|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
304-631 |
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: 530.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 304 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 382
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 383 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 459
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 460 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 539
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 540 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 619
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 224967075 620 LRFAERVRSVEL 631
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
312-629 |
1.47e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 437.00 E-value: 1.47e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 312 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 388
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 389 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 468
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 469 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 545
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 546 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFA 623
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 224967075 624 ERVRSV 629
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
306-633 |
1.27e-144 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 424.68 E-value: 1.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 381
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 382 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 461
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 462 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 539
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 540 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 617
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 224967075 618 YSLRFAERVRSVELGP 633
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
306-627 |
1.55e-125 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 375.44 E-value: 1.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 382
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 383 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 460
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 461 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 538
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 539 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 617
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 224967075 618 YSLRFAERVR 627
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
306-629 |
4.20e-108 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 330.96 E-value: 4.20e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 377
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 378 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 454
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 455 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 530
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 531 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 609
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 224967075 610 EKNTSETLYSLRFAERVRSV 629
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
307-630 |
4.01e-105 |
|
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: 323.51 E-value: 4.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 307 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 384
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 385 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 458
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 459 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 528
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 529 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 605
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 224967075 606 VSPVEKNTSETLYSLRFAERVRSVE 630
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
306-629 |
7.55e-96 |
|
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: 299.64 E-value: 7.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 368
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 369 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 447
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 448 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 526
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 527 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 601
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 224967075 602 MVVQVSPVEKNTSETLYSLRFAERVRSV 629
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
306-629 |
2.56e-92 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 289.61 E-value: 2.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 383
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 384 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 460
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 461 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 540
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 541 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 619
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 224967075 620 LRFAERVRSV 629
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
305-629 |
3.52e-91 |
|
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: 288.10 E-value: 3.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 305 GNIRVIARVRPVTKEDGEGPeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQE 369
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 370 VQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDLL 447
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 448 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 522
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 523 TGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 592
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 224967075 593 SLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSV 629
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
306-629 |
2.85e-90 |
|
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: 284.23 E-value: 2.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 384
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 385 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 464
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 465 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT---GKLNLVDLAGSER 541
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvrvSTLNLIDLAGSER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 542 VGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 619
Cdd:cd01374 232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
330
....*....|
gi 224967075 620 LRFAERVRSV 629
Cdd:cd01374 312 LKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
306-629 |
3.03e-87 |
|
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: 277.28 E-value: 3.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 380
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 381 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 449
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 450 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 524
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 525 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 604
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 224967075 605 QVSPVEKNTSETLYSLRFAERVRSV 629
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
290-630 |
3.87e-80 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 265.45 E-value: 3.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 290 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 369
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 370 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 448
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 449 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 528
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 529 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 606
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 224967075 607 SPVEKNTSETLYSLRFAERVRSVE 630
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
307-624 |
3.62e-78 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 253.47 E-value: 3.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 307 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 375
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 376 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 451
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 452 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 526
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 527 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 598
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 224967075 599 KTLMVVQVSPVEKNTSETLYSLRFAE 624
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
306-627 |
6.77e-78 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 252.81 E-value: 6.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 384
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 385 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgkEP- 451
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 452 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 528
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 529 gKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 604
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 224967075 605 QVSPVEKNTSETLYSLRFAERVR 627
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
306-627 |
7.98e-73 |
|
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: 7.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 382
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 383 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 462
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 463 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 541
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 542 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLR 621
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 224967075 622 FAERVR 627
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
307-627 |
1.27e-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: 235.55 E-value: 1.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 307 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 375
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 376 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 452
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 453 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 527
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 528 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 606
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 224967075 607 SPVEKNTSETLYSLRFAERVR 627
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
306-626 |
1.76e-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: 224.48 E-value: 1.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 306 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 377
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 378 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 453
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 454 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 533
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 534 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 611
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 224967075 612 NTSETLYSLRFAERV 626
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
307-630 |
7.88e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 215.57 E-value: 7.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 307 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 385
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 386 FAYGQTGAGKTYTMEGtPENP-----------GINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLgk 449
Cdd:PLN03188 170 FAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 450 EP-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLR 526
Cdd:PLN03188 247 DPsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 527 T--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSK 599
Cdd:PLN03188 325 SfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAK 404
|
330 340 350
....*....|....*....|....*....|.
