|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
441-768 |
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: 532.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 441 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 519
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 520 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 596
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 597 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 676
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 677 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 756
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 224967071 757 LRFAERVRSVEL 768
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
449-766 |
2.39e-148 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 438.55 E-value: 2.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 449 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 525
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 526 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 605
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 606 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 682
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 683 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFA 760
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 224967071 761 ERVRSV 766
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
443-770 |
1.45e-143 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 426.60 E-value: 1.45e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 518
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 519 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 598
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 599 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 676
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 677 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 754
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 224967071 755 YSLRFAERVRSVELGP 770
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
443-764 |
2.26e-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: 376.60 E-value: 2.26e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 519
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 520 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 597
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 598 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 675
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 676 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 754
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 224967071 755 YSLRFAERVR 764
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
443-766 |
7.11e-107 |
|
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: 331.35 E-value: 7.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 514
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 515 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 591
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 592 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 667
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 668 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 746
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 224967071 747 EKNTSETLYSLRFAERVRSV 766
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
444-767 |
6.27e-104 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 323.90 E-value: 6.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 444 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 521
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 522 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 595
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 596 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 665
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 666 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 742
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 224967071 743 VSPVEKNTSETLYSLRFAERVRSVE 767
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
443-766 |
7.22e-95 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 300.42 E-value: 7.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 505
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 506 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 584
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 585 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 663
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 664 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 738
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 224967071 739 MVVQVSPVEKNTSETLYSLRFAERVRSV 766
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
443-766 |
1.12e-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: 291.54 E-value: 1.12e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 520
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 521 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 597
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 598 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 677
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 678 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 756
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 224967071 757 LRFAERVRSV 766
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
442-766 |
3.06e-90 |
|
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: 288.87 E-value: 3.06e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 442 GNIRVIARVRPVTKEDGEGPeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQE 506
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 507 VQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDLL 584
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 585 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 659
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 660 TGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 729
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 224967071 730 SLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSV 766
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
443-766 |
3.22e-89 |
|
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: 284.61 E-value: 3.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 521
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 522 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 601
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 602 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 677
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 678 RVGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 755
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 224967071 756 SLRFAERVRSV 766
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
443-766 |
1.02e-86 |
|
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: 279.21 E-value: 1.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 517
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 518 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 586
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 587 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 661
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 662 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 741
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 224967071 742 QVSPVEKNTSETLYSLRFAERVRSV 766
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
427-767 |
1.39e-80 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 270.07 E-value: 1.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 427 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 506
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 507 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 585
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 586 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 665
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 666 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 743
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 224967071 744 SPVEKNTSETLYSLRFAERVRSVE 767
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
444-761 |
1.25e-77 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 255.01 E-value: 1.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 444 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 512
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 513 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 588
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 589 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 663
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 664 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 735
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 224967071 736 KTLMVVQVSPVEKNTSETLYSLRFAE 761
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
443-764 |
4.01e-77 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 253.58 E-value: 4.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 521
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 522 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgkEP- 588
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 589 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 665
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 666 gKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 741
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 224967071 742 QVSPVEKNTSETLYSLRFAERVR 764
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
443-764 |
7.50e-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: 238.56 E-value: 7.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 519
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 520 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 599
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 600 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 678
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 679 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLR 758
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 224967071 759 FAERVR 764
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
444-764 |
4.27e-71 |
|
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: 237.09 E-value: 4.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 444 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 512
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 513 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 589
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 590 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 664
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 665 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 743
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 224967071 744 SPVEKNTSETLYSLRFAERVR 764
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
443-763 |
7.83e-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: 225.25 E-value: 7.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 443 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 514
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 515 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 590
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 591 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 670
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 671 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 748
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 224967071 749 NTSETLYSLRFAERV 763
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
444-767 |
2.88e-58 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 216.72 E-value: 2.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 444 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 522
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 523 FAYGQTGAGKTYTMEGtPENP-----------GINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLgk 586
Cdd:PLN03188 170 FAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 587 EP-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLR 663
Cdd:PLN03188 247 DPsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 664 T--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSK 736
Cdd:PLN03188 325 SfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAK 404
|
330 340 350
....*....|....*....|....*....|.
gi 224967071 737 TLMVVQVSPVEKNTSETLYSLRFAERVRSVE 767
Cdd:PLN03188 405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
423-584 |
4.53e-42 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 150.06 E-value: 4.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 423 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 502
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 503 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 582
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 224967071 583 LL 584
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
491-710 |
6.05e-22 |
|
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: 93.56 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 491 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 569
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 570 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 649
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224967071 650 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 710
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-427 |
8.98e-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: 72.40 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKlISQAQEVSRLRSELggtdAEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKL 182
Cdd:TIGR02168 201 QLKSLERQ-AEKAERYKELKAEL----RELELALLVLRLEELREELEELQEELKEAE-------------EELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLaeveLRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVE 262
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 263 SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT--------------VQLRAQIAMYEAELER--AHGQM 326
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 327 LEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIG 406
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAERELA 485
|
330 340
....*....|....*....|...
gi 224967071 407 QAIEEVNS--NNQELLRKYRREL 427
Cdd:TIGR02168 486 QLQARLDSleRLQENLEGFSEGV 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-387 |
9.66e-13 |
|
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: 72.41 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 92 PRSPHRLY-LTVQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQ--------P 162
Cdd:TIGR02169 677 QRLRERLEgLKRELSSLQSELRRIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDlssleqeiE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 163 VVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLS------------ELNLEVQQKTDRLAEVELRLKDCLAEKAQEEER 230
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 231 ---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQ-------- 299
Cdd:TIGR02169 835 iqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEeleaqiek 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 300 -NSHQLTVQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEEDKNRAIE--EAFARAQVEMKAV 355
Cdd:TIGR02169 915 kRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLAIQeyEEVLKRLDELKEK 994
|
330 340 350
....*....|....*....|....*....|..
