|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
606-933 |
0e+00 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 542.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 606 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFN 684
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 685 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 761
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 762 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 841
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 842 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 921
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 530423880 922 LKFAERVRSVEL 933
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
614-931 |
1.99e-150 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 448.95 E-value: 1.99e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 614 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVCIFAY 690
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 691 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 770
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 771 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 847
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 848 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 925
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 530423880 926 ERVRSV 931
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
608-935 |
6.60e-144 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 432.38 E-value: 6.60e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDVFQEVQA-LVTSCIDGF 683
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 684 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 763
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 764 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 841
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 842 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 919
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 530423880 920 YSLKFAERVRSVELGP 935
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
608-929 |
2.16e-124 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 381.22 E-value: 2.16e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPvtKEDGEGPEATNAVTFDADDDSIIHL--LHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFN 684
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 685 VCIFAYGQTGAGKTYTMEGTAEN-PGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 762
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 763 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 840
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 841 SERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 919
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 530423880 920 YSLKFAERVR 929
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
608-931 |
4.36e-105 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 330.96 E-value: 4.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVT-KEDGEGpeATNAVTFDADDDSIIhlLHKGK------PVSFELDKVFSPQASQQDVFQE-VQALVTSC 679
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 680 IDGFNVCIFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEK 756
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 757 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 832
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 833 LNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 911
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 530423880 912 EKNTSETLYSLKFAERVRSV 931
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
609-932 |
2.61e-103 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 326.21 E-value: 2.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 609 IRVIARVRPVT-KEDGEGPEatNAVTFDADDDSIIhllhKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 686
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 687 IFAYGQTGAGKTYTMEGTA------ENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIR 760
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 761 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 830
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 831 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 907
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 530423880 908 VSPVEKNTSETLYSLKFAERVRSVE 932
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
608-931 |
4.45e-94 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 301.96 E-value: 4.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDADDDSIIHLL----------HKGKPVSFELDKVFSPQASQQDVFQ 670
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 671 E-VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLL 749
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 750 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 828
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 829 --TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 903
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 530423880 904 MVVQVSPVEKNTSETLYSLKFAERVRSV 931
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
608-931 |
8.62e-92 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 295.01 E-value: 8.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVTKEDgegPEATNAVTFDADDDSIIHllHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFNVC 686
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 687 IFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkASDWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 766
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 767 GQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 842
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 843 RVGKSGAEGSRLREAQHINKSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 920
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 530423880 921 SLKFAERVRSV 931
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
608-931 |
2.72e-91 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 293.85 E-value: 2.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVTKEDGEGPeatNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 686
Cdd:cd01369 3 NIKVVCRFRPLNELEVLQG---SKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFaAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 687 IFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGkepQEKLEIRLCP 763
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 764 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSER 843
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 844 VGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSL 922
Cdd:cd01369 237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316
|
....*....
gi 530423880 923 KFAERVRSV 931
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
608-931 |
3.20e-88 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 286.53 E-value: 3.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVTKEDgegPEATNAVTFDADDDS----IIHLLHKGKPV--SFELDKVFSPQASQQDVFQEVQA-LVTSCI 680
Cdd:cd01364 3 NIQVVVRCRPFNLRE---RKASSHSVVEVDPVRkevsVRTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 681 DGFNVCIFAYGQTGAGKTYTMEG--------TAENP---GINQRALQLLFSEVQEkaSDWEYTITVSAAEIYNEVLRDLL 749
Cdd:cd01364 80 MGYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDplaGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 750 GKEPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG- 826
Cdd:cd01364 158 SPSSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 827 --LRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLM 904
Cdd:cd01364 238 eeLVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340
....*....|....*....|....*..
gi 530423880 905 VVQVSPVEKNTSETLYSLKFAERVRSV 931
Cdd:cd01364 318 IATISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
607-931 |
1.30e-86 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 282.70 E-value: 1.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 607 GNIRVIARVRPVTK-EDGEGpeATNAVTFDADDDSIIHL--------LHKGKPVSFELDKVF-------SPQASQQDVFQ 670
Cdd:cd01365 1 ANVKVAVRVRPFNSrEKERN--SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 671 EVQA-LVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASD-WEYTITVSAAEIYNEVLRDL 748
Cdd:cd01365 79 DLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 749 LGKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHAL--LIVTVRGVDC 823
Cdd:cd01365 159 LNPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 824 STGLRT--TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQ 893
Cdd:cd01365 237 ETNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLK 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 530423880 894 DSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 931
Cdd:cd01365 317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
592-932 |
8.15e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 279.32 E-value: 8.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 592 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE 671
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 672 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 750
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 751 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 830
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 831 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 908
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 530423880 909 SPVEKNTSETLYSLKFAERVRSVE 932
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
608-929 |
6.53e-78 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 258.59 E-value: 6.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVTKEDGEGpEATNAVTFDADDDSIihlLHKGKPVSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVC 686
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 687 IFAYGQTGAGKTYTMEGTAENP--------GINQRALQLLFSEVQ---EKASD-WEYTITVSAAEIYNEVLRDLLgkEP- 753
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 754 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 830
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 831 gKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 906
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 530423880 907 QVSPVEKNTSETLYSLKFAERVR 929
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
609-926 |
8.57e-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: 8.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 609 IRVIARVRPVTKEDGEGPEA-------TNAVTFDADDDSIIHLLHKG---KPVSFELDKVFSPQASQQDVFQEV-QALVT 677
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 678 SCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkasdweYTITVSAAEIYNEVLRDLL----GKEP 753
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 754 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 828
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 829 ---TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 900
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 530423880 901 KTLMVVQVSPVEKNTSETLYSLKFAE 926
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
609-929 |
6.24e-73 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 244.41 E-value: 6.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 609 IRVIARVRPVTKEDGEGpeatnaVTFDADDDSI-IHLL---------HKGKPVSFELDKVFSpQASQQDVFQEV-QALVT 677
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLH-NASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 678 SCIDGFNVCIFAYGQTGAGKTYTMEGTAEN---PGINQRALQLLFSEVQEKASDwEYTITVSAAEIYNEVLRDLLGKEPQ 754
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 755 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 829
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 830 TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 908
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 530423880 909 SPVEKNTSETLYSLKFAERVR 929
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
608-929 |
9.14e-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: 240.87 E-value: 9.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVtkEDGEGPEATNAVTFDADDDSII--HLLHKGKPVSFELDKVFSPQASQQDVF-QEVQALVTSCIDGFN 684
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 685 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKAsdWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 764
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 765 GSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 843
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 844 VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 923
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 530423880 924 FAERVR 929
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
608-928 |
9.18e-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: 227.18 E-value: 9.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 608 NIRVIARVRPVTKEDgEGPEATNAVTFDADDDSIIH-------LLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSC 679
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 680 IDGFNVCIFAYGQTGAGKTYTMEG----TAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLgkepQE 755
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 756 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 835
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 836 VDLAGSER-VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 913
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 530423880 914 NTSETLYSLKFAERV 928
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
609-932 |
8.41e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 214.41 E-value: 8.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 609 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVCI 687
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 688 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLgkE 752
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL--D 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 753 P-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT 829
Cdd:PLN03188 248 PsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 830 --TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKT 902
Cdd:PLN03188 326 fkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350
....*....|....*....|....*....|
gi 530423880 903 LMVVQVSPVEKNTSETLYSLKFAERVRSVE 932
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
588-749 |
4.31e-44 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 156.23 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 588 YRRELQLRKKCHNELVRLKGNIRVIARVRPvtkedgegpEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQD 667
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRP---------ELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 668 VFQEVQALVTSCIDGFNVCIFAYGQTGAGktytmegtaENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRD 747
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 530423880 748 LL 749
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
656-875 |
2.37e-23 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 97.80 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 656 DKVFSPQASQQDVFQEVQALVTSCIDGFNV-CIFAYGQTGAGKTYTMEgtaenpGINQRALQLLFSEVQEKASDWEYTIT 734
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 735 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfghTNRTTEfTNLNEHSSRSHALL 814
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423880 815 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegsrlreaqhINKSLSALGDVIAALR 875
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
239-577 |
8.37e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 8.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 239 QLQEELVVLQ-ERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCE 317
Cdd:COG1196 217 ELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 318 AELQELRTkpagpcpGCEHSQE-SAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERL 396
Cdd:COG1196 295 AELARLEQ-------DIARLEErRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 397 SRRLRDSHETIaslraqsppvkyviktvevessktkQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQ 476
Cdd:COG1196 368 LEAEAELAEAE-------------------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 477 IAMYESELERAHGQMLEEMQSLEEDKNRA--IEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 554
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340
....*....|....*....|...
gi 530423880 555 FPLLLQEALRSVKAEIGQAIEEV 577
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-552 |
2.25e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 197 VENTGGRLFGSRRCSSLSG-PPGAAPMVLRMVEAMSQLQDEKTQLQEELVVLQERL-ALRD--SDQQATSTQLQNQVEHL 272
Cdd:TIGR02169 649 FEKSGAMTGGSRAPRGGILfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdELSQelSDASRKIGEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 273 KEKLISQAQEVSRLRSELggtdlekhrDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQL 352
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDL---------SSLEQEIENVKSELKELEARIEELEEDLH------KLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 353 EmaESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESS 429
Cdd:TIGR02169 794 P--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 430 KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQS---------SHQLTARLRAQIAMYE-SELERAHGQMLE------ 493
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqiekkrKRLSELKAKLEALEEElSEIEDPKGEDEEipeeel 951
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530423880 494 --------------EMQSLEEDKNRAIE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 552
Cdd:TIGR02169 952 sledvqaelqrveeEIRALEPVNMLAIQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-576 |
1.75e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 264 QLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQL 343
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 344 RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLS----------RRLRDSHETIASLRAQ 413
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltllnEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 414 sppVKYVIKTVEvESSKTKQALSESQARNQHLQEQvamQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErahgQMLE 493
Cdd:TIGR02168 833 ---IAATERRLE-DLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELE----ELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 494 EMQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND-YNGLKRQVRGFPLLLQEALRSVKaEIGQ 572
Cdd:TIGR02168 902 ELRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLK-RLEN 979
|
....
