|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-372 |
0e+00 |
|
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: 603.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 7 CCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 87 GQTGAGKTYTMGTGFDTVTSEEEQGIIPRAIAHLFRGIDERKrraqekgvTGPEFKVSAQFLELYNEEILDLFDStrdpd 166
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDP----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 167 ARHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVCAQPDLVN 246
Cdd:cd01372 148 ETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 247 ETVtglpdgaaptgtEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDS 326
Cdd:cd01372 228 ADD------------KNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDS 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 86990454 327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372 296 KLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
14-371 |
3.24e-138 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 429.69 E-value: 3.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 14 RIRPQLSKEKIEGCHICTSVTPGEPQVLL-------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 87 GQTGAGKTYTMGTgfdtvtSEEEQGIIPRAIAHLFRGIDERKRRaqekgvtgPEFKVSAQFLELYNEEILDLFDSTRDPd 166
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPSNKN- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 167 arhrRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVCaqpdlvn 246
Cdd:pfam00225 146 ----KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRS------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 247 etvtglpdgaapTGTEYETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRD 325
Cdd:pfam00225 215 ------------TGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK--HIPYRD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 86990454 326 SKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225 281 SKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
9-378 |
8.23e-138 |
|
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: 428.91 E-value: 8.23e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVL-------LGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNA 81
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 82 TVLAYGQTGAGKTYTMGTgfdtvtSEEEQGIIPRAIAHLFRGIDERKrraqekgvTGPEFKVSAQFLELYNEEILDLFDS 161
Cdd:smart00129 82 TIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 162 trdpdarhRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVCAQ 241
Cdd:smart00129 148 --------SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 242 PDlvnetvtglpdgaaptgteyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVvHV 321
Cdd:smart00129 220 SG--------------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR-HI 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 86990454 322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 378
Cdd:smart00129 279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
9-369 |
2.10e-124 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 392.00 E-value: 2.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKiEGCHICTSVTPG------EPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:cd00106 2 VRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 83 VLAYGQTGAGKTYTMGTGFDtvtseEEQGIIPRAIAHLFRGIDERKRraqekgvTGPEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd00106 81 IFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRKE-------TKSSFSVSASYLEIYNEKIYDLLSPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 163 RdpdarhrRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRvcaqP 242
Cdd:cd00106 149 P-------KKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN----R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 243 DLVNETVTGlpdgaaptgteyetltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKvvHVP 322
Cdd:cd00106 218 EKSGESVTS----------------SKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 86990454 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd00106 280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
8-373 |
1.71e-103 |
|
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: 334.18 E-value: 1.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 8 CVKVAVRIRPQLSKEKIE-GCHICTSVTPGEPQVLLGKD---KAFTYDFVFDLDTWQEQIYSTcVSKLIEGCFEGYNATV 83
Cdd:cd01366 3 NIRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 84 LAYGQTGAGKTYTM-GTgfdtvtsEEEQGIIPRAIAHLFRGIDERKrraqEKGVTgpeFKVSAQFLELYNEEILDLFDST 162
Cdd:cd01366 82 FAYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELK----EKGWS---YTIKASMLEIYNETIRDLLAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 163 RDPDARHrrsNIKiHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrvcaqp 242
Cdd:cd01366 148 NAPQKKL---EIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 243 DLVNETvtglpdgaapTGteyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdqSKKVVHVP 322
Cdd:cd01366 215 SGRNLQ----------TG---EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIP 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 86990454 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 373
Cdd:cd01366 279 YRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
8-371 |
3.89e-103 |
|
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: 333.27 E-value: 3.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 8 CVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKA--------FTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGY 79
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 80 NATVLAYGQTGAGKTYTMGtGFDTvtSEEEQGIIPRAIAHLFRGIDerkrRAQEKgvtgPEFKVSAQFLELYNEEILDLF 159
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTME-GKRE--DPELRGIIPNSFAHIFGHIA----RSQNN----QQFLVRVSYLEIYNEEIRDLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 160 dsTRDPDARhrrsnIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHL-CQMRV 238
Cdd:cd01371 151 --GKDQTKR-----LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeCSEKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 239 caqpdlvnetvtglpdgaapTGTEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqsKKV 318
Cdd:cd01371 224 --------------------EDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD--GKS 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 86990454 319 VHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01371 282 THIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
9-371 |
1.39e-102 |
|
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: 332.39 E-value: 1.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGCHICTSVT--------PGEPQVLL--------------GKDKAFTYDFVFDLDTWQEQIYST 66
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 67 CVSKLIEGCFEGYNATVLAYGQTGAGKTYTMgtgfdtVTSEEEQGIIPRAIAHLFRGIDERKrraQEKgvtgpEFKVSAQ 146
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESLK---DEK-----EFEVSMS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 147 FLELYNEEILDLFDSTRDPdarhrrsnIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSH 226
Cdd:cd01370 148 YLEIYNETIRDLLNPSSGP--------LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 227 AIFTIHLCQmrvcaQPDLVNETvtglpdgaaptgteYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGN 306
Cdd:cd01370 220 AVLQITVRQ-----QDKTASIN--------------QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGN 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86990454 307 VISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01370 281 CINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