gi 224967075 600 TLMVVQVSPVEKNTSETLYSLRFAERVRSVE 630
Cdd:PLN03188 405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
286-447 |
1.46e-41 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 147.75 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 286 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 365
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 366 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 445
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 224967075 446 LL 447
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
354-573 |
4.89e-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: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 354 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 432
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 433 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 512
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224967075 513 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 573
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-277 |
4.53e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 6 QLRQELRRCEVELQELRAQpvvpcegcehsqessQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR------ 79
Cdd:TIGR02168 217 ELKAELRELELALLVLRLE---------------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselee 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 80 ----LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLK 155
Cdd:TIGR02168 282 eieeLQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 156 EMEQQLQNSHQLT--------------VQLRAQIAMYEAELER--AHGQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVH 219
Cdd:TIGR02168 362 ELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleARLERLEDRRERLQQEIEELLKKLEEA--ELKELQ 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 224967075 220 ENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNS 277
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAERELAQLQARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
5-207 |
2.43e-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: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRAQ---PVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE---- 77
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKnglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspv 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 78 -LRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLK 155
Cdd:COG3206 265 iQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLA 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224967075 156 EMEQQLQNSHQLTVQLRAQIAMYEAeLERAHGQMLEEMQSLEEDKNRAIEEA 207
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEV-ARELYESLLQRLEEARLAEALTVGNV 388
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-250 |
2.54e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLS------------ELNLEVQQKTDR 72
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKS------ELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 73 LAEVELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAM 149
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 150 QRQVLKEMEQQLQ---------NSHQLTVQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEED 199
Cdd:TIGR02169 894 LEAQLRELERKIEeleaqiekkRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPV 973
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 224967075 200 KNRAIE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 250
Cdd:TIGR02169 974 NMLAIQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-292 |
2.85e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkd 82
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELE------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 cLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQ 162
Cdd:COG1196 297 -LARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 163 NSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLT 240
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 224967075 241 NDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 292
Cdd:COG1196 449 EEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-274 |
2.97e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkd 82
Cdd:COG1196 254 ELEELEAELAELEAELEELR-------------LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER--- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 cLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQ 162
Cdd:COG1196 318 -LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 163 NSHQLTVQLRAQIAMYEAELERahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 242
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270
....*....|....*....|....*....|..
gi 224967075 243 YNGLKRQVRGfpLLLQEALRSVKAEIGQAIEE 274
Cdd:COG1196 472 AALLEAALAE--LLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-290 |
1.78e-09 |
|
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: 61.24 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKD 82
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQ------ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 CLAEKAQEEERLSrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKtkqalsesqtrnqhLQEQVAMQRQVLKEMEQQLQ 162
Cdd:TIGR02169 763 LEARIEELEEDLH-KLEEALNDLEARLSHSR-----IPEIQAELSK--------------LEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 163 NSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLT 240
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 224967075 241 NDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRREL 290
Cdd:TIGR02169 903 RKIEELEAQI--------EKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-307 |
1.06e-08 |
|
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: 58.53 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 35 SQESSQL--RDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 112
Cdd:TIGR02168 667 KTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 113 PPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG----- 187
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanl 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 188 ----QMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRS 263
Cdd:TIGR02168 823 rerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 224967075 264 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 307
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-314 |
1.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 40 QLRDKLSQLQLEVAENKgmLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIaslraqsppvkyvi 119
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEEL-------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 120 ktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 199
Cdd:COG1196 280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 200 KN--RAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNS 277
Cdd:COG1196 357 EAelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAE 432
|
250 260 270
....*....|....*....|....*....|....*..