gi 530423880 573 AIEE 576
Cdd:TIGR02168 980 KIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
223-489 |
4.03e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 223 VLRMVEA---MSQLQDEKTQLQEELVVLQERLALRDSDQQAT---STQLQNQVEHLKEKLISQAQEVSRlrselggtdLE 296
Cdd:TIGR02168 231 VLRLEELreeLEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISR---------LE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 297 KHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 376
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLD------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 377 EVE---LRLKDCLAEKAQEE--------------ERLSRRLRDSHETIASLRAQSPPVKyvIKTVEVESSKTKQALSESQ 439
Cdd:TIGR02168 376 ELEeqlETLRSKVAQLELQIaslnneierlearlERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530423880 440 ARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHG 489
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-516 |
5.77e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 232 QLQDEKTQLQEELVVLQERLALRDSDQQ---ATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENER 308
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 309 LRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 388
Cdd:COG1196 314 LEERLEELEEELAELE-------------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 389 KAQEEERLSRRLRDSHETIASLRAQsppvKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQ 468
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 530423880 469 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 516
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-592 |
6.16e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 265 LQNQVEHLKEKlISQAQEVSRLRSELGgtdlEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaqlr 344
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE-------------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 345 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA---QEEERLSRRLRDSHETIASLRAQsppvkyvI 421
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQ-------L 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 422 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT--------------ARLRAQIAMYESELER- 486
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERl 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 487 -AHGQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRS 565
Cdd:TIGR02168 406 eARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDA 479
|
330 340
....*....|....*....|....*....
gi 530423880 566 VKAEIGQAIEEVNS--NNQELLRKYRREL 592
Cdd:TIGR02168 480 AERELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
247-500 |
1.03e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 72.36 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 247 LQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMvenerlrQEMRRCEAELQELRTk 326
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-------QQLSELESQLAEARA- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 327 pagpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 404
Cdd:COG3206 234 ------------ELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 405 ETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSshqlTARLRAQIAMYESE 483
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLERE 359
|
250
....*....|....*..
gi 530423880 484 LERAHGQMLEEMQSLEE 500
Cdd:COG3206 360 VEVARELYESLLQRLEE 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-514 |
2.41e-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: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQ---ERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 304
Cdd:COG1196 246 AELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 305 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELN---LEVQQKTDRLAEVELR 381
Cdd:COG1196 324 ELAELEEELEELEEELEELE-------------EELEEAEEELEEAEAELAEAEEALLEAEaelAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 382 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQ 461
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 530423880 462 QLQSSHQLTARLRAQIAMYESELERAHGQ--MLEEMQSLEEDKNRAIEEAFARAQ 514
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
590-874 |
4.19e-11 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 66.69 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 590 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDADDDSIihllhKGKPV------------SFELDK 657
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 658 VFSPQASQQDVFQEVQALVTSCIDGfnvcIFAYGQTGAGKTYTMEgtAENPGINQRALQLLFSEVQ-EKASDWEYTITVS 736
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 737 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvddinkvfEFGHTNRTTEFTNLNEHSSRS 810
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--------EKASKLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530423880 811 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGSRLREAQHINKSLSALGDVIAAL 874
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
233-590 |
8.25e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 233 LQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLMVENERL 309
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDLG--NAEDFLEELREERDEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 310 RQEMRRCEAELQELRTK--------PAGPCPGC-------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDr 374
Cdd:PRK02224 425 REREAELEATLRTARERveeaeallEAGKCPECgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 375 LAEVELRLKDcLAEKAqeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQ 454
Cdd:PRK02224 504 LVEAEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 455 VLKEMEQQLQSSHQLTARLrAQIAMYESELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENL 524
Cdd:PRK02224 580 KLAELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDK 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423880 525 AGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 590
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
310-609 |
9.01e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 310 RQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELRLkdclAEK 389
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL----ARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 390 AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQL 469
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 470 TARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK 549
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 550 RQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 609
Cdd:TIGR02168 887 EAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-587 |
2.66e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 231 SQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLR 310
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL--EKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 311 QEMRRCEAELQELRtkpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdclaeka 390
Cdd:TIGR02169 272 QLLEELNKKIKDLG------------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI-------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 391 qeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT 470
Cdd:TIGR02169 332 ---DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 471 ARLRAQIAMYESELERAHgqmlEEMQSLEEDKNrAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR 550
Cdd:TIGR02169 409 DRLQEELQRLSEELADLN----AAIAGIEAKIN-ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350
....*....|....*....|....*....|....*....
gi 530423880 551 QVRGfpllLQEALRSVKAEIGQAIEEVNSN--NQELLRK 587
Cdd:TIGR02169 484 ELSK----LQRELAEAEAQARASEERVRGGraVEEVLKA 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
228-584 |
6.54e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERL--ALRDSDQ-QATSTQLQNQVE------HLKEKLISQAQEVS-RLRSELGGTDLEK 297
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELteARTERDQfSQESGNLDDQLQklladlHKREKELSLEKEQNkRLWDRDTGNSITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 298 hrDLLMVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESA-----QLRDKLSQLQLEMAESKGMLSELNLEVQQKT 372
Cdd:pfam15921 415 --DHLRRELDDRNMEVQRLEALLKAMKSE----CQGQMERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 373 DRLAEVELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQARNQHLQEQVAM 451
Cdd:pfam15921 489 MTLESSERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 452 QRQVLKEMEQQLQSSHQLTA---RLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH--- 521
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvn 639
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530423880 522 ---ENLAGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 584
Cdd:pfam15921 640 agsERLRAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-610 |
2.23e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 223 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQA--TSTQLQNQVEHLKEKLisQAQEVSRLRSELggTDLEKHRD 300
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRL--TGLTPEKLEKEL--EELEKAKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 301 LLMVENERLRQEMRRCEAELQELRT------KPAGPCPGC------EH---------------SQESAQLRDKLSQLQLE 353
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKaieelkKAKGKCPVCgrelteEHrkelleeytaelkriEKELKEIEEKERKLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 354 MAESKGMLS-ELNLEVQQKT-DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIASLRAQsppvkyvIKTVEVESSKT 431
Cdd:PRK03918 482 LRELEKVLKkESELIKLKELaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIKLKGE-------IKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 432 KQALSESQARNQHLQEQVAMQRQVLKEMEQQ-LQSSHQLTARLRaqiamyesELERAHGQMLEEMQSleEDKNRAIEEAF 510
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLK--------ELEPFYNEYLELKDA--EKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 511 ARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVKAEIGQA---IEEVNSNNQEL-- 584
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELekrREEIKKTLEKLke 701
|
410 420 430
....*....|....*....|....*....|
gi 530423880 585 ----LRKYRRELQLRKKCHNELVRLKGNIR 610
Cdd:PRK03918 702 eleeREKAKKELEKLEKALERVEELREKVK 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
230-614 |
3.09e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 230 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQ-----------AQEVSRLRSELggtdLEKH 298
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQnsmymrqlsdlESTVSQLRSEL----REAK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 299 RdllMVEN--ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKgmlSELNLEVQQKT---- 372
Cdd:pfam15921 338 R---MYEDkiEELEKQLVLANSELTEARTERD------QFSQESGNLDDQLQKLLADLHKRE---KELSLEKEQNKrlwd 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 373 -----------------DRLAEVElRLKDCL-AEKAQEEERLSRRL------RDSHETIASLRAQSPPVKYVIKTVEVES 428
Cdd:pfam15921 406 rdtgnsitidhlrreldDRNMEVQ-RLEALLkAMKSECQGQMERQMaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 429 SKTKQALSESQARNQHLQEQvamqrqvLKEMEQQLQSSHQLTARLRAQIAMYESELE--RAHGQMLEEMQSLEE------ 500
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTAS-------LQEKERAIEATNAEITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEalklqm 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 501 -DKNRAIEeaFARAQVE----MKAVHENLAGvrtnllTLQPALRTLTNDYNGLKRQVRGFPLLLQE---ALRSVKAEIG- 571
Cdd:pfam15921 558 aEKDKVIE--ILRQQIEnmtqLVGQHGRTAG------AMQVEKAQLEKEINDRRLELQEFKILKDKkdaKIRELEARVSd 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 530423880 572 ---QAIEEVNSNNQEL--LRKYRRE----LQLRKKCHNELVRLKGNIRVIAR 614
Cdd:pfam15921 630 lelEKVKLVNAGSERLraVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKR 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
228-413 |
7.56e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQE-RLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVEN 306
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL--DALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 --------ERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEV 378
Cdd:COG4913 333 rgnggdrlEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|....*
gi 530423880 379 ELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ 413
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
231-597 |
2.69e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 231 SQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENE 307
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 308 RLRQemrrceaelqelrtkpagpcpgcehsQEsaqlrDKLSQLQLEMAESKGMLSELNLEVQQktdrlaevelrLKDCLA 387
Cdd:TIGR04523 315 ELKN--------------------------QE-----KKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 388 EKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQssh 467
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 468 qltaRLRAQIAMYESELERahgqMLEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 544
Cdd:TIGR04523 430 ----RLKETIIKNNSEIKD----LTNQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 530423880 545 YNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKyrrELQLRKK 597
Cdd:TIGR04523 498 LKKLNEEKK----ELEEKVKDLTKKISSLKEKIEKLESEKKEK---ESKISDL 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-520 |
4.70e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 305 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 384
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 385 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPP---------VKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 450
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 451 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 520
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 ... |
229-576 |
6.08e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.11 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 229 AMSQLQDEKTQLQEELVVLqeRLALRDS-----DQQATSTQLQNQVEHLKEKL---------------ISQAQEVSRLRS 288
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEAL--KTELEDTldttaAQQELRSKREQEVTELKKALeeetrsheaqlqemrQKHTQALEELTE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 289 EL-----GGTDLEKHRDLLMVENERLRQEMR--------------RCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQ 349
Cdd:pfam01576 364 QLeqakrNKANLEKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQARLS------ESERQRAELAEKLSK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 350 LQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSPPVKYVIKTVE 425
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 426 VESSKTKQALSESQARnqhlQEQVAMQRQVLKEMEQQLQS-SHQLTARLRAQIAMYEsELERAHGQMLEEMQSL--EEDK 502
Cdd:pfam01576 517 RQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQReLEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDH 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 503 NRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALR 564
Cdd:pfam01576 592 QRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQLRAEM-EDLV 670
|
410
....*....|..