9-378 |
7.63e-99 |
|
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: 322.38 E-value: 7.63e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGC--------HICTSVTPGEPQVLLGKDKAFTYDFVFDLDTW-----------QEQIYSTCVS 69
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSkcivqmsgKETTLKNPKQADKNNKATREVPKSFSFDYSYWshdsedpnyasQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 70 KLIEGCFEGYNATVLAYGQTGAGKTYTMgTGFDtvtseEEQGIIPRAIAHLFrgidERKRRAQEKGVTgpeFKVSAQFLE 149
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLF----SRIADTTNQNMS---YSVEVSYME 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 150 LYNEEILDLFDstrdPDARHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIF 229
Cdd:cd01365 150 IYNEKVRDLLN----PKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 230 TIHLCQMRVcaqpdlvnETVTGLPdgaaptgteyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVIS 309
Cdd:cd01365 226 TIVLTQKRH--------DAETNLT----------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVIS 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86990454 310 ALGDQSKKV-----VHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 378
Cdd:cd01365 288 ALADMSSGKskkksSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
9-380 |
4.15e-96 |
|
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: 314.06 E-value: 4.15e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGK-DKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYG 87
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 88 QTGAGKTYTM--GTGFDTVTSEEEQGIIPRAIAHLFRGIDerkrRAQEKGVTGPEFKVSAQFLELYNEEILDLFDSTRdp 165
Cdd:cd01373 83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQ----REKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPAS-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 166 darhrrSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMrvCAQPDLV 245
Cdd:cd01373 157 ------RNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESW--EKKACFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 246 NetvtglpdgaaptgteyeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSK-KVVHVPYR 324
Cdd:cd01373 229 N------------------IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYR 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 86990454 325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQD 380
Cdd:cd01373 291 DSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
9-380 |
4.19e-94 |
|
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: 308.49 E-value: 4.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLL--------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYN 80
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 81 ATVLAYGQTGAGKTYTMgTGFDTVTSE------EEQGIIPRAIAHLFRGIDErkrraqekgvTGPEFKVSAQFLELYNEE 154
Cdd:cd01364 84 CTIFAYGQTGTGKTYTM-EGDRSPNEEytweldPLAGIIPRTLHQLFEKLED----------NGTEYSVKVSYLEIYNEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 155 ILDLFDSTRDPdarhrRSNIKIHEDAN--GGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIH 232
Cdd:cd01364 153 LFDLLSPSSDV-----SERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSIT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 233 LcQMRVcaqpdlvnetvtglpdgaapTGTEYETL--TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 310
Cdd:cd01364 228 I-HIKE--------------------TTIDGEELvkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 311 LGDQSKkvvHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQD 380
Cdd:cd01364 287 LVERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
6-371 |
5.60e-94 |
|
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: 307.33 E-value: 5.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 6 DCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKD--KAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATV 83
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 84 LAYGQTGAGKTYTM-GTGFDtvtsEEEQGIIPRAIAHLFRGIderkrRAQEKGVtgpEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd01369 81 FAYGQTSSGKTYTMeGKLGD----PESMGIIPRIVQDIFETI-----YSMDENL---EFHVKVSYFEIYMEKIRDLLDVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 163 RDpdarhrrsNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVcaqp 242
Cdd:cd01369 149 KT--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENV---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 243 dlvnetvtglpdgaaptgTEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqsKKVVHVP 322
Cdd:cd01369 217 ------------------ETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIP 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 86990454 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01369 277 YRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
9-371 |
8.38e-91 |
|
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: 298.09 E-value: 8.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQ 88
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 89 TGAGKTYTMgTGfdtvtSEEEQGIIPRAIAHLFRGIDERKRRaqekgvtgpEFKVSAQFLELYNEEILDLFDSTRdpdar 168
Cdd:cd01374 82 TSSGKTFTM-SG-----DEDEPGIIPLAIRDIFSKIQDTPDR---------EFLLRVSYLEIYNEKINDLLSPTS----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 169 hrrSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIhlcQMRVCAQPDLVNET 248
Cdd:cd01374 142 ---QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRI---TIESSERGELEEGT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 249 VTglpdgaaptgteYETLTakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqSKKVVHVPYRDSKL 328
Cdd:cd01374 216 VR------------VSTLN----LIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKL 278
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 86990454 329 TRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01374 279 TRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
43-508 |
3.12e-90 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 305.51 E-value: 3.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 43 GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMgtgfdtVTSEEEQGIIPRAIAHLFR 122
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 123 GIDERKRRAqekgvtgpEFKVSAQFLELYNEEILDLFDSTRDPdarhrrsnIKIHEDANGGIYTTGVTSRLINSQEELIQ 202
Cdd:COG5059 127 KLEDLSMTK--------DFAVSISYLEIYNEKIYDLLSPNEES--------LNIREDSLLGVKVAGLTEKHVSSKEEILD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 203 CLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQmrvcaqpdlvNETVTGlpdgaaptgteyETLTAKFHFVDLAGSERLK 282
Cdd:COG5059 191 LLRKGEKNRTTASTEINDESSRSHSIFQIELAS----------KNKVSG------------TSETSKLSLVDLAGSERAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 283 RTGATGERAKEGISINCGLLALGNVISALGDQsKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 363 KYANRARNIKNKVVVNQDK-TSQQISALRAEIARLQMELMEYKAGKRVIGEDgtegySDLFRENAMLQKengaLRLRVKA 441
Cdd:COG5059 328 KFASRAKSIKNKIQVNSSSdSSREIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQS----LKKETET 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86990454 442 MQEAIDAINNRVTQLMSQEANLLLAKaGDGNEAIGALIQNYI----REIEELRTKLLESEAMNESLRRSLS 508
Cdd:COG5059 399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIdrllLLREEELSKKKTKIHKLNKLRHDLS 468
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
9-369 |
7.02e-71 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 240.87 E-value: 7.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEGCHICTSVTpGEPQVLL------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 83 VLAYGQTGAGKTYTMgtgfdtVTSEEEQGIIPRAIAHLFRGIDErkrraqekgvTGPEFKVSAQFLELYNEEILDLFDSt 162
