|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
465-792 |
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: 541.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 465 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFN 543
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 544 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 620
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 621 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 700
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 701 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 780
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 973353096 781 LKFAERVRSVEL 792
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
473-790 |
1.56e-151 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 447.40 E-value: 1.56e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 473 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVCIFAY 549
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 550 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 629
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 630 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 706
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 707 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 784
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 973353096 785 ERVRSV 790
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
467-794 |
3.81e-145 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 431.23 E-value: 3.81e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDVFQEVQA-LVTSCIDGF 542
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 543 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 622
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 623 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 700
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 701 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 778
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 973353096 779 YSLKFAERVRSVELGP 794
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
467-788 |
1.67e-125 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 380.06 E-value: 1.67e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPvtKEDGEGPEATNAVTFDADDDSIIHL--LHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFN 543
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 544 VCIFAYGQTGAGKTYTMEGTAEN-PGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 621
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 622 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 699
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 700 SERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 778
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 973353096 779 YSLKFAERVR 788
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
467-790 |
2.19e-106 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 330.96 E-value: 2.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVT-KEDGEGpeATNAVTFDADDDSIIhlLHKGK------PVSFELDKVFSPQASQQDVFQE-VQALVTSC 538
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 539 IDGFNVCIFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEK 615
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 616 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 691
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 692 LNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 770
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 973353096 771 EKNTSETLYSLKFAERVRSV 790
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
468-791 |
1.85e-104 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 326.21 E-value: 1.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 468 IRVIARVRPVT-KEDGEGPEatNAVTFDADDDSIIhllhKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 545
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 546 IFAYGQTGAGKTYTMEGTA------ENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIR 619
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 620 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 689
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 690 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 766
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 973353096 767 VSPVEKNTSETLYSLKFAERVRSVE 791
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
467-790 |
5.51e-95 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 301.19 E-value: 5.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDADDDSIIHLL----------HKGKPVSFELDKVFSPQASQQDVFQ 529
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 530 E-VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLL 608
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 609 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 687
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 688 --TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 762
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 973353096 763 MVVQVSPVEKNTSETLYSLKFAERVRSV 790
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
467-790 |
6.89e-93 |
|
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: 6.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVTKEDgegPEATNAVTFDADDDSIIHllHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFNVC 545
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 546 IFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkASDWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 625
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 626 GQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 701
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 702 RVGKSGAEGSRLREAQHINKSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 779
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 973353096 780 SLKFAERVRSV 790
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
467-790 |
2.11e-92 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 293.85 E-value: 2.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVTKEDGEGPeatNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 545
Cdd:cd01369 3 NIKVVCRFRPLNELEVLQG---SKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFaAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 546 IFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGkepQEKLEIRLCP 622
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 623 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSER 702
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 703 VGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSL 781
Cdd:cd01369 237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316
|
....*....
gi 973353096 782 KFAERVRSV 790
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
467-790 |
6.07e-89 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 285.76 E-value: 6.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVTKEDgegPEATNAVTFDADDDS----IIHLLHKGKPV--SFELDKVFSPQASQQDVFQEVQA-LVTSCI 539
Cdd:cd01364 3 NIQVVVRCRPFNLRE---RKASSHSVVEVDPVRkevsVRTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 540 DGFNVCIFAYGQTGAGKTYTMEG--------TAENP---GINQRALQLLFSEVQEkaSDWEYTITVSAAEIYNEVLRDLL 608
Cdd:cd01364 80 MGYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDplaGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 609 GKEPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG- 685
Cdd:cd01364 158 SPSSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 686 --LRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLM 763
Cdd:cd01364 238 eeLVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340
....*....|....*....|....*..
gi 973353096 764 VVQVSPVEKNTSETLYSLKFAERVRSV 790
Cdd:cd01364 318 IATISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
466-790 |
2.30e-87 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 281.93 E-value: 2.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 466 GNIRVIARVRPVTK-EDGEGpeATNAVTFDADDDSIIHL--------LHKGKPVSFELDKVF-------SPQASQQDVFQ 529
Cdd:cd01365 1 ANVKVAVRVRPFNSrEKERN--SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 530 EVQA-LVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASD-WEYTITVSAAEIYNEVLRDL 607
Cdd:cd01365 79 DLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 608 LGKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHAL--LIVTVRGVDC 682
Cdd:cd01365 159 LNPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 683 STGLRT--TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQ 752
Cdd:cd01365 237 ETNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLK 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 973353096 753 DSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 790
Cdd:cd01365 317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
451-791 |
2.29e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 277.78 E-value: 2.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 451 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE 530
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 531 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 609
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 610 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 689
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 690 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 767
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 973353096 768 SPVEKNTSETLYSLKFAERVRSVE 791
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
468-785 |
1.01e-78 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 258.09 E-value: 1.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 468 IRVIARVRPVTKEDGEGPEA-------TNAVTFDADDDSIIHLLHKG---KPVSFELDKVFSPQASQQDVFQEV-QALVT 536
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 537 SCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkasdweYTITVSAAEIYNEVLRDLL----GKEP 612
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 613 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 687
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 688 ---TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 759
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 973353096 760 KTLMVVQVSPVEKNTSETLYSLKFAE 785
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
467-788 |
1.40e-78 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 257.82 E-value: 1.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVTKEDGEGpEATNAVTFDADDDSIihlLHKGKPVSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVC 545
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 546 IFAYGQTGAGKTYTMEGTAENP--------GINQRALQLLFSEVQ---EKASD-WEYTITVSAAEIYNEVLRDLLgkEP- 612
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 613 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 689
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 690 gKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 765
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 973353096 766 QVSPVEKNTSETLYSLKFAERVR 788
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
468-788 |
1.54e-73 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 244.03 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 468 IRVIARVRPVTKEDGEGpeatnaVTFDADDDSI-IHLL---------HKGKPVSFELDKVFSpQASQQDVFQEV-QALVT 536
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLH-NASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 537 SCIDGFNVCIFAYGQTGAGKTYTMEGTAEN---PGINQRALQLLFSEVQEKASDwEYTITVSAAEIYNEVLRDLLGKEPQ 613
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 614 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 688
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 689 TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 767
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 973353096 768 SPVEKNTSETLYSLKFAERVR 788
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
467-788 |
1.86e-72 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 240.48 E-value: 1.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVtkEDGEGPEATNAVTFDADDDSII--HLLHKGKPVSFELDKVFSPQASQQDVF-QEVQALVTSCIDGFN 543
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 544 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKAsdWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 623
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 624 GSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 702
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 703 VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 782
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 973353096 783 FAERVR 788
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
467-787 |
4.47e-67 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 226.41 E-value: 4.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 467 NIRVIARVRPVTKEDgEGPEATNAVTFDADDDSIIH-------LLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSC 538
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 539 IDGFNVCIFAYGQTGAGKTYTMEG----TAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLgkepQE 614
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 615 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 694
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 695 VDLAGSER-VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 772
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 973353096 773 NTSETLYSLKFAERV 787
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
468-791 |
9.21e-58 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 215.57 E-value: 9.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 468 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVCI 546
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 547 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLgkE 611
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL--D 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 612 P-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT 688
Cdd:PLN03188 248 PsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 689 --TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKT 761
Cdd:PLN03188 326 fkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350
....*....|....*....|....*....|
gi 973353096 762 LMVVQVSPVEKNTSETLYSLKFAERVRSVE 791
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
447-608 |
3.19e-44 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 156.23 E-value: 3.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 447 YRRELQLRKKCHNELVRLKGNIRVIARVRPvtkedgegpEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQD 526
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRP---------ELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 527 VFQEVQALVTSCIDGFNVCIFAYGQTGAGktytmegtaENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRD 606
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 973353096 607 LL 608
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
515-734 |
1.97e-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: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 515 DKVFSPQASQQDVFQEVQALVTSCIDGFNV-CIFAYGQTGAGKTYTMEgtaenpGINQRALQLLFSEVQEKASDWEYTIT 593
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 594 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfghTNRTTEfTNLNEHSSRSHALL 673
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353096 674 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegsrlreaqhINKSLSALGDVIAALR 734
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-435 |
1.65e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLR 203
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 204 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLS----------RRLRDSHETIASLRAQs 273
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltllnEEAANLRERLESLERR- 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 274 ppVKYVIKTVEvESSKTKQALSESQARNQHLQEQvamQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErahgQMLEE 353
Cdd:TIGR02168 833 --IAATERRLE-DLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELE----ELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 354 MQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND-YNGLKRQVRGFPLLLQEALRSVKaEIGQA 432
Cdd:TIGR02168 903 LRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLK-RLENK 980
|
...