gi 530423880 565 SVKAEIGQAIEE 576
Cdd:pfam01576 671 SSKDDVGKNVHE 682
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
219-593 |
7.52e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 219 AAPMVLRMVEAMSQlQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKH 298
Cdd:PRK04863 333 ASDHLNLVQTALRQ-QEKIERYQADLEELEERLE----EQNEVVEEADEQQEENEARAEAAEEEVDELKSQL--ADYQQA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 299 RDLLMVENERLRQEMRRCEaELQELRTKPAgpcpgcehsqesaqlrdklsqlqLEMAESKGMLSELNLEVQQKTDRLAEV 378
Cdd:PRK04863 406 LDVQQTRAIQYQQAVQALE-RAKQLCGLPD-----------------------LTADNAEDWLEEFQAKEQEATEELLSL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 379 ELRLKDCLAEKAQEEE--RLSRRLRDshetiaslraqsppvkyviktvEVESSKTKQALSE--SQARNQ-HLQEQVAMQR 453
Cdd:PRK04863 462 EQKLSVAQAAHSQFEQayQLVRKIAG----------------------EVSRSEAWDVAREllRRLREQrHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 454 QVLKEMEQQLQSSHQLTARLR----AQIAMY--ESELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLA 525
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLAefckRLGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423880 526 GVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 593
Cdd:PRK04863 600 ARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-577 |
1.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 303 MVEN----ERLRQEMRRCEAELQELRtkpagpcPGCEHSQESAQLRDKLSQLQLemaeskgMLSELNLEVQQKTDRLAEV 378
Cdd:COG4913 230 LVEHfddlERAHEALEDAREQIELLE-------PIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 379 EL-RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqALSESQARNQHLQEQVAMQRQVLK 457
Cdd:COG4913 296 ELeELRAELARLEAELERLEARLDALREELDELEAQ--------------------IRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 458 EMEQQLQSSHQLTARLRAQIAMYESELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 537
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530423880 538 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 577
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
230-606 |
1.24e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 55.47 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 230 MSQLQDEKTQLQEELVVLQERLALRDSDQQATS------TQLQNQVEHLKEKL--ISQAQEVSRLRSElggtDLEKHRDL 301
Cdd:pfam05622 23 VSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 302 LMVENERLR---QEMRRCEAELQELRtkpagpcpgcehsqESAqlrDKLSQLQLEMAESKGMLSELN-LEVQQKTdrlae 377
Cdd:pfam05622 99 LQHRNEELTslaEEAQALKDEMDILR--------------ESS---DKVKKLEATVETYKKKLEDLGdLRRQVKL----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 378 velrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSE---SQARNQHLQ---EQVAM 451
Cdd:pfam05622 157 ----LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQkekERLII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 452 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEedknraIEEAFARAQVEMKAVHENLAGvrtNL 531
Cdd:pfam05622 233 ERDTLRETNEELRCAQLQQAELSQADALLSPSSD-PGDNLAAEIMPAE------IREKLIRLQHENKMLRLGQEG---SY 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530423880 532 LTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRsvkaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 606
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNRLANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-607 |
1.51e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 227 VEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEK------LISQAQEVSRLR---------SELG 291
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKVKELKELKekaeeyiklSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 292 GTDLEKHRDlLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNlEVQQK 371
Cdd:PRK03918 303 EEYLDELRE-IEKRLSRLEEEINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELYE-EAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 372 TDRLAEVELRLKDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTV-----EVESSKTKQALSESQARNQHL 445
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELkkaieELKKAKGKCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 446 QEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELER-----AHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 520
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 521 HENLAGVRTNLLTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHN 600
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
....*..
gi 530423880 601 ELVRLKG 607
Cdd:PRK03918 603 EYLELKD 609
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-614 |
1.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 273 KEKLISQAQEVSRLRSELGGTDLEKHR--DLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaQLRDKLSQL 350
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELE-----------------ELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 351 QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEKAQEEERLSR-------RLRDSHETIASLRAQS 414
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 415 PPVKYVIKtvevESSKTKQALSESQARNQHLQEQVAmqrqVLKEMEQQLQSSHQLTA---RLRAQIAMYESE-------- 483
Cdd:PRK03918 324 NGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHELYEEAKAKKEeleRLKKRLTGLTPEklekelee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 484 LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----------------MKAVHENLAGVRTNLLTLQPA 537
Cdd:PRK03918 396 LEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530423880 538 LRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 614
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-487 |
1.85e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenE 307
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQEL----------------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 308 RLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQlQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdcLA 387
Cdd:COG4942 80 ALEAELAELEKEIAELR-------------AELEAQKEELAE-LLRALYRLGRQPPLALLLSPEDFLDAVRRLQY---LK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 388 EKAQEEERLSRRLRDSHETIASLRAQsppvkyviktVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSH 467
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAE----------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|
gi 530423880 468 QLTARLRAQIAMYESELERA 487
Cdd:COG4942 213 AELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-399 |
2.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 174 LWKRQAPAPRRAREAREAGGTMNVENTGGRLFGSRRCSSLSGPPGAAPMVLRMVEAMSQLQDEKTQLQEEL---VVLQER 250
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqleELEQEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 251 LALRDSDQQATSTQLQNQVEHlKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagp 330
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE------ 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530423880 331 cpgcehsQESAQLRDKLSQL--QLEMAESKGMLSELNLEVQQKTDRLAEVE-----LRLKDCLAEKAQEEERLSRR 399
Cdd:COG4717 446 -------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAeewaaLKLALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-595 |
4.03e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 232 QLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQN-----QVEHLKEKLISQAQEVSRLRSELggtdleKHRDLLMVEN 306
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQEMRRCEAELQELRTKPAGpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdcl 386
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 387 aEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQARNQHLQEQVA 450
Cdd:COG4717 237 -EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 451 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEmkavheNLAGVRt 529
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVE------DEEELR- 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423880 530 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 595
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
374-606 |
4.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 374 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQR 453
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 454 QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 531
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530423880 532 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 606
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-597 |
5.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLAL---RDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLMV 304
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 305 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE---LR 381
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEE------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeeeEA 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 382 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARnqHLQEQVAMQRQVLKEMEQ 461
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 462 QL---------QSSHQLTARLRAQIAMYESE-LERAHGQMLEEMQ--SLEEDKNRAIEEAFARAQVEMKAVHENLAgVRT 529
Cdd:COG1196 539 ALeaalaaalqNIVVEDDEVAAAAIEYLKAAkAGRATFLPLDKIRarAALAAALARGAIGAAVDLVASDLREADAR-YYV 617
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530423880 530 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 597
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-610 |
1.81e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 231 SQLQDEKTQLQEELVVLQERLA---LRDSDQQATSTQLQNQ------VEHLKEKLISQAQEVSRLRSELggTDLEKHRDl 301
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGelkLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSEL--RQARKRRD- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 302 lmVENERLRQEMRRCE---AELQELRTKpAGPCPGCEH---SQESAQLRDKLSQL-QLEMAESKGMLSELNLEVQQKTDR 374
Cdd:pfam12128 503 --QASEALRQASRRLEerqSALDELELQ-LFPQAGTLLhflRKEAPDWEQSIGKViSPELLHRTDLDPEVWDGSVGGELN 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 375 LAEVELRLKDCLA-EKAQEEERLSRR-------LRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQAR----- 441
Cdd:pfam12128 580 LYGVKLDLKRIDVpEWAASEEELRERldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlf 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 442 NQHLQEQVAMQRQV---LKEMEQQLQS-SHQLTARLRAQIAMYES---ELERAHGQMLEEMQSLEEDKNRA---IEEAFA 511
Cdd:pfam12128 660 DEKQSEKDKKNKALaerKDSANERLNSlEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVVEGALDAQlalLKAAIA 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 512 RAQVEMKA--------VHENLAGV---RTNLLTLQPALRTLT---NDYNGLKRQVRGFPLLLQE-------ALRSVKAEI 570
Cdd:pfam12128 740 ARRSGAKAelkaletwYKRDLASLgvdPDVIAKLKREIRTLErkiERIAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNI 819
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 530423880 571 GQAIEEVNSNNQELLRKYRRELQL----RKKCHNELVRLKGNIR 610
Cdd:pfam12128 820 ERAISELQQQLARLIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-416 |
2.60e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLIS--QAQEVSRLRSELGGTDLEKH-RDLLMV 304
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAvRRLQYL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 305 E--NERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRL 382
Cdd:COG4942 142 KylAPARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|....
