMEQQ-LQSSHQLTARLRaqiamyesELERAHGQMLEEMQSleEDKNRAIEEAFARAQV 465
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELgFESVEELEERLK--------ELEPFYNEYLELKDA--EKELEREEKELKKLEE 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 466 EMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVKAEIGQA---IEEVNSNNQEL------L 535
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELekrREEIKKTLEKLkeeleeR 706
|
410 420
....*....|....*....|....*
gi 2462548931 536 RKYRRELQLRKKCHNELVRLKGNIR 560
Cdd:PRK03918 707 EKAKKELEKLEKALERVEELREKVK 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
180-564 |
3.14e-09 |
|
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: 60.90 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 180 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQ-----------AQEVSRLRSELggtdLEKH 248
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQnsmymrqlsdlESTVSQLRSEL----REAK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 249 RdllMVEN--ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKgmlSELNLEVQQKT---- 322
Cdd:pfam15921 338 R---MYEDkiEELEKQLVLANSELTEARTERD------QFSQESGNLDDQLQKLLADLHKRE---KELSLEKEQNKrlwd 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 323 -----------------DRLAEVElRLKDCL-AEKAQEEERLSRRL------RDSHETIASLRAQSPPVKYVIKTVEVES 378
Cdd:pfam15921 406 rdtgnsitidhlrreldDRNMEVQ-RLEALLkAMKSECQGQMERQMaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 379 SKTKQALSESQARNQHLQEQvamqrqvLKEMEQQLQSSHQLTARLRAQIAMYESELE--RAHGQMLEEMQSLEE------ 450
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTAS-------LQEKERAIEATNAEITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEalklqm 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 451 -DKNRAIEeaFARAQVE----MKAVHENLAGvrtnllTLQPALRTLTNDYNGLKRQVRGFPLLLQE---ALRSVKAEIG- 521
Cdd:pfam15921 558 aEKDKVIE--ILRQQIEnmtqLVGQHGRTAG------AMQVEKAQLEKEINDRRLELQEFKILKDKkdaKIRELEARVSd 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462548931 522 ---QAIEEVNSNNQEL--LRKYRRE----LQLRKKCHNELVRLKGNIRVIAR 564
Cdd:pfam15921 630 lelEKVKLVNAGSERLraVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKR 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-363 |
6.71e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQE-RLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVEN 256
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL--DALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 --------ERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEV 328
Cdd:COG4913 333 rgnggdrlEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|....*
gi 2462548931 329 ELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ 363
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-547 |
3.79e-08 |
|
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: 57.34 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 181 SQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENE 257
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 258 RLRQemrrceaelqelrtkpagpcpgcehsQEsaqlrDKLSQLQLEMAESKGMLSELNLEVQQktdrlaevelrLKDCLA 337
Cdd:TIGR04523 315 ELKN--------------------------QE-----KKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 338 EKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQssh 417
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 418 qltaRLRAQIAMYESELERahgqMLEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 494
Cdd:TIGR04523 430 ----RLKETIIKNNSEIKD----LTNQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462548931 495 YNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKyrrELQLRKK 547
Cdd:TIGR04523 498 LKKLNEEKK----ELEEKVKDLTKKISSLKEKIEKLESEKKEK---ESKISDL 543
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
179-526 |
4.37e-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: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 179 AMSQLQDEKTQLQEELVVLqeRLALRDS-----DQQATSTQLQNQVEHLKEKL---------------ISQAQEVSRLRS 238
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEAL--KTELEDTldttaAQQELRSKREQEVTELKKALeeetrsheaqlqemrQKHTQALEELTE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 239 EL-----GGTDLEKHRDLLMVENERLRQEMR--------------RCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQ 299
Cdd:pfam01576 364 QLeqakrNKANLEKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQARLS------ESERQRAELAEKLSK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 300 LQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSPPVKYVIKTVE 375
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 376 VESSKTKQALSESQARnqhlQEQVAMQRQVLKEMEQQLQS-SHQLTARLRAQIAMYEsELERAHGQMLEEMQSL--EEDK 452
Cdd:pfam01576 517 RQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQReLEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDH 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 453 NRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALR 514
Cdd:pfam01576 592 QRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQLRAEM-EDLV 670
|
410
....*....|..
gi 2462548931 515 SVKAEIGQAIEE 526
Cdd:pfam01576 671 SSKDDVGKNVHE 682
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-470 |
4.44e-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: 56.31 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 255 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 334
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 335 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPP---------VKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 400
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 401 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 470
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
169-543 |
6.80e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 169 AAPMVLRMVEAMSQlQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKH 248
Cdd:PRK04863 333 ASDHLNLVQTALRQ-QEKIERYQADLEELEERLE----EQNEVVEEADEQQEENEARAEAAEEEVDELKSQL--ADYQQA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 249 RDLLMVENERLRQEMRRCEaELQELRTKPAgpcpgcehsqesaqlrdklsqlqLEMAESKGMLSELNLEVQQKTDRLAEV 328
Cdd:PRK04863 406 LDVQQTRAIQYQQAVQALE-RAKQLCGLPD-----------------------LTADNAEDWLEEFQAKEQEATEELLSL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 329 ELRLKDCLAEKAQEEE--RLSRRLRDshetiaslraqsppvkyviktvEVESSKTKQALSE--SQARNQ-HLQEQVAMQR 403
Cdd:PRK04863 462 EQKLSVAQAAHSQFEQayQLVRKIAG----------------------EVSRSEAWDVAREllRRLREQrHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 404 QVLKEMEQQLQSSHQLTARLR----AQIAMY--ESELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLA 475
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLAefckRLGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 476 GVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 543
Cdd:PRK04863 600 ARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-527 |
9.83e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 253 MVEN----ERLRQEMRRCEAELQELRtkpagpcPGCEHSQESAQLRDKLSQLQLemaeskgMLSELNLEVQQKTDRLAEV 328
Cdd:COG4913 230 LVEHfddlERAHEALEDAREQIELLE-------PIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 329 EL-RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqALSESQARNQHLQEQVAMQRQVLK 407
Cdd:COG4913 296 ELeELRAELARLEAELERLEARLDALREELDELEAQ--------------------IRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 408 EMEQQLQSSHQLTARLRAQIAMYESELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 487
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462548931 488 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 527
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
180-556 |
1.02e-07 |
|
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: 55.85 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 180 MSQLQDEKTQLQEELVVLQERLALRDSDQQATS------TQLQNQVEHLKEKL--ISQAQEVSRLRSElggtDLEKHRDL 251
Cdd:pfam05622 23 VSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 252 LMVENERLR---QEMRRCEAELQELRtkpagpcpgcehsqESAqlrDKLSQLQLEMAESKGMLSELN-LEVQQKTdrlae 327
Cdd:pfam05622 99 LQHRNEELTslaEEAQALKDEMDILR--------------ESS---DKVKKLEATVETYKKKLEDLGdLRRQVKL----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 328 velrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSE---SQARNQHLQ---EQVAM 401
Cdd:pfam05622 157 ----LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQkekERLII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 402 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEedknraIEEAFARAQVEMKAVHENLAGvrtNL 481
Cdd:pfam05622 233 ERDTLRETNEELRCAQLQQAELSQADALLSPSSD-PGDNLAAEIMPAE------IREKLIRLQHENKMLRLGQEG---SY 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462548931 482 LTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRsvkaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 556
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNRLANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
177-557 |
1.64e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 177 VEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEK------LISQAQEVSRLR---------SELG 241
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKVKELKELKekaeeyiklSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 242 GTDLEKHRDlLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNlEVQQK 321
Cdd:PRK03918 303 EEYLDELRE-IEKRLSRLEEEINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELYE-EAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 322 TDRLAEVELRLKDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTV-----EVESSKTKQALSESQARNQHL 395
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELkkaieELKKAKGKCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 396 QEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELER-----AHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 470
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 471 HENLAGVRTNLLTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHN 550
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
....*..