gi 224967075 278 NNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVR 314
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-275 |
1.53e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRAQPVVPCEGCEHSQE-SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC 83
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEErRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 84 LAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvikTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV-LKEMEQQLQ 162
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEEL---------AEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 163 NSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 242
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
250 260 270
....*....|....*....|....*....|....*..
gi 224967075 243 YNGLKR--QVRGFPLLLQE--ALRSVKAEIGQAIEEV 275
Cdd:COG1196 507 LEGVKAalLLAGLRGLAGAvaVLIGVEAAYEAALEAA 543
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
5-282 |
8.99e-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: 55.51 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRAQPVVPCEGCEHSQE--------SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEV 76
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMErqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 77 ELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQRQVLK 155
Cdd:pfam15921 495 ERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIE 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 156 EMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENL 222
Cdd:pfam15921 566 ILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERL 645
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 223 AGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 282
Cdd:pfam15921 646 RAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
288-572 |
1.43e-07 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 54.74 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 288 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 355
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 356 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 434
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 435 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 508
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224967075 509 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 572
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3-224 |
1.93e-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: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKD 82
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELA------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQ 152
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224967075 153 VLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENLAG 224
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-275 |
2.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 1 MVENeqlRQELRRCEVELQELRAQpvvpcegCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVEL-R 79
Cdd:COG4913 230 LVEH---FDDLERAHEALEDAREQ-------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 80 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQRQVLKEME 158
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 159 QQLQNSHQLTVQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRT 238
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
250 260 270
....*....|....*....|....*....|....*..
gi 224967075 239 LTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 275
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
46-268 |
4.05e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 46 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK-----AQEEERLSRRLRDSHETIASLRAQSPPVKYVIK 120
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 121 TVEVESSKTKQALSE--SQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSlEE 198
Cdd:COG3206 244 ALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA-EL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 199 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpLLLQEALRSVKAEI 268
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVRV 390
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
15-250 |
7.21e-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: 52.65 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 15 EVELQELRAQPV-VPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNL-------------------------EVQQ 68
Cdd:COG3096 835 EAELAALRQRRSeLERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLladetladrleelreeldaaqeaqaFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 69 KTDRLAEVElRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVES-SKTKQALSESQTRNQHLQEQv 147
Cdd:COG3096 915 HGKALAQLE-PLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLGENSDLNEKLRAR- 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 148 amqrqvLKEMEQQLQNSHQLTVQLRAQIAMYEAELE------RAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEMKAVHE 220
Cdd:COG3096 993 ------LEQAEEARREAREQLRQAQAQYSQYNQVLAslkssrDAKQQTLQElEQELEELGVQADAEAEERARIRRDELHE 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 224967075 221 NL---AGVRTNLLT-----------LQPALRTLTNDYNGLKRQV 250
Cdd:COG3096 1067 ELsqnRSRRSQLEKqltrceaemdsLQKRLRKAERDYKQEREQV 1110
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
12-274 |
1.66e-06 |
|
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: 51.71 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 12 RRCEVELQELRAQpvvpceGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEE 91
Cdd:pfam01576 408 KKLEGQLQELQAR------LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 92 ER----LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQ 166
Cdd:pfam01576 481 TRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEA 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 167 LTVQLRAQIAMYEaELERAHGQMLEEMQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR----------- 226
Cdd:pfam01576 557 LTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaeareke 635
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 224967075 227 TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKAEIGQAIEE 274
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEM-EDLVSSKDDVGKNVHE 682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-293 |
9.49e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 85 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 164
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 165 HQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 230
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967075 231 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 293
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
5-112 |
1.13e-05 |
|
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: 47.70 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRAQPVvPCEGCEhSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 84
Cdd:smart00787 175 PKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELN 252
|
90 100
....*....|....*....|....*....
gi 224967075 85 AEKAQEEE-RLSRRLRDSHEtIASLRAQS 112
Cdd:smart00787 253 TEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-284 |
1.71e-05 |
|
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: 48.13 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 51 EVAENKGMLSELNLEvqQKTDRLAEVELRLK--DCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYviKTVEVESSK 128
Cdd:TIGR02168 175 KETERKLERTRENLD--RLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLRLEELREEL--EELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 129 TKQALSESQTRNQHLQEQVAMQRQVLKEMEQQ-------LQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKN 201
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 202 RAIEEAFARAQVEmkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQE 281
Cdd:TIGR02168 331 KLDELAEELAELE-----EKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNE 401
|
...