gi 530423880 383 KDCLAEKAQEEERLSRRLRDSHETIASLRAQSPP 416
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
228-594 |
3.11e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQ---NQVEHLKEKLISQAQEVSRLRS--ELGGTDLEKH---- 298
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAahSFVVTEFEATtcsl 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 299 RDLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELN--LEVQQKTDRLA 376
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKK----------SSELEEMTKFKNNKEVELEELKKILAEDEklLDEKKQFEKIA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 377 EvELrlkdclaeKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKtvEVESSKTKqaLSESQARNQHLQEQVAMqr 453
Cdd:pfam05483 432 E-EL--------KGKEQELiflLQAREKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTE--LEKEKLKNIELTAHCDK-- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 454 qVLKEMEQQLQSSHQLTARLRAQ---IAMYESELERahgqMLEEMQSLEE------DKNRAIEEAFARAQVEMKA----V 520
Cdd:pfam05483 497 -LLLENKELTQEASDMTLELKKHqedIINCKKQEER----MLKQIENLEEkemnlrDELESVREEFIQKGDEVKCkldkS 571
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530423880 521 HENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 594
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
341-618 |
3.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 341 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyv 420
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 421 iktvevessktKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEE 500
Cdd:COG4913 677 -----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 501 DKNRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAI 574
Cdd:COG4913 746 ELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYL 818
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530423880 575 EEVNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 618
Cdd:COG4913 819 ALLDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
293-414 |
5.96e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 293 TDLEKHRDLLMVENERLRQEMRRC--------------EAELQELR--TKPAGPCPgcehSQESAQLRDKLSQLQLEMAE 356
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLnsikpklrdrkdalEEELRQLKqlEDELEDCD----PTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530423880 357 SKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 414
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-590 |
6.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 223 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRdSDQQATSTQLQNQVEHLKEKLiSQAQEVSRLRSELGGTDLEKHRDLL 302
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEEL-EELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 303 MVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESAQLRDKLSQLQLeMAESKGMLSELNLEVQQKTDRLAEVELRL 382
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEE----LEQLENELEAAALEERLKEARL-LLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 383 KDCLA---------EKAQEEERLSRRLRDSHETIASLRAQSppVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQR 453
Cdd:COG4717 280 FLVLGllallflllAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 454 QVLKEMEQQlQSSHQLTARLRAQIAMYESELERAHGQmLEEMQSLEEDKNRAIEE-AFARAQVEMKAVHENLAGVRTNLL 532
Cdd:COG4717 358 ELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELE 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530423880 533 TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVK-AEIGQAIEEVNSNNQELLRKYRR 590
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAA 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
231-508 |
6.14e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 231 SQLQDEKTQLQ---EELVVlqERLALRDSDQqaTSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrDLLMVENE 307
Cdd:pfam15921 468 AQLESTKEMLRkvvEELTA--KKMTLESSER--TVSDLTASLQEKERAIEATNAEITKLRSRV---------DLKLQELQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 308 RLRQE---MRRCEAELQELRTKPAGPCPGCE---------------HSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQ 369
Cdd:pfam15921 535 HLKNEgdhLRNVQTECEALKLQMAEKDKVIEilrqqienmtqlvgqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 370 QKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLRAQSPPVK--YVIKTVEVESSK 430
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKrnFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 431 TKQALSESQArnqhlQEQVAMQRQVLKEMEQQ--------LQSSHQLTARlRAQIAMYESE---LERAHGQMLEEMQSLE 499
Cdd:pfam15921 695 NKLKMQLKSA-----QSELEQTRNTLKSMEGSdghamkvaMGMQKQITAK-RGQIDALQSKiqfLEEAMTNANKEKHFLK 768
|
....*....
gi 530423880 500 EDKNRAIEE 508
Cdd:pfam15921 769 EEKNKLSQE 777
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
226-604 |
6.82e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 226 MVEAMSQLQDEKTQLQEELVVLQERLALRdSDQQATSTQlqnQVEHLKEKLISQAQEVSRLRSELggtdlekhrDLLMVE 305
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETL-TNQNSDCKQ---HIEVLKESLTAKEQRAAILQTEV---------DALRLR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 306 NERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRD--------KLSQLQLEMAESKGMLSELNLEVQQ-KTDR-- 374
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKErkinvlqkKIENLQEQLRDKDKQLAGLKERVKSlQTDSsn 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 375 ----LAEVElrlkDCLAEKAQEEERL----SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQ 446
Cdd:pfam10174 434 tdtaLTTLE----EALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 447 EQVAMQRQVLKEMEQQLQSSHQLTARLRAQI--AMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMkavhENL 524
Cdd:pfam10174 510 SSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEES-GKAQAEV----ERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 525 AGvrtnlltlqpALRTLTNDYNGLKRQVRGFPLLlqeALRSVKaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 604
Cdd:pfam10174 585 LG----------ILREVENEKNDKDKKIAELESL---TLRQMK-EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
224-508 |
7.48e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.29 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 224 LRMVEAMSQLQDEKTQLQEELVVLQERLALRDSdQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGG--TDLEKHRDL 301
Cdd:PLN02939 152 LQALEDLEKILTEKEALQGKINILEMRLSETDA-RIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLcvHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 302 LMVENERLRQEMRRCEAELQELrtkpagpcpgcehsqesAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELR 381
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEV-----------------AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 382 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEvESSKTKQALSESqarnqhlQEQVAMQRQVLKEMEQ 461
Cdd:PLN02939 294 QYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE-ASLKEANVSKFS-------SYKVELLQQKLKLLEE 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 530423880 462 QLQSSHQltaRLRAQIAMYESELERAHgqmlEEMQSL-EEDKNRAIEE 508
Cdd:PLN02939 366 RLQASDH---EIHSYIQLYQESIKEFQ----DTLSKLkEESKKRSLEH 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
223-513 |
1.15e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 223 VLRMVEAMSQLQDEKTQLQEELVVLQERLAL---RDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHR 299
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL--LEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 300 DLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 379
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQ----------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 380 LRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEm 459
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAA------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA- 517
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 530423880 460 eqQLQSSHQLTARLRAQIAMYESELE-RAHGQMLEEMQSLEEDKNRAIEEAFARA 513
Cdd:COG1196 518 --GLRGLAGAVAVLIGVEAAYEAALEaALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
221-516 |
1.73e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 221 PMVLRMVEAMSQlQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHL--KEKLISQAQEVSRLRSelggtdlekh 298
Cdd:pfam17380 227 PHTLAPYEKMER-RKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIvqHQKAVSERQQQEKFEK---------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 299 rdllmVENERLRQEMRRCEAELQELRTkpagpcpgCEHSQESAQLR-DKLSQLQLEMaESKGMLSELNLEVQQKTDRLAE 377
Cdd:pfam17380 296 -----MEQERLRQEKEEKAREVERRRK--------LEEAEKARQAEmDRQAAIYAEQ-ERMAMERERELERIRQEERKRE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 378 VELRLKDCLA---EKAQEEERL-------SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARN-QHLQ 446
Cdd:pfam17380 362 LERIRQEEIAmeiSRMRELERLqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLE 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530423880 447 EQVA--MQRQVLKEMEQQLQSS---HQLTARLRAQIAMYESELERAHGQMLEEM---QSLEEDKNRAIEEAFARAQVE 516
Cdd:pfam17380 442 EERAreMERVRLEEQERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
273-472 |
1.80e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.83 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 273 KEKLISQAQEVSRLRSELGGT-------DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpagpcpgcEHSQESAQLRD 345
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEA---------QQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 346 KLSQLQLEMAESKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 425
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530423880 426 VESSKTKQALSESQARNQHLQEQVAMQRQV----LKEMEQQLQSSHQLTAR 472
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQGEGSN 216
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
341-595 |
1.94e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 341 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYV 420
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 421 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQsleE 500
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE---A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 501 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSN 580
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*
gi 530423880 581 NQELLRKYRRELQLR 595
Cdd:COG4372 260 IEELELAILVEKDTE 274
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
240-534 |
3.30e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 240 LQEELVVLQERLALRDSDQQATStqLQNQVEhlKEKLISQAQEVSRLRSELG-----GTDLEKHRDLLMVENERLR---- 310
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIK--LQKTIK--REKKLRETEEVEFSLKAEVliqkfGRSLKAKKRFSLLKKETIYlqsa 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 311 QEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAE-SKGMLSELNLEVQQKTDRLAEVElrlkdCLAEK 389
Cdd:COG5022 875 QRVELAERQLQELK----------IDVKSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLK-----KLLNN 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 390 AQEEERLSRRLRDS------HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV----AMQRQV--LK 457
Cdd:COG5022 940 IDLEEGPSIEYVKLpelnklHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSkqygALQESTkqLK 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 458 EMEQQLQSSHQLTARLRA-----QIAMYESELERAHgqMLEEMQSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLL 532
Cdd:COG5022 1020 ELPVEVAELQSASKIISSestelSILKPLQKLKGLL--LLENNQLQARYKALKLRR---ENSLLDDKQLYQLESTENLLK 1094
|
..
gi 530423880 533 TL 534
Cdd:COG5022 1095 TI 1096
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
224-595 |
3.99e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 224 LRMVEAMSQLQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLM 303
Cdd:COG3096 336 LNLVQTALRQQEKIERYQEDLEELTERLE----EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 304 VENERLRQEMRRCEaELQELrtkpagpcpgCEhsqesaqlrdkLSQLQLEMAEskGMLSELNLEVQQKTDRLAEVELRLK 383
Cdd:COG3096 410 TRAIQYQQAVQALE-KARAL----------CG-----------LPDLTPENAE--DYLAAFRAKEQQATEEVLELEQKLS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 384 DCLAEKAQEEERLsrrlrdshetiASLRAQSPPVkyvikTVEVESSKTKQALSesQARNQ-HLQEQVAMQRQVLKEMEQQ 462
Cdd:COG3096 466 VADAARRQFEKAY-----------ELVCKIAGEV-----ERSQAWQTARELLR--RYRSQqALAQRLQQLRAQLAELEQR 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 463 LQSSH-------QLTARLRAQIAMYEsELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNLLTLQ 535
Cdd:COG3096 528 LRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARA 601
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530423880 536 PALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 595
Cdd:COG3096 602 PAWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
236-591 |
4.35e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.44 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 236 EKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLE---KHRDLLMVENERLRQE 312
Cdd:pfam07111 243 ERQELLDTMQHLQEDRA----DLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkKCRSLLNRWREKVFAL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 313 MRRCEAelQELrtkpagpcpgcEHSQESAQLRDKLSQLQ-------------------------LEMAESKGMLSELNLE 367
Cdd:pfam07111 319 MVQLKA--QDL-----------EHRDSVKQLRGQVAELQeqvtsqsqeqailqralqdkaaeveVERMSAKGLQMELSRA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 368 VQ---QKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQH 444
Cdd:pfam07111 386 QEarrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 445 ---------LQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQiamyesELERAHGQMLEEMQSLEEDKNRaIEEAFARAQv 515
Cdd:pfam07111 466 cpppppappVDADLSLELEQLREERNRLDAELQLSAHLIQQ------EVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530423880 516 emkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 591
Cdd:pfam07111 538 ------ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
225-478 |
4.65e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 225 RMVEAMSQLQDEKTQLQEElvvlQERlALRDSDQQATSTQLQNQVEhlkeKLISQAQevSRLRSELGGTDLEKHRDLLMV 304
Cdd:PRK10929 110 EILQVSSQLLEKSRQAQQE----QDR-AREISDSLSQLPQQQTEAR----RQLNEIE--RRLQTLGTPNTPLAQAQLTAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 305 ENERLRQEMRRCEAELQELrtkpagpcpgcehsqeSAQLRDKLSQLQLEMAESK---------GMLSELNLEVQQKTDR- 374
Cdd:PRK10929 179 QAESAALKALVDELELAQL----------------SANNRQELARLRSELAKKRsqqldaylqALRNQLNSQRQREAERa 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 375 LAEVELrlkdcLAEKAQE-EERLSRRLRDSHETIASLRAQSppvkyviKTVEVESSKTKQALSESQarnqhlqeQVamqR 453
Cdd:PRK10929 243 LESTEL-----LAEQSGDlPKSIVAQFKINRELSQALNQQA-------QRMDLIASQQRQAASQTL--------QV---R 299
|
250 260
....*....|....*....|....*...