gi 224967071 356 HENLAGVRTnlltlqpALRTLTNDYNGLKRQV 387
Cdd:TIGR02169 995 RAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-412 |
6.71e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 96 HRLYLTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLmvENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQE- 174
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL--ELEELELELEEAQAEEYELLAELARLEQDIARLEEr 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 175 SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvky 254
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL------ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 255 vikTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV-LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSL 333
Cdd:COG1196 385 ---AEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 334 EEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQE--ALRSVKAEIGQAI 409
Cdd:COG1196 462 LELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalLLAGLRGLAGAvaVLIGVEAAYEAAL 540
|
...
gi 224967071 410 EEV 412
Cdd:COG1196 541 EAA 543
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-429 |
7.91e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 114 QAQEVSRLRSELGGTDAE---KHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehsqessqlrdkLSQLQLEVA 190
Cdd:COG1196 211 KAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAE--------------------LAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 191 ENKGMLSELNLEVQQKTDRLAEVELRlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQAL 270
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 271 SESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARA 348
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeeALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 349 QVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQ 428
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
.
gi 224967071 429 L 429
Cdd:COG1196 496 L 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
99-344 |
2.86e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 99 YLTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehsqessql 178
Cdd:COG3206 179 FLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR----------------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 179 rdkLSQLQLEVAENKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSHETIASLRAQsppvkyvI 256
Cdd:COG3206 242 ---LAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNHPDVIALRAQ-------I 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 257 KTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAeLERAHGQMLEEMQSLEE 335
Cdd:COG3206 301 AALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV-ARELYESLLQRLEEARL 379
|
....*....
gi 224967071 336 DKNRAIEEA 344
Cdd:COG3206 380 AEALTVGNV 388
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-473 |
5.05e-09 |
|
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: 60.07 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 172 SQESSQL--RDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 249
Cdd:TIGR02168 667 KTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 250 PPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG----- 324
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanl 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 325 ----QMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRS 400
Cdd:TIGR02168 823 rerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRS 894
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224967071 401 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI-RVIARVRPVTKEDGEGPEA-TNAVTFDPDD 473
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEAlENKIEDDEEE 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-451 |
7.07e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 177 QLRDKLSQLQLEVAENKgmLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIaslraqsppvkyvi 256
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEEL-------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 257 ktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 336
Cdd:COG1196 280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 337 KN--RAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNS 414
Cdd:COG1196 357 EAelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAE 432
|
250 260 270
....*....|....*....|....*....|....*..
gi 224967071 415 NNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVR 451
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-419 |
1.93e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.21 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 135 DRLMVENEQLRQELRRCEVELQELRAQpvvpCEGCEHSQESS-----QLRDKLSQLQLEVAENKGMLSELNLEVQQKTDR 209
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSE----CQGQMERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 210 LAEVELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQR 288
Cdd:pfam15921 491 LESSERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 289 QVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH----- 356
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnag 641
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967071 357 -ENLAGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 419
Cdd:pfam15921 642 sERLRAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
425-709 |
4.57e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 56.67 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 425 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 492
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 493 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 571
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 572 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 645
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224967071 646 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 709
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-449 |
6.24e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 108 KEKLISQAQEVSRLRSELGGTDAEKHR--DRLMVENEQLRQELRRCEVELQELRAqpvvpcegcehsqessqLRDKLSQL 185
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELEE-----------------LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 186 QLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEKAQEEERLSR-------RLRDSHETIASLRAQS 249
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 250 PPVKYVIKtvevESSKTKQALSESQTRNQHLQEQVAmqrqVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAE-------- 318
Cdd:PRK03918 324 NGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHELYEEAKAKKEElerLKKRLTGLTPEklekelee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 319 LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----------------MKAVHENLAGVRTNLLTLQPA 372
Cdd:PRK03918 396 LEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967071 373 LRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 449
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
109-411 |
7.60e-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: 56.34 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 109 EKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELR--------------RCEVELQELRAQpvvpceGCEHSQE 174
Cdd:pfam01576 359 EELTEQLEQAKRNKANL-----EKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQAR------LSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 175 SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSP 250
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 251 PVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQLTVQLRAQIAMYEaELERAHGQMLEE 329
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYD-KLEKTKNRLQQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 330 MQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRG 389
Cdd:pfam01576 582 LDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQ 661
|
330 340
....*....|....*....|..
gi 224967071 390 FPLLLqEALRSVKAEIGQAIEE 411
Cdd:pfam01576 662 LRAEM-EDLVSSKDDVGKNVHE 682
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
102-428 |
1.21e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 102 VQVENLKEKLISQAQEV---SRLRSELGgTDAEKHRDRLMVENEQLRQE--LRRCEVELQELRAQPVVPCEGCEHSQES- 175
Cdd:PRK04863 300 RQLAAEQYRLVEMARELaelNEAESDLE-QDYQAASDHLNLVQTALRQQekIERYQADLEELEERLEEQNEVVEEADEQq 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 176 SQLRDKLSQLQLEVAENKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKDCLAE-KAQEEERLSRR 234
Cdd:PRK04863 379 EENEARAEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAEDWLEEfQAKEQEATEEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 235 LR-----DSHETIASLRAQSppVKYVIKTV-EVESSKTKQALSE--SQTRNQ-HLQEQVAMQRQVLKEMEQQLQNsHQLT 305
Cdd:PRK04863 459 LSleqklSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRMRLSELEQRLRQ-QQRA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 306 VQLRAQ-----IAMY--EAELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLAGVRTNLLTLQPA---L 373
Cdd:PRK04863 536 ERLLAEfckrlGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLAARAPAWLAAQDAlarL 615
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 224967071 374 RTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 428
Cdd:PRK04863 616 REQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
130-361 |
1.44e-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: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 130 AEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDR 209
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 210 LAEVELRLKDCLAEKAQEEERLSRRLR-----DSHETIASLRAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQH 279
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 280 LQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENL 359
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERT 243
|
..
gi 224967071 360 AG 361
Cdd:COG4942 244 PA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-412 |
1.99e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 136 RLMVENeqlRQELRRCEVELQELRAQpvvpcegCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVEL 215
Cdd:COG4913 228 DALVEH---FDDLERAHEALEDAREQ-------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 216 -RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQRQVLKE 293
Cdd:COG4913 298 eELRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 294 MEQQLQNSHQLTVQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPAL 373
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260 270
....*....|....*....|....*....|....*....