gi 224967075 282 LLR 284
Cdd:TIGR02168 402 IER 404
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-302 |
3.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 9 QELRRCEVELQELRAQPvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 86
Cdd:COG4717 71 KELKELEEELKEAEEKE----------EEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 87 KAQEEERLsRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALsesqtrNQHLQEQVAMQRQVLKEMEQQLQNSHQ 166
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE-------LEELEAELAELQEEL------EELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 167 LTVQLRAQIAMYEAELERAHGQMLE-EMQSLEEDKNRAIEEAFARAQVemkavhenlAGVRTNLLTLQPALRTLTNDYNG 245
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLI---------AAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224967075 246 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 302
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2-250 |
3.26e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 2 VENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQlevaenkGMLSELN-LEVQQKTDRLAEVELRL 80
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ------QQRSQLEQAKEGLSALN-------RLLPRLNlLADETLADRVEEIREQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 81 KDclAEKAQ-----------EEERLSRRLRDSHETIASLRAQSPPVKYVIKTV--------EVESSKTKQALSESQ---T 138
Cdd:PRK04863 904 DE--AEEAKrfvqqhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAkqqafaltEVVQRRAHFSYEDAAemlA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 139 RNQHLQEQVamqRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE------RAHGQMLEE-MQSLEEDKNRAIEEAFARA 211
Cdd:PRK04863 982 KNSDLNEKL---RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLAslkssyDAKRQMLQElKQELQDLGVPADSGAEERA 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 224967075 212 QVEMKAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 250
Cdd:PRK04863 1059 RARRDELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
50-291 |
5.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 50 LEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsrrlrdshETIASLRAQSPPvkyviktvEVESSKT 129
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAY--------QLVRKIAGEVSR--------SEAWDVA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 130 KQALSESQTRnQHLQEQVAMQRQVLKEMEQQLQNsHQLTVQLRAQ-----IAMY--EAELERAHGQMLEEMQSLEEDKNR 202
Cdd:PRK04863 499 RELLRRLREQ-RHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEfckrlGKNLddEDELEQLQEELEARLESLSESVSE 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 203 AIEEAFA--RAQVEMKAVHENLAGVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNS 277
Cdd:PRK04863 577 ARERRMAlrQQLEQLQARIQRLAARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAA 652
|
250
....*....|....
gi 224967075 278 NNQELLRKYRRELQ 291
Cdd:PRK04863 653 RKQALDEEIERLSQ 666
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3-243 |
6.51e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEV----ELQELRAQPVVPCEGCEHSQESSQlRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVEl 78
Cdd:pfam17380 361 ELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 79 RLKDclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYviKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEME 158
Cdd:pfam17380 439 RLEE---ERAREMERVRLEEQERQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 159 QQLQNSHQLTVQlraQIAMYE------AELERAHGQMLEEMQSLEEDKNRAIEE-----AFARAQVEMKAVHENLAG--- 224
Cdd:pfam17380 514 KRKLLEKEMEER---QKAIYEeerrreAEEERRKQQEMEERRRIQEQMRKATEErsrleAMEREREMMRQIVESEKArae 590
|
250 260
....*....|....*....|.
gi 224967075 225 --VRTNLLTLQPALRTLTNDY 243
Cdd:pfam17380 591 yeATTPITTIKPIYRPRISEY 611
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-316 |
1.11e-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: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 59 LSELNLEVQQKTDRLAEVELRLkdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEvESSKTKQALSESQT 138
Cdd:COG4913 612 LAALEAELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 139 RNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE---- 214
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDaver 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 215 --MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAIEEVNS-NNQELLRKYRRELQ 291
Cdd:COG4913 766 elRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYLALLDRlEEDGLPEYEERFKE 838
|
250 260 270
....*....|....*....|....*....|.