gi 2462548931 551 ELVRLKG 557
Cdd:PRK03918 603 EYLELKD 609
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-437 |
1.72e-07 |
|
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: 54.38 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenE 257
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQEL----------------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 258 RLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQlQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdcLA 337
Cdd:COG4942 80 ALEAELAELEKEIAELR-------------AELEAQKEELAE-LLRALYRLGRQPPLALLLSPEDFLDAVRRLQY---LK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 338 EKAQEEERLSRRLRDSHETIASLRAQsppvkyviktVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSH 417
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAE----------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|
gi 2462548931 418 QLTARLRAQIAMYESELERA 437
Cdd:COG4942 213 AELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
124-349 |
1.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 124 LWKRQAPAPRRAREAREAGGTMNVENTGGRLFGSRRCSSLSGPPGAAPMVLRMVEAMSQLQDEKTQLQEEL---VVLQER 200
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqleELEQEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 201 LALRDSDQQATSTQLQNQVEHlKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagp 280
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE------ 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548931 281 cpgcehsQESAQLRDKLSQL--QLEMAESKGMLSELNLEVQQKTDRLAEVE-----LRLKDCLAEKAQEEERLSRR 349
Cdd:COG4717 446 -------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAeewaaLKLALELLEEAREEYREERL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-564 |
1.88e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 223 KEKLISQAQEVSRLRSELGGTDLEKHR--DLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaQLRDKLSQL 300
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELE-----------------ELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 301 QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEKAQEEERLSR-------RLRDSHETIASLRAQS 364
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 365 PPVKYVIKtvevESSKTKQALSESQARNQHLQEQVAmqrqVLKEMEQQLQSSHQLTA---RLRAQIAMYESE-------- 433
Cdd:PRK03918 324 NGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHELYEEAKAKKEeleRLKKRLTGLTPEklekelee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 434 LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----------------MKAVHENLAGVRTNLLTLQPA 487
Cdd:PRK03918 396 LEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548931 488 LRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 564
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-545 |
2.82e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 182 QLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQN-----QVEHLKEKLISQAQEVSRLRSELggtdleKHRDLLMVEN 256
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQEMRRCEAELQELRTKPAGpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdcl 336
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 337 aEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQARNQHLQEQVA 400
Cdd:COG4717 237 -EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 401 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEmkavheNLAGVRt 479
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVE------DEEELR- 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 480 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 545
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-556 |
3.76e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 324 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQR 403
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 404 QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 481
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462548931 482 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 556
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-547 |
4.89e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLAL---RDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLMV 254
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 255 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE---LR 331
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEE------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeeeEA 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 332 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARnqHLQEQVAMQRQVLKEMEQ 411
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 412 QL---------QSSHQLTARLRAQIAMYESE-LERAHGQMLEEMQ--SLEEDKNRAIEEAFARAQVEMKAVHENLAgVRT 479
Cdd:COG1196 539 ALeaalaaalqNIVVEDDEVAAAAIEYLKAAkAGRATFLPLDKIRarAALAAALARGAIGAAVDLVASDLREADAR-YYV 617
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548931 480 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 547
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
181-560 |
1.71e-06 |
|
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: 52.15 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 181 SQLQDEKTQLQEELVVLQERLA---LRDSDQQATSTQLQNQ------VEHLKEKLISQAQEVSRLRSELggTDLEKHRDl 251
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGelkLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSEL--RQARKRRD- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 252 lmVENERLRQEMRRCE---AELQELRTKpAGPCPGCEH---SQESAQLRDKLSQL-QLEMAESKGMLSELNLEVQQKTDR 324
Cdd:pfam12128 503 --QASEALRQASRRLEerqSALDELELQ-LFPQAGTLLhflRKEAPDWEQSIGKViSPELLHRTDLDPEVWDGSVGGELN 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 325 LAEVELRLKDCLA-EKAQEEERLSRR-------LRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQAR----- 391
Cdd:pfam12128 580 LYGVKLDLKRIDVpEWAASEEELRERldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlf 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 392 NQHLQEQVAMQRQV---LKEMEQQLQS-SHQLTARLRAQIAMYES---ELERAHGQMLEEMQSLEEDKNRA---IEEAFA 461
Cdd:pfam12128 660 DEKQSEKDKKNKALaerKDSANERLNSlEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVVEGALDAQlalLKAAIA 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 462 RAQVEMKA--------VHENLAGV---RTNLLTLQPALRTLT---NDYNGLKRQVRGFPLLLQE-------ALRSVKAEI 520
Cdd:pfam12128 740 ARRSGAKAelkaletwYKRDLASLgvdPDVIAKLKREIRTLErkiERIAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNI 819
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462548931 521 GQAIEEVNSNNQELLRKYRRELQL----RKKCHNELVRLKGNIR 560
Cdd:pfam12128 820 ERAISELQQQLARLIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-366 |
2.44e-06 |
|
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: 50.92 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLIS--QAQEVSRLRSELGGTDLEKH-RDLLMV 254
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAvRRLQYL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 255 E--NERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRL 332
Cdd:COG4942 142 KylAPARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|....
gi 2462548931 333 KDCLAEKAQEEERLSRRLRDSHETIASLRAQSPP 366
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
178-544 |
2.63e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQ---NQVEHLKEKLISQAQEVSRLRS--ELGGTDLEKH---- 248
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAahSFVVTEFEATtcsl 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 249 RDLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELN--LEVQQKTDRLA 326
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKK----------SSELEEMTKFKNNKEVELEELKKILAEDEklLDEKKQFEKIA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 327 EvELrlkdclaeKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKtvEVESSKTKqaLSESQARNQHLQEQVAMqr 403
Cdd:pfam05483 432 E-EL--------KGKEQELiflLQAREKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTE--LEKEKLKNIELTAHCDK-- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 404 qVLKEMEQQLQSSHQLTARLRAQ---IAMYESELERahgqMLEEMQSLEE------DKNRAIEEAFARAQVEMKA----V 470
Cdd:pfam05483 497 -LLLENKELTQEASDMTLELKKHqedIINCKKQEER----MLKQIENLEEkemnlrDELESVREEFIQKGDEVKCkldkS 571
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462548931 471 HENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 544
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
291-568 |
2.76e-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: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 291 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyv 370
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 371 iktvevessktKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEE 450
Cdd:COG4913 677 -----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 451 DKNRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAI 524
Cdd:COG4913 746 ELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYL 818
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 525 EEVNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 568
Cdd:COG4913 819 ALLDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-540 |
4.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 173 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRdSDQQATSTQLQNQVEHLKEKLiSQAQEVSRLRSELGGTDLEKHRDLL 252
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEEL-EELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 253 MVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESAQLRDKLSQLQLeMAESKGMLSELNLEVQQKTDRLAEVELRL 332
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEE----LEQLENELEAAALEERLKEARL-LLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 333 KDCLA---------EKAQEEERLSRRLRDSHETIASLRAQSppVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQR 403
Cdd:COG4717 280 FLVLGllallflllAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 404 QVLKEMEQQlQSSHQLTARLRAQIAMYESELERAHGQmLEEMQSLEEDKNRAIEE-AFARAQVEMKAVHENLAGVRTNLL 482
Cdd:COG4717 358 ELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELE 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548931 483 TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVK-AEIGQAIEEVNSNNQELLRKYRR 540
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAA 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
181-458 |
6.01e-06 |
|
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: 50.50 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 181 SQLQDEKTQLQ---EELVVlqERLALRDSDQqaTSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrDLLMVENE 257
Cdd:pfam15921 468 AQLESTKEMLRkvvEELTA--KKMTLESSER--TVSDLTASLQEKERAIEATNAEITKLRSRV---------DLKLQELQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 258 RLRQE---MRRCEAELQELRTKPAGPCPGCE---------------HSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQ 319
Cdd:pfam15921 535 HLKNEgdhLRNVQTECEALKLQMAEKDKVIEilrqqienmtqlvgqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 320 QKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLRAQSPPVK--YVIKTVEVESSK 380
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKrnFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 381 TKQALSESQArnqhlQEQVAMQRQVLKEMEQQ--------LQSSHQLTARlRAQIAMYESE---LERAHGQMLEEMQSLE 449
Cdd:pfam15921 695 NKLKMQLKSA-----QSELEQTRNTLKSMEGSdghamkvaMGMQKQITAK-RGQIDALQSKiqfLEEAMTNANKEKHFLK 768
|
....*....