Cdd:cd01376 81 VFAYGSTGAGKTFTM------LGSPEQPGLMPLTVMDLLQMTRK----------EAWALSFTMSYLEIYQEKILDLLEP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 163 rdpdarhRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIhlcqmRVCAQP 242
Cdd:cd01376 144 -------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLI-----KVDQRE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 243 DLVNetvtglpdgaaptgteYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdqSKKVVHVP 322
Cdd:cd01376 212 RLAP----------------FRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIP 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 86990454 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd01376 273 YRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
45-369 |
4.33e-70 |
|
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: 239.02 E-value: 4.33e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 45 DKAFTYDFVFDlDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGfdtVTSEEEQGIIPRAIAHLFRGI 124
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGG---TENYKHRGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 125 DERKRRAqekgvtgpeFKVSAQFLELYNEEILDLFDSTrdPDARHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCL 204
Cdd:cd01375 123 EERPTKA---------YTVHVSYLEIYNEQLYDLLSTL--PYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 205 KQGALSRTTASTQMNVQSSRSHAIFTIHLcQMRvcaQPDLVNETVtglpdgaaptgteyetLTAKFHFVDLAGSERLKRT 284
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIHL-EAH---SRTLSSEKY----------------ITSKLNLVDLAGSERLSKT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 285 GATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKY 364
Cdd:cd01375 252 GVEGQVLKEATYINKSLSFLEQAIIALSDKDRT--HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRF 329
|
....*
gi 86990454 365 ANRAR 369
Cdd:cd01375 330 ASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
9-367 |
6.48e-68 |
|
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: 232.57 E-value: 6.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKIEG-CHICTSVTPGEPQVLLGKDK----------AFTYDFVFDLDTWQEQIYSTCVSKLIEGCFE 77
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 78 GYNATVLAYGQTGAGKTYTMGTGFDtvTSEEEQGIIPRAIAHLFRGIDERKRRAQekgvtgpeFKVSAQFLELYNEEILD 157
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDFS--GQEESKGIYALAARDVFRLLNKLPYKDN--------LGVTVSFFEIYGGKVFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 158 LFdstrdpdarHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmr 237
Cdd:cd01367 152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 238 vcaqpdlvnetvtglpdgaAPTGTeyETLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDQSk 316
Cdd:cd01367 219 -------------------RDRGT--NKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK- 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 86990454 317 kvVHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 367
Cdd:cd01367 277 --AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
9-365 |
1.05e-67 |
|
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: 232.67 E-value: 1.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 9 VKVAVRIRPQLSKEKI---EGC-HI--CTSVTPGEPQVLLG---------KDKAFTYDFVFDLDTWQEQIYSTCVSKLIE 73
Cdd:cd01368 3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 74 GCFEGYNATVLAYGQTGAGKTYTMgTGfdtvtSEEEQGIIPRAIAHLFRGIderkrraqekgvtgPEFKVSAQFLELYNE 153
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTM-QG-----SPGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 154 EILDLFDSTRDPDARHRRSnIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHL 233
Cdd:cd01368 143 YIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 234 CQmrvcAQPDLVNETVTglpDGAAPTgteyetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368 222 VQ----APGDSDGDVDQ---DKDQIT-------VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 86990454 314 Q--SKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368 288 NqlQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-405 |
8.41e-66 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 246.00 E-value: 8.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 3 GQGDCCVKVAVRIRPQLSKEKIEgchicTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGEEGE-----MIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 83 VLAYGQTGAGKTYTMGTGFDTVTSE----EEQGIIPRAIAHLFRGIDERKRRAQEKGVtgpEFKVSAQFLELYNEEILDL 158
Cdd:PLN03188 169 VFAYGQTGSGKTYTMWGPANGLLEEhlsgDQQGLTPRVFERLFARINEEQIKHADRQL---KYQCRCSFLEIYNEQITDL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 159 FDSTrdpdarhrRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTihlCqmrv 238
Cdd:PLN03188 246 LDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---C---- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 239 caqpdLVNETVTGLPDGAAPTGteyetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD--QSK 316
Cdd:PLN03188 311 -----VVESRCKSVADGLSSFK------TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisQTG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 317 KVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDkTSQQISALRAEIARL 396
Cdd:PLN03188 380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458
|
....*....
gi 86990454 397 QMELMEYKA 405
Cdd:PLN03188 459 RDELQRVKA 467
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1302-1615 |
7.97e-63 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 216.43 E-value: 7.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1302 CISMAEGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSS-SYIKVWDI 1378
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1379 RDSaKCIRTLTSSgqvisgdaciatstraitsaqgEHQINQMALSPSGSMLYVASG-NAVRIWELNRFQPIGKLTGHIGP 1457
Cdd:cd00200 81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1458 VMCLTVTQTSnqhDLVVTGSKDHYVKMFQLgdcvtGTIGPTHNFEpPHYDGIECLAIQGD--ILFSGSRDNGIKKWDLDQ 1535
Cdd:cd00200 138 VNSVAFSPDG---TFVASSSQDGTIKLWDL-----RTGKCVATLT-GHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1536 QELIQQIPnAHKDWVCALAFVPGRPMLLSACRAGFIKVWNVDNFTPIGEIKGHDSPINAIC--TNSKHIFTASSDLTVKF 1613
Cdd:cd00200 209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRI 287
|
..
gi 86990454 1614 WS 1615
Cdd:cd00200 288 WD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1296-1617 |
8.34e-48 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 177.03 E-value: 8.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1296 RTAPLQCISMAEGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYcSHSG-LVFSVSSSY 1372
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF-SPDGkLLASGSDDG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1373 -IKVWDIrDSAKCIRTLTSSgqvisgdaciatstraitsaqgEHQINQMALSPSGSMLYVASG-NAVRIWELNRFQPIGK 1450
Cdd:COG2319 185 tVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLLRT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1451 LTGHIGPVMCLTVtqtSNQHDLVVTGSKDHYVKMFQLGdcvTGTIGPTHnfePPHYDGIECLAI--QGDILFSGSRDNGI 1528
Cdd:COG2319 242 LTGHSGSVRSVAF---SPDGRLLASGSADGTVRLWDLA---TGELLRTL---TGHSGGVNSVAFspDGKLLASGSDDGTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1529 KKWDLDQQELIQQIPnAHKDWVCALAFVPGRPMLLSACRAGFIKVWNVDNFTPIGEIKGHDSPINAIC--TNSKHIFTAS 1606
Cdd:COG2319 313 RLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAfsPDGRTLASGS 391
|
330
....*....|.
gi 86990454 1607 SDLTVKFWSIR 1617
Cdd:COG2319 392 ADGTVRLWDLA 402
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
930-1011 |
1.21e-42 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.