gi 224967075 292 LRKKCHNELV-----RLKGNIRVI-ARVRPV 316
Cdd:COG4913 839 LLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
33-239 |
1.20e-04 |
|
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: 44.75 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 33 EHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 112
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 113 PPVKYVIKTVEVESSKTKQAL-------SESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQiamyEAELERA 185
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----RAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 224967075 186 HGQMLEEMQSLEEDKNRAiEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTL 239
Cdd:COG4942 180 LAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
36-212 |
1.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 36 QESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 108
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 109 RAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEA---ELE 183
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 224967075 184 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 212
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-312 |
1.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 7 LRQELRRCEVELQELRaqpvvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC--- 83
Cdd:PRK03918 212 ISSELPELREELEKLE----------KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeek 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 84 ------LAEKAQEEERLSR-------RLRDSHETIASLRAQSPPVKYVIKtvevESSKTKQALSESQTRNQHLQEQVAmq 150
Cdd:PRK03918 282 vkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLE-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 151 rqVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAE--------LERAH----------GQMLEEMQSLEEDKNRAIEEaFA 209
Cdd:PRK03918 356 --ELEERHELYEEAKAKKEElerLKKRLTGLTPEklekeleeLEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 210 RAQVE----------------MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIE 273
Cdd:PRK03918 433 KAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEE 510
|
330 340 350
....*....|....*....|....*....|....*....
gi 224967075 274 EVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 312
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
15-293 |
2.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 15 EVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAEnkgmLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERL 94
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEE----LEQLREELEQAREELEQLEEELE----QARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 95 SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQ 174
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 175 IAMYEAELERAHGQMLEEMQsleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFP 254
Cdd:COG4372 159 LESLQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 224967075 255 LLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 293
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
5-308 |
2.62e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVElrlkdcl 84
Cdd:COG4372 41 DKLQEELEQLREELEQAR-------------EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 85 aekaQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNs 164
Cdd:COG4372 101 ----EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 165 hQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYN 244
Cdd:COG4372 176 -LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967075 245 GLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIR 308
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-276 |
3.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRAQpvvpCEGCEhsQESSQLRDKLSQLQ--LEVAENKGMLSELNLEVQQKTDRLAEVEL---- 78
Cdd:COG4913 613 AALEAELAELEEELAEAEER----LEALE--AELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 79 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQTRNQHLQEQV--AM 149
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 150 QRQVLKEMEQQLQNSHQltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 229
Cdd:COG4913 760 GDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 224967075 230 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 276
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
35-299 |
4.41e-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: 43.88 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 35 SQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 112
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 113 PPVKYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERa 185
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 186 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 262
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 224967075 263 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 299
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
35-307 |
4.85e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 35 SQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQ--------KTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIA 106
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 107 SLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLK-------EMEQQLQNSHQLTVQLRAQIAMYE 179
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqinDLESKIQNQEKLNQQKDEQIKKLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 180 AELErahgQMLEEMQSLEEDKNRAIEE--AFARAQVEMKAVHENLAGVRTnllTLQPALRTLTNDYNGLKR----QVRGF 253