gi 973353096 433 IEE 435
Cdd:TIGR02168 981 IKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-451 |
2.43e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKlISQAQEVSRLRSELGgtdlEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaqlrDKL 206
Cdd:TIGR02168 201 QLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE--------------------EEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 207 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA---QEEERLSRRLRDSHETIASLRAQsppvkyvIKTV 283
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 284 EVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT--------------ARLRAQIAMYESELER--AH 347
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 348 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 427
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330 340
....*....|....*....|....*.
gi 973353096 428 EIGQAIEEVNS--NNQELLRKYRREL 451
Cdd:TIGR02168 483 ELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
124-436 |
2.37e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQE-SAQL 202
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 203 RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIaslraqsppvkyvikt 282
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---------------- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 283 vevessktkQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKN 362
Cdd:COG1196 379 ---------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353096 363 RA--IEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 436
Cdd:COG1196 450 EEaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-456 |
1.33e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 168 LRQEMRRCEAELQELRTKpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdclaE 247
Cdd:COG1196 218 LKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 248 KAQEEER-LSRRLRDSHETIASLRAQsppvkyviktveveSSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSH 326
Cdd:COG1196 285 EAQAEEYeLLAELARLEQDIARLEER--------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 327 QLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEafARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNG 406
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 973353096 407 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 456
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-411 |
3.49e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 139 AQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaESKG 218
Cdd:TIGR02169 729 EQEEEKLKERL--EELEEDLSSLEQEIENVKSELKELEARIEELEEDLH------KLEEALNDLEARLSHSRIP--EIQA 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 219 MLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALS 295
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 296 ESQARNQHLQEQVAMQRQVLKEMEQQLQS---------SHQLTARLRAQIAMYE-SELERAHGQMLE------------- 352
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEEleaqiekkrKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqa 958
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973353096 353 -------EMQSLEEDKNRAIE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 411
Cdd:TIGR02169 959 elqrveeEIRALEPVNMLAIQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-468 |
3.95e-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: 67.00 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 169 RQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELRLkdclAEK 248
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL----ARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 249 AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQL 328
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 329 TARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK 408
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 409 RQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 468
Cdd:TIGR02168 887 EAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
449-733 |
4.98e-11 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 66.30 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 449 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDADDDSIihllhKGKPV------------SFELDK 516
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 517 VFSPQASQQDVFQEVQALVTSCIDGfnvcIFAYGQTGAGKTYTMEgtAENPGINQRALQLLFSEVQ-EKASDWEYTITVS 595
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 596 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvddinkvfEFGHTNRTTEFTNLNEHSSRS 669
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--------EKASKLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353096 670 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGSRLREAQHINKSLSALGDVIAAL 733
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
123-359 |
2.58e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 123 YLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMvenerlrQEMRRCEAELQELRTkpagpcpgcehsqESAQL 202
Cdd:COG3206 179 FLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-------QQLSELESQLAEARA-------------ELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 203 RDKLSQLQLEMAESKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSHETIASLRAQsppvkyvI 280
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNHPDVIALRAQ-------I 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 281 KTVEVE-SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSshqlTARLRAQIAMYESELERAHGQMLEEMQSLEE 359
Cdd:COG3206 301 AALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-475 |
6.05e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 201 QLRDKLSQLQLEMAESKgmLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIaslraqsppvkyvi 280
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEEL-------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 281 ktvEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEED 360
Cdd:COG1196 280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 361 KN--RAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNS 438
Cdd:COG1196 357 EAelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAE 432
|
250 260 270
....*....|....*....|....*....|....*..
gi 973353096 439 NNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVR 475
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
127-449 |
1.07e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRSELGGT-----DLEKHRDLLMVENERLRQEMRRCEAELQELRTK--------PAGPCPGC 193
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDApvdlgNAEDFLEELREERDELREREAELEATLRTARERveeaeallEAGKCPEC 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 194 -------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDrLAEVELRLKDcLAEKAqeeERLSRRLRDSHETI 266
Cdd:PRK02224 458 gqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIER-LEERR---EDLEELIAERRETI 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 267 ASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLrAQIAMYESELERA 346
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERL 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 347 HGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPL 416
Cdd:PRK02224 612 REK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
330 340 350
....*....|....*....|....*....|....*...
gi 973353096 417 LLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 449
Cdd:PRK02224 689 ELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-379 |
1.56e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 164 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 243
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 244 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPP---------VKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 309
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 310 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 379
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-435 |
2.13e-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: 58.26 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 154 LEKHRDLLMVENERLRQEMR--------------RCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGM 219
Cdd:pfam01576 375 LEKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQARLS------ESERQRAELAEKLSKLQSELESVSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 220 LSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALS 295
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 296 ESQARnqhlQEQVAMQRQVLKEMEQQLQS-SHQLTARLRAQIAMYEsELERAHGQMLEEMQSL--EEDKNRAIEEAFARA 372
Cdd:pfam01576 528 DMKKK----LEEDAGTLEALEEGKKRLQReLEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDHQRQLVSNLEKK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 373 Q-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKAEIGQAIE 434
Cdd:pfam01576 603 QkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQLRAEM-EDLVSSKDDVGKNVH 681
|
.