Pssm-ID: 410203 [Multi-domain] Cd Length: 82 Bit Score: 150.34 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 930 QRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEE 1009
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 86990454 1010 TK 1011
Cdd:cd22262 81 TK 82
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1414-1617 |
3.31e-37 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 142.47 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1414 EHQINQMALSPSGSMLYVASGNA-VRIWELNRFQPIGKLTGHIGPVMCLtvtQTSNQHDLVVTGSKDHYVKMFQLGDCVt 1492
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPVRDV---AASADGTYLASGSSDKTIRLWDLETGE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1493 gtigPTHNFEPpHYDGIECLAIQ--GDILFSGSRDNGIKKWDLDQQELIQQIpNAHKDWVCALAFVPGRPMLLSACRAGF 1570
Cdd:cd00200 85 ----CVRTLTG-HTSYVSSVAFSpdGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 86990454 1571 IKVWNVDNFTPIGEIKGHDSPINAIC--TNSKHIFTASSDLTVKFWSIR 1617
Cdd:cd00200 159 IKLWDLRTGKCVATLTGHTGEVNSVAfsPDGEKLLSSSSDGTIKLWDLS 207
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1301-1575 |
1.36e-36 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 140.55 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1301 QCISMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSS-SYIKVWD 1377
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAfsPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1378 IRdSAKCIRTLTSSgqvisgdaciatstraitsaqgEHQINQMALSPSGSMLYVASG-NAVRIWELNRFQPIGKLTGHIG 1456
Cdd:cd00200 164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1457 PVMCLTVTQTsnqhdlvvtgskdhyvkmfqlgdcvtgtigpthnfepphydgieclaiqGDILFSGSRDNGIKKWDLDQQ 1536
Cdd:cd00200 221 GVNSVAFSPD-------------------------------------------------GYLLASGSEDGTIRVWDLRTG 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 86990454 1537 ELIQQIPnAHKDWVCALAFVPGRPMLLSACRAGFIKVWN 1575
Cdd:cd00200 252 ECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
930-1011 |
2.84e-28 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 109.25 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 930 QRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEE 1009
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 86990454 1010 TK 1011
Cdd:cd22263 81 AK 82
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
930-1011 |
1.03e-26 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 104.98 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 930 QRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKgLQELAEEIEVLAANIDYINDSITDCQATIVQLEE 1009
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKDESV-LRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 86990454 1010 TK 1011
Cdd:cd22248 80 SK 81
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
7-158 |
2.80e-17 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 80.34 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 7 CCVKVAVRIRPQLSKEkiegCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCvSKLIEGCFEGYNATVLAY 86
Cdd:pfam16796 20 GNIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAY 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86990454 87 GQTGAGKTYTMgtgfdtvtseeeqgiIPRAIAHLFRGIDERKRraqekgvtGPEFKVSAQFLELYNEEILDL 158
Cdd:pfam16796 95 GQTGSGSNDGM---------------IPRAREQIFRFISSLKK--------GWKYTIELQFVEIYNESSQDL 143
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
11-310 |
1.20e-14 |
|
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: 73.53 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 11 VAVRIRPQLSKEKIEGCHICTSvtpgepqvllgkdkaftyDFVFDLDTWQEQIYSTCvSKLIEGCFEGYN-ATVLAYGQT 89
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVF------------------YRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 90 GAGKTYTMgtgfdtvtseeeQGIIPRAIAHLFRGIDerkrraqeKGVTGPEFKVSAQFLELYNeEILDLFDSTrdpdarh 169
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAFNGIN--------KGETEGWVYLTEITVTLED-QILQANPIL------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 170 rrsnikiheDANGgiyttgvtsrlinsqeeliqclkqgalsrtTASTQMNVQSSRSHAIFTIhlcqmrvcaqpdlvnetv 249
Cdd:cd01363 114 ---------EAFG------------------------------NAKTTRNENSSRFGKFIEI------------------ 136
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86990454 250 tglpdgaaptgteyetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 310
Cdd:cd01363 137 ----------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
634-831 |
1.23e-13 |
|
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: 74.42 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 634 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV---LQNLSTMECYTEEKANKIKAD 710
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 711 YEKRLR---------------------EMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE 769
Cdd:COG4942 106 LAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86990454 770 EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMS 831
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
643-1066 |
2.19e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.19 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 643 EIEIKQKLIDELENSQRRLQTL---KHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTE-EKANKIKADYEKRLREM 718
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 719 NRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlveTKRNREIAQLKKEQRRQEFQ 798
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL---AELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 799 IRALESQKRQQEIVLRRKTQEVSA---------------LRRLAKPMSERVAGRVGLKPPNMDSGAEVSASTTSSEAESG 863
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLliaaallallglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 864 ARSVSSIVRQwnRKIDHFLGDRPTATVNGGRPARKKFQ-----KKGASQSFSKAARLKWQSLERRIIDIVmqRMTIVNLE 938
Cdd:COG4717 309 ALPALEELEE--EELEELLAALGLPPDLSPEELLELLDrieelQELLREAEELEEELQLEELEQEIAALL--AEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 939 ADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQ-----ELAEEIEVLAANIDYINDSITDCQATIVQLEETKEE 1013
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 86990454 1014 LDSTDTsvvisscsLAEARLLLDNfLKASIDkglQVAQKEAQIRLLEGRLRQT 1066
Cdd:COG4717 465 LEEDGE--------LAELLQELEE-LKAELR---ELAEEWAALKLALELLEEA 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-1014 |
4.55e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 473 EAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARnpyslgaspagpafggspatsMEDASEVIRKAKQDLERL 552
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELE---------------------LEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 553 KKKEVRQRRKSPEKEAFKKRAKLQAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKE-- 630
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEee 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 631 -VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteekankika 709
Cdd:COG1196 381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL---------------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 710 dyEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQMREEQQ-----RRRLVETKRNRE 784
Cdd:COG1196 445 --EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 785 IAQLKKEQRRQEFQIRAL---ESQKRQQEIVLRRKTQEVSALRRLAkpmsERVAGRVGLKPPNMDSGAEVSASTTSSEAE 861
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAAleaALAAALQNIVVEDDEVAAAAIEYLK----AAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 862 SGARSVSSIVRQWNRKIDHFLGD---------------------------RPTATVNGGRPARKKFQKKGASQSFSKAAR 914
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDtllgrtlvaarleaalrravtlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 915 LKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYIN 994
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580
....*....|....*....|..