gi 224967071 374 RTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 412
Cdd:COG4913 422 RELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-322 |
2.96e-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: 53.61 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKL 182
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKEL--AALKKEEKALLKQLAALERRIAALARRIRALEQELA------ALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLRAQSPPVKYV 255
Cdd:COG4942 93 AELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967071 256 IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERA 322
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-405 |
3.14e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK-----AQEEERLSRRLRDSHETIASLRAQSPPVKYVIK 257
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 258 TVEVESSKTKQALSE--SQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSlEE 335
Cdd:COG3206 244 ALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA-EL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 336 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpLLLQEALRSVKAEI 405
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVRV 390
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
103-249 |
3.77e-07 |
|
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: 52.71 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvPCEGCEhSQESSQLRDKL 182
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLL-----MKELELLNSIKPKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 249
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
152-387 |
5.98e-07 |
|
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: 53.42 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 152 EVELQELRAQPV-VPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNL-------------------------EVQQ 205
Cdd:COG3096 835 EAELAALRQRRSeLERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLladetladrleelreeldaaqeaqaFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 206 KTDRLAEVElRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVES-SKTKQALSESQTRNQHLQEQv 284
Cdd:COG3096 915 HGKALAQLE-PLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLGENSDLNEKLRAR- 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 285 amqrqvLKEMEQQLQNSHQLTVQLRAQIAMYEAELE------RAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEMKAVHE 357
Cdd:COG3096 993 ------LEQAEEARREAREQLRQAQAQYSQYNQVLAslkssrDAKQQTLQElEQELEELGVQADAEAEERARIRRDELHE 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 224967071 358 NL---AGVRTNLLT-----------LQPALRTLTNDYNGLKRQV 387
Cdd:COG3096 1067 ELsqnRSRRSQLEKqltrceaemdsLQKRLRKAERDYKQEREQV 1110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-248 |
6.45e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN--------EQLRQELRRCEVELQELRaqpvvpcegceh 171
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARL--DALREELDELEAQIrgnggdrlEQLEREIERLERELEERE------------ 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967071 172 sQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ 248
Cdd:COG4913 359 -RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-442 |
1.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRsELGGtDAEKHRdRLMVENEQLRQELRRCEVEL----QELRAQPVVPCEGCEHSQESSQL 178
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELK-ELKE-KAEEYI-KLSEFYEEYLDELREIEKRLsrleEEINGIEERIKELEEKEERLEEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 179 RDKLSQLQLEVAENKGMLSELNlEVQQKTDRLAEVELRLKDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIK 257
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 258 TV-----EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELER-----AHGQML 327
Cdd:PRK03918 423 ELkkaieELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELA 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 328 EEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQ 407
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL----EELKKKLA----ELEKKLDELEEELAE 574
|
330 340 350
....*....|....*....|....*....|....*
gi 224967071 408 AIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKG 442
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
108-303 |
2.56e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.14 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 108 KEKLISQAQEVSRLRSELGGT-------DAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegceHSQESSQLRD 180
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEAQ---------QQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 181 KLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 260
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 224967071 261 VESSKTKQALSESQTRNQHLQEQVAMQRQV----LKEMEQQLQNSHQ 303
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQG 212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
102-425 |
2.75e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 102 VQVENLKEKLISQAQEVSRLRSELGGT-----DAEKHRDRLMVENEQLRQELRRCEVELQELR----------------- 159
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDApvdlgNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkcpe 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 160 -AQPVvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDrLAEVELRLKDcLAEKAqeeERLSRRLRDS 238
Cdd:PRK02224 457 cGQPV---EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIER-LEERR---EDLEELIAER 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 239 HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLrAQIAMYEAE 318
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDE 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 319 LERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVR 388
Cdd:PRK02224 608 IERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIG 684
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 224967071 389 GFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 425
Cdd:PRK02224 685 AVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-323 |
3.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 110 KLISQAQEVSRLRSELggtdaeKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQL--QL 187
Cdd:COG4717 65 KPELNLKELKELEEEL------KEAEEKEEEYAELQEELEELEEELEELE-------------AELEELREELEKLekLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 188 EVAENKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPvkyviktvevessKTK 267
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSL-------------ATE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224967071 268 QALSESQTRNQHLQEQVAMQRQVLKEMEQQLQnshqltvQLRAQIAMYEAELERAH 323
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELE-------ELEEELEQLENELEAAA 240
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
116-380 |
7.35e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 116 QEVSRLRSELGGTDAEKHRD--RLMVE----NEQLRQELRRC------EVELQELRAQPVVPCEGCEHSQESSQLRDkLS 183
Cdd:pfam17380 360 RELERIRQEEIAMEISRMREleRLQMErqqkNERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQRE-VR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 184 QLQLEVAENKGMLSELNLEVQQKTDRL--AEVELRLKDCLAEKAQEEERLSRRLRDshetiaslraqsppvkyviKTVEV 261
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKLELEKEKRDRKRAEEQRR-------------------KILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 262 ESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQlqnshqltvqlraqiamYEAELERAHGQMLEEMQSLEEDKNRAI 341
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-----------------REAEEERRKQQEMEERRRIQEQMRKAT 562
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 224967071 342 EE-----AFARAQVEMKAVHENLAG-----VRTNLLTLQPALRTLTNDY 380
Cdd:pfam17380 563 EErsrleAMEREREMMRQIVESEKAraeyeATTPITTIKPIYRPRISEY 611
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-430 |
9.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 222 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 301
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 302 HQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 367
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967071 368 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 430
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
152-430 |
2.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 152 EVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQlEVAENkgmLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERL 231
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEE---LEQLREELEQAREELEQLEEELE----QARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 232 SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQ 311
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 312 IAMYEAELERAHGQMLEEMQsleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFP 391
Cdd:COG4372 159 LESLQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 224967071 392 LLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 430
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
139-387 |
2.29e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 139 VENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQlevaenkGMLSELN-LEVQQKTDRLAEVELRL 217
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ------QQRSQLEQAKEGLSALN-------RLLPRLNlLADETLADRVEEIREQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 218 KDclAEKAQ-----------EEERLSRRLRDSHETIASLRAQSPPVKYVIKTV--------EVESSKTKQALSESQ---T 275
Cdd:PRK04863 904 DE--AEEAKrfvqqhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAkqqafaltEVVQRRAHFSYEDAAemlA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 276 RNQHLQEQVamqRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE------RAHGQMLEE-MQSLEEDKNRAIEEAFARA 348
Cdd:PRK04863 982 KNSDLNEKL---RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLAslkssyDAKRQMLQElKQELQDLGVPADSGAEERA 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 224967071 349 QVEMKAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 387
Cdd:PRK04863 1059 RARRDELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
106-344 |
3.72e-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: 46.99 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 106 NLKEKLISQAQEVSRLRSElggtdaekhRDRLMVENEQLR--QELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLS 183
Cdd:pfam05622 215 KLEEKLEALQKEKERLIIE---------RDTLRETNEELRcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 184 QLQLEvaeNKgMLSELnlEVQQKTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVES 263
Cdd:pfam05622 286 RLQHE---NK-MLRLG--QEGSYRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 264 SKT------KQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVqlraqiamyeAELERAHGQMLEEMQSLEEDK 337
Cdd:pfam05622 353 SKAedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERY 422
|
....*..