gi 530423880 454 QVL---KEMEQQLQSSHQLTARLRAQIA 478
Cdd:PRK10929 300 QALntlREQSQWLGVSNALGEALRAQVA 327
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
230-531 |
5.13e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 230 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEK---LISQAQEVSRLRSELGGTDL----------E 296
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKdkqLAGLKERVKSLQTDSSNTDTalttleealsE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 297 KHRDLLMVENERLRQEMRRCEaELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 376
Cdd:pfam10174 448 KERIIERLKEQREREDRERLE-ELESLK-------------KENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 377 EVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAqSPPVKYVIKTVEVESSKTKQALSESQARNQHLQE---QVA 450
Cdd:pfam10174 514 KKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRIRLLEQEVARYKEESGKAQAEVERLLGilrEVE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 451 MQR----QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-----IEE---AFARAQVEMK 518
Cdd:pfam10174 593 NEKndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNsqqlqLEElmgALEKTRQELD 672
|
330
....*....|...
gi 530423880 519 AVHENLAGVRTNL 531
Cdd:pfam10174 673 ATKARLSSTQQSL 685
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
387-595 |
5.28e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 387 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALsesqarnqhLQEQVAMQRQVLKEMEQQLQSS 466
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 467 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 532
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530423880 533 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 595
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-604 |
6.58e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 311 QEMRRCEAELQELRTKPAgpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 388
Cdd:COG4717 71 KELKELEEELKEAEEKEE----------EYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 389 KAQEEERLsRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQARNQhlQEQVAMQRQVLKEMEQQLQSSHQ 468
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE------------------LEELEAELAELQ--EELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 469 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGL 548
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530423880 549 KRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 604
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
307-578 |
6.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ--LEMAESKGMLSELNLEVQQKTDRLAEVEL---- 380
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE------ALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 381 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQARNQHLQEQV--AM 451
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 452 QRQVLKEMEQQLQSShqlTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 531
Cdd:COG4913 760 GDAVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 530423880 532 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 578
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
337-601 |
7.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 337 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 414
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 415 PPVKYVIKTVEVESS-------KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERa 487
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 488 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 564
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 530423880 565 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 601
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
231-509 |
7.62e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 231 SQLQDEKTQLQEelvvLQERLalrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSElggtdlekhRDLLMVENERLR 310
Cdd:pfam05622 183 GQLETYKRQVQE----LHGKL----SEESKKADKLEFEYKKLEEKLEALQKEKERLIIE---------RDTLRETNEELR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 311 qemrrCeAELQELRTKPAGPCPGCEHSQE--------SAQLRDKLSQLQLEmaesKGMLSELnlEVQQKTDRLAEVELRL 382
Cdd:pfam05622 246 -----C-AQLQQAELSQADALLSPSSDPGdnlaaeimPAEIREKLIRLQHE----NKMLRLG--QEGSYRERLTELQQLL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 383 KDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVESSKT------KQALSESQARNQHLQEQVAMQRQVL 456
Cdd:pfam05622 314 ED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHEAQSELQKKKEQI 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 530423880 457 KEMEQQLQSSHQLTArlraqiamyeSELERAHGQMLEEMQSLEEDKNRAIEEA 509
Cdd:pfam05622 387 EELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
239-552 |
7.71e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 239 QLQEELVVLQERLALRDSDQQatstQLQNQVEHLKEKLISQA------------QEVSRLRSELGgTDLEKHRDllmvEN 306
Cdd:PRK04863 790 QLRAEREELAERYATLSFDVQ----KLQRLHQAFSRFIGSHLavafeadpeaelRQLNRRRVELE-RALADHES----QE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQL-RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVElRLKDC 385
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALN----------RLLPRLNLLaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE-PIVSV 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 386 LAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE-------VESSKTKQALSES-QARNQHLQEQVAMQRQVLK 457
Cdd:PRK04863 930 LQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKNSDLNEKlRQRLEQAEQERTRAREQLR 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 458 EMEQQLQSSHQLTARLRAQIamyeseleRAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRT------- 529
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAEERARARRDELHARLSANRSrrnqlek 1081
|
330 340 350
....*....|....*....|....*....|
gi 530423880 530 -------NLLTLQPALRTLTNDYNGLKRQV 552
Cdd:PRK04863 1082 qltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
263-589 |
7.72e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 263 TQLQNQVEHLKEkLISQAQEVsrLRSELggTDLEK-HRDL-----------LMVENERLRQEMRRCEAELQELRTKPAgp 330
Cdd:PRK04778 208 AALEQIMEEIPE-LLKELQTE--LPDQL--QELKAgYRELveegyhldhldIEKEIQDLKEQIDENLALLEELDLDEA-- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 331 cpgcehSQESAQLRDKL----SQLQLEMAESKgmlselnlEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHET 406
Cdd:PRK04778 281 ------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 407 IASLRAQSPPVKYVIKTVEVesskTKQALSESQARNQHLQEQVAMQRQVLKEME-QQLQSSHQLtarlraqIAMYESELE 485
Cdd:PRK04778 347 LESVRQLEKQLESLEKQYDE----ITERIAEQEIAYSELQEELEEILKQLEEIEkEQEKLSEML-------QGLRKDELE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 486 rAHgQMLEEMQS-LEEDKnRAIE------------EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR-- 550
Cdd:PRK04778 416 -AR-EKLERYRNkLHEIK-RYLEksnlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEet 492
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 530423880 551 -----QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRKYR 589
Cdd:PRK04778 493 eelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFREYD 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
231-603 |
8.42e-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: 46.55 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 231 SQLQDEKTQLQEELVV---LQERLALRDSDQQatstQLQNQVEHLKEKLISQAQEVSRLRS-----ELGGTDLEKHRDLL 302
Cdd:TIGR04523 391 SQINDLESKIQNQEKLnqqKDEQIKKLQQEKE----LLEKEIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 303 MVENERLRQEMRRCEAEL----QELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEV 378
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLeqkqKELKSK----------EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 379 ELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKE 458
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKEN----------------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 459 MEQQLQSSHQLTARLRAQIamyeSELERAHGQMLEEMQSLEEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQ 535
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKEL----EKAKKENEKLSSIIKNIKSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKI 668
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423880 536 PALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIEevNSNNQELLRKYR---RELQLRKKCHNELV 603
Cdd:TIGR04523 669 KESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR--IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
228-499 |
1.10e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLALRD--SDQQATSTQLQNQVEHLKE--KLISQAQEVSRLR------SELGGTDLEK 297
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQllKQLRARIEELRAQEAVLEEtqERINRARKAAPLAahikavTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 298 HRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESaQLRDKLSQLQLEMAESKGMLSELN--LEVQQKTDRL 375
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI-HIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 376 AEVELRLKDCL----AEKAQEEERLSRRlRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQARNQHLQEqvam 451
Cdd:TIGR00618 392 TQKLQSLCKELdilqREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE---- 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 530423880 452 QRQVLKEMEQQLQSSHQLTARlraqiamyESELERAHGQMLEEMQSLE 499
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEP 503
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
399-606 |
1.29e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 399 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQAR--------NQHLQEQVAMQRQVLK-EMEQQLQS 465
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 466 SH-----QLTARLRAQIAMYESELErahgqMLEE-------MQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVR 528
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFQKVIK-----MYEKggvcptcTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIM 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530423880 529 TNLLTLQPALRTLTNDYNGLKRQVrgfpLLLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 606
Cdd:PHA02562 330 DEFNEQSKKLLELKNKISTNKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
225-578 |
1.51e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 225 RMVEAMSQL--QDEK-----TQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLisqaQEVSRLRSElgGTDLEK 297
Cdd:PRK04778 123 QILEELQELleSEEKnreevEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTES--GDYVEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 298 HRDLLMVENE--RLRQEMRRCEAELQELRTKpagpcpgcehsqesaqLRDKLSQLQL---EMAESKGMLSELNL--EVQQ 370
Cdd:PRK04778 197 REILDQLEEElaALEQIMEEIPELLKELQTE----------------LPDQLQELKAgyrELVEEGYHLDHLDIekEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 371 KTDRLAEVELRLKDC-LAEKAQEEERLSRRLRDSHETIAslraqsppvKYVI--KTVEVESSKTKQALSESQARNQHLQE 447
Cdd:PRK04778 261 LKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDILE---------REVKarKYVEKNSDTLPDFLEHAKEQNKELKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 448 QVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQ-----MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHE 522
Cdd:PRK04778 332 EIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRK 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423880 523 NLAGVRTNLLTLQPALRTltndyngLKRQVR-----GFPLLLQEALRSVKAEIGQAIEEVN 578
Cdd:PRK04778 412 DELEAREKLERYRNKLHE-------IKRYLEksnlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
338-514 |
1.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 338 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 410
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 411 RAQSPP-----VKYViKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 485
Cdd:COG3883 110 GSESFSdfldrLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 530423880 486 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 514
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
228-388 |
1.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQ-----LQNQVEHLKE---KLISQAQEVSRLRSELggTDLEKHR 299
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDAssdDLAALEEQLEELEAEL--EELEEEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 300 DLLMVENERLRQEMRRCEAELQELRTKpAGPCPGCEHSQESAQLRDKLSQLQLEMAESKgMLSELNLEVQQKTDRLAEVE 379
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDR-LEAAEDLARLELRALLEERFAAALGDAVERE-LRENLEERIDALRARLNRAE 786
|
....*....