gi 2462548931 450 EDKNRAIEE 458
Cdd:pfam15921 769 EEKNKLSQE 777
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
243-364 |
6.01e-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: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 243 TDLEKHRDLLMVENERLRQEMRRC--------------EAELQELR--TKPAGPCPgcehSQESAQLRDKLSQLQLEMAE 306
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLnsikpklrdrkdalEEELRQLKqlEDELEDCD----PTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548931 307 SKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 364
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
176-554 |
6.61e-06 |
|
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: 50.21 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 176 MVEAMSQLQDEKTQLQEELVVLQERLALRdSDQQATSTQlqnQVEHLKEKLISQAQEVSRLRSELggtdlekhrDLLMVE 255
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETL-TNQNSDCKQ---HIEVLKESLTAKEQRAAILQTEV---------DALRLR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 256 NERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRD--------KLSQLQLEMAESKGMLSELNLEVQQ-KTDR-- 324
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKErkinvlqkKIENLQEQLRDKDKQLAGLKERVKSlQTDSsn 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 325 ----LAEVElrlkDCLAEKAQEEERL----SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQ 396
Cdd:pfam10174 434 tdtaLTTLE----EALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 397 EQVAMQRQVLKEMEQQLQSSHQLTARLRAQI--AMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMkavhENL 474
Cdd:pfam10174 510 SSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEES-GKAQAEV----ERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 475 AGvrtnlltlqpALRTLTNDYNGLKRQVRGFPLLlqeALRSVKaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 554
Cdd:pfam10174 585 LG----------ILREVENEKNDKDKKIAELESL---TLRQMK-EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-458 |
7.31e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 174 LRMVEAMSQLQDEKTQLQEELVVLQERLALRDSdQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGG--TDLEKHRDL 251
Cdd:PLN02939 152 LQALEDLEKILTEKEALQGKINILEMRLSETDA-RIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLcvHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 252 LMVENERLRQEMRRCEAELQELrtkpagpcpgcehsqesAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELR 331
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEV-----------------AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 332 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEvESSKTKQALSESqarnqhlQEQVAMQRQVLKEMEQ 411
Cdd:PLN02939 294 QYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE-ASLKEANVSKFS-------SYKVELLQQKLKLLEE 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462548931 412 QLQSSHQltaRLRAQIAMYESELERAHgqmlEEMQSL-EEDKNRAIEE 458
Cdd:PLN02939 366 RLQASDH---EIHSYIQLYQESIKEFQ----DTLSKLkEESKKRSLEH 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-463 |
1.00e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 173 VLRMVEAMSQLQDEKTQLQEELVVLQERLAL---RDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHR 249
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL--LEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 250 DLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 329
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQ----------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 330 LRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEm 409
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAA------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA- 517
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462548931 410 eqQLQSSHQLTARLRAQIAMYESELE-RAHGQMLEEMQSLEEDKNRAIEEAFARA 463
Cdd:COG1196 518 --GLRGLAGAVAVLIGVEAAYEAALEaALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
171-466 |
1.02e-05 |
|
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: 49.35 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 171 PMVLRMVEAMSQlQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHL--KEKLISQAQEVSRLRSelggtdlekh 248
Cdd:pfam17380 227 PHTLAPYEKMER-RKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIvqHQKAVSERQQQEKFEK---------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 249 rdllmVENERLRQEMRRCEAELQELRTkpagpcpgCEHSQESAQLR-DKLSQLQLEMaESKGMLSELNLEVQQKTDRLAE 327
Cdd:pfam17380 296 -----MEQERLRQEKEEKAREVERRRK--------LEEAEKARQAEmDRQAAIYAEQ-ERMAMERERELERIRQEERKRE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 328 VELRLKDCLA---EKAQEEERL-------SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARN-QHLQ 396
Cdd:pfam17380 362 LERIRQEEIAmeiSRMRELERLqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLE 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548931 397 EQVA--MQRQVLKEMEQQLQSS---HQLTARLRAQIAMYESELERAHGQMLEEM---QSLEEDKNRAIEEAFARAQVE 466
Cdd:pfam17380 442 EERAreMERVRLEEQERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
291-545 |
1.78e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 291 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYV 370
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 371 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQsleE 450
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE---A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 451 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSN 530
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*
gi 2462548931 531 NQELLRKYRRELQLR 545
Cdd:COG4372 260 IEELELAILVEKDTE 274
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
223-422 |
1.88e-05 |
|
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: 47.83 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 223 KEKLISQAQEVSRLRSELGGT-------DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpagpcpgcEHSQESAQLRD 295
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEA---------QQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 296 KLSQLQLEMAESKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 375
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 376 VESSKTKQALSESQARNQHLQEQVAMQRQV----LKEMEQQLQSSHQLTAR 422
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQGEGSN 216
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
186-541 |
2.85e-05 |
|
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: 47.82 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 186 EKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLE---KHRDLLMVENERLRQE 262
Cdd:pfam07111 243 ERQELLDTMQHLQEDRA----DLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkKCRSLLNRWREKVFAL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 263 MRRCEAelQELrtkpagpcpgcEHSQESAQLRDKLSQLQ-------------------------LEMAESKGMLSELNLE 317
Cdd:pfam07111 319 MVQLKA--QDL-----------EHRDSVKQLRGQVAELQeqvtsqsqeqailqralqdkaaeveVERMSAKGLQMELSRA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 318 VQ---QKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQH 394
Cdd:pfam07111 386 QEarrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 395 ---------LQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQiamyesELERAHGQMLEEMQSLEEDKNRaIEEAFARAQv 465
Cdd:pfam07111 466 cpppppappVDADLSLELEQLREERNRLDAELQLSAHLIQQ------EVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548931 466 emkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 541
Cdd:pfam07111 538 ------ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
174-545 |
3.44e-05 |
|
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: 48.02 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 174 LRMVEAMSQLQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLM 253
Cdd:COG3096 336 LNLVQTALRQQEKIERYQEDLEELTERLE----EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 254 VENERLRQEMRRCEaELQELrtkpagpcpgCEhsqesaqlrdkLSQLQLEMAEskGMLSELNLEVQQKTDRLAEVELRLK 333
Cdd:COG3096 410 TRAIQYQQAVQALE-KARAL----------CG-----------LPDLTPENAE--DYLAAFRAKEQQATEEVLELEQKLS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 334 DCLAEKAQEEERLsrrlrdshetiASLRAQSPPVkyvikTVEVESSKTKQALSesQARNQ-HLQEQVAMQRQVLKEMEQQ 412
Cdd:COG3096 466 VADAARRQFEKAY-----------ELVCKIAGEV-----ERSQAWQTARELLR--RYRSQqALAQRLQQLRAQLAELEQR 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 413 LQSSH-------QLTARLRAQIAMYEsELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNLLTLQ 485
Cdd:COG3096 528 LRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARA 601
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548931 486 PALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 545
Cdd:COG3096 602 PAWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
190-484 |
4.27e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 190 LQEELVVLQERLALRDSDQQATStqLQNQVEhlKEKLISQAQEVSRLRSELG-----GTDLEKHRDLLMVENERLR---- 260
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIK--LQKTIK--REKKLRETEEVEFSLKAEVliqkfGRSLKAKKRFSLLKKETIYlqsa 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 261 QEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAE-SKGMLSELNLEVQQKTDRLAEVE--LRLKDCLA 337
Cdd:COG5022 875 QRVELAERQLQELK----------IDVKSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKklLNNIDLEE 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 338 EKAQEEERLSRRLRDsHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV----AMQRQV--LKEMEQ 411
Cdd:COG5022 945 GPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPV 1023
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548931 412 QLQSSHQLTARLRA-----QIAMYESELERAHgqMLEEMQSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 484
Cdd:COG5022 1024 EVAELQSASKIISSestelSILKPLQKLKGLL--LLENNQLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
175-428 |
4.36e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 175 RMVEAMSQLQDEKTQLQEElvvlQERlALRDSDQQATSTQLQNQVEhlkeKLISQAQevSRLRSELGGTDLEKHRDLLMV 254
Cdd:PRK10929 110 EILQVSSQLLEKSRQAQQE----QDR-AREISDSLSQLPQQQTEAR----RQLNEIE--RRLQTLGTPNTPLAQAQLTAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 255 ENERLRQEMRRCEAELQELrtkpagpcpgcehsqeSAQLRDKLSQLQLEMAESK---------GMLSELNLEVQQKTDR- 324
Cdd:PRK10929 179 QAESAALKALVDELELAQL----------------SANNRQELARLRSELAKKRsqqldaylqALRNQLNSQRQREAERa 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 325 LAEVELrlkdcLAEKAQE-EERLSRRLRDSHETIASLRAQSppvkyviKTVEVESSKTKQALSESQarnqhlqeQVamqR 403
Cdd:PRK10929 243 LESTEL-----LAEQSGDlPKSIVAQFKINRELSQALNQQA-------QRMDLIASQQRQAASQTL--------QV---R 299
|
250 260
....*....|....*....|....*...