gi 224967071 338 NRAIEEA 344
Cdd:pfam05622 423 KKYVEKA 429
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
173-349 |
6.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 173 QESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 245
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 246 RAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEA---ELE 320
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 224967071 321 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 349
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-432 |
8.23e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQ------------LRQELRRCEVELQELRAQPVVPCE 167
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeLEKQLNQLKSEISDLNNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 168 GCEHSQESSQlRDKLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDSHETIASLRA 247
Cdd:TIGR04523 310 KELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 248 QSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIamyeAELErahgqml 327
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KDLT------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 328 EEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKAE 404
Cdd:TIGR04523 447 NQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK----ELEEKVKDLTKK 518
|
330 340
....*....|....*....|....*...
gi 224967071 405 IGQAIEEVNSNNQELLRKYRRELQLRKK 432
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
100-430 |
8.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvPCEGCEHSQESSQLR 179
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER---LEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 180 DKLSQLQLEVAE--------NKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHE-------- 240
Cdd:COG4717 170 AELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEEELEEAqeeLEELEEELEQLENELEAAALeerlkear 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 241 -------TIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQ 299
Cdd:COG4717 250 lllliaaALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 300 NSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVemkavhENLAGVRtNLLTLQPALRTLTN 378
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGV------EDEEELR-AALEQAEEYQELKE 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 224967071 379 DYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 430
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-397 |
9.20e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSElggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQ--PVVPCEGcEHSQESSQLRD 180
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNE------GDHLRNVQTECEALKLQMAEKDKVIEILRQQieNMTQLVG-QHGRTAGAMQV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 181 KLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIA 243
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELN 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 244 SLRAQSPPVKYVIKT----VEVESSKTKQALSESQTrnqhlqeQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAEL 319
Cdd:pfam15921 671 SLSEDYEVLKRNFRNkseeMETTTNKLKMQLKSAQS-------ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224967071 320 ErahgQMLEEMQSLEEDKNRAIEEAFARAQvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEA 397
Cdd:pfam15921 744 D----ALQSKIQFLEEAMTNANKEKHFLKE-EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
131-430 |
9.93e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 131 EKHRDRLM----VENEQLRQELRRCEVELQELRAQpVVPCEGcEHSQESSQLRDKLSQLQLEVAENKgmLSELNLEVQQK 206
Cdd:PRK03918 447 EEHRKELLeeytAELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESELIKLKELAEQLKELEEK--LKKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 207 TDRLAEvelRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppVKYVIKTVEVESSKTKQALSES-----QTRNQHLQ 281
Cdd:PRK03918 523 KAEEYE---KLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELgfesvEELEERLK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 282 EQVAMQRQV--LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENL 359
Cdd:PRK03918 596 ELEPFYNEYleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967071 360 AGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAE---IGQAIEEVnSNNQELLRKYRRELQLR 430
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKElekLEKALERV-EELREKVKKYKALLKER 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-413 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 127 GTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQlEVAENKGMLSELNLEVQQK 206
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAE----------LDALQERREALQRLA-EYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 207 TDRLAEVEL------RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQT 275
Cdd:COG4913 674 EAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 276 RNQHLQEQV--AMQRQVLKEMEQQLQNSHQltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMK 353
Cdd:COG4913 747 LRALLEERFaaALGDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYL 818
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 354 AVHENLagVRTNLLTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 413
Cdd:COG4913 819 ALLDRL--EEDGLPEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
172-436 |
1.73e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 172 SQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 249
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 250 PPVKYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERa 322
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 323 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 399
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 224967071 400 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 436
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
177-343 |
3.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 177 QLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIASLRAqsppvkYVI 256
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNKE------YEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 257 KTVEVESSKTKQALSESQTRNqhLQEQVAMQRQVLKEMEQQLQnshqltvQLRAQIAMYEAELERAHGQMLEEMQSLEED 336
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 224967071 337 KNRAIEE 343
Cdd:COG1579 165 REELAAK 171
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
134-349 |
3.87e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 134 RDRLMVEneqlRQELRRCEVELQElraqpvvpcegcehsQESSQLRdKLSQLQLEVAENkgMLSELNLEVQQKTDRLAEV 213
Cdd:pfam15709 335 RDRLRAE----RAEMRRLEVERKR---------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLR 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 214 ELRLKDclAEKAQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQV 290
Cdd:pfam15709 393 KQRLEE--ERQRQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKR 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224967071 291 LKEMEQQlqnsHQLTVQLRAQiamyEAElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 349
Cdd:pfam15709 468 LMEMAEE----ERLEYQRQKQ----EAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
116-352 |
3.89e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 116 QEVSRLRSELggtdAEKHRDRLmveneqlrqelrrcEVELQELRaqpvvpcegcehSQESSQlRDKLSQLQLE----VAE 191
Cdd:PRK10929 203 QELARLRSEL----AKKRSQQL--------------DAYLQALR------------NQLNSQ-RQREAERALEstelLAE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 192 NKGMLSELNLEvQQKTDRlaevelRLKDCLAEKAQEEERLSRRLRdsheTIASlraQSPPVKYVIKTVEVESsktkQALS 271
Cdd:PRK10929 252 QSGDLPKSIVA-QFKINR------ELSQALNQQAQRMDLIASQQR----QAAS---QTLQVRQALNTLREQS----QWLG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 272 ESQTRNQHLQEQVAMqrqvLKEME--QQLQNShqlTVQLRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRaIEEAFA 346
Cdd:PRK10929 314 VSNALGEALRAQVAR----LPEMPkpQQLDTE---MAQLRVQRLRYEDLLNKQPQLRqirQADGQPLTAEQNR-ILDAQL 385
|
....*.