gi 86990454 995 D--SITDCQATIVQLEETKEEL 1014
Cdd:COG1196 758 EppDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-1065 |
5.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 542 IRKAKQDLERLKKKEVRQRRKspEKEAFKKRAKLQAEnseetdeneaeeeeeerDESGCEEEEGREDEDEDSGSEESLVD 621
Cdd:COG1196 234 LRELEAELEELEAELEELEAE--LEELEAELAELEAE-----------------LEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 622 SDSDPEEKEVNF-QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYT 700
Cdd:COG1196 295 AELARLEQDIARlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 701 EEKANKIKADYEKRLREMNR---DLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLV 777
Cdd:COG1196 375 AEAEEELEELAEELLEALRAaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 778 ETKRNREIAQLKKEQRRQEFQIRALESQKRQ-QEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEV----S 852
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEElAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigveA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 853 ASTTSSEAESGARSVSSIVRQWNR--KIDHFLGDR--------PTATVNGGRPARKKFQKKGASQSFSKAARLKWQSLER 922
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVaaAAIEYLKAAkagratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 923 ----------RIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDY 992
Cdd:COG1196 615 yyvlgdtllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 993 INDSITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARL-----------LLDNFLKASIDKGLQVAQKEAQIRLLEG 1061
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREelleelleeeeLLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 86990454 1062 RLRQ 1065
Cdd:COG1196 775 EIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-1095 |
3.47e-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: 65.09 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 367 RARNIKNKVVVNQDKTSQQISALRAEIARLQME---LMEYKAGKRVIGEdgTEGYSDLFRENAMLqKENGALRLRVKAMQ 443
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKRE--YEGYELLKEKEALE-RQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 444 EAIDAINNRVTQLmSQEANLLLAKAGDGNEAIGALIQNyirEIEELRTKLLESEAMNESLRRSLsRASARNpyslgaspa 523
Cdd:TIGR02169 251 EELEKLTEEISEL-EKRLEEIEQLLEELNKKIKDLGEE---EQLRVKEKIGELEAEIASLERSI-AEKERE--------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 524 gpafggspatsMEDASEVIRKAKQDLERLKKkEVRQRRKSPEKEAfKKRAKLQAENSEetdeneaeeeeeerdesgceee 603
Cdd:TIGR02169 317 -----------LEDAEERLAKLEAEIDKLLA-EIEELEREIEEER-KRRDKLTEEYAE---------------------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 604 egredededsgSEESLVDSDSDPEEKEVNFQAdladltceieikqkLIDELEnsqrrlqtlkhQYEEKLILLQNKIRDTQ 683
Cdd:TIGR02169 362 -----------LKEELEDLRAELEEVDKEFAE--------------TRDELK-----------DYREKLEKLKREINELK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 684 LERDRVLQNLSTMECYTEEKANKIKA-------------DYEKRLREMNRDLQKLQA----AQKEHARLLKNQSRYEREL 746
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGieakineleeekeDKALEIKKQEWKLEQLAAdlskYEQELYDLKEEYDRVEKEL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 747 KKLQAEVAEMKKAKvalmKQMREEQQRRRLVET--KRNRE-----IAQLKKEQRRqefQIRALESQ--KRQQEIVLrrKT 817
Cdd:TIGR02169 486 SKLQRELAEAEAQA----RASEERVRGGRAVEEvlKASIQgvhgtVAQLGSVGER---YATAIEVAagNRLNNVVV--ED 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 818 QEVSAlrRLAKPMSERVAGRVGLKPPN--MDSGAEVSASttsseAESGARSVSSIVRQWNRKID----HFLGDrpTATVN 891
Cdd:TIGR02169 557 DAVAK--EAIELLKRRKAGRATFLPLNkmRDERRDLSIL-----SEDGVIGFAVDLVEFDPKYEpafkYVFGD--TLVVE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 892 GGRPARKK-------------FQKKGA----------SQSFSKAARLKWQSLERRIIDivmqrmtivnLEADMERLIKKR 948
Cdd:TIGR02169 628 DIEAARRLmgkyrmvtlegelFEKSGAmtggsraprgGILFSRSEPAELQRLRERLEG----------LKRELSSLQSEL 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 949 EELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQatiVQLEETKEELDSTDTSVVISSCSL 1028
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE---QEIENVKSELKELEARIEELEEDL 774
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86990454 1029 AEARLLLDNfLKASID------KGLQVAQKEAQIRLLEGRLRQTDMTGSSQnHLLLDALREKAEahpELQALI 1095
Cdd:TIGR02169 775 HKLEEALND-LEARLShsripeIQAELSKLEEEVSRIEARLREIEQKLNRL-TLEKEYLEKEIQ---ELQEQR 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
627-1085 |
3.91e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLIDELEnsqRRLQTLKHQYEE----KLILLQNKIRDTQLERDRVLQNLSTME--CYT 700
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALR---EELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEalLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 701 -EEKANKIKADYEKRLREMNRDLQKLQ----AAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRR 775
Cdd:COG4913 371 lGLPLPASAEEFAALRAEAAALLEALEeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 776 LVETKRNREIA--------QLKKEQRRQEFQI-RALESQKRQQeIVLRRKTQEVS-ALRRLakPMSERV-AGRVGLKPPN 844
Cdd:COG4913 449 LAEALGLDEAElpfvgeliEVRPEEERWRGAIeRVLGGFALTL-LVPPEHYAAALrWVNRL--HLRGRLvYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 845 mdsgaevsASTTSSEAESGARSVS---SIVRQWnrkIDHFLGDR---------------PTA-TVNG-----GRPARKKF 900
Cdd:COG4913 526 --------PERPRLDPDSLAGKLDfkpHPFRAW---LEAELGRRfdyvcvdspeelrrhPRAiTRAGqvkgnGTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 901 QKKGASQS---FSKAARLKWqsLERRIidivmqrmtiVNLEADMERLIKKREELFLLQEALRRKREHLQ--AESPEEEKG 975