gi 973353096 435 E 435
Cdd:pfam01576 682 E 682
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-443 |
3.27e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 130 HLKEKLISQAQEVS-RLRSELGGTDLEKhrDLLMVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESA-----QLR 203
Cdd:pfam15921 387 HKREKELSLEKEQNkRLWDRDTGNSITI--DHLRRELDDRNMEVQRLEALLKAMKSE----CQGQMERQMAAiqgknESL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 204 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTV 283
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 284 EVESSKTK-QALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTA---RLRAQIAMYESELERAHGQM---LEEMQS 356
Cdd:pfam15921 532 ELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKI 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 357 LEEDKNRAIEEAFAR-AQVEMKAVH------ENLAGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQ 419
Cdd:pfam15921 612 LKDKKDAKIRELEARvSDLELEKVKlvnagsERLRAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
330 340
....*....|....*....|....
gi 973353096 420 EALRSVKAEIGQAIEEVNSNNQEL 443
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-346 |
5.68e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKL 206
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKEL--AALKKEEKALLKQLAALERRIAALARRIRALEQELA------ALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 207 SQLQLEMAESKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLRAQSPPVKYV 279
Cdd:COG4942 93 AELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353096 280 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERA 346
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-436 |
5.99e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 162 MVEN----ERLRQEMRRCEAELQELRtkpagpcPGCEHSQESAQLRDKLSQLQLemaeskgMLSELNLEVQQKTDRLAEV 237
Cdd:COG4913 230 LVEHfddlERAHEALEDAREQIELLE-------PIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 238 EL-RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqALSESQARNQHLQEQVAMQRQVLK 316
Cdd:COG4913 296 ELeELRAELARLEAELERLEARLDALREELDELEAQ--------------------IRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 317 EMEQQLQSSHQLTARLRAQIAMYESELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 396
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 973353096 397 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 436
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-473 |
1.12e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 132 KEKLISQAQEVSRLRSELGG--TDLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaQLRDKLSQL 209
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKelEEVLREINEISSELPELREELEKLEKEVKELE-----------------ELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 210 QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEKAQEEERLSR-------RLRDSHETIASLRAQS 273
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 274 PPVKYVIKtvevESSKTKQALSESQARNQHLQEQVAmqrqVLKEMEQQLQSSHQLTA---RLRAQIAMYESE-------- 342
Cdd:PRK03918 324 NGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHELYEEAKAKKEeleRLKKRLTGLTPEklekelee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 343 LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----------------MKAVHENLAGVRTNLLTLQPA 396
Cdd:PRK03918 396 LEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353096 397 LRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 473
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
129-452 |
2.59e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 129 EHLKEKLISQAQEVSRLRSELGgTDLEKHRDLL--MVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQES-AQLRDK 205
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLE-QDYQAASDHLnlVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQqEENEAR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 206 LSQLQLEMAESKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKDCLAE-KAQEEERLSRRLR---- 260
Cdd:PRK04863 385 AEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAEDWLEEfQAKEQEATEELLSleqk 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 261 -DSHETIASLRAQSppVKYVIKTV-EVESSKTKQALSE--SQARNQ-HLQEQVAMQRQVLKEMEQQLQSSHQLTARLR-- 333
Cdd:PRK04863 465 lSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRMRLSELEQRLRQQQRAERLLAef 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 334 --AQIAMY--ESELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLAGVRTNLLTLQPA---LRTLTNDY 404
Cdd:PRK04863 543 ckRLGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLAARAPAWLAAQDAlarLREQSGEE 622
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 973353096 405 NGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 452
Cdd:PRK04863 623 FEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-429 |
3.24e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 207 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK-----AQEEERLSRRLRDSHETIASLRAQSPPVKYVIK 281
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 282 TVEVESSKTKQALSESQA--RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSlEE 359
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA-EL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 360 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpLLLQEALRSVKAEI 429
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVRV 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-469 |
3.69e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 132 KEKLISQAQEVSRLRSELggtdlEKHRDLLMVENERLRQEMRRCEAELQELRtKPAGPCPGC------EH---------- 195
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCgrelteEHrkelleeyta 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 196 -----SQESAQLRDKLSQLQLEMAESKGMLS-ELNLEVQQKT-DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIAS 268
Cdd:PRK03918 460 elkriEKELKEIEEKERKLRKELRELEKVLKkESELIKLKELaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 269 LRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQ-LQSSHQLTARLRaqiamyesELERAH 347
Cdd:PRK03918 537 LKGE-------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLK--------ELEPFY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 348 GQMLEEMQSleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVK 426
Cdd:PRK03918 602 NEYLELKDA--EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLR 679
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 973353096 427 AEIGQA---IEEVNSNNQEL------LRKYRRELQLRKKCHNELVRLKGNIR 469
Cdd:PRK03918 680 AELEELekrREEIKKTLEKLkeeleeREKAKKELEKLEKALERVEELREKVK 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-360 |
1.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLK------EKLISQAQEVSRLRSELGGTDLEKHR---DLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsQ 197
Cdd:COG4913 250 QIELLEpirelaERYAAARERLAELEYLRAALRLWFAQrrlELLEAELEELRAELARLEAELERLE-------------A 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 198 ESAQLRDKLSQLQLEMAESKG-MLSELNLEVQQKTDRLAEVELRLKDcLAEKAQeeeRLSRRLRDSHETIASLRAQSPpv 276
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRAR-LEALLA---ALGLPLPASAEEFAALRAEAA-- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 277 kyviktvevessKTKQALSESQARnqhLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQS 356
Cdd:COG4913 391 ------------ALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGL 455
|
....
gi 973353096 357 LEED 360
Cdd:COG4913 456 DEAE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-477 |
1.84e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 200 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyv 279
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 280 iktvevessktKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEE 359
Cdd:COG4913 677 -----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 360 DKNRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAI 433
Cdd:COG4913 746 ELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYL 818
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 973353096 434 EEVNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 477
Cdd:COG4913 819 ALLDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
125-272 |
3.64e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 125 TLQVEHLKEKLISQAQEVSRLRSELGGTD-----LEKHRDLLMVENERLRQEMR--------RCEAELQELRTKPAgpcp 191
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEaelerLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELE---- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 192 gcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRA 271
Cdd:COG4913 356 --ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
.