gi 224967071 347 RAQVEM 352
Cdd:PRK10929 386 RTQREL 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-360 |
4.05e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 107 LKEKLISQAQEVSRLRSELggtdAEKHRdrlmvENEQLRQELRRCEVELQELRAQpvvpCEGCEHSQESSQLRdkLSQLQ 186
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSI----AEKER-----ELEDAEERLAKLEAEIDKLLAE----IEELEREIEEERKR--RDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 187 LEVAENKgmlSELNLEVQqktdRLAEVELRLKDCLAEKAQEEERLS---RRLRDSHETIASLRAQSPPVKYVIKTVEVES 263
Cdd:TIGR02169 357 EEYAELK---EELEDLRA----ELEEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAI 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 264 SKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELerahgqmleemqsleEDKNRAIEE 343
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---------------SKLQRELAE 494
|
250
....*....|....*..
gi 224967071 344 AFARAQVEMKAVHENLA 360
Cdd:TIGR02169 495 AEAQARASEERVRGGRA 511
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
105-369 |
4.13e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 105 ENLKEKLISQAQEVSRLRSELggtdaekhRDRLMVENEQLRQELRRcevELQELRAQpvvpcegcehSQESSQLRDKLSQ 184
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFSLLK--------KETIYLQSAQRVELAER---QLQELKID----------VKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 185 LQLEVAENKGML-SELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLRAQSPPVKYVIKTVEV 261
Cdd:COG5022 904 LESEIIELKKSLsSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTI 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 262 ESSKTKQALSESQTRNQHLQEQV----AMQRQV--LKEMEQQLQNSHQLTVQLRA-----QIAMYEAELERAHgqMLEEM 330
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQKLKGLL--LLENN 1060
|
250 260 270
....*....|....*....|....*....|....*....
gi 224967071 331 QSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 369
Cdd:COG5022 1061 QLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
114-334 |
4.31e-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: 44.19 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 114 QAQEV-SRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQ----ELRAQPVVPCEGCEHSQESSQLRDKLSQLQle 188
Cdd:TIGR00618 308 QAQRIhTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqeiHIRDAHEVATSIREISCQQHTLTQHIHTLQ-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 189 vaENKGMLSELNLEVQQKTDRLAEvelrlkdclaEKAQEEERLSRRlRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQ 268
Cdd:TIGR00618 386 --QQKTTLTQKLQSLCKELDILQR----------EQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224967071 269 alsESQTRNQHLQEQvamqRQVLKEMEQQLQNSHQLTVQlraqiamyEAELERAHGQMLEEMQSLE 334
Cdd:TIGR00618 453 ---CEKLEKIHLQES----AQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEP 503
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
175-337 |
4.88e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 42.29 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 175 SSQLRDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 248
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 249 SPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLE 328
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASE--------------LKKEFEEVSELIKS 175
|
....*....
gi 224967071 329 EMQSLEEDK 337
Cdd:cd07627 176 ELERFERER 184
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-486 |
8.31e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKL--ISQAQEVSRLRSELGGTDAEKHRDRlmvENEQLRQELRRCEVELQelRAQPVVPCEGCEHSQESSQLRD 180
Cdd:PTZ00121 1458 KAEEAKKKAeeAKKADEAKKKAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 181 KLSQLQLEVAENKGMLSELnlevqQKTDRLAEVELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVE 260
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL-----KKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 261 VESS-KTKQALSESQTRNQhlQEQVAMQRQVLKEMEQ-------------QLQNSHQLTVQLRAQIAMYEAELERAhgqm 326
Cdd:PTZ00121 1603 EEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK---- 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 327 LEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIG 406
Cdd:PTZ00121 1677 AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEA 1735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 407 QAIEEVNSNNQELLRKYRRE----LQLRKKCHNELVRLKGNIRVIARvRPVTKEDGEGPEATNAVTFDPDDDS--IIHLL 480
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGG 1814
|
....*.