gi 530423880 380 LRLKDCLAE 388
Cdd:COG4913 787 EELERAMRA 795
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
301-621 |
2.04e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 301 LLMVENERLRQEMRRcEAELQELRTKPAGPCPGCEH-SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 379
Cdd:pfam05557 11 LSQLQNEKKQMELEH-KRARIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 380 LRLKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQARNQHLQEQVAMQRQVLKEM 459
Cdd:pfam05557 90 KKLN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 460 EQ---QLQSSHQLTA-------RLRAQIAMYES----------------ELERAHGQMLEE---MQSLEEDKNRAIEEAF 510
Cdd:pfam05557 152 EQlrqNLEKQQSSLAeaeqrikELEFEIQSQEQdseivknskselaripELEKELERLREHnkhLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 511 araqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL 584
Cdd:pfam05557 232 -----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 530423880 585 --LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 621
Cdd:pfam05557 307 rqLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
227-473 |
2.07e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 227 VEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELG--GTDLEKHRDLLMV 304
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAqrDTQVLQLQDTITT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 305 ENERLRQEMRRcEAELQELRTKPAGPCPGCEHSQESAQ-LRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLK 383
Cdd:pfam07888 218 LTQKLTTAHRK-EAENEALLEELRSLQERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 384 DCLAEKAQEEERLSRRLRDSHETIASLRA---------QSPPVKYVIKTVEVESSKTKQALSESQARNQhLQEQVAMQRQ 454
Cdd:pfam07888 297 EGRARWAQERETLQQSAEADKDRIEKLSAelqrleerlQEERMEREKLEVELGREKDCNRVQLSESRRE-LQELKASLRV 375
|
250 260
....*....|....*....|....*.
gi 530423880 455 VLKEMEQQ-------LQSSHQLTARL 473
Cdd:pfam07888 376 AQKEKEQLqaekqelLEYIRQLEQRL 401
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-516 |
2.34e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 227 VEAMSQLQDEKTQLQEELVVLQERLalrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVEN 306
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREEL----EQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcl 386
Cdd:COG4372 111 EELQEELEELQKERQDLE-------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 387 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSS 466
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530423880 467 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 516
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
228-537 |
2.40e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELvvlqerlalrdSDQQATSTQLQNQVEHLKEKLisqaQEVSRLRSELGGTDLEKHRDLLmvenE 307
Cdd:COG3096 836 AELAALRQRRSELEREL-----------AQHRAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLADRL----E 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 308 RLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAEskgmLSELNLEVQQKTDRLAEVELRLkDCLA 387
Cdd:COG3096 897 ELREELDAAQEAQAFIQ----------QHGKALAQLEPLVAVLQSDPEQ----FEQLQADYLQAKEQQRRLKQQI-FALS 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 388 EKAQEEERLS-----RRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQAR-NQHLQEQVAMQ------RQV 455
Cdd:COG3096 962 EVVQRRPHFSyedavGLLGENSDLNEKLRAR-------LEQAEEARREAREQLRQAQAQySQYNQVLASLKssrdakQQT 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 456 LKEMEQQLQ-------SSHQLTARLR-------------------AQIAMYESELERAHGQMLEemqsLEED---KNRAI 506
Cdd:COG3096 1035 LQELEQELEelgvqadAEAEERARIRrdelheelsqnrsrrsqleKQLTRCEAEMDSLQKRLRK----AERDykqEREQV 1110
|
330 340 350
....*....|....*....|....*....|.
gi 530423880 507 EEAFARAQVEMKAVHENlaGVRTNLLTLQPA 537
Cdd:COG3096 1111 VQAKAGWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-413 |
2.76e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 225 RMVEAMSQLQDEKTQLQEELVVLQE---RLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrDL 301
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL---------EE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 302 LMVENERLRQEMRRCEAELQELRTkpagpcpgcehsqesaqlrdKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELR 381
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELRE--------------------KLAQLELR-------LEGLEVRIDNLQERLSEEYSL 951
|
170 180 190
....*....|....*....|....*....|..
gi 530423880 382 LKDCLAEKAQEEERLSRRLRDShetIASLRAQ 413
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRR---LKRLENK 980
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
340-527 |
2.94e-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: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 340 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 413
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 414 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 493
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 530423880 494 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 527
Cdd:cd07627 181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
310-597 |
3.09e-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: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 310 RQEMRRCEAELQELRTKPAGPCpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE------LRLK 383
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKAC----------EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlskiMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 384 D---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEME 460
Cdd:TIGR00606 269 NeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 461 QQL---QSSHQLTA-RLRAQIAMYESelERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMKAVHENLAGVRTN 530
Cdd:TIGR00606 343 TELlveQGRLQLQAdRHQEHIRARDS--LIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530423880 531 LLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQLRKK 597
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEK 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
343-537 |
3.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 343 LRDKLSQLQLEMAESKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 421
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 422 KTVEV--ESSKTKQALSESQARNQHLQEQVamqrQVLKEMEQQLQsshqltaRLRAQIAMYESELERAHGQ----MLEEM 495
Cdd:COG4717 126 QLLPLyqELEALEAELAELPERLEELEERL----EELRELEEELE-------ELEAELAELQEELEELLEQlslaTEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530423880 496 QSLEEDKNRA------IEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 537
Cdd:COG4717 195 QDLAEELEELqqrlaeLEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
228-402 |
3.84e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERLALrdsdQQATSTQLQNQVEHLKEKLISQAQEVSRLRSEL-----GGTDLEKHRDLL 302
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 303 MVENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQ--LEMAESKGmlselnlevQQKTDRLAEVEL 380
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLN-------------QQIAALRRQLAALEaaLDASEKRD---------RESQAKIADLGR 179
|
170 180
....*....|....*....|....*....
gi 530423880 381 RLKDCLAEKAQEeerLSR-------RLRD 402
Cdd:PRK09039 180 RLNVALAQRVQE---LNRyrseffgRLRE 205
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
228-561 |
3.94e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVL----QERLALRDSDQQATSTQ----LQNQVEHLKEKLISQAQEVSRLRSELGGTDLEkhr 299
Cdd:TIGR00618 339 SIEEQRRLLQTLHSQEIHIRdaheVATSIREISCQQHTLTQhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTR--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 300 dllMVENERLRQEMRRCEAElQELRTKPAGPCPgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAE-- 377
Cdd:TIGR00618 416 ---TSAFRDLQGQLAHAKKQ-QELQQRYAELCA--AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkk 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 378 -VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTV---EVESSKTKQALSESQARNQHLQEQVAMQR 453
Cdd:TIGR00618 490 aVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYaqlETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 454 QVLKEMEQQLQSS-------HQLTARLRAQIAMyESELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAg 526
Cdd:TIGR00618 570 QSFSILTQCDNRSkedipnlQNITVRLQDLTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK- 644
|
330 340 350
....*....|....*....|....*....|....*.
gi 530423880 527 vrtnLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQE 561
Cdd:TIGR00618 645 ----LTALHALQLTLTQERVREHaLSIRVLPKELLA 676
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
346-508 |
4.81e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 346 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHETIASLRAQSPPVK---- 418
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 419 YVIKTVEVESSKTKQALSESQARNqhLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYESELERAHGQMLEEMQSL 498
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 530423880 499 EEDKNRAIEE 508
Cdd:COG1579 162 EAEREELAAK 171
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
230-401 |
6.00e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 230 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQnQVEHLKEKLISQAQEVSRLRSELGGTDLEkhrdllmvenerl 309
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP-KLRDRKDALEEELRQLKQLEDELEDCDPT------------- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 310 rqEMRRCEAELQELrtkpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK 389
Cdd:smart00787 205 --ELDRAKEKLKKL-------------LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFT 269
|
170
....*....|..
gi 530423880 390 AQEEERLSRRLR 401
Cdd:smart00787 270 FKEIEKLKEQLK 281
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
250-544 |
7.87e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 250 RLALRD--SDQQATSTQLQNQVEHLKEKLISQAqeVSRLRSELGGTDLEKHRdllmVENERLRQEMRRCEAE--LQELRt 325
Cdd:PRK02224 175 RLGVERvlSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIER----YEEQREQARETRDEADevLEEHE- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 326 kpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAqeeerlsrrLRDSHE 405
Cdd:PRK02224 248 ---------ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG---------LDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 406 TIASLRaqsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQlqsshqlTARLRAQIAMYESELE 485
Cdd:PRK02224 310 EAVEAR---------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER-------AEELREEAAELESELE 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530423880 486 RAHGQMLEEMQSLEE--DKNRAIEEAFARAQVEM-------KAVHENLAGVRTNLLTLQPALRTLTND 544
Cdd:PRK02224 374 EAREAVEDRREEIEEleEEIEELRERFGDAPVDLgnaedflEELREERDELREREAELEATLRTARER 441
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
230-402 |
8.30e-04 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 41.44 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 230 MSQLQDEKTQLQEELVVLQERLA--LRDSDQQATST---------QLQNQVEHLKEKLISQAQEVSRLRSELG-----GT 293
Cdd:pfam13870 1 MRAKRNELSKLRLELITLKHTLAkiQEKLEQKEELGegltmidflQLQIENQALNEKIEERNKELKRLKLKVTntvhaLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 294 DLEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSelnlevqqKTD 373
Cdd:pfam13870 81 HLKEKLHFLSAELSRLKKELRERQELLAKLR----------KELYRVKLERDKLRKQNKKLRQQGGLLH--------VPA 142
|
170 180
....*....|....*....|....*....