Cdd:COG4913 595 RRRIRSRYvlgFDNRAKLAA--LEAEL----------AELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEID 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 976 LQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDstdtsvvisscslaEARLLLDNFLKASIDKGLQVAQKEAQ 1055
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE--------------ELEEELDELKGEIGRLEKELEQAEEE 728
|
490 500 510
....*....|....*....|....*....|
gi 86990454 1056 IRLLEGRLRQTDMTGSSQNHLLLDALREKA 1085
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAA 758
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
634-841 |
8.25e-10 |
|
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: 63.92 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 634 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDtqLERDRVLQNlstmecyteEKANKIKADYEK 713
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR--LEQQKQILR---------ERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 714 RLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLvetkrNREIAQLKKEQ 792
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElEEQLETL-----RSKVAQLELQI 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 86990454 793 RRQEFQIRALESQKRQQEIVLRRKTQEVSAL-RRLAKPMSERVAGRVGLK 841
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEEL 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-1095 |
1.64e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 384 QQISALRAEIARLQMELMEYKAGKRVIGEDgtegYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANL 463
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 464 LlakagDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARNPYSLGASPAGpafggspATSMEDASEVIR 543
Cdd:TIGR02168 315 E-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-------ESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 544 KAKQDLERLKKKE----VRQRRKSPEKEAFKKR-AKLQAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEES 618
Cdd:TIGR02168 383 TLRSKVAQLELQIaslnNEIERLEARLERLEDRrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 619 LVDSDSDPEEKevnfQADLADLTCEIEIKQKLIDELENSQRRLQTLkhqYEEKLILLQNKIRDTQLeRDRVLQNLSTMEC 698
Cdd:TIGR02168 463 LEELREELEEA----EQALDAAERELAQLQARLDSLERLQENLEGF---SEGVKALLKNQSGLSGI-LGVLSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 699 Y------------------TEEKANK-IKADYEKRLREMN---RDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEM 756
Cdd:TIGR02168 535 YeaaieaalggrlqavvveNLNAAKKaIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 757 KKA----------------KVALMKQMREEQQ--------------------RRRLVETKRNREIAQLKKEQRRQEFQIR 800
Cdd:TIGR02168 615 RKAlsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIA 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 801 ALESQKRQQEIVLRRKTQEVSALRRlakpmservagrvglkppnmdsgAEVSASTTSSEAESGARSVSSIVRQWNRKIDH 880
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRK-----------------------ELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 881 FLGDRPTATVNggrpARKKFQKKGASQSFSKAARLKWQSLERRIidivmQRMTIvNLEADMERLIKKREELFLLQEALRR 960
Cdd:TIGR02168 752 LSKELTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQI-----EQLKE-ELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 961 KR---EHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQAtivQLEETKEELDSTDTSVVISSCSLAEARLLLDN 1037
Cdd:TIGR02168 822 LRerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86990454 1038 FlkasiDKGLQVAQKEAQiRLLEGRLRQTDMTGSSQNHL---------LLDALREK----AEAHPELQALI 1095
Cdd:TIGR02168 899 L-----SEELRELESKRS-ELRRELEELREKLAQLELRLeglevridnLQERLSEEysltLEEAEALENKI 963
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
633-1094 |
1.89e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.83 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 633 FQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMecytEEKANKIKADYE 712
Cdd:pfam15921 315 YMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL----DDQLQKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 713 KRLREMNrdLQKLQaAQKEHARLLKNQ---SRYERELKKLQAEVAEMKkakvALMKQMREEQQrrrlveTKRNREIAQLK 789
Cdd:pfam15921 388 KREKELS--LEKEQ-NKRLWDRDTGNSitiDHLRRELDDRNMEVQRLE----ALLKAMKSECQ------GQMERQMAAIQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 790 KEQRRQEfQIRALESQKRQQEIVLRRKTQEVSAlRRLAKPMSERVA-------------------------GRVGLKPPN 844
Cdd:pfam15921 455 GKNESLE-KVSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVsdltaslqekeraieatnaeitklrSRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 845 M----DSGAEVSASTTSSEA----ESGARSVSSIVRQWNRKIDHFLGDRptatvngGRPARKKFQKKGASQSFSKAARLK 916
Cdd:pfam15921 533 LqhlkNEGDHLRNVQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQH-------GRTAGAMQVEKAQLEKEINDRRLE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 917 WQ--------------SLERRIIDIVMQRMTIVNleADMERLIKKREelfllqeaLRRKREHLQAESPEEEKGLQELAEE 982
Cdd:pfam15921 606 LQefkilkdkkdakirELEARVSDLELEKVKLVN--AGSERLRAVKD--------IKQERDQLLNEVKTSRNELNSLSED 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 983 IEVLAANIDYINDSI-TDCQATIVQLEETKEELDSTDTSVVISSCSLAEArllldnfLKASIDKGLQVAQKEAQIRLLEG 1061
Cdd:pfam15921 676 YEVLKRNFRNKSEEMeTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA-------MKVAMGMQKQITAKRGQIDALQS 748
|
490 500 510
....*....|....*....|....*....|....*.