gi 2462548931 404 QVL---KEMEQQLQSSHQLTARLRAQIA 428
Cdd:PRK10929 300 QALntlREQSQWLGVSNALGEALRAQVA 327
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
261-554 |
4.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 261 QEMRRCEAELQELRTKPAgpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 338
Cdd:COG4717 71 KELKELEEELKEAEEKEE----------EYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 339 KAQEEERLsRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQARNQhlQEQVAMQRQVLKEMEQQLQSSHQ 418
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE------------------LEELEAELAELQ--EELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 419 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGL 498
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548931 499 KRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 554
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
180-481 |
4.86e-05 |
|
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: 47.12 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 180 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEK---LISQAQEVSRLRSELGGTDL----------E 246
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKdkqLAGLKERVKSLQTDSSNTDTalttleealsE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 247 KHRDLLMVENERLRQEMRRCEaELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 326
Cdd:pfam10174 448 KERIIERLKEQREREDRERLE-ELESLK-------------KENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 327 EVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAqSPPVKYVIKTVEVESSKTKQALSESQARNQHLQE---QVA 400
Cdd:pfam10174 514 KKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRIRLLEQEVARYKEESGKAQAEVERLLGilrEVE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 401 MQR----QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-----IEE---AFARAQVEMK 468
Cdd:pfam10174 593 NEKndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNsqqlqLEElmgALEKTRQELD 672
|
330
....*....|...
gi 2462548931 469 AVHENLAGVRTNL 481
Cdd:pfam10174 673 ATKARLSSTQQSL 685
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
337-545 |
4.91e-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: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 337 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALsesqarnqhLQEQVAMQRQVLKEMEQQLQSS 416
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 417 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 482
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548931 483 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 545
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-528 |
5.92e-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: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ--LEMAESKGMLSELNLEVQQKTDRLAEVEL---- 330
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE------ALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 331 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQARNQHLQEQV--AM 401
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 402 QRQVLKEMEQQLQSShqlTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 481
Cdd:COG4913 760 GDAVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462548931 482 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 528
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
181-459 |
6.19e-05 |
|
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: 46.61 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 181 SQLQDEKTQLQEelvvLQERLalrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSElggtdlekhRDLLMVENERLR 260
Cdd:pfam05622 183 GQLETYKRQVQE----LHGKL----SEESKKADKLEFEYKKLEEKLEALQKEKERLIIE---------RDTLRETNEELR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 261 qemrrCeAELQELRTKPAGPCPGCEHSQE--------SAQLRDKLSQLQLEmaesKGMLSELnlEVQQKTDRLAEVELRL 332
Cdd:pfam05622 246 -----C-AQLQQAELSQADALLSPSSDPGdnlaaeimPAEIREKLIRLQHE----NKMLRLG--QEGSYRERLTELQQLL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 333 KDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVESSKT------KQALSESQARNQHLQEQVAMQRQVL 406
Cdd:pfam05622 314 ED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHEAQSELQKKKEQI 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462548931 407 KEMEQQLQSSHQLTArlraqiamyeSELERAHGQMLEEMQSLEEDKNRAIEEA 459
Cdd:pfam05622 387 EELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
189-502 |
6.82e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 189 QLQEELVVLQERLALRDSDQQatstQLQNQVEHLKEKLISQA------------QEVSRLRSELGgTDLEKHRDllmvEN 256
Cdd:PRK04863 790 QLRAEREELAERYATLSFDVQ----KLQRLHQAFSRFIGSHLavafeadpeaelRQLNRRRVELE-RALADHES----QE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQL-RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVElRLKDC 335
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALN----------RLLPRLNLLaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE-PIVSV 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 336 LAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE-------VESSKTKQALSES-QARNQHLQEQVAMQRQVLK 407
Cdd:PRK04863 930 LQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKNSDLNEKlRQRLEQAEQERTRAREQLR 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 408 EMEQQLQSSHQLTARLRAQIamyeseleRAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRT------- 479
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAEERARARRDELHARLSANRSrrnqlek 1081
|
330 340 350
....*....|....*....|....*....|
gi 2462548931 480 -------NLLTLQPALRTLTNDYNGLKRQV 502
Cdd:PRK04863 1082 qltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-551 |
6.93e-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: 46.96 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 287 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 364
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 365 PPVKYVIKTVEVESS-------KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERa 437
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 438 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 514
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462548931 515 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 551
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
178-449 |
7.14e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLALRD--SDQQATSTQLQNQVEHLKE--KLISQAQEVSRLR------SELGGTDLEK 247
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQllKQLRARIEELRAQEAVLEEtqERINRARKAAPLAahikavTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 248 HRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESaQLRDKLSQLQLEMAESKGMLSELN--LEVQQKTDRL 325
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI-HIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 326 AEVELRLKDCL----AEKAQEEERLSRRlRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQARNQHLQEqvam 401
Cdd:TIGR00618 392 TQKLQSLCKELdilqREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE---- 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462548931 402 QRQVLKEMEQQLQSSHQLTARlraqiamyESELERAHGQMLEEMQSLE 449
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEP 503
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
213-539 |
7.44e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 213 TQLQNQVEHLKEkLISQAQEVsrLRSELggTDLEK-HRDL-----------LMVENERLRQEMRRCEAELQELRTKPAgp 280
Cdd:PRK04778 208 AALEQIMEEIPE-LLKELQTE--LPDQL--QELKAgYRELveegyhldhldIEKEIQDLKEQIDENLALLEELDLDEA-- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 281 cpgcehSQESAQLRDKL----SQLQLEMAESKgmlselnlEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHET 356
Cdd:PRK04778 281 ------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 357 IASLRAQSPPVKYVIKTVEVesskTKQALSESQARNQHLQEQVAMQRQVLKEME-QQLQSSHQLtarlraqIAMYESELE 435
Cdd:PRK04778 347 LESVRQLEKQLESLEKQYDE----ITERIAEQEIAYSELQEELEEILKQLEEIEkEQEKLSEML-------QGLRKDELE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 436 rAHgQMLEEMQS-LEEDKnRAIE------------EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR-- 500
Cdd:PRK04778 416 -AR-EKLERYRNkLHEIK-RYLEksnlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEet 492
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462548931 501 -----QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRKYR 539
Cdd:PRK04778 493 eelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFREYD 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-553 |
1.16e-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: 46.17 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 181 SQLQDEKTQLQEELVV---LQERLALRDSDQQatstQLQNQVEHLKEKLISQAQEVSRLRS-----ELGGTDLEKHRDLL 252
Cdd:TIGR04523 391 SQINDLESKIQNQEKLnqqKDEQIKKLQQEKE----LLEKEIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 253 MVENERLRQEMRRCEAEL----QELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEV 328
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLeqkqKELKSK----------EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 329 ELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKE 408
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKEN----------------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 409 MEQQLQSSHQLTARLRAQIamyeSELERAHGQMLEEMQSLEEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQ 485
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKEL----EKAKKENEKLSSIIKNIKSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKI 668
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 486 PALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIEevNSNNQELLRKYR---RELQLRKKCHNELV 553
Cdd:TIGR04523 669 KESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR--IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
288-464 |
1.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 288 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 360
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 361 RAQSPP-----VKYViKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 435
Cdd:COG3883 110 GSESFSdfldrLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 2462548931 436 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 464
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
349-556 |
1.43e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 349 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQAR--------NQHLQEQVAMQRQVLK-EMEQQLQS 415
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 416 SH-----QLTARLRAQIAMYESELE--RAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 483
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548931 484 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 556
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
175-528 |
1.43e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 175 RMVEAMSQL--QDEK-----TQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLisqaQEVSRLRSElgGTDLEK 247
Cdd:PRK04778 123 QILEELQELleSEEKnreevEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTES--GDYVEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 248 HRDLLMVENE--RLRQEMRRCEAELQELRTKpagpcpgcehsqesaqLRDKLSQLQL---EMAESKGMLSELNL--EVQQ 320
Cdd:PRK04778 197 REILDQLEEElaALEQIMEEIPELLKELQTE----------------LPDQLQELKAgyrELVEEGYHLDHLDIekEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 321 KTDRLAEVELRLKDC-LAEKAQEEERLSRRLRDSHETIAslraqsppvKYVI--KTVEVESSKTKQALSESQARNQHLQE 397
Cdd:PRK04778 261 LKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDILE---------REVKarKYVEKNSDTLPDFLEHAKEQNKELKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 398 QVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQ-----MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHE 472
Cdd:PRK04778 332 EIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRK 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548931 473 NLAGVRTNLLTLQPALRTltndyngLKRQVR-----GFPLLLQEALRSVKAEIGQAIEEVN 528
Cdd:PRK04778 412 DELEAREKLERYRNKLHE-------IKRYLEksnlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-338 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQ-----LQNQVEHLKE---KLISQAQEVSRLRSELggTDLEKHR 249
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDAssdDLAALEEQLEELEAEL--EELEEEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 250 DLLMVENERLRQEMRRCEAELQELRTKpAGPCPGCEHSQESAQLRDKLSQLQLEMAESKgMLSELNLEVQQKTDRLAEVE 329
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDR-LEAAEDLARLELRALLEERFAAALGDAVERE-LRENLEERIDALRARLNRAE 786
|
....*....