gi 530423880 374 RLAEVElRLKDCLAEKAQEEERLSRRLRD 402
Cdd:pfam13870 143 LLHDYD-KTKAEVEEKRKSVKKLRRKVKI 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
224-651 |
8.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 224 LRMVEAMSQLQDEKTQLQEELVVLQErlALRDSDQQATSTQLQNQVEHLK--EKLISQAQEVSRLRSELGGTDLEKHRDL 301
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 302 LMVENERLRQEMRrcEAELQELRTKPAGPCPGCEHSQESAQLR---DKLSQLQLEMAESKGMLSELnlevqQKTDRLAEV 378
Cdd:PTZ00121 1488 AKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADEL-----KKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 379 ELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVEVESS-KTKQALSESQARNQhlQEQVAMQRQVLK 457
Cdd:PTZ00121 1561 EEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIK--AEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 458 EMEQ-------------QLQSSHQLTARLRAQIAMYESELERAhgqmLEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnl 524
Cdd:PTZ00121 1634 KVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE-- 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 525 agvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE----LQLRKKCHN 600
Cdd:PTZ00121 1707 -------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEK 1768
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 530423880 601 ELVRLKGNIRVIARvRPVTKEDGEGPEATNAVTFDADDDS--IIHLLHKGKPV 651
Cdd:PTZ00121 1769 KAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGGKEGNLV 1820
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
254-532 |
8.48e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 254 RDSDQQATStqLQNQVEHLKEKLISQAQEVSRLRsELGGTDLEKHRDLLmvenERLRQEMRrceaelqelrtkpagpcpg 333
Cdd:PHA02562 177 RELNQQIQT--LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 334 cEHSQESAQLRDKLSQLQLEMAESKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrlrdsh 404
Cdd:PHA02562 231 -TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 405 etiaslraqsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESEL 484
Cdd:PHA02562 304 ----------------IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530423880 485 ERAHGQML---EEMQSLEEDKNRAIEEafaRAQVEMKAVHEnlaGVRTNLL 532
Cdd:PHA02562 368 EELQAEFVdnaEELAKLQDELDKIVKT---KSELVKEKYHR---GIVTDLL 412
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
307-517 |
1.05e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 41.57 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQktdRLAEVELRLKDCL 386
Cdd:cd07596 7 EEAKDYILKLEEQLKKLSKQ----------AQRLVKRRRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 387 AEKAQEEERLSRR--------LRDSHETIASLRAqsppvkyVIKT-----VEVESSKtkQALSESQARNQHLQEQVAMQR 453
Cdd:cd07596 74 EELSSLSEAQANQelvkllepLKEYLRYCQAVKE-------TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530423880 454 QVLKEMEQQLQSSHQLTARLRAqiamyesELERAHGQMLEEMQSLEEDKNRAIEEA---FARAQVEM 517
Cdd:cd07596 145 AKVEELEEELEEAESALEEARK-------RYEEISERLKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
225-353 |
1.18e-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: 42.31 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 225 RMVEAMSQLQDEKTQLQEELVVLQErlaLRDSDQQATSTQLQNqvehLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 304
Cdd:smart00787 169 LLNSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELDR----AKEKLKKLLQEIMIKVKKL--EELEEELQELES 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530423880 305 ENERLRQEMRRCEAELQELRTKPAgPCPGCEHSqESAQLRDKLSQLQLE 353
Cdd:smart00787 240 KIEDLTNKKSELNTEIAEAEKKLE-QCRGFTFK-EIEKLKEQLKLLQSL 286
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
227-413 |
1.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 227 VEAMSQLQDEKTQLQEELVVLQERLA-----LRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtdlEKHRDL 301
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAalraqLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT----PNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 302 LmveneRLRQEMRRCEAELQElrtkpagpcpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEvelr 381
Cdd:COG3206 294 I-----ALRAQIAALRAQLQQ-------------------EAQRILASLEAELEALQAREASLQAQLAQLEARLAE---- 345
|
170 180 190
....*....|....*....|....*....|..
gi 530423880 382 lkdcLAEKAQEEERLSRRLRDSHETIASLRAQ 413
Cdd:COG3206 346 ----LPELEAELRRLEREVEVARELYESLLQR 373
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
219-443 |
1.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 219 AAPMVLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELG---- 291
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELealQAEIDKLQAEIAEAEAEIEERREELGerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 292 -----GTDLEKHRDLLMVEN--------ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESK 358
Cdd:COG3883 94 alyrsGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKA------ELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 359 GMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSES 438
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*
gi 530423880 439 QARNQ 443
Cdd:COG3883 248 GAGAA 252
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
230-396 |
1.34e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 230 MSQLQDEKTQLQEELvvlqerlalrdsdqqatsTQLQNQVEHLKEKLISQAQEVSRL-RSELGGTDLEKHRDLLMVENER 308
Cdd:pfam13851 49 MSEIQQENKRLTEPL------------------QKAQEEVEELRKQLENYEKDKQSLkNLKARLKVLEKELKDLKWEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 309 LRQEMRRCEAELQELRTKpagpcpgCEHSQESAQ---------LRDKLSQLQLEM----AESKGMLSELNLEvqqkTDRL 375
Cdd:pfam13851 111 LEQRFEKVERERDELYDK-------FEAAIQDVQqktglknllLEKKLQALGETLekkeAQLNEVLAAANLD----PDAL 179
|
170 180
....*....|....*....|.
gi 530423880 376 AEVELRLKDCLAEKAQEEERL 396
Cdd:pfam13851 180 QAVTEKLEDVLESKNQLIKDL 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-616 |
1.45e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 452 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVhENLAGVRTNl 531
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQ- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 532 ltLQPALRTLTNDYNGLKRQVRGFPLLLQEALR---SVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGN 608
Cdd:TIGR02168 752 --LSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
....*...
gi 530423880 609 IRVIARVR 616
Cdd:TIGR02168 830 ERRIAATE 837
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
241-597 |
1.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 241 QEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenERLRQEMRRCEAEL 320
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL----------------EQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 321 QELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVElrlkdclaekaQEEERLSRRL 400
Cdd:COG4372 76 EQLE-------------EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----------KERQDLEQQR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 401 RDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAmqRQVLKEMEQQLQSSHQLTARLRAQIAMY 480
Cdd:COG4372 132 KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 481 ESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 560
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 530423880 561 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 597
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
236-595 |
1.60e-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: 42.65 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 236 EKTQLQEELVVL--QERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEvsRLRSElggTDLEKHRDLLMVENERLRQEM 313
Cdd:TIGR00618 418 AFRDLQGQLAHAkkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ--SLKER---EQQLQTKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 314 RRCEAELQELrtkpagPCPGCEHSQESAQlrdKLSQLQLEMAESKGMLSELNlEVQQKTDRLAEVELRLkDCLAEKAQEE 393
Cdd:TIGR00618 493 LARLLELQEE------PCPLCGSCIHPNP---ARQDIDNPGPLTRRMQRGEQ-TYAQLETSEEDVYHQL-TSERKQRASL 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 394 ERLSRRLRDSHETIASLRAQSP--------PVKYVIKTVEVESSKTKQALSESQAR------NQHLQEQVAMQRQVLKEM 459
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKedipnlqnITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDLQDVRLHLQQCSQEL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 460 EQQLQSSHQLTARLraqiaMYESELERAHGQMLEEMQSLEEDKNraieeafarAQVEMKAVHENLAGVRTNLLTLQPALR 539
Cdd:TIGR00618 642 ALKLTALHALQLTL-----TQERVREHALSIRVLPKELLASRQL---------ALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530423880 540 TLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 595
Cdd:TIGR00618 708 ELETHIEEYDREFNE----IENASSSLGSDLAAREDALNQSLKELMHQARTVLKAR 759
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
170-514 |
1.66e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 170 KEEKLWKRQAPAPRRAREAREAGGTMNVENTGGRLFGSRRCSSLSGPpGAAPmvlrmveAMSQLQDE----KTQLQEELV 245
Cdd:pfam15709 220 KSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETEDASER-GAFS-------SDSVVEDPwlssKYDAEESQV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 246 VLQERLAlrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSElggtdleKHRDLLMVEnerlRQEMRRCEAELQElrt 325
Cdd:pfam15709 292 SIDGRSS---PTQTFVVTGNMESEEERSEEDPSKALLEKREQEK-------ASRDRLRAE----RAEMRRLEVERKR--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 326 kpagpcpgcehsQESAQLRdKLSQLQLEMAESkgMLSELNLEVQQKTDRLAEVELRLKDclAEKAQEEERLSRRLRdshE 405
Cdd:pfam15709 355 ------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQ---L 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 406 TIASLRAQSPPVKYVIKTVEVESSKTKQALSESQA---RNQHLQEQVAMQRQVLKEMEQQlqsshqltARLRAQIAMYES 482
Cdd:pfam15709 415 QAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAEE--------ERLEYQRQKQEA 486
|
330 340 350
....*....|....*....|....*....|..