Cdd:TIGR04523 419 QEKE----LLEKEIERLKETIIKNNSEikDLTNQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQnleqKQKEL 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 224967075 254 PLLLQE--ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 307
Cdd:TIGR04523 492 KSKEKElkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
40-206 |
6.53e-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: 41.83 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 40 QLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIASLRAqsppvkYVI 119
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNKE------YEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 120 KTVEVESSKTKQALSESQTRNqhLQEQVAMQRQVLKEMEQQLQnshqltvQLRAQIAMYEAELERAHGQMLEEMQSLEED 199
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 224967075 200 KNRAIEE 206
Cdd:COG1579 165 REELAAK 171
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
38-167 |
8.41e-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: 41.52 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 38 SSQLRDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 111
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 224967075 112 SPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQL 167
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKE 165
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-295 |
1.17e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 4 NEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQlRDKLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDC 83
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 84 LAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQN 163
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 164 SHQLTVQLRAQIamyeAELErahgqmlEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLT 240
Cdd:TIGR04523 431 LKETIIKNNSEI----KDLT-------NQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 224967075 241 NDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 295
Cdd:TIGR04523 496 KELKKLNEEKK----ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
93-216 |
1.41e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 93 RLSRRLRDshETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 162
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224967075 163 -------NSHQLtVQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 216
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
8-212 |
2.40e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 8 RQELRRCEVELQElraqpvvpcegcehsQESSQLRdKLSQLQLEVAENkgMLSELNLEVQQKTDRLAEVELRLKDclAEK 87
Cdd:pfam15709 342 RAEMRRLEVERKR---------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 88 AQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQVLKEMEQQlqns 164
Cdd:pfam15709 402 RQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKRLMEMAEE---- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224967075 165 HQLTVQLRAQiamyEAElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 212
Cdd:pfam15709 475 ERLEYQRQKQ----EAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5-293 |
2.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVELQELRaqpvvpcegcehsqESSQLRDKLSQLqlEVAENKgmLSELNLEVQQKTDRLAEvelRLKDCL 84
Cdd:PRK03918 476 RKLRKELRELEKVLKKES--------------ELIKLKELAEQL--KELEEK--LKKYNLEELEKKAEEYE---KLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 85 AEKAQEEERLSRRLRDSHETIASLRAqsppVKYVIKTVEVESSKTKQALSES-----QTRNQHLQEQVAMQRQV--LKEM 157
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYleLKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 158 EQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALR 237
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 224967075 238 TLTNDYNGLKRQVrgfplllqEALRSVKAE---IGQAIEEVnSNNQELLRKYRRELQLR 293
Cdd:PRK03918 691 EIKKTLEKLKEEL--------EEREKAKKElekLEKALERV-EELREKVKKYKALLKER 740
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
3-215 |
3.34e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQL----RQELRRCEVELQELRAQPVvpcegcehSQESSQLRDKL-SQLQLEvaenkgmlSELNLEvqqKTDRLAEVE 77
Cdd:PRK10929 193 ELAQLsannRQELARLRSELAKKRSQQL--------DAYLQALRNQLnSQRQRE--------AERALE---STELLAEQS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 78 LRLKDCLAEKAQEEERLSRRLRD---SHETIASLR----AQSPPVKYVIKTVEVESsktkQALSESQTRNQHLQEQVAMq 150
Cdd:PRK10929 254 GDLPKSIVAQFKINRELSQALNQqaqRMDLIASQQrqaaSQTLQVRQALNTLREQS----QWLGVSNALGEALRAQVAR- 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 151 rqvLKEME--QQLQNShqlTVQLRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRaIEEAFARAQVEM 215
Cdd:PRK10929 329 ---LPEMPkpQQLDTE---MAQLRVQRLRYEDLLNKQPQLRqirQADGQPLTAEQNR-ILDAQLRTQREL 391
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
46-314 |
3.96e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 46 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDShetiasLRAQ 111
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKN------LTVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 112 SPPVKYVIkTVEVESSKTKQA-------------------LSESQTRNQHLQEQVAMQRQVLKEMEQQLQN---SHQLtV 169
Cdd:COG3206 131 PVKGSNVI-EISYTSPDPELAaavanalaeayleqnlelrREEARKALEFLEEQLPELRKELEEAEAALEEfrqKNGL-V 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 170 QLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHEN--LAGVRTNLLTLQPALRTLTNDYNG 245
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARlaALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224967075 246 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLrkyRRELQLRKkchnELVRLKGNIRVIARVR 314
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ---AREASLQA----QLAQLEARLAELPELE 350
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
5-228 |