gi 2462548931 330 LRLKDCLAE 338
Cdd:COG4913 787 EELERAMRA 795
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
177-423 |
1.70e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 177 VEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELG--GTDLEKHRDLLMV 254
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAqrDTQVLQLQDTITT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 255 ENERLRQEMRRcEAELQELRTKPAGPCPGCEHSQESAQ-LRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLK 333
Cdd:pfam07888 218 LTQKLTTAHRK-EAENEALLEELRSLQERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 334 DCLAEKAQEEERLSRRLRDSHETIASLRA---------QSPPVKYVIKTVEVESSKTKQALSESQARNQhLQEQVAMQRQ 404
Cdd:pfam07888 297 EGRARWAQERETLQQSAEADKDRIEKLSAelqrleerlQEERMEREKLEVELGREKDCNRVQLSESRRE-LQELKASLRV 375
|
250 260
....*....|....*....|....*.
gi 2462548931 405 VLKEMEQQ-------LQSSHQLTARL 423
Cdd:pfam07888 376 AQKEKEQLqaekqelLEYIRQLEQRL 401
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
251-571 |
1.87e-04 |
|
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: 45.12 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 251 LLMVENERLRQEMRRcEAELQELRTKPAGPCPGCEH-SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 329
Cdd:pfam05557 11 LSQLQNEKKQMELEH-KRARIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 330 LRLKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQARNQHLQEQVAMQRQVLKEM 409
Cdd:pfam05557 90 KKLN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 410 EQ---QLQSSHQLTA-------RLRAQIAMYES----------------ELERAHGQMLEE---MQSLEEDKNRAIEEAF 460
Cdd:pfam05557 152 EQlrqNLEKQQSSLAeaeqrikELEFEIQSQEQdseivknskselaripELEKELERLREHnkhLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 461 araqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL 534
Cdd:pfam05557 232 -----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462548931 535 --LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 571
Cdd:pfam05557 307 rqLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
177-466 |
2.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 177 VEAMSQLQDEKTQLQEELVVLQERLalrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVEN 256
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREEL----EQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcl 336
Cdd:COG4372 111 EELQEELEELQKERQDLE-------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 337 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSS 416
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462548931 417 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 466
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
178-487 |
2.09e-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: 45.33 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELvvlqerlalrdSDQQATSTQLQNQVEHLKEKLisqaQEVSRLRSELGGTDLEKHRDLLmvenE 257
Cdd:COG3096 836 AELAALRQRRSELEREL-----------AQHRAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLADRL----E 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 258 RLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAEskgmLSELNLEVQQKTDRLAEVELRLkDCLA 337
Cdd:COG3096 897 ELREELDAAQEAQAFIQ----------QHGKALAQLEPLVAVLQSDPEQ----FEQLQADYLQAKEQQRRLKQQI-FALS 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 338 EKAQEEERLS-----RRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQAR-NQHLQEQVAMQ------RQV 405
Cdd:COG3096 962 EVVQRRPHFSyedavGLLGENSDLNEKLRAR-------LEQAEEARREAREQLRQAQAQySQYNQVLASLKssrdakQQT 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 406 LKEMEQQLQ-------SSHQLTARLR-------------------AQIAMYESELERAHGQMLEemqsLEED---KNRAI 456
Cdd:COG3096 1035 LQELEQELEelgvqadAEAEERARIRrdelheelsqnrsrrsqleKQLTRCEAEMDSLQKRLRK----AERDykqEREQV 1110
|
330 340 350
....*....|....*....|....*....|.
gi 2462548931 457 EEAFARAQVEMKAVHENlaGVRTNLLTLQPA 487
Cdd:COG3096 1111 VQAKAGWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
293-487 |
2.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 293 LRDKLSQLQLEMAESKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 371
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 372 KTVEV--ESSKTKQALSESQARNQHLQEQVamqrQVLKEMEQQLQsshqltaRLRAQIAMYESELERAHGQ----MLEEM 445
Cdd:COG4717 126 QLLPLyqELEALEAELAELPERLEELEERL----EELRELEEELE-------ELEAELAELQEELEELLEQlslaTEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462548931 446 QSLEEDKNRA------IEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 487
Cdd:COG4717 195 QDLAEELEELqqrlaeLEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
178-511 |
2.53e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVL----QERLALRDSDQQATSTQ----LQNQVEHLKEKLISQAQEVSRLRSELGGTDLEkhr 249
Cdd:TIGR00618 339 SIEEQRRLLQTLHSQEIHIRdaheVATSIREISCQQHTLTQhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTR--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 250 dllMVENERLRQEMRRCEAElQELRTKPAGPCPgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAE-- 327
Cdd:TIGR00618 416 ---TSAFRDLQGQLAHAKKQ-QELQQRYAELCA--AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkk 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 328 -VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTV---EVESSKTKQALSESQARNQHLQEQVAMQR 403
Cdd:TIGR00618 490 aVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYaqlETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 404 QVLKEMEQQLQSS-------HQLTARLRAQIAMyESELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAg 476
Cdd:TIGR00618 570 QSFSILTQCDNRSkedipnlQNITVRLQDLTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK- 644
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462548931 477 vrtnLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQE 511
Cdd:TIGR00618 645 ----LTALHALQLTLTQERVREHaLSIRVLPKELLA 676
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-363 |
2.61e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 175 RMVEAMSQLQDEKTQLQEELVVLQE---RLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrDL 251
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL---------EE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 252 LMVENERLRQEMRRCEAELQELRTkpagpcpgcehsqesaqlrdKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELR 331
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELRE--------------------KLAQLELR-------LEGLEVRIDNLQERLSEEYSL 951
|
170 180 190
....*....|....*....|....*....|..
gi 2462548931 332 LKDCLAEKAQEEERLSRRLRDShetIASLRAQ 363
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRR---LKRLENK 980
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
290-477 |
2.88e-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: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 290 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 363
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 364 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 443
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462548931 444 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 477
Cdd:cd07627 181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
260-547 |
3.08e-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: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 260 RQEMRRCEAELQELRTKPAGPCpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE------LRLK 333
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKAC----------EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlskiMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 334 D---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEME 410
Cdd:TIGR00606 269 NeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 411 QQL---QSSHQLTA-RLRAQIAMYESelERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMKAVHENLAGVRTN 480
Cdd:TIGR00606 343 TELlveQGRLQLQAdRHQEHIRARDS--LIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548931 481 LLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQLRKK 547
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEK 492
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
178-352 |
3.64e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERLALrdsdQQATSTQLQNQVEHLKEKLISQAQEVSRLRSEL-----GGTDLEKHRDLL 252
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 253 MVENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQ--LEMAESKGmlselnlevQQKTDRLAEVEL 330
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLN-------------QQIAALRRQLAALEaaLDASEKRD---------RESQAKIADLGR 179
|
170 180
....*....|....*....|....*....