gi 530423880 483 ElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 514
Cdd:pfam15709 487 E-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
228-552 |
1.99e-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: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 228 EAMSQLQDEKTQLQEELVVLQERL-ALRDSDQQATSTQLQNQVEhlkekliSQAQEVSRLRSELGGTDLEKHRDLLMVEN 306
Cdd:pfam10174 60 EQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVD-------GEDKFSTPELTEENFRRLQSEHERQAKEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQEMrrceaELQELRTkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcL 386
Cdd:pfam10174 133 FLLRKTL-----EEMELRI---------ETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGH-L 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 387 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKqalseSQARNqhlqeqvamqrqvLKEMEQQLQSs 466
Cdd:pfam10174 198 EVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERN-------------IRDLEDEVQM- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 467 hqltARLRAQIAMYESElerahgqmlEEMQSLEEDKNRAieeAFARAQVEMkaVHENLAGVRTNLLTLQPALRTLTNDYN 546
Cdd:pfam10174 259 ----LKTNGLLHTEDRE---------EEIKQMEVYKSHS---KFMKNKIDQ--LKQELSKKESELLALQTKLETLTNQNS 320
|
....*.
gi 530423880 547 GLKRQV 552
Cdd:pfam10174 321 DCKQHI 326
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-407 |
2.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 232 QLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQnQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVEN----- 306
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELE-QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAverel 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 --------ERLRQEMRRCEAELQELRT--KPAGPCPGCEHSQESAQLRDKLSQLQlemaeskgmlselnlevQQKTDRLA 376
Cdd:COG4913 768 renleeriDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYLALLD-----------------RLEEDGLP 830
|
170 180 190
....*....|....*....|....*....|..
gi 530423880 377 EVELRLKDCLAEKAQEE-ERLSRRLRDSHETI 407
Cdd:COG4913 831 EYEERFKELLNENSIEFvADLLSKLRRAIREI 862
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
365-593 |
2.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 365 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQ 433
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 434 ALSESQARNQ--HLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAieeafA 511
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA-----Q 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 512 RAQVEMKavhenLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 588
Cdd:COG3206 272 LAELEAE-----LAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 530423880 589 RRELQ 593
Cdd:COG3206 340 EARLA 344
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
225-502 |
2.83e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 225 RMVEAMSQLQDEKTQLQEELVVLQERLA-----LRDSDQQATSTqlqNQVEHLKEKLISQAQEvsRLRSELGG-TDLEKH 298
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISeftsnLAEEEEKAKSL---SKLKNKHEAMISDLEE--RLKKEEKGrQELEKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 299 RDLLMVENERLRQEMRRCEAELQELRTKPAGPcpgcEHSQESAQLR-----DKLSQLQLEMAESKGMLSELNLEVQQKTD 373
Cdd:pfam01576 210 KRKLEGESTDLQEQIAELQAQIAELRAQLAKK----EEELQAALARleeetAQKNNALKKIRELEAQISELQEDLESERA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 374 RLAEVELRLKDcLAEkaqEEERLSRRLRDSHETIAS---LRAQSppvkyviktvEVESSKTKQAL-SESQARNQHLQEQV 449
Cdd:pfam01576 286 ARNKAEKQRRD-LGE---ELEALKTELEDTLDTTAAqqeLRSKR----------EQEVTELKKALeEETRSHEAQLQEMR 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 530423880 450 AMQRQVLKEMEQQLQSSHqltaRLRAQIAMYESELERAHGQMLEEMQSLEEDK 502
Cdd:pfam01576 352 QKHTQALEELTEQLEQAK----RNKANLEKAKQALESENAELQAELRTLQQAK 400
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-514 |
4.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 225 RMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL--QNQVEHLKEK------------LISQAQEVSRLRSEL 290
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEArlllliaaallaLLGLGGSLLSLILTI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 291 GG-------------TDLEKHRDLLMVENERLRQEMRRCEAELQEL-RTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAE 356
Cdd:COG4717 276 AGvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELeELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 357 SKGMLSELNLEVQQKTDR--LAEV------ELRLKdclAEKAQEEERLSRRLRDSHETIASLRAqsppvkyviktvEVES 428
Cdd:COG4717 356 AEELEEELQLEELEQEIAalLAEAgvedeeELRAA---LEQAEEYQELKEELEELEEQLEELLG------------ELEE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 429 SKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYE-----SELERAHGQMLEEMQSLEED-- 501
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELREEL-------AELEAELEQLEedgelAELLQELEELKAELRELAEEwa 493
|
330
....*....|...
gi 530423880 502 KNRAIEEAFARAQ 514
Cdd:COG4717 494 ALKLALELLEEAR 506
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
219-561 |
4.61e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 219 AAPMVLRMVEAMSQLQDEKTQlqeelvvlQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVsrlRSELGGTdlEKH 298
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQ--------EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKS--EEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 299 RDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEH-SQESAQLRDKLS--QLQLEMAESKgmLSELNLEVQQKTDRL 375
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElHQENKALKKKGSaeNKQLNAYEIK--VNKLELELASAKQKF 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 376 AEVELRLKDCLAEKAQEEERLSRrlrdshetiaslraqsppvkyviktvEVESSKTKqalsesqarnqhLQEQVAMQRQV 455
Cdd:pfam05483 653 EEIIDNYQKEIEDKKISEEKLLE--------------------------EVEKAKAI------------ADEAVKLQKEI 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 456 LKEMEQQLQSSHQLTARLRAQiamyeseleraHGQMLEEMQS-LEEDKNRAIEEAFARAQVEMKavhenLAGVRTNLLTL 534
Cdd:pfam05483 695 DKRCQHKIAEMVALMEKHKHQ-----------YDKIIEERDSeLGLYKNKEQEQSSAKAALEIE-----LSNIKAELLSL 758
|
330 340
....*....|....*....|....*..
gi 530423880 535 QPALRTLTNDYNGLKRQVRGFPLLLQE 561
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
339-598 |
5.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 339 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSppvk 418
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 419 yviKTVEVESSKTKQALSESQARNQHL----------QEQVAMQRQVLKEMEQQLQSSHQlTARLRAQiaMYESELERAh 488
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE-ECRVAAQ--AHNEEAESL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 489 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 568
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422
|
250 260 270
....*....|....*....|....*....|..
gi 530423880 569 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 598
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
223-522 |
6.72e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.90 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 223 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGT-------DL 295
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIveriqeeDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 296 EKHRDLLMvENERLRQEMRRCEAELQELRTKPAGpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRL 375
Cdd:pfam13868 116 AEAEEKLE-KQRQLREEIDEFNEEQAEWKELEKE-----EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 376 AEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSppvkyviktvevESSKTKQALSESQARNQHLQEQVAMQRQV 455
Cdd:pfam13868 190 RAQQEKAQD---EKAERDELRAKLYQEEQERKERQKERE------------EAEKKARQRQELQQAREEQIELKERRLAE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 456 LKEMEQQLQssHQLTARLRAQIAMYESELERAHGQMLE---EMQSLEEDKNRAIEEAFARAQVEMKAVHE 522
Cdd:pfam13868 255 EAEREEEEF--ERMLRKQAEDEEIEQEEAEKRRMKRLEhrrELEKQIEEREEQRAAEREEELEEGERLRE 322
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
361-485 |
6.89e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 361 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQA 440
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530423880 441 RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 485
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
344-496 |
8.05e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 344 RDK-LSQLQLEMAESKGMLS-------ELNLEVQQKTDRLAEVEL---RLKDCLAEKAQEEERLSRRLRDSHETIASLRA 412
Cdd:PRK09039 51 KDSaLDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 413 QSppvkyviktvevessktkqalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML 492
Cdd:PRK09039 131 VS---------------------ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....
gi 530423880 493 EEMQ 496
Cdd:PRK09039 190 QELN 193
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
342-497 |
8.75e-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: 39.66 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 342 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 421
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQ-------VRTLREEKERSVSQVQELETSLAELKNQAAVPPAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 422 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVlkemeqQLQSSHQLTaRLRAQIAMYESELERA----------HGQM 491
Cdd:pfam15070 74 EQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQA------QVQDNEQLS-RLNQEQEQRLLELERAaerwgeqaedRKQI 146
|
....*.
gi 530423880 492 LEEMQS 497
Cdd:pfam15070 147 LEDMQS 152
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-474 |
8.81e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 232 QLQDEKTQLQEELVVLQERLALRDSDQqatstqlqNQVEHLKEKLISQAQEVSRLRS-----ELggtdLEKHRDLLMVEn 306
Cdd:COG3096 445 AFRAKEQQATEEVLELEQKLSVADAAR--------RQFEKAYELVCKIAGEVERSQAwqtarEL----LRRYRSQQALA- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 307 ERLRQemrrCEAELQELRTKpagpcpgcEHSQESAQ-LRDKLSQLQLEMAESKGMLSELnlevqqktdrLAEVELRLKDC 385
Cdd:COG3096 512 QRLQQ----LRAQLAELEQR--------LRQQQNAErLLEEFCQRIGQQLDAAEELEEL----------LAELEAQLEEL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 386 LAEKAQEEERLS--RRLRDSHET-IASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQ 462
Cdd:COG3096 570 EEQAAEAVEQRSelRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDEL 649
|
250
....*....|..
gi 530423880 463 LQSSHQLTARLR 474
Cdd:COG3096 650 AARKQALESQIE 661
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-485 |
1.00e-02 |
|
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: 39.77 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 232 QLQDEKTQLQEELVVLQERLalrdsdqqATSTQLQNQVEHLKEKLISQAQEV--------SRLRSElggtdlEKHRDLLM 303
Cdd:pfam01576 30 ELEKKHQQLCEEKNALQEQL--------QAETELCAEAEEMRARLAARKQELeeilheleSRLEEE------EERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 304 VENERLRQEMRRCEAELQE---LRTK-------PAGPCPGCEH------------SQESAQLRDKLSQLQLEMAESKGML 361
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDEeeaARQKlqlekvtTEAKIKKLEEdillledqnsklSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423880 362 SELNLEVQQKTDRLAEVELRLKDClaEKA-QEEERLSRRLR----DSHETIASLRAQSPPVKYVIKTVEVESSKTKQALS 436
Cdd:pfam01576 176 KSLSKLKNKHEAMISDLEERLKKE--EKGrQELEKAKRKLEgestDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 530423880 437 ESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 485
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| |