gi 86990454 1062 RLR--QTDMTGSS-QNHLLLDalrEKAEAHPELQAL 1094
Cdd:pfam15921 749 KIQflEEAMTNANkEKHFLKE---EKNKLSQELSTV 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-1093 |
2.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 702 EKANKIKAdyEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVAL---MKQMREEQQRRRLVE 778
Cdd:COG1196 213 ERYRELKE--ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 779 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAgrvglkppnmDSGAEVSASTTS- 857
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE----------EAEEELEEAEAEl 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 858 SEAESGARSVSSIVRQWNRKIDHFlgdrptatvnggrpARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNL 937
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEEL--------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 938 EADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDST 1017
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86990454 1018 DTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMTGSSQNHLLLDALREKAEAHPELQA 1093
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
634-1015 |
1.05e-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: 60.46 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 634 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcYTEEKANKIKADYEK 713
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 714 RLREMNRDLQKLQAAQKEHarllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQR----RRLVETKRNReIAQLK 789
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEA----------EAEIEELEAQIEQLKEELKALREALDELRAEltllNEEAANLRER-LESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 790 KEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPpnmdsgaevSASTTSSEAESGARSVSS 869
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------SLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 870 IVRQWNRKIdhflgdrptatvnggRPARKKFQKKGASQSfskAARLKWQSLERRIIDIvMQRMT---IVNLEADMERLIK 946
Cdd:TIGR02168 902 ELRELESKR---------------SELRRELEELREKLA---QLELRLEGLEVRIDNL-QERLSeeySLTLEEAEALENK 962
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86990454 947 KREELFLLQEALRRKREHLQA------ESPEEekgLQELAEEIEVLAANIDYINDSITdcqativQLEETKEELD 1015
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKElgpvnlAAIEE---YEELKERYDFLTAQKEDLTEAKE-------TLEEAIEEID 1027
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
624-897 |
1.19e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 624 SDPEEKEVnfQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEklilLQNKIRDTQLERDRVLQNLSTmecyTEEK 703
Cdd:COG3883 14 ADPQIQAK--QKELSELQAEL---EAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAE----AEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 704 ANKIKADYEKRLREMNRD----------------------LQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 761
Cdd:COG3883 81 IEERREELGERARALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 762 ALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLK 841
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 86990454 842 PPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIDHFLGDRPTATVNGGRPAR 897
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-1016 |
1.77e-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: 59.69 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 703 KANKIKAdyEKRLREMNRDLQKLQAAQKEHARLLKN---QSRYERELKKLQAEVAEMKKAKVAL-MKQMREEQQRRRLVE 778
Cdd:TIGR02168 171 KERRKET--ERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELALLVLrLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 779 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVA-GRVGLKPPNMDsgaEVSASTTS 857
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQiLRERLANLERQ---LEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 858 SEAESGARSVSSIVRQWNRKIDHFLGDRpTATVNGGRPARKKFQkkgASQSFSKAARLKWQSLERRIIDIVMQ----RMT 933
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEEL-ESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQiaslNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 934 IVNLEADMERLIKKREELFLLQEALRRK-----REHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLE 1008
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
....*...
gi 86990454 1009 ETKEELDS 1016
Cdd:TIGR02168 482 RELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
627-835 |
5.87e-08 |
|
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: 57.77 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDtqLERDRVLQNLSTMECYTEeKANK 706
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELS-KLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 707 IKADYEKRLREMNRDLQKL----QAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRn 782
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL- 884
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 86990454 783 reiAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVA 835
Cdd:TIGR02169 885 ---GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
666-842 |
1.13e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 56.79 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 666 HQYEEKLILLQNKI-RDTQLE--RDRVLQNLS----------TMECYTEEKANKIKADYEKRLREMNRDLQKLQ---AAQ 729
Cdd:COG2433 346 DAYKNKFERVEKKVpPDVDRDevKARVIRGLSieealeelieKELPEEEPEAEREKEHEERELTEEEEEIRRLEeqvERL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 730 KEHARLLKNQSR-YERELKKLQAEVAEMKKakvalmkQMREEQQRRRLVeTKRNREIAQLKKEQRRQEFQIRALESQ--- 805
Cdd:COG2433 426 EAEVEELEAELEeKDERIERLERELSEARS-------EERREIRKDREI-SRLDREIERLERELEEERERIEELKRKler 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 86990454 806 -KRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKP 842
Cdd:COG2433 498 lKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-1063 |
1.22e-07 |
|
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: 56.99 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 702 EKANKIKaDYEKRLREMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVEtkr 781
Cdd:TIGR02168 674 ERRREIE-ELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 782 nREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVagrvglkppnmdsgaevsasttsSEAE 861
Cdd:TIGR02168 747 -ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----------------------KALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 862 SGARSVSSIVRQWNRKIDhflgdrptatvnggrparkkfqkkgasqsfskAARLKWQSLERRIID----IVMQRMTIVNL 937
Cdd:TIGR02168 803 EALDELRAELTLLNEEAA--------------------------------NLRERLESLERRIAAterrLEDLEEQIEEL 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 938 EADMERLIKKREELFLLQEALRRKREHLQAESPEEE-------KGLQELAEEIEVLAANIDYINDSITDCQATIVQLEET 1010
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEealallrSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 86990454 1011 KEELDSTDTSvvISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRL 1063
Cdd:TIGR02168 931 LEGLEVRIDN--LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
438-832 |
2.68e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 438 RVKAMQEAIDAINNRVTQLMSQEANLllakagdgNEAIGALIQNYiREIEELRTKLLESEAMNESLRRSLSRASARnpys 517