4.00e-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: 40.49 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 5 EQLRQELRRCEVE----LQELRAQPVVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 79
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 80 LKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 159
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224967075 160 ---QLQNSHQLTVQLRAQIAMYEAELErahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTN 228
Cdd:pfam05557 154 lrqNLEKQQSSLAEAEQRIKELEFEIQ------SQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-223 |
4.64e-03 |
|
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: 40.44 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQELRAQpvvpCEGCEHSQESSQLRdkLSQLQLEVAENKgmlSELNLEVQqktdRLAEVELRLKD 82
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAE----IEELEREIEEERKR--RDKLTEEYAELK---EELEDLRA----ELEEVDKEFAE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 CLAEKAQEEERLS---RRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 159
Cdd:TIGR02169 383 TRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967075 160 QLQNSHQLTVQLRAQIAMYEAELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 223
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3-197 |
4.91e-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: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQlevaENKGMLSELNLEVQQKTDRLAEvelrlkd 82
Cdd:TIGR00618 339 SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKELDILQR------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 claEKAQEEERLSRRlRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQTRNQHLQEQvamqRQVLKEMEQQLQ 162
Cdd:TIGR00618 408 ---EQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQES----AQSLKEREQQLQ 476
|
170 180 190
....*....|....*....|....*....|....*
gi 224967075 163 NSHQLTVQlraqiamyEAELERAHGQMLEEMQSLE 197
Cdd:TIGR00618 477 TKEQIHLQ--------ETRKKAVVLARLLELQEEP 503
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
59-183 |
5.35e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 59 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQT 138
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 224967075 139 RNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE 183
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
38-207 |
5.96e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.67 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 38 SSQLRDKLSQLQLEvaeNKgMLSELnlEVQQKTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKY 117
Cdd:pfam05622 277 PAEIREKLIRLQHE---NK-MLRLG--QEGSYRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 118 VIKTVEVESSKT------KQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVqlraqiamyeAELERAHGQMLE 191
Cdd:pfam05622 344 LQKALQEQGSKAedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDE 413
|
170
....*....|....*.
gi 224967075 192 EMQSLEEDKNRAIEEA 207
Cdd:pfam05622 414 DMKAMEERYKKYVEKA 429
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
6-183 |
6.53e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 6 QLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 85
Cdd:COG1579 21 RLEHRLKELPAELAELE-------------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 86 EK-----AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVamqRQVLKEMEQQ 160
Cdd:COG1579 88 NKeyealQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAE 157
|
170 180
....*....|....*....|...
gi 224967075 161 LQnshqltvQLRAQIAMYEAELE 183
Cdd:COG1579 158 LE-------ELEAEREELAAKIP 173
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
97-304 |
6.69e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 97 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 163
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 164 SH-----QLTVQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 231
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224967075 232 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 304
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-349 |
7.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 3 ENEQLRQELRRCEVELQelRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELnlevqQKTDRLAEVELRLKd 82
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL-----KKAEELKKAEEKKK- 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 83 cLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVEVESS-KTKQALSESQTRNQhlQEQVAMQRQVLKEMEQ-- 159
Cdd:PTZ00121 1566 -AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQlk 1639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 160 -----------QLQNSHQLTVQLRAQIAMYEAELERAhgqmLEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagvrtn 228
Cdd:PTZ00121 1640 kkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE-------- 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 229 lltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIR 308
Cdd:PTZ00121 1707 -------LKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 224967075 309 VIARV---RPVTKEDGEGPEATNAVTFDPDDDS--IIHLLHKGKPV 349
Cdd:PTZ00121 1775 KEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFanIIEGGKEGNLV 1820
|
|
| BAR_Bin3 |
cd07590 |
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ... |
139-223 |
8.81e-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: 38.50 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967075 139 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAqIAMYEAELERAHGQMLEEMQSLEEDKNRAIE---EAFARAQV 213
Cdd:cd07590 117 REQSLQEYERLQAKVekLAEKEKTGPNLAKLEQAEKA-LAAARADFEKQNIKLLEELPKFYNGRTDYFQpcfEALIKSQV 195
|
90
....*....|....
gi 224967075 214 ----EMKAVHENLA 223
Cdd:cd07590 196 lyysQSTKIFTQLA 209
|
|
| |