gi 973353096 272 Q 272
Cdd:COG4913 434 R 434
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
152-273 |
4.18e-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: 49.63 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 152 TDLEKHRDLLMVENERLRQEMRRC--------------EAELQELR--TKPAGPCPgcehSQESAQLRDKLSQLQLEMAE 215
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLnsikpklrdrkdalEEELRQLKqlEDELEDCD----PTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 973353096 216 SKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 273
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
200-454 |
4.57e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 200 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYV 279
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 280 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQsleE 359
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE---A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 360 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSN 439
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*
gi 973353096 440 NQELLRKYRRELQLR 454
Cdd:COG4372 260 IEELELAILVEKDTE 274
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
132-331 |
7.40e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 132 KEKLISQAQEVSRLRSELGGT-------DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpagpcpgcEHSQESAQLRD 204
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEA---------QQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 205 KLSQLQLEMAESKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 284
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 973353096 285 VESSKTKQALSESQARNQHLQEQVAMQRQV----LKEMEQQLQSSHQLTAR 331
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQGEGSN 216
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-453 |
1.27e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKlISQAQEVSRLRSELGGTDLEKhRDLLMVENERLRQEMRRC-------------------------EAE 178
Cdd:pfam05483 259 LTFLLEESRDK-ANQLEEKTKLQDENLKELIEK-KDHLTKELEDIKMSLQRSmstqkaleedlqiatkticqlteekEAQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 179 LQEL-RTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRL---------AEVELR-LKDCLAE 247
Cdd:pfam05483 337 MEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELeemtkfknnKEVELEeLKKILAE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 248 KA------QEEERLSRRLRDS-HETIASLRAQSPPVK------YVIKTVEVESSKTKQALsESQARNQHLQ--EQVAMQR 312
Cdd:pfam05483 417 DEklldekKQFEKIAEELKGKeQELIFLLQAREKEIHdleiqlTAIKTSEEHYLKEVEDL-KTELEKEKLKniELTAHCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 313 QVLKEMEQQLQSSHQLTARLRAQ---IAMYESELERahgqMLEEMQSLEE------DKNRAIEEAFARAQVEMKA----V 379
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHqedIINCKKQEER----MLKQIENLEEkemnlrDELESVREEFIQKGDEVKCkldkS 571
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973353096 380 HENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 453
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-367 |
2.62e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRSElggtdlEKHRDLLMVENERLRQEMRRCEAELQELR------TKPAGpcpgcEHSQESA 200
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNE------GDHLRNVQTECEALKLQMAEKDKVIEILRqqienmTQLVG-----QHGRTAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 201 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSH 263
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSR 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 264 ETIASLRAQSPPVK--YVIKTVEVESSKTKQALSESQArnqhlQEQVAMQRQVLKEMEQQ--------LQSSHQLTARlR 333
Cdd:pfam15921 667 NELNSLSEDYEVLKrnFRNKSEEMETTTNKLKMQLKSA-----QSELEQTRNTLKSMEGSdghamkvaMGMQKQITAK-R 740
|
250 260 270
....*....|....*....|....*....|....*..
gi 973353096 334 AQIAMYESE---LERAHGQMLEEMQSLEEDKNRAIEE 367
Cdd:pfam15921 741 GQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQE 777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-454 |
2.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 246 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALsesqarnqhLQEQVAMQRQVLKEMEQQLQSS 325
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 326 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 391
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353096 392 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 454
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
170-463 |
3.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 170 QEMRRCEAELQELRTKPAgpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 247
Cdd:COG4717 71 KELKELEEELKEAEEKEE----------EYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 248 KAQEEERLsRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQARNQhlQEQVAMQRQVLKEMEQQLQSSHQ 327
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE------------------LEELEAELAELQ--EELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 328 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGL 407
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353096 408 KRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 463
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
196-460 |
3.07e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 196 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 273
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 274 PPVKYVIKTVEVESS-------KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERa 346
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 347 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 423
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 973353096 424 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 460
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-437 |
3.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 166 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ--LEMAESKGMLSELNLEVQQKTDRLAEVEL---- 239
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE------ALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 240 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQARNQHLQEQV--AM 310
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 311 QRQVLKEMEQQLQSShqlTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 390
Cdd:COG4913 760 GDAVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 973353096 391 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 437
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
160-480 |
5.37e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 160 LLMVENERLRQEMRRcEAELQELRTKPAGPCPGCEH-SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 238
Cdd:pfam05557 11 LSQLQNEKKQMELEH-KRARIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 239 LRLKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQARNQHLQEQVAMQRQVLKEM 318
Cdd:pfam05557 90 KKLN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 319 EQ---QLQSSHQLTA-------RLRAQIAMYES----------------ELERAHGQMLEE---MQSLEEDKNRAIEEAF 369
Cdd:pfam05557 152 EQlrqNLEKQQSSLAeaeqrikELEFEIQSQEQdseivknskselaripELEKELERLREHnkhLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 370 araqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL 443
Cdd:pfam05557 232 -----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 973353096 444 --LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 480
Cdd:pfam05557 307 rqLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
127-470 |
5.92e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRSELGG------------TDLEKHRDLLMVE-------NERLRQEMRRCEAELQELRTKpa 187
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKlnnkyndlkkqkEELENELNLLEKEklniqknIDKIKNKLLKLELLLSNLKKK-- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 188 gpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHE 264
Cdd:TIGR04523 210 --------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 265 TIASLRAQsppvkyvIKTVEVESSKTKQalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 344
Cdd:TIGR04523 282 KIKELEKQ-------LNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 345 RAHGQMLEEMQSLEEdKNRAIEeafaraqvemKAVHENlagvRTNLLTLQpalrTLTNDYNGLKRQvrgfpllLQEAlRS 424
Cdd:TIGR04523 353 NSESENSEKQRELEE-KQNEIE----------KLKKEN----QSYKQEIK----NLESQINDLESK-------IQNQ-EK 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 973353096 425 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRV 470
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-373 |
6.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 197 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 269
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 270 RAQSpPVKYV--IKTVEVESSKTKQALSE---SQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 344
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 973353096 345 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 373
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
125-468 |
9.79e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 125 TLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLL--------------------MVENE----RLRQEMRRCEAELQ 180
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelkselknqekkleeiqnqISQNNkiisQLNEQISQLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 181 ELRTkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGML----------SELNLEVQQKTDRLAEVELRLKDCLAEK-- 248
Cdd:TIGR04523 353 NSES---------ENSEKQRELEEKQNEIEKLKKENQSYKqeiknlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKel 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 249 -AQEEERLSRRLRDSHETIASLRAQSPPVKYVIKtvEVESSKTKQ-----ALSESQARNQHLQEQvamQRQVLKEMEQQL 322
Cdd:TIGR04523 424 lEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK--NLDNTRESLetqlkVLSRSINKIKQNLEQ---KQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 323 QSSHQLTARLRAQIamyeSELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENL--AGVRTNLLTLQPALRTL 400
Cdd:TIGR04523 499 KKLNEEKKELEEKV----KDLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEEL 573
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973353096 401 TNDYNGLKRQVRGFPLLLQEaLRSVKAEIGQAIEEvnsnNQELLRKYRRELQLRKKCHNELVRLKGNI 468
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQ-KEKEKKDLIKEIEE----KEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
258-465 |
1.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 258 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQAR--------NQHLQEQVAMQRQVLK-EMEQQLQS 324