gi 224967071 481 HKGKPV 486
Cdd:PTZ00121 1815 KEGNLV 1820
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
103-366 |
1.15e-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: 42.50 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSELGGTD---AEKHR--DRLMVENEQLRQELRRcevELQELRaqpvvpcegcehsQESSQ 177
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEealSEKERiiERLKEQREREDRERLE---ELESLK-------------KENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 178 LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAqSPPVKY 254
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRT-NPEIND 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 255 VIKTVEVESSKTKQALSESQTRNQHLQE---QVAMQR----QVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQML 327
Cdd:pfam10174 559 RIRLLEQEVARYKEESGKAQAEVERLLGilrEVENEKndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 224967071 328 EEMQSLEEDKNRA-----IEE---AFARAQVEMKAVHENLAGVRTNL 366
Cdd:pfam10174 639 EEARRREDNLADNsqqlqLEElmgALEKTRQELDATKARLSSTQQSL 685
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
230-353 |
1.29e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 230 RLSRRLRDshETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 299
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224967071 300 -------NSHQLtVQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 353
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-437 |
1.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 105 ENLKEKLISQAQEVSRLRSE---------LGGTDAE---KHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGC-EH 171
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEErddllaeagLDDADAEaveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAdDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 172 SQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAQ 248
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdLGNAEDFLEELREERDELREREAELEAT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 249 SPPVKYVIKTVE--------------VESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLtVQLRAQIAM 314
Cdd:PRK02224 435 LRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 315 YEAELERAHGQMLEEMQSLEEDKNRAIE--------EAFARAQVE-MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR 385
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEElreraaelEAEAEEKREaAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 224967071 386 qvrgfplllQEALRSVKAEIGQAIEEVNSNNQEL--LRKYRRE-LQLRKKCHNEL 437
Cdd:PRK02224 594 ---------IRTLLAAIADAEDEIERLREKREALaeLNDERRErLAEKRERKREL 639
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
114-343 |
1.48e-03 |
|
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: 41.80 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 114 QAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcEGCEHSQESSQLRDKLSQ----LQLEV 189
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE---ELEEKYKELSASSEELSEekdaLLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 190 AENKGMLSELNLEVQQKTDRLAEVELRLkDCLAEKAqeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQA 269
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETEL-ERMKERA---KKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967071 270 LSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAElERAHGQMLEEMQSLEEDKNRAIEE 343
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS-ERKVEGLGEELSSMAAQRDRTQAE 273
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
100-367 |
1.64e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKLISQAQEVSRLRsELGGTDAEKHRDRLmvenEQLRQELRrcevelqelraqpvvpcegcEHSQESSQLR 179
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK--------------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 180 DKLSQLQLEVAENKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrLRDSHETIAslraqsp 250
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK-IKDKLKELQ------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 251 pvkyviktvevessktkQALSESQTRNQHLQE---QVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQML 327
Cdd:PHA02562 313 -----------------HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 224967071 328 EEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 367
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
142-365 |
1.77e-03 |
|
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: 42.04 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 142 EQLRQELRRCEVE----LQELRAQPVVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 216
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 217 LKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 296
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224967071 297 ---QLQNSHQLTVQLRAQIAMYEAELErahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTN 365
Cdd:pfam05557 154 lrqNLEKQQSSLAEAEQRIKELEFEIQ------SQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN 219
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
97-432 |
1.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 97 RLYLTVQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESS 176
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEEL---------EQLREELEQAREELEQLEEELEQAR-------------SELE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 177 QLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAevelRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 256
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAE----ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 257 KTVEVESSKTKQALSESQTRNQHLQEQVAmqRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 336
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 337 KNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN 416
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
330
....*....|....*.
gi 224967071 417 QELLRKYRRELQLRKK 432
Cdd:COG4372 311 GALEDALLAALLELAK 326
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
108-430 |
2.63e-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: 41.48 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 108 KEKLISQAQEVSRLRSELGG-TDAEKH--------RDRLMVENEQLRQE--LRRCEVELQELRAQPVVPCEGCEHSQES- 175
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEElSARESDleqdyqaaSDHLNLVQTALRQQekIERYQEDLEELTERLEEQEEVVEEAAEQl 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 176 SQLRDKLSQLQLEVAENKGMLSELN--LEVQQK--------TDRLAEVELRL----------KDCLAE-KAQEEER---- 230
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQqaLDVQQTraiqyqqaVQALEKARALCglpdltpenaEDYLAAfRAKEQQAteev 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 231 --LSRRLRDSHETIASLRAQSPPVKYVIKTVEVES--SKTKQALSESQTRnQHLQEQVAMQRQVLKEMEQQLQNSH---- 302
Cdd:COG3096 458 leLEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ-QALAQRLQQLRAQLAELEQRLRQQQnaer 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 303 ---QLTVQLRAQIAMYEaELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNLLTLQPALRTltnd 379
Cdd:COG3096 537 lleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARAPAWLA---- 606
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 224967071 380 ynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 430
Cdd:COG3096 607 --------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-451 |
2.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDShetiasLRAQ 248
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKN------LTVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 249 SPPVKYVIkTVEVESSKTKQA-------------------LSESQTRNQHLQEQVAMQRQVLKEMEQQLQN---SHQLtV 306
Cdd:COG3206 131 PVKGSNVI-EISYTSPDPELAaavanalaeayleqnlelrREEARKALEFLEEQLPELRKELEEAEAALEEfrqKNGL-V 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 307 QLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHEN--LAGVRTNLLTLQPALRTLTNDYNG 382
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARlaALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224967071 383 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLrkyRRELQLRKkchnELVRLKGNIRVIARVR 451
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ---AREASLQA----QLAQLEARLAELPELE 350
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
93-438 |
2.85e-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: 41.25 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 93 RSPHRLYLT---VQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQLRQELRRCEVELQELRAQpvvpcegc 169
Cdd:pfam05483 344 KAAHSFVVTefeATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS--SELEEMTKFKNNKEVELEELKKI-------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 170 ehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclAEKAQEEERLSRRLRDSHETIASLRAQS 249
Cdd:pfam05483 414 --LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 250 PPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEE 329
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 330 MQSLEEDKnRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAI 409
Cdd:pfam05483 568 LDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA----ENKQLNAYEIKVNKLE 642
|
330 340 350
....*....|....*....|....*....|..
gi 224967071 410 EEVNSNNQ---ELLRKYRRELQLRKKCHNELV 438
Cdd:pfam05483 643 LELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
234-441 |
3.24e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 234 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 300
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 301 SH-----QLTVQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 368
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224967071 369 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 441
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-248 |
3.57e-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: 41.20 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKL 182
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEEALALLRSELEELSEELR------ELESKRSELRREL 917
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDShetIASLRAQ 248
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR---LKRLENK 980
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
137-424 |
3.74e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 137 LMVENEQLRQELRRCEVELQELRAQPVvpcegcehSQESSQLRDKL----SQLQLEVAENKgmlselnlEVQQKTDRLAE 212
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEA--------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 213 VELRLKDCLAEKAQEEERLSRrlrdshetiaslraqsppvKYVIKTVEVESSKTKQA-LSESQTRNQHLQEQVAMQRQV- 290
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVKQ-------------------SYTLNESELESVRQLEKqLESLEKQYDEITERIAEQEIAy 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 291 ------LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHgQMLEEMQS-LEEDKnRAIE------------EAFARAQVE 351
Cdd:PRK04778 379 selqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR-EKLERYRNkLHEIK-RYLEksnlpglpedylEMFFEVSDE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 352 MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRK 422
Cdd:PRK04778 457 IEALAEELEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFRE 532
|
..