gi 2462548931 331 RLKDCLAEKAQEeerLSR-------RLRD 352
Cdd:PRK09039 180 RLNVALAQRVQE---LNRyrseffgRLRE 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
296-458 |
4.03e-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: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 296 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHETIASLRAQSPPVK---- 368
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 369 YVIKTVEVESSKTKQALSESQARNqhLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYESELERAHGQMLEEMQSL 448
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 2462548931 449 EEDKNRAIEE 458
Cdd:COG1579 162 EAEREELAAK 171
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
180-351 |
6.39e-04 |
|
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: 43.08 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 180 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQnQVEHLKEKLISQAQEVSRLRSELGGTDLEkhrdllmvenerl 259
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP-KLRDRKDALEEELRQLKQLEDELEDCDPT------------- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 260 rqEMRRCEAELQELrtkpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK 339
Cdd:smart00787 205 --ELDRAKEKLKKL-------------LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFT 269
|
170
....*....|..
gi 2462548931 340 AQEEERLSRRLR 351
Cdd:smart00787 270 FKEIEKLKEQLK 281
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
200-494 |
7.15e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 200 RLALRD--SDQQATSTQLQNQVEHLKEKLISQAqeVSRLRSELGGTDLEKHRdllmVENERLRQEMRRCEAE--LQELRt 275
Cdd:PRK02224 175 RLGVERvlSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIER----YEEQREQARETRDEADevLEEHE- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 276 kpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAqeeerlsrrLRDSHE 355
Cdd:PRK02224 248 ---------ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG---------LDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 356 TIASLRaqsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQlqsshqlTARLRAQIAMYESELE 435
Cdd:PRK02224 310 EAVEAR---------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER-------AEELREEAAELESELE 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548931 436 RAHGQMLEEMQSLEE--DKNRAIEEAFARAQVEM-------KAVHENLAGVRTNLLTLQPALRTLTND 494
Cdd:PRK02224 374 EAREAVEDRREEIEEleEEIEELRERFGDAPVDLgnaedflEELREERDELREREAELEATLRTARER 441
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
174-601 |
7.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 174 LRMVEAMSQLQDEKTQLQEELVVLQErlALRDSDQQATSTQLQNQVEHLK--EKLISQAQEVSRLRSELGGTDLEKHRDL 251
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 252 LMVENERLRQEMRrcEAELQELRTKPAGPCPGCEHSQESAQLR---DKLSQLQLEMAESKGMLSELnlevqQKTDRLAEV 328
Cdd:PTZ00121 1488 AKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADEL-----KKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 329 ELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVEVESS-KTKQALSESQARNQhlQEQVAMQRQVLK 407
Cdd:PTZ00121 1561 EEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIK--AEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 408 EMEQ-------------QLQSSHQLTARLRAQIAMYESELERAhgqmLEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnl 474
Cdd:PTZ00121 1634 KVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE-- 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 475 agvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE----LQLRKKCHN 550
Cdd:PTZ00121 1707 -------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEK 1768
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462548931 551 ELVRLKGNIRVIARvRPVTKEDGEGPEATNAVTFDADDDS--IIHLLHKGKPV 601
Cdd:PTZ00121 1769 KAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGGKEGNLV 1820
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
257-467 |
7.80e-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: 41.96 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQktdRLAEVELRLKDCL 336
Cdd:cd07596 7 EEAKDYILKLEEQLKKLSKQ----------AQRLVKRRRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 337 AEKAQEEERLSRR--------LRDSHETIASLRAqsppvkyVIKT-----VEVESSKtkQALSESQARNQHLQEQVAMQR 403
Cdd:cd07596 74 EELSSLSEAQANQelvkllepLKEYLRYCQAVKE-------TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548931 404 QVLKEMEQQLQSSHQLTARLRAqiamyesELERAHGQMLEEMQSLEEDKNRAIEEA---FARAQVEM 467
Cdd:cd07596 145 AKVEELEEELEEAESALEEARK-------RYEEISERLKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
180-352 |
9.45e-04 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 41.05 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 180 MSQLQDEKTQLQEELVVLQERLA--LRDSDQQATST---------QLQNQVEHLKEKLISQAQEVSRLRSELG-----GT 243
Cdd:pfam13870 1 MRAKRNELSKLRLELITLKHTLAkiQEKLEQKEELGegltmidflQLQIENQALNEKIEERNKELKRLKLKVTntvhaLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 244 DLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSelnlevqqKTD 323
Cdd:pfam13870 81 HLKEKLHFLSAELSRLKKELRERQELLAKLR----------KELYRVKLERDKLRKQNKKLRQQGGLLH--------VPA 142
|
170 180
....*....|....*....|....*....
gi 2462548931 324 RLAEVElRLKDCLAEKAQEEERLSRRLRD 352
Cdd:pfam13870 143 LLHDYD-KTKAEVEEKRKSVKKLRRKVKI 170
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
204-482 |
1.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 204 RDSDQQATStqLQNQVEHLKEKLISQAQEVSRLRsELGGTDLEKHRDLLmvenERLRQEMRrceaelqelrtkpagpcpg 283
Cdd:PHA02562 177 RELNQQIQT--LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 284 cEHSQESAQLRDKLSQLQLEMAESKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrlrdsh 354
Cdd:PHA02562 231 -TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 355 etiaslraqsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESEL 434
Cdd:PHA02562 304 ----------------IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462548931 435 ERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 482
Cdd:PHA02562 368 EELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
169-393 |
1.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 169 AAPMVLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELG---- 241
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELealQAEIDKLQAEIAEAEAEIEERREELGerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 242 -----GTDLEKHRDLLMVEN--------ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESK 308
Cdd:COG3883 94 alyrsGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKA------ELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 309 GMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSES 388
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*
gi 2462548931 389 QARNQ 393
Cdd:COG3883 248 GAGAA 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
186-545 |
1.08e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 186 EKTQLQEELVVL--QERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEvsRLRSElggTDLEKHRDLLMVENERLRQEM 263
Cdd:TIGR00618 418 AFRDLQGQLAHAkkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ--SLKER---EQQLQTKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 264 RRCEAELQELrtkpagPCPGCEHSQESAQlrdKLSQLQLEMAESKGMLSELNlEVQQKTDRLAEVELRLkDCLAEKAQEE 343
Cdd:TIGR00618 493 LARLLELQEE------PCPLCGSCIHPNP---ARQDIDNPGPLTRRMQRGEQ-TYAQLETSEEDVYHQL-TSERKQRASL 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 344 ERLSRRLRDSHETIASLRAQSP--------PVKYVIKTVEVESSKTKQALSESQAR------NQHLQEQVAMQRQVLKEM 409
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKedipnlqnITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDLQDVRLHLQQCSQEL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 410 EQQLQSSHQLTARLraqiaMYESELERAHGQMLEEMQSLEEDKNraieeafarAQVEMKAVHENLAGVRTNLLTLQPALR 489
Cdd:TIGR00618 642 ALKLTALHALQLTL-----TQERVREHALSIRVLPKELLASRQL---------ALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548931 490 TLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 545
Cdd:TIGR00618 708 ELETHIEEYDREFNE----IENASSSLGSDLAAREDALNQSLKELMHQARTVLKAR 759
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
120-464 |
1.19e-03 |
|
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: 42.63 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 120 KEEKLWKRQAPAPRRAREAREAGGTMNVENTGGRLFGSRRCSSLSGPpGAAPmvlrmveAMSQLQDE----KTQLQEELV 195
Cdd:pfam15709 220 KSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETEDASER-GAFS-------SDSVVEDPwlssKYDAEESQV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 196 VLQERLAlrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSElggtdleKHRDLLMVEnerlRQEMRRCEAELQElrt 275
Cdd:pfam15709 292 SIDGRSS---PTQTFVVTGNMESEEERSEEDPSKALLEKREQEK-------ASRDRLRAE----RAEMRRLEVERKR--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 276 kpagpcpgcehsQESAQLRdKLSQLQLEMAESkgMLSELNLEVQQKTDRLAEVELRLKDclAEKAQEEERLSRRLRdshE 355
Cdd:pfam15709 355 ------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQ---L 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 356 TIASLRAQSPPVKYVIKTVEVESSKTKQALSESQA---RNQHLQEQVAMQRQVLKEMEQQlqsshqltARLRAQIAMYES 432
Cdd:pfam15709 415 QAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAEE--------ERLEYQRQKQEA 486
|
330 340 350
....*....|....*....|....*....|..