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 325 SH-----QLTARLRAQIAMYESELErahgqMLEE-------MQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVR 387
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFQKVIK-----MYEKggvcptcTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIM 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973353096 388 TNLLTLQPALRTLTNDYNGLKRQVrgfpLLLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 465
Cdd:PHA02562 330 DEFNEQSKKLLELKNKISTNKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
170-411 |
1.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 170 QEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELN-LEVQQKTDRLAEVELRLKDCLAEK 248
Cdd:PRK04863 837 AELRQLNRRRVELERALA------DHESQEQQQRSQLEQAKEGLSALNRLLPRLNlLADETLADRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 249 A-----------------------QEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE-------VESSKTKQALSES- 297
Cdd:PRK04863 911 RfvqqhgnalaqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKNSDLNEKl 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 298 QARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyeseleRAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEM 376
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAEERARARR 1062
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 973353096 377 KAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 411
Cdd:PRK04863 1063 DELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
202-396 |
1.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 202 LRDKLSQLQLEMAESKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 280
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 281 KTVEV--ESSKTKQALSESQARNQHLQEQVamqrQVLKEMEQQLQsshqltaRLRAQIAMYESELERAHGQ----MLEEM 354
Cdd:COG4717 126 QLLPLyqELEALEAELAELPERLEELEERL----EELRELEEELE-------ELEAELAELQEELEELLEQlslaTEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 973353096 355 QSLEEDKNRA------IEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 396
Cdd:COG4717 195 QDLAEELEELqqrlaeLEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
161-448 |
1.31e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 161 LMVENERLRQEMRRCEAELQELRTKPAgpcpgcehSQESAQLRDKL----SQLQLEMAESKgmlselnlEVQQKTDRLAE 236
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEA--------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 237 VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVesskTKQALSESQARNQHLQEQVAMQRQVLK 316
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDE----ITERIAEQEIAYSELQEELEEILKQLE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 317 EME-QQLQSSHQLtarlraqIAMYESELErAHgQMLEEMQS-LEEDKnRAIE------------EAFARAQVEMKAVHEN 382
Cdd:PRK04778 394 EIEkEQEKLSEML-------QGLRKDELE-AR-EKLERYRNkLHEIK-RYLEksnlpglpedylEMFFEVSDEIEALAEE 463
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973353096 383 LAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRKYR 448
Cdd:PRK04778 464 LEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFREYD 534
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
98-334 |
1.44e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 98 AARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKE---KLISQAQEVSRLRSELGGTDLEK---HRDLLMVENERLRQE 171
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLDAELQLSAHLIQQEVGRAREQgeaERQQLSEVAQQLEQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 172 MRRCEAELQELRTKPAGPCPGCEHS-QESAQLRDKLSQLQlemaeskgmlselNLEVQQKTDRLAEVELRLKDCLAEKaq 250
Cdd:pfam07111 533 LQRAQESLASVGQQLEVARQGQQEStEEAASLRQELTQQQ-------------EIYGQALQEKVAEVETRLREQLSDT-- 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 251 eEERLSRRLRDSHETIASLRA-QSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT 329
Cdd:pfam07111 598 -KRRLNEARREQAKAVVSLRQiQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQ 676
|
....*
gi 973353096 330 ARLRA 334
Cdd:pfam07111 677 QRLLA 681
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
169-456 |
1.47e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 169 RQEMRRCEAELQELRTKPAGPCpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE------LRLK 242
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKAC----------EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlskiMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 243 D---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEME 319
Cdd:TIGR00606 269 NeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 320 QQL---QSSHQLTA-RLRAQIAMYESelERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMKAVHENLAGVRTN 389
Cdd:TIGR00606 343 TELlveQGRLQLQAdRHQEHIRARDS--LIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353096 390 LLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQLRKK 456
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEK 492
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
126-393 |
2.12e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 126 LQVEHLKEKLISQAQEVSRLRSELG-----GTDLEKHRDLLMVENERLR----QEMRRCEAELQELRtkpagpcpgcEHS 196
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVliqkfGRSLKAKKRFSLLKKETIYlqsaQRVELAERQLQELK----------IDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 197 QESAQLRDKLSQLQLEMAE-SKGMLSELNLEVQQKTDRLAEVElrlkdCLAEKAQEEERLSRRLRDS------HETIASL 269
Cdd:COG5022 892 KSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLK-----KLLNNIDLEEGPSIEYVKLpelnklHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 270 RAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV----AMQRQV--LKEMEQQLQSSHQLTARLRA-----QIAM 338
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILK 1046
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 973353096 339 YESELERAHgqMLEEMQSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 393
Cdd:COG5022 1047 PLQKLKGLL--LLENNQLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
163-375 |
2.13e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 163 VENERLRQEMRRCEAELQELRTkpagpcpgCEHSQESAQLR-DKLSQLQLEMaESKGMLSELNLEVQQKTDRLAEVELRL 241
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRK--------LEEAEKARQAEmDRQAAIYAEQ-ERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 242 KDCLA---EKAQEEERL-------SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARN-QHLQEQVA- 309
Cdd:pfam17380 367 QEEIAmeiSRMRELERLqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAr 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973353096 310 -MQRQVLKEMEQQLQSS---HQLTARLRAQIAMYESELERAHGQMLEEM---QSLEEDKNRAIEEAFARAQVE 375
Cdd:pfam17380 447 eMERVRLEEQERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
199-386 |
2.38e-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: 43.45 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 199 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 272
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 273 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 352
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 973353096 353 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 386
Cdd:cd07627 181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
131-390 |
2.43e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 131 LKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehsqeSAQLRDKLSQLQ 210
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESEL--KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK-------------LQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 211 LEMAESKGMLSELNLEVQQKTDRLAEVEL--RLKDCLAEKAQEEERLSRRLR--DSHETIASLRAQSPPVKYVIKTVEVE 286
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTImeRFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 287 SSKTKQALSESQARNQHLQE---QVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR 363
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
250 260
....*....|....*....|....*..
gi 973353096 364 AiEEAFARAQVEMKAVHENLAGVRTNL 390
Cdd:TIGR00606 925 K-EELISSKETSNKKAQDKVNDIKEKV 950
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
205-367 |
3.10e-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: 43.37 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 205 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHETIASLRAQSPPVK---- 277
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 278 YVIKTVEVESSKTKQALSESQARNqhLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYESELERAHGQMLEEMQSL 357
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 973353096 358 EEDKNRAIEE 367
Cdd:COG1579 162 EAEREELAAK 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
128-469 |
3.42e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 128 VEHLKEKLISQAQEVSRLRSELggTDLEKHRDllmVENERLRQEMRRCE---AELQELRTKpAGPCPGCEH---SQESAQ 201
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSEL--RQARKRRD---QASEALRQASRRLEerqSALDELELQ-LFPQAGTLLhflRKEAPD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 202 LRDKLSQL-QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLA-EKAQEEERLSRR-------LRDSHETIASLRAQ 272
Cdd:pfam12128 547 WEQSIGKViSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVpEWAASEEELRERldkaeeaLQSAREKQAAAEEQ 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 273 SPPVKYVIKTVEVESSKTKQALSESQAR-----NQHLQEQVAMQRQV---LKEMEQQLQS-SHQLTARLRAQIAMYES-- 341
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKALaerKDSANERLNSlEAQLKQLDKKHQAWLEEqk 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 342 -ELERAHGQMLEEMQSLEEDKNRA---IEEAFARAQVEMKA--------VHENLAGV---RTNLLTLQPALRTLT---ND 403
Cdd:pfam12128 707 eQKREARTEKQAYWQVVEGALDAQlalLKAAIAARRSGAKAelkaletwYKRDLASLgvdPDVIAKLKREIRTLErkiER 786
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353096 404 YNGLKRQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL----RKKCHNELVRLKGNIR 469
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-384 |
4.31e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKLISQAQEVSRLRSELGGTDlEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQE-SAQL 202
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEErLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 203 RDKLSQLQLEMAESKGMLSELNLEVQQKTD--------------RLAEVELRLKDCLAEKAQEEERLS---RRLRDSHET 265
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelkeeledlraELEEVDKEFAETRDELKDYREKLEklkREINELKRE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 266 IASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELer 345
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL-- 485
|
250 260 270
....*....|....*....|....*....|....*....