gi 224967071 423 YR 424
Cdd:PRK04778 533 YD 534
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-419 |
3.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSELggtdaeKHRDRLMVENEQLRQELRRCEVELQELRAQPVVpcegcEHSQESSQLRDKL 182
Cdd:COG4717 133 ELEALEAELAELPERLEELEERL------EELRELEEELEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclaEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV- 259
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIa 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 260 -------------EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQM 326
Cdd:COG4717 277 gvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 327 LEEMQSLEEDKNRA-IEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLL------------ 393
Cdd:COG4717 357 EELEEELQLEELEQeIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldeeeleeelee 436
|
330 340
....*....|....*....|....*.
gi 224967071 394 LQEALRSVKAEIGQAIEEVNSNNQEL 419
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAEL 462
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
100-426 |
3.94e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRdrlmveneQLRQELRRCEVELQELRAQpvVPCEGCEHSQESSQLR 179
Cdd:pfam07111 268 LQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPK--------KCRSLLNRWREKVFALMVQ--LKAQDLEHRDSVKQLR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 180 DKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAE--KAQEEERLSRRLRDS------------------- 238
Cdd:pfam07111 338 GQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsRAQEARRRQQQQTASaeeqlkfvvnamsstqiwl 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 239 -------HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVA---MQRQVLKEMEQQLQNSHQLTVQL 308
Cdd:pfam07111 418 ettmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPappVDADLSLELEQLREERNRLDAEL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 309 RAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQvemkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVR 388
Cdd:pfam07111 498 QLSAHLIQQEVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-------ESLASVGQQLEVARQGQQESTEEAASLRQELT 569
|
330 340 350
....*....|....*....|....*....|....*...
gi 224967071 389 GFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 426
Cdd:pfam07111 570 QQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
100-358 |
4.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLmvenEQLRQELRRCEVELQELRAQPVVpCEGCEhsQESSQLR 179
Cdd:PRK04863 863 QRSQLEQAKEGL----SALNRLLPRLNLLADETLADRV----EEIREQLDEAEEAKRFVQQHGNA-LAQLE--PIVSVLQ 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 180 ---DKLSQLQLEVAENKGMLSElnleVQQKTDRLAEVELRL--------KDCLAEKAQEEERLSRRLRDSHETIASLRAQ 248
Cdd:PRK04863 932 sdpEQFEQLKQDYQQAQQTQRD----AKQQAFALTEVVQRRahfsyedaAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ 1007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 249 sppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEM-------------------EQQLQNSHQLTVQLR 309
Cdd:PRK04863 1008 -------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgaeerararrdelHARLSANRSRRNQLE 1080
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 224967071 310 AQIAMYEAELERAHGQmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHEN 358
Cdd:PRK04863 1081 KQLTFCEAEMDNLTKK-LRKLERDYHEMREQVVNAKAGWCAVLRLVKDN 1128
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
108-234 |
4.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 108 KEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQL-- 185
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE-------------EELEELREELAELea 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 224967071 186 QLEVAENKGMLSELNLEVQQKTDRLAEVE-----LRLKDCLAEKAQEEERLSRR 234
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAeewaaLKLALELLEEAREEYREERL 514
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
103-363 |
4.44e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRqELRRcevELQELRAQpvVPcegcEHSQESSQLRDKL 182
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEI-----EELKEKRDELNEELK-ELAE---KRDELNAQ--VK----ELREEAQELREKR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVElRLKDCLAEKAQEEERLSR---RLRDSHET--------------IASL 245
Cdd:COG1340 67 DELNEKVKELKEERDELNEKLNELREELDELR-KELAELNKAGGSIDKLRKeieRLEWRQQTevlspeeekelvekIKEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 246 RAQsppvkyvIKTVEVESSKTKQaLSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQ 325
Cdd:COG1340 146 EKE-------LEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 224967071 326 MLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVR 363
Cdd:COG1340 218 IVEAQEKADE-----LHEEIIELQKELRELRKELKKLR 250
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
116-437 |
5.16e-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: 40.34 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 116 QEVSRLRSELGGTDAE-----KHRDRLMVENEQLRQELRRCEVELQELRA------QPVVPCEgcEHSQESSQLRDKL-- 182
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQltserKQRASLKEQMQEIQQSFSILTQCDNRSKEdipnlqNITVRLQ--DLTEKLSEAEDMLac 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 -SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKyviktvev 261
Cdd:TIGR00618 613 eQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK-------- 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 262 ESSKTKQALSESQTRNqHLQEQVAMQRQVLKEMEQQLqnsHQLTVQLRAQIAMYEAELErAHGQMLEEMQSLEEDKNRAI 341
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLA-QCQTLLRELETHIEEYDREF---NEIENASSSLGSDLAARED-ALNQSLKELMHQARTVLKAR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 342 EEAFARAQVEMkavhenlagvrtnlltlqPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLR 421
Cdd:TIGR00618 760 TEAHFNNNEEV------------------TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNL 821
|
330
....*....|....*.
gi 224967071 422 KYRRELQLRKKCHNEL 437
Cdd:TIGR00618 822 QCETLVQEEEQFLSRL 837
|
|
| BAR_Bin3 |
cd07590 |
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ... |
276-360 |
6.01e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153274 Cd Length: 225 Bit Score: 39.27 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 276 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAqIAMYEAELERAHGQMLEEMQSLEEDKNRAIE---EAFARAQV 350
Cdd:cd07590 117 REQSLQEYERLQAKVekLAEKEKTGPNLAKLEQAEKA-LAAARADFEKQNIKLLEELPKFYNGRTDYFQpcfEALIKSQV 195
|
90
....*....|....