gi 2462548931 433 ElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 464
Cdd:pfam15709 487 E-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
175-303 |
1.19e-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: 41.93 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 175 RMVEAMSQLQDEKTQLQEELVVLQErlaLRDSDQQATSTQLQNqvehLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 254
Cdd:smart00787 169 LLNSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELDR----AKEKLKKLLQEIMIKVKKL--EELEEELQELES 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462548931 255 ENERLRQEMRRCEAELQELRTKPAgPCPGCEHSqESAQLRDKLSQLQLE 303
Cdd:smart00787 240 KIEDLTNKKSELNTEIAEAEKKLE-QCRGFTFK-EIEKLKEQLKLLQSL 286
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
180-346 |
1.22e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 180 MSQLQDEKTQLQEELvvlqerlalrdsdqqatsTQLQNQVEHLKEKLISQAQEVSRL-RSELGGTDLEKHRDLLMVENER 258
Cdd:pfam13851 49 MSEIQQENKRLTEPL------------------QKAQEEVEELRKQLENYEKDKQSLkNLKARLKVLEKELKDLKWEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 259 LRQEMRRCEAELQELRTKpagpcpgCEHSQESAQ---------LRDKLSQLQLEM----AESKGMLSELNLEvqqkTDRL 325
Cdd:pfam13851 111 LEQRFEKVERERDELYDK-------FEAAIQDVQqktglknllLEKKLQALGETLekkeAQLNEVLAAANLD----PDAL 179
|
170 180
....*....|....*....|.
gi 2462548931 326 AEVELRLKDCLAEKAQEEERL 346
Cdd:pfam13851 180 QAVTEKLEDVLESKNQLIKDL 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
402-566 |
1.37e-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: 42.74 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 402 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVhENLAGVRTNl 481
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQ- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 482 ltLQPALRTLTNDYNGLKRQVRGFPLLLQEALR---SVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGN 558
Cdd:TIGR02168 752 --LSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
....*...
gi 2462548931 559 IRVIARVR 566
Cdd:TIGR02168 830 ERRIAATE 837
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
191-547 |
1.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 191 QEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenERLRQEMRRCEAEL 270
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL----------------EQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 271 QELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVElrlkdclaekaQEEERLSRRL 350
Cdd:COG4372 76 EQLE-------------EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----------KERQDLEQQR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 351 RDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAmqRQVLKEMEQQLQSSHQLTARLRAQIAMY 430
Cdd:COG4372 132 KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 431 ESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 510
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462548931 511 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 547
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
177-363 |
1.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 177 VEAMSQLQDEKTQLQEELVVLQERLA-----LRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtdlEKHRDL 251
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAalraqLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT----PNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 252 LmveneRLRQEMRRCEAELQElrtkpagpcpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEvelr 331
Cdd:COG3206 294 I-----ALRAQIAALRAQLQQ-------------------EAQRILASLEAELEALQAREASLQAQLAQLEARLAE---- 345
|
170 180 190
....*....|....*....|....*....|..
gi 2462548931 332 lkdcLAEKAQEEERLSRRLRDSHETIASLRAQ 363
Cdd:COG3206 346 ----LPELEAELRRLEREVEVARELYESLLQR 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-357 |
1.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 182 QLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQnQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVEN----- 256
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELE-QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAverel 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 --------ERLRQEMRRCEAELQELRT--KPAGPCPGCEHSQESAQLRDKLSQLQlemaeskgmlselnlevQQKTDRLA 326
Cdd:COG4913 768 renleeriDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYLALLD-----------------RLEEDGLP 830
|
170 180 190
....*....|....*....|....*....|..
gi 2462548931 327 EVELRLKDCLAEKAQEE-ERLSRRLRDSHETI 357
Cdd:COG4913 831 EYEERFKELLNENSIEFvADLLSKLRRAIREI 862
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
178-502 |
1.88e-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: 42.12 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 178 EAMSQLQDEKTQLQEELVVLQERL-ALRDSDQQATSTQLQNQVEhlkekliSQAQEVSRLRSELGGTDLEKHRDLLMVEN 256
Cdd:pfam10174 60 EQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVD-------GEDKFSTPELTEENFRRLQSEHERQAKEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQEMrrceaELQELRTkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcL 336
Cdd:pfam10174 133 FLLRKTL-----EEMELRI---------ETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGH-L 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 337 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKqalseSQARNqhlqeqvamqrqvLKEMEQQLQSs 416
Cdd:pfam10174 198 EVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERN-------------IRDLEDEVQM- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 417 hqltARLRAQIAMYESElerahgqmlEEMQSLEEDKNRAieeAFARAQVEMkaVHENLAGVRTNLLTLQPALRTLTNDYN 496
Cdd:pfam10174 259 ----LKTNGLLHTEDRE---------EEIKQMEVYKSHS---KFMKNKIDQ--LKQELSKKESELLALQTKLETLTNQNS 320
|
....*.
gi 2462548931 497 GLKRQV 502
Cdd:pfam10174 321 DCKQHI 326
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
175-452 |
2.13e-03 |
|
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: 42.08 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 175 RMVEAMSQLQDEKTQLQEELVVLQERLA-----LRDSDQQATSTqlqNQVEHLKEKLISQAQEvsRLRSELGG-TDLEKH 248
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISeftsnLAEEEEKAKSL---SKLKNKHEAMISDLEE--RLKKEEKGrQELEKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 249 RDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcehsQESAQLRDKLSQLQLEMA----------ESKGMLSELNLEV 318
Cdd:pfam01576 210 KRKLEGESTDLQEQIAELQAQIAELRAQLA---------KKEEELQAALARLEEETAqknnalkkirELEAQISELQEDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 319 QQKTDRLAEVELRLKDcLAEkaqEEERLSRRLRDSHETIAS---LRAQSppvkyviktvEVESSKTKQAL-SESQARNQH 394
Cdd:pfam01576 281 ESERAARNKAEKQRRD-LGE---ELEALKTELEDTLDTTAAqqeLRSKR----------EQEVTELKKALeEETRSHEAQ 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548931 395 LQEQVAMQRQVLKEMEQQLQSSHqltaRLRAQIAMYESELERAHGQMLEEMQSLEEDK 452
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQALESENAELQAELRTLQQAK 400
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
173-472 |
2.81e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 173 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGT-------DL 245
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIveriqeeDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 246 EKHRDLLMvENERLRQEMRRCEAELQELRTKPAGpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRL 325
Cdd:pfam13868 116 AEAEEKLE-KQRQLREEIDEFNEEQAEWKELEKE-----EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 326 AEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSppvkyviktvevESSKTKQALSESQARNQHLQEQVAMQRQV 405
Cdd:pfam13868 190 RAQQEKAQD---EKAERDELRAKLYQEEQERKERQKERE------------EAEKKARQRQELQQAREEQIELKERRLAE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 406 LKEMEQQLQssHQLTARLRAQIAMYESELERAHGQMLE---EMQSLEEDKNRAIEEAFARAQVEMKAVHE 472
Cdd:pfam13868 255 EAEREEEEF--ERMLRKQAEDEEIEQEEAEKRRMKRLEhrrELEKQIEEREEQRAAEREEELEEGERLRE 322
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
315-543 |
3.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 315 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQ 383
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 384 ALSESQARNQ--HLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAieeafA 461
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA-----Q 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 462 RAQVEMKavhenLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 538
Cdd:COG3206 272 LAELEAE-----LAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 2462548931 539 RRELQ 543
Cdd:COG3206 340 EARLA 344
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-464 |
3.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 175 RMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL--QNQVEHLKEK------------LISQAQEVSRLRSEL 240
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEArlllliaaallaLLGLGGSLLSLILTI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 241 GG-------------TDLEKHRDLLMVENERLRQEMRRCEAELQEL-RTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAE 306
Cdd:COG4717 276 AGvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELeELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 307 SKGMLSELNLEVQQKTDR--LAEV------ELRLKdclAEKAQEEERLSRRLRDSHETIASLRAqsppvkyviktvEVES 378
Cdd:COG4717 356 AEELEEELQLEELEQEIAalLAEAgvedeeELRAA---LEQAEEYQELKEELEELEEQLEELLG------------ELEE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 379 SKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYE-----SELERAHGQMLEEMQSLEED-- 451
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELREEL-------AELEAELEQLEedgelAELLQELEELKAELRELAEEwa 493
|
330
....*....|...