gi 973353096 346 ahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 384
Cdd:TIGR02169 486 -------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
176-411 |
4.51e-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: 44.17 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 176 EAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESK--------------GMLSELNL---------------- 225
Cdd:COG3096 835 EAELAALR-------------QRRSELERELAQHRAQEQQLRqqldqlkeqlqllnKLLPQANLladetladrleelree 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 226 ---------EVQQKTDRLAEVElRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVES-SKTKQALS 295
Cdd:COG3096 902 ldaaqeaqaFIQQHGKALAQLE-PLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 296 ESQARNQHLQEQ-VAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESelERAHGQMLEE-MQSLEEDKNRAIEEAFARAQ 373
Cdd:COG3096 981 ENSDLNEKLRARlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS--RDAKQQTLQElEQELEELGVQADAEAEERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 973353096 374 VEMKAVHENL---AGVRTNLLT-----------LQPALRTLTNDYNGLKRQV 411
Cdd:COG3096 1059 IRRDELHEELsqnRSRRSQLEKqltrceaemdsLQKRLRKAERDYKQEREQV 1110
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
169-373 |
5.01e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 169 RQEMRRCEAELQElrtkpagpcpgcehsQESAQLRdKLSQLQLEMAESkgMLSELNLEVQQKTDRLAEVELRLKDclAEK 248
Cdd:pfam15709 342 RAEMRRLEVERKR---------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 249 AQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQA---RNQHLQEQVAMQRQVLKEMEQQlqss 325
Cdd:pfam15709 402 RQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAEE---- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 973353096 326 hqltARLRAQIAMYESElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 373
Cdd:pfam15709 475 ----ERLEYQRQKQEAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
131-368 |
5.64e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 131 LKEKLISQAQEVSRLRSElggtdlekhRDLLMVENERLRqemrrCeAELQELRTKPAGPCPGCEHSQE--------SAQL 202
Cdd:pfam05622 216 LEEKLEALQKEKERLIIE---------RDTLRETNEELR-----C-AQLQQAELSQADALLSPSSDPGdnlaaeimPAEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 203 RDKLSQLQLEmaesKGMLSELnlEVQQKTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKT 282
Cdd:pfam05622 281 REKLIRLQHE----NKMLRLG--QEGSYRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 283 VEVESSKT------KQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTArlraqiamyeSELERAHGQMLEEMQS 356
Cdd:pfam05622 348 LQEQGSKAedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKA 417
|
250
....*....|..
gi 973353096 357 LEEDKNRAIEEA 368
Cdd:pfam05622 418 MEERYKKYVEKA 429
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
124-391 |
6.25e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKLISQAQEVSRLRsELGGTDLEKHRDLLmvenERLRQEMRrceaelqelrtkpagpcpgcEHSQESAQLR 203
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK--------------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 204 DKLSQLQLEMAESKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrlrdshetiaslraqsp 274
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK----------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 275 pvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML--- 351
Cdd:PHA02562 304 -----IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVdna 378
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 973353096 352 EEMQSLEEDKNRAIEEafaRAQVEMKAVHEnlaGVRTNLL 391
Cdd:PHA02562 379 EELAKLQDELDKIVKT---KSELVKEKYHR---GIVTDLL 412
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
166-376 |
6.40e-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: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 166 ERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQktdRLAEVELRLKDCL 245
Cdd:cd07596 7 EEAKDYILKLEEQLKKLSKQ----------AQRLVKRRRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 246 AEKAQEEERLSRR--------LRDSHETIASLRAqsppvkyVIKT-----VEVESSKtkQALSESQARNQHLQEQVAMQR 312
Cdd:cd07596 74 EELSSLSEAQANQelvkllepLKEYLRYCQAVKE-------TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353096 313 QVLKEMEQQLQSSHQLTARLRAqiamyesELERAHGQMLEEMQSLEEDKNRAIEEA---FARAQVEM 376
Cdd:cd07596 145 AKVEELEEELEEAESALEEARK-------RYEEISERLKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-475 |
8.80e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 311 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVhENLAGVRTNl 390
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQ- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 391 ltLQPALRTLTNDYNGLKRQVRGFPLLLQEALR---SVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGN 467
Cdd:TIGR02168 752 --LSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
....*...
gi 973353096 468 IRVIARVR 475
Cdd:TIGR02168 830 ERRIAATE 837
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
124-454 |
9.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcPGCEHSQESAQLR 203
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE---ELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 204 DKLSQLQLEMAE--------SKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHE-------- 264
Cdd:COG4717 170 AELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEEELEEAqeeLEELEEELEQLENELEAAALeerlkear 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 265 -------TIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQ 323
Cdd:COG4717 250 lllliaaALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 324 SSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEmkavheNLAGVRtNLLTLQPALRTLTN 402
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVE------DEEELR-AALEQAEEYQELKE 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 973353096 403 DYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 454
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
202-437 |
9.67e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 202 LRDKLSQLQL---EMAESKGMLSELNL--EVQQKTDRLAEVELRLKDC-LAEKAQEEERLSRRLRDSHETIAslraqspp 275
Cdd:PRK04778 228 LPDQLQELKAgyrELVEEGYHLDHLDIekEIQDLKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDILE-------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 276 vKYVI--KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQ---- 349
Cdd:PRK04778 300 -REVKarKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQeiay 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 350 -MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTltndyngLKRQVR-----GFPLLLQEALR 423
Cdd:PRK04778 379 sELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHE-------IKRYLEksnlpGLPEDYLEMFF 451
|
250
....*....|....
gi 973353096 424 SVKAEIGQAIEEVN 437
Cdd:PRK04778 452 EVSDEIEALAEELE 465
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
131-456 |
1.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 131 LKEKLISQAQEVSRLRSELggtdlekhrDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ 210
Cdd:COG4372 29 LSEQLRKALFELDKLQEEL---------EQLREELEQAREELEQLEEELEQARSELE------QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 211 LEMAESKGMLSELNLEVQQKTDRLAEVElrlkdclaekaQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKT 290
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQ-----------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 291 KQALSESQARNQHLQEQVAmqRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFA 370
Cdd:COG4372 163 QEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 371 RAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 450
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
....*.