gi 224967071 351 ----EMKAVHENLA 360
Cdd:cd07590 196 lyysQSTKIFTQLA 209
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
179-352 |
6.15e-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: 38.88 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 179 RDKLSQLQLEVAENKGMLSELNLEVQQktdRLAEVELRLKDCLAEKAQEEERLSRR--------LRDSHETIASLRAqsp 250
Cdd:cd07596 34 RRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAAEELSSLSEAQANQelvkllepLKEYLRYCQAVKE--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 251 pvkyVIKT-----VEVESSKtkQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAqiamyeaELERAHGQ 325
Cdd:cd07596 108 ----TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARK-------RYEEISER 174
|
170 180 190
....*....|....*....|....*....|
gi 224967071 326 MLEEMQSLEEDKNRAIEEA---FARAQVEM 352
Cdd:cd07596 175 LKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
196-320 |
6.33e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 196 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQT 275
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 224967071 276 RNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE 320
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
132-432 |
7.09e-03 |
|
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: 40.03 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 132 KHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEgcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLA 211
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACE----------IRDQITSKEAQLESSREIVKSYENELDPLKNRLK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 212 EVE------LRLKD---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQTRNQHLQE 282
Cdd:TIGR00606 256 EIEhnlskiMKLDNeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 283 QVAMQRQVLKEMEQQLQNsHQLTVQLRA---QIAMYEAELERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMK 353
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLV-EQGRLQLQAdrhQEHIRARDSLIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 354 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQ 428
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELS 488
|
....
gi 224967071 429 LRKK 432
Cdd:TIGR00606 489 KAEK 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
100-247 |
7.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 100 LTVQVENLKEKL--ISQAQEVSRLRSELGGTDAEKHRDRLMV--ENEQLRQELRRCEVELQELRAqpvvPCEGCEHSQES 175
Cdd:COG4717 352 LLREAEELEEELqlEELEQEIAALLAEAGVEDEEELRAALEQaeEYQELKEELEELEEQLEELLG----ELEELLEALDE 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224967071 176 SQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEveLRLKDCLAEKAQEEERLSRRLRDSHETIASLRA 247
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
103-372 |
7.77e-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: 39.94 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLmvenEQLRQELRRCEVELQELRaqpvvpcegcEHSQESSQLRDKL 182
Cdd:COG3096 865 QLDQLKEQL----QLLNKLLPQANLLADETLADRL----EELREELDAAQEAQAFIQ----------QHGKALAQLEPLV 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 183 SQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLkDCLAEKAQEEERLS-----RRLRDSHETIASLRAQsppvkyvIK 257
Cdd:COG3096 927 AVLQSDPEQFE----QLQADYLQAKEQQRRLKQQI-FALSEVVQRRPHFSyedavGLLGENSDLNEKLRAR-------LE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 258 TVEVESSKTKQALSESQTR-NQHLQEQVAMQ------RQVLKEMEQ--------------------------QLQNSHQL 304
Cdd:COG3096 995 QAEEARREAREQLRQAQAQySQYNQVLASLKssrdakQQTLQELEQeleelgvqadaeaeerarirrdelheELSQNRSR 1074
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224967071 305 TVQLRAQIAMYEAELERAHGQMLEemqsLEED---KNRAIEEAFARAQVEMKAVHENlaGVRTNLLTLQPA 372
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRK----AERDykqEREQVVQAKAGWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
102-445 |
8.66e-03 |
|
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: 39.82 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 102 VQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRlmvENEQLRQELRRCE---VELQELRAQPVVPCEGCEH--SQESS 176
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSEL--RQARKRRDQ---ASEALRQASRRLEerqSALDELELQLFPQAGTLLHflRKEAP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 177 QLRDKLSQL-QLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA-EKAQEEERLSRR-------LRDSHETIASLRA 247
Cdd:pfam12128 546 DWEQSIGKViSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVpEWAASEEELRERldkaeeaLQSAREKQAAAEE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 248 QSPPVKYVIKTVEVESSKTKQALSESQTR-----NQHLQEQVAMQRQV---LKEMEQQLQN-SHQLTVQLRAQIAMYEA- 317
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKALaerKDSANERLNSlEAQLKQLDKKHQAWLEEq 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 318 --ELERAHGQMLEEMQSLEEDKNRA---IEEAFARAQVEMKA--------VHENLAGV---RTNLLTLQPALRTLT---N 378
Cdd:pfam12128 706 keQKREARTEKQAYWQVVEGALDAQlalLKAAIAARRSGAKAelkaletwYKRDLASLgvdPDVIAKLKREIRTLErkiE 785
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224967071 379 DYNGLKRQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL----RKKCHNELVRLKGNIR 445
Cdd:pfam12128 786 RIAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
178-379 |
8.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 178 LRDKLSQLQLEVAENKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyvi 256
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELRE--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 257 ktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqlTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 336
Cdd:COG4717 117 ---ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224967071 337 KNRAIEEA---FARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 379
Cdd:COG4717 190 TEEELQDLaeeLEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
256-335 |
8.90e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.28 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 256 IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQMLEEMQS 332
Cdd:pfam12718 23 VKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNnenLTRKIQLLEEELEESDKRLKETTEK 102
|
...
gi 224967071 333 LEE 335
Cdd:pfam12718 103 LRE 105
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
115-236 |
8.97e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.44 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 115 AQEVSRLRSELGGTDAE-KHRDRLMVE-NEQLRQ---ELRRCEVELQELRAqpvvpcegcehsqESSQLRDKLSQLQLEV 189
Cdd:pfam06818 30 LNEIVALRAQLRELRAKlEEKEEQIQElEDSLRSktlELEVCENELQRKKN-------------EAELLREKVGKLEEEV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 224967071 190 AENKGMLSELNLEVQQKTDRLAEVELRLK--DCLAEKAQEEERLSRRLR 236
Cdd:pfam06818 97 SGLREALSDVSPSGYESVYESDEAKEQRQeeADLGSLRREVERLRAELR 145
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-438 |
9.87e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 103 QVENLKEKLISQAQEVSRLRS-----ELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQ 177
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK------SKEKELKK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 178 LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVKYVIK 257
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN----------------LEKEID 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 258 TVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSLEEDK 337
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK----LSSIIKNIKSKK 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967071 338 NRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQPALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIEevNS 414
Cdd:TIGR04523 641 NKLKQEV--------KQIKETIKEIRnkwPEIIKKIKESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR--IK 704
|
330 340
....*....|....*....|....*..
gi 224967071 415 NNQELLRKYR---RELQLRKKCHNELV 438
Cdd:TIGR04523 705 DLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| |