gi 2462548931 452 KNRAIEEAFARAQ 464
Cdd:COG4717 494 ALKLALELLEEAR 506
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
169-511 |
4.06e-03 |
|
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: 40.86 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 169 AAPMVLRMVEAMSQLQDEKTQlqeelvvlQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVsrlRSELGGTdlEKH 248
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQ--------EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKS--EEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 249 RDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEH-SQESAQLRDKLS--QLQLEMAESKgmLSELNLEVQQKTDRL 325
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElHQENKALKKKGSaeNKQLNAYEIK--VNKLELELASAKQKF 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 326 AEVELRLKDCLAEKAQEEERLSRrlrdshetiaslraqsppvkyviktvEVESSKTKqalsesqarnqhLQEQVAMQRQV 405
Cdd:pfam05483 653 EEIIDNYQKEIEDKKISEEKLLE--------------------------EVEKAKAI------------ADEAVKLQKEI 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 406 LKEMEQQLQSSHQLTARLRAQiamyeseleraHGQMLEEMQS-LEEDKNRAIEEAFARAQVEMKavhenLAGVRTNLLTL 484
Cdd:pfam05483 695 DKRCQHKIAEMVALMEKHKHQ-----------YDKIIEERDSeLGLYKNKEQEQSSAKAALEIE-----LSNIKAELLSL 758
|
330 340
....*....|....*....|....*..
gi 2462548931 485 QPALRTLTNDYNGLKRQVRGFPLLLQE 511
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
289-548 |
4.92e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 289 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSppvk 368
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 369 yviKTVEVESSKTKQALSESQARNQHL----------QEQVAMQRQVLKEMEQQLQSSHQlTARLRAQiaMYESELERAh 438
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE-ECRVAAQ--AHNEEAESL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 439 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 518
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422
|
250 260 270
....*....|....*....|....*....|..
gi 2462548931 519 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 548
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
171-491 |
6.35e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 171 PMVLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQA---TSTQLQNQVEHLKEKLisQAQEVSRL-RSELGG---- 242
Cdd:PRK10246 294 PHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHaakQSAELQAQQQSLNTWL--AEHDRFRQwNNELAGwraq 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 243 -TDLEKHRDLLMVENERLRQEMRR----------------CEAELQELRTKPAGPCPGCEHSQ------ESAQLRDKLSQ 299
Cdd:PRK10246 372 fSQQTSDREQLRQWQQQLTHAEQKlnalpaitltltadevAAALAQHAEQRPLRQRLVALHGQivpqqkRLAQLQVAIQN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 300 LQLEMAESKGMLSELNLEVQQKTDRLAEV------ELRLKDCLAEKAQEEE-----------------------RLSRRL 350
Cdd:PRK10246 452 VTQEQTQRNAALNEMRQRYKEKTQQLADVkticeqEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalepGVNQSR 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 351 RDSHETI--------ASLRAQsppVKYVIKTVEVESSKTKQALSESQARNQHLQEQVA---MQRQV-------LKEMEQQ 412
Cdd:PRK10246 532 LDALEKEvkklgeegAALRGQ---LDALTKQLQRDESEAQSLRQEEQALTQQWQAVCAslnITLQPqddiqpwLDAQEEH 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 413 LQSSHQLTAR--LRAQIAMYESELERAHGQMLEEMQSLEEDKNR----------------AIEEAFARAQvemkAVHENL 474
Cdd:PRK10246 609 ERQLRLLSQRheLQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSWQ----QRQNEL 684
|
410
....*....|....*..
gi 2462548931 475 AGVRTNLLTLQPALRTL 491
Cdd:PRK10246 685 TALQNRIQQLTPLLETL 701
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
311-435 |
6.43e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 311 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQA 390
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462548931 391 RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 435
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
292-447 |
7.12e-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: 40.05 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 292 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 371
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQ-------VRTLREEKERSVSQVQELETSLAELKNQAAVPPAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 372 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVlkemeqQLQSSHQLTaRLRAQIAMYESELERA----------HGQM 441
Cdd:pfam15070 74 EQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQA------QVQDNEQLS-RLNQEQEQRLLELERAaerwgeqaedRKQI 146
|
....*.
gi 2462548931 442 LEEMQS 447
Cdd:pfam15070 147 LEDMQS 152
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
182-554 |
7.68e-03 |
|
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: 40.16 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 182 QLQDEKTQLQEELVVLQERLalrdsdqqATSTQLQNQVEHLKEKLISQAQEV--------SRLRSElggtdlEKHRDLLM 253
Cdd:pfam01576 30 ELEKKHQQLCEEKNALQEQL--------QAETELCAEAEEMRARLAARKQELeeilheleSRLEEE------EERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 254 VENERLRQEMRRCEAELQElrtkpagpcpgcehsQESAQLRDKLSQLQLEmAESKGMLSELNLEVQQKTDRLAE---VEL 330
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDE---------------EEAARQKLQLEKVTTE-AKIKKLEEDILLLEDQNSKLSKErklLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 331 RLKDCLAEKAQEEERLS--RRLRDSHETiaslraqsppvkyVIKTVEVESSKtkqalsESQARnqhlQEQVAMQRQvlke 408
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKslSKLKNKHEA-------------MISDLEERLKK------EEKGR----QELEKAKRK---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 409 MEQQLQSSHQLTARLRAQIAmyesELERAHGQMLEEMQSLEedkNRAIEEAFARAQVeMKAVHENLAGvrtnLLTLQPAL 488
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIA----ELRAQLAKKEEELQAAL---ARLEEETAQKNNA-LKKIRELEAQ----ISELQEDL 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548931 489 RTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSnNQELLRKYRRELQLRKKCHNELVR 554
Cdd:pfam01576 281 ESERAARNKAEKQRRD----LGEELEALKTELEDTLDTTAA-QQELRSKREQEVTELKKALEEETR 341
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
182-424 |
7.68e-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: 40.32 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 182 QLQDEKTQLQEELVVLQERLALRDSDQqatstqlqNQVEHLKEKLISQAQEVSRLRS-----ELggtdLEKHRDLLMVEn 256
Cdd:COG3096 445 AFRAKEQQATEEVLELEQKLSVADAAR--------RQFEKAYELVCKIAGEVERSQAwqtarEL----LRRYRSQQALA- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 257 ERLRQemrrCEAELQELRTKpagpcpgcEHSQESAQ-LRDKLSQLQLEMAESKGMLSELnlevqqktdrLAEVELRLKDC 335
Cdd:COG3096 512 QRLQQ----LRAQLAELEQR--------LRQQQNAErLLEEFCQRIGQQLDAAEELEEL----------LAELEAQLEEL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 336 LAEKAQEEERLS--RRLRDSHET-IASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQ 412
Cdd:COG3096 570 EEQAAEAVEQRSelRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDEL 649
|
250
....*....|..
gi 2462548931 413 LQSSHQLTARLR 424
Cdd:COG3096 650 AARKQALESQIE 661
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
294-446 |
7.72e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 294 RDK-LSQLQLEMAESKGMLS-------ELNLEVQQKTDRLAEVEL---RLKDCLAEKAQEEERLSRRLRDSHETIASLRA 362
Cdd:PRK09039 51 KDSaLDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 363 QSppvkyviktvevessktkqalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML 442
Cdd:PRK09039 131 VS---------------------ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....
gi 2462548931 443 EEMQ 446
Cdd:PRK09039 190 QELN 193
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
188-363 |
9.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 188 TQLQEELVVLQErlalrDSDQQAtstQLQNQVEHLKEKLISQAQ------EVSRLRSELGGTD----LEKHRDLlmveNE 257
Cdd:PRK04863 921 AQLEPIVSVLQS-----DPEQFE---QLKQDYQQAQQTQRDAKQqafaltEVVQRRAHFSYEDaaemLAKNSDL----NE 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548931 258 RLRQEMRRCEaelqelrtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC-- 335
Cdd:PRK04863 989 KLRQRLEQAE--------------------QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgv 1048
|
170 180 190
....*....|....*....|....*....|....
gi 2462548931 336 -----LAEKAQE-EERLSRRLRDSHETIASLRAQ 363
Cdd:PRK04863 1049 padsgAEERARArRDELHARLSANRSRRNQLEKQ 1082
|
|
| |