gi 973353096 451 LQLRKK 456
Cdd:COG4372 321 LLELAK 326
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
167-344 |
1.09e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 167 RLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLA 246
Cdd:COG1579 21 RLEHRLKELPAELAELE-------------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 247 EK-----AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVamqRQVLKEMEQQ 321
Cdd:COG1579 88 NKeyealQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAE 157
|
170 180
....*....|....*....|...
gi 973353096 322 LqsshqltARLRAQIAMYESELE 344
Cdd:COG1579 158 L-------EELEAEREELAAKIP 173
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-258 |
1.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 132 KEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQL-- 209
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE-------------EELEELREELAELea 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 973353096 210 QLEMAESKGMLSELNLEVQQKTDRLAEVE-----LRLKDCLAEKAQEEERLSRR 258
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAeewaaLKLALELLEEAREEYREERL 514
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
140-376 |
1.27e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 140 QEVSRLRSELggtdLEKHRDllmvenerlrqemrRCEAELQELRtkpagpcpgcehSQESAQlRDKLSQLQLEMAEskgM 219
Cdd:PRK10929 203 QELARLRSEL----AKKRSQ--------------QLDAYLQALR------------NQLNSQ-RQREAERALESTE---L 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 220 LSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRdsheTIASlraQSPPVKYVIKTVEVESsktkQALSESQA 299
Cdd:PRK10929 249 LAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQR----QAAS---QTLQVRQALNTLREQS----QWLGVSNA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 300 RNQHLQEQVAMqrqvLKEME--QQLQSShqlTARLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRaIEEAFARAQV 374
Cdd:PRK10929 318 LGEALRAQVAR----LPEMPkpQQLDTE---MAQLRVQRLRYEDLLNKQPQLRqirQADGQPLTAEQNR-ILDAQLRTQR 389
|
..
gi 973353096 375 EM 376
Cdd:PRK10929 390 EL 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
127-462 |
1.31e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRS-----ELGGTDLEKHRDLLMVENERLRQEMRRCEAEL----QELRTKpagpcpgcehSQ 197
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLeqkqKELKSK----------EK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 198 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVK 277
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN----------------LE 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 278 YVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyeSELERAHGQMLEEMQSL 357
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL----EKAKKENEKLSSIIKNI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 358 EEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQPALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIE 434
Cdd:TIGR04523 637 KSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKIKESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR 702
|
330 340 350
....*....|....*....|....*....|.
gi 973353096 435 evNSNNQELLRKYR---RELQLRKKCHNELV 462
Cdd:TIGR04523 703 --IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
127-472 |
1.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKL 206
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEEL----------------EQARSELEQLEEELEELNEQLQ------AAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 207 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKtvEVE 286
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 287 SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIE 366
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 367 EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRK 446
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
330 340
....*....|....*....|....*.
gi 973353096 447 YRRELQLRKKCHNELVRLKGNIRVIA 472
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
124-450 |
1.52e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 124 LTLQVEHLKEKLISQAQEVSRLRSELGGTDLE---KHRDLLMVENERLRQEMRRCEAelQELrtkpagpcpgcEHSQESA 200
Cdd:pfam07111 268 LQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkKCRSLLNRWREKVFALMVQLKA--QDL-----------EHRDSVK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 201 QLRDKLSQLQ-------------------------LEMAESKGMLSELNLEVQ---QKTDRLAEVELRLKDCLAEKAQEE 252
Cdd:pfam07111 335 QLRGQVAELQeqvtsqsqeqailqralqdkaaeveVERMSAKGLQMELSRAQEarrRQQQQTASAEEQLKFVVNAMSSTQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 253 ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQH---------LQEQVAMQRQVLKEMEQQLQ 323
Cdd:pfam07111 415 IWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScpppppappVDADLSLELEQLREERNRLD 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 324 SSHQLTARLRAQiamyesELERAHGQMLEEMQSLEEDKNRaIEEAFARAQvemkavhENLAGVRTNLLTLQPALRTLTND 403
Cdd:pfam07111 495 AELQLSAHLIQQ------EVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-------ESLASVGQQLEVARQGQQESTEE 560
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 973353096 404 YNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 450
Cdd:pfam07111 561 AASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
128-454 |
1.58e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 128 VEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESA-QLRDKL 206
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQL----------------AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiQYQQAV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 207 SQLQlemaESKGMLSELNLEVQQKTDRLAEVELRlkdclaEKAQEEERLS--RRLRDSHETIASLRAQSPPVKYVIKTVE 284
Cdd:COG3096 420 QALE----KARALCGLPDLTPENAEDYLAAFRAK------EQQATEEVLEleQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 285 VES--SKTKQALSesQARNQ-HLQEQVAMQRQVLKEMEQQLQSSH-------QLTARLRAQIAMYEsELERAHGQMLEEM 354
Cdd:COG3096 490 RSQawQTARELLR--RYRSQqALAQRLQQLRAQLAELEQRLRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQL 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 355 QSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNLLTLQPALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE 434
Cdd:COG3096 567 EELEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARAPAWLA------------------AQDALERLREQSGEALA 623
|
330 340
....*....|....*....|...
gi 973353096 435 ---EVNSNNQELLRKYRRELQLR 454
Cdd:COG3096 624 dsqEVTAAMQQLLEREREATVER 646
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
127-390 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 127 QVEHLKEKLISQAQEVSRLRSELGGTD---LEKHRDLLMVENERLRQEMRRCEaELQELRtkpagpcpgcehsQESAQLR 203
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEealSEKERIIERLKEQREREDRERLE-ELESLK-------------KENKDLK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 204 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAqSPPVKYVI 280
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRI 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 281 KTVEVESSKTKQALSESQARNQHLQE---QVAMQR----QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEE 353
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVERLLGilrEVENEKndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE 640
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 973353096 354 MQSLEEDKNRA-----IEE---AFARAQVEMKAVHENLAGVRTNL 390
Cdd:pfam10174 641 ARRREDNLADNsqqlqLEElmgALEKTRQELDATKARLSSTQQSL 685
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-510 |
2.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 164 ENERLRQEMRRCEAElqelrTKPAGPCPGCEHSQESAQLR---DKLSQLQLEMAESKGMLSELnlevqQKTDRLAEVELR 240
Cdd:PTZ00121 1494 EAKKKADEAKKAAEA-----KKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADEL-----KKAEELKKAEEK 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 241 LKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVEVESS-KTKQALSESQARNQhlQEQVAMQRQVLKEME 319
Cdd:PTZ00121 1564 KK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 320 Q-------------QLQSSHQLTARLRAQIAMYESELERAhgqmLEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagv 386
Cdd:PTZ00121 1637 QlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE----- 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 387 rtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE----LQLRKKCHNELV 462
Cdd:PTZ00121 1707 ----------LKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAE 1771
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 973353096 463 RLKGNIRVIARvRPVTKEDGEGPEATNAVTFDADDDS--IIHLLHKGKPV 510
Cdd:PTZ00121 1772 EIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGGKEGNLV 1820
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
201-356 |
3.37e-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: 40.82 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 201 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyVI 280
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQ-------VRTLREEKERSVSQVQELETSLAELKNQA-----AV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 281 KTVEVES-----SKTKQALSESQARNQHLQEQVAMQRQVlkemeqQLQSSHQLTaRLRAQIAMYESELERA--------- 346
Cdd:pfam15070 69 PPAEEEQppagpSEEEQRLQEEAEQLQKELEALAGQLQA------QVQDNEQLS-RLNQEQEQRLLELERAaerwgeqae 141
|
170
....*....|.
gi 973353096 347 -HGQMLEEMQS 356
Cdd:pfam15070 142 dRKQILEDMQS 152
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-475 |
3.39e-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: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 207 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDShetiasLRAQ 272
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKN------LTVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 273 SPPVKYVIkTVEVESSKTKQA-------------------LSESQARNQHLQEQVAMQRQVLKEMEQQLQ---SSHQLTA 330
Cdd:COG3206 131 PVKGSNVI-EISYTSPDPELAaavanalaeayleqnlelrREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGLVD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 331 rLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHEN--LAGVRTNLLTLQPALRTLTNDYNG 406
Cdd:COG3206 210 -LSEEAKLLLQQLSELESQLAEARAELAEAEARlaALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973353096 407 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLrkyRRELQLRKkchnELVRLKGNIRVIARVR 475
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ---AREASLQA----QLAQLEARLAELPELE 350
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
153-403 |
3.54e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 153 DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpaGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD 232
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLES---GDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 233 RLAEVELRLKDC--LAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktveVESSKTK-QALSESQARNQHLQEQVA 309
Cdd:pfam05622 95 EVLELQHRNEELtsLAEEAQALKDEMDILRESSDKVKKLEAT------------VETYKKKlEDLGDLRRQVKLLEERNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 310 MQRQVLKEMEQQLQSshqlTARLRAQIAMYESELERAHGQMLEEMQSLEedknraieeafaRAQVEMKAVHENLAGV--- 386
Cdd:pfam05622 163 EYMQRTLQLEEELKK----ANALRGQLETYKRQVQELHGKLSEESKKAD------------KLEFEYKKLEEKLEALqke 226
|
250
....*....|....*..
gi 973353096 387 RTNLLTLQPALRTlTND 403
Cdd:pfam05622 227 KERLIIERDTLRE-TNE 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
132-269 |
3.85e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 132 KEKLISQAQEVSRLRSELggtdlekhRDLLMVENERLRQ------EMRRC-EAELQELRTKPAGPCpgcehsQESAQLRD 204
Cdd:smart00787 160 YKLLMKELELLNSIKPKL--------RDRKDALEEELRQlkqledELEDCdPTELDRAKEKLKKLL------QEIMIKVK 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973353096 205 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEerlsRRLRDSHETIASL 269
Cdd:smart00787 226 KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEI----EKLKEQLKLLQSL 286
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-457 |
3.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 198 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSppvk 277
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 278 yviKTVEVESSKTKQALSESQARNQHL----------QEQVAMQRQVLKEMEQQLQSSHQlTARLRAQiaMYESELERAh 347
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE-ECRVAAQ--AHNEEAESL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 348 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 427
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422
|
250 260 270
....*....|....*....|....*....|..
gi 973353096 428 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 457
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
220-344 |
4.24e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 220 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQA 299
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 973353096 300 RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 344
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
203-355 |
4.71e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 203 RDK-LSQLQLEMAESKGMLS-------ELNLEVQQKTDRLAEVEL---RLKDCLAEKAQEEERLSRRLRDSHETIASLRA 271
Cdd:PRK09039 51 KDSaLDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 272 QSppvkyviktvevessktkqalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML 351
Cdd:PRK09039 131 VS---------------------ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....
gi 973353096 352 EEMQ 355
Cdd:PRK09039 190 QELN 193
|
|
| Vps5 |
pfam09325 |
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
203-375 |
8.31e-03 |
|
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.
Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 38.80 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 203 RDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---QSPPV 276
Cdd:pfam09325 54 RKELASATGEFAKSLASLASLELStgLSRALSQLAEVEERIKELLERQALQDVLtLGETIDEYLRLIGSVKAvfnQRVKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 277 KYVIKTVEVESSKTKQALSESQARNQHLQEQVAmqrQVLKEMEqqlqsshqlTARLRAQIAmyESELERAHGQMLEEMQS 356
Cdd:pfam09325 134 WQSWQNAEQELSKKKEQLEKLLRANKSQNDKLQ---QAKKEVE---------ELERRVQQA--EKEFEDISELIKKELER 199
|
170 180
....*....|....*....|..
gi 973353096 357 LEEDKN---RAIEEAFARAQVE 375
Cdd:pfam09325 200 FELERVddfKNSVEIYLESAIE 221
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
211-368 |
8.33e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.74 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 211 LEMAESKGMLSELNLEVQQKTDRLAE----VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEV- 285
Cdd:pfam09731 280 LSNDDLNSLIAHAHREIDQLSKKLAElkkrEEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIr 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 286 ---ESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARlraqiAMYESELERAHGQmLEEMQSLEEDKN 362
Cdd:pfam09731 360 esyEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEER-----AGRLLKLNELLAN-LKGLEKATSSHS 433
|
....*.
gi 973353096 363 RAIEEA 368
Cdd:pfam09731 434 EVEDEN 439
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
120-458 |
8.66e-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: 39.95 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 120 HGLYLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEkhrdllMVENERLRQEMRRCEAElQELRTKPAGPCPgcEHSQES 199
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR------TSAFRDLQGQLAHAKKQ-QELQQRYAELCA--AAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 200 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAE---VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPV 276
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 277 KYVIKTV---EVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSS-------HQLTARLRAQIAMyESELERa 346
Cdd:TIGR00618 531 QRGEQTYaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSkedipnlQNITVRLQDLTEK-LSEAED- 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 347 hgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAgvrtnLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQE----- 420
Cdd:TIGR00618 609 --MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK-----LTALHALQLTLTQERVREHaLSIRVLPKELLAsrqla 681
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 973353096 421 --ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCH 458
Cdd:TIGR00618 682 lqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
196-342 |
9.33e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.29 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 196 SQESAQLRDKLSQLQLEMAESKGMLSELN-LEVQQKTDR--LAE-------------VELRLKdclAEKAQEEERL---- 255
Cdd:PRK11637 85 SQASRKLRETQNTLNQLNKQIDELNASIAkLEQQQAAQErlLAAqldaafrqgehtgLQLILS---GEESQRGERIlayf 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353096 256 -----SRRlrdshETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLqEQVAMQRQ--------VLKEMEQQL 322
Cdd:PRK11637 162 gylnqARQ-----ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKL-EQARNERKktltglesSLQKDQQQL 235
|
170 180
....*....|....*....|
gi 973353096 323 QSSHQLTARLRAQIAMYESE 342
Cdd:PRK11637 236 SELRANESRLRDSIARAERE 255
|
|
| |