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPEL--------REELEKLEKEV-KELEELKEEIEELEKELESLEGSKRKLEEK---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 518 lgaspagpafggspatsMEDASEVIRKAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQaenseetdeneaeeeeeerde 597
Cdd:PRK03918 261 -----------------IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY--------------------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 598 sgceeeegredededsgseeslvdsdSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLqN 677
Cdd:PRK03918 303 --------------------------EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-E 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 678 KIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLqaaQKEHARLLKNQSRYERELKKLQAEVAEMK 757
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI---EEEISKITARIGELKKEIKELKKAIEELK 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86990454 758 KAK--VALMKQMREEQQRRRLVEtKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLrRKTQEVSALRRLAKPMSE 832
Cdd:PRK03918 433 KAKgkCPVCGRELTEEHRKELLE-EYTAELKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKELAEQLKE 507
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
671-1063 |
3.16e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 671 KLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKAD---YEKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELK 747
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRVAELK---EELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 748 KLQAEVAEMKKAKVALMKQMREEQQRRRLVE----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKT 817
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 818 QEvsaLRRLAKP-------MSERVAGRVGLKPP-NMDSGAEVSASTTSSEAESGARSVSSivrqwnrkidhfLGDRPTAT 889
Cdd:pfam07888 185 EE---LRSLSKEfqelrnsLAQRDTQVLQLQDTiTTLTQKLTTAHRKEAENEALLEELRS------------LQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 890 VNGGRPARKKFQKKGASQSFSKA----ARLKWQSLERRIIDIVMQ-----------RMTIV-NLEADMERLIKkreelfl 953
Cdd:pfam07888 250 ERKVEGLGEELSSMAAQRDRTQAelhqARLQAAQLTLQLADASLAlregrarwaqeRETLQqSAEADKDRIEK------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 954 LQEALRRKREHLQAESPEEEKGLQELAEEievlaanidyindsiTDCqaTIVQLEETKEELDStdtsvvisscslaearl 1033
Cdd:pfam07888 323 LSAELQRLEERLQEERMEREKLEVELGRE---------------KDC--NRVQLSESRRELQE----------------- 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 86990454 1034 lldnfLKASidkgLQVAQKEAQ------------IRLLEGRL 1063
Cdd:pfam07888 369 -----LKAS----LRVAQKEKEqlqaekqelleyIRQLEQRL 401
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
650-1013 |
3.25e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 650 LIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKLQAAQ 729
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL--------EQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 730 KEHARLLKnqsRYERELKKLQAEVAEMKKAKVALM---KQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALEsqK 806
Cdd:COG4372 97 AQAQEELE---SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE--Q 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 807 RQQEIVLRRKTQEVSALRRLAKPMSERVagrvglKPPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIDHFlgdrp 886
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKE------EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 887 taTVNGGRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQ 966
Cdd:COG4372 241 --ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 86990454 967 AESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEE 1013
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-984 |
3.55e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 354 DFMETLNTLK------YANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELM-------EYKAGKRVIGEDGTEGYSD 420
Cdd:PTZ00121 1019 DFNQNFNIEKieelteYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLkpsykdfDFDAKEDNRADEATEEAFG 1098
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 421 LFRENAmlQKENGAL---RLRVKAMQEAIDAinNRVTQLMSQEAnllLAKAGDGNEAIGALIQNYIREIEELRtKLLESE 497
Cdd:PTZ00121 1099 KAEEAK--KTETGKAeeaRKAEEAKKKAEDA--RKAEEARKAED---ARKAEEARKAEDAKRVEIARKAEDAR-KAEEAR 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 498 AMNESLRRSLSRASARNPYSLGASPAGPAFGGSPATSMEDA--SEVIRKAKqdlERLKKKEVRQRRKSPEKEAFKKRAKL 575
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErkAEEARKAE---DAKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 576 QAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEvnfQADLADLTCEieiKQKLIDEL- 654
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK---KADEAKKKAE---EAKKADEAk 1321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 655 ---ENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV--------LQNLSTMECYTEEKANKIKADYEKRLREMNR--- 720
Cdd:PTZ00121 1322 kkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeAAEKKKEEAKKKADAAKKKAEEKKKADEAKKkae 1401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 721 ------DLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMK--QMREEQQRRRLVETKRNREIAQLKKEQ 792
Cdd:PTZ00121 1402 edkkkaDELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 793 RRQ--EFQIRALESQKRQQEivLRRKTQEVSALRRLAKPMSERVAGRV-----GLKPPNMDSGAEVSASTTSSEAES--G 863
Cdd:PTZ00121 1482 AKKadEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADEAkkaeeAKKADEAKKAEEKKKADELKKAEElkK 1559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 864 ARSVSSIVRQWNRKIDHFLGDRPTATVNGGRPAR-KKFQKKGASQSFSKAARLKWQSLERRIIDIVMQ----RMTIVNLE 938
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeeeKKKVEQLK 1639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 86990454 939 ADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIE 984
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
534-823 |
4.17e-07 |
|
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: 55.07 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 534 SMEDASEVIRKAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQAENseetdeneaeeeeeerdesgceeeegredededs 613
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---------------------------------- 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 614 gSEESLVDSDSDPEEKE---VNFQADLADLtcEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLER---D 687
Cdd:TIGR02169 756 -VKSELKELEARIEELEedlHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeylE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 688 RVLQNLSTMECYTEEKANKIKADYE---KRLREMNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKkakvalm 764
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRD----------LESRLGDLKKERDELE------- 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86990454 765 KQMREEQQRRRLVETKRNRE---IAQLKKEQRRQEFQIRALESQKRQ-QEIV------------LRRKTQEVSAL 823
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEdEEIPeeelsledvqaeLQRVEEEIRAL 970
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
647-819 |
4.93e-07 |
|
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: 54.74 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 647 KQKLIDEleNSQRRLQTLKHQYE----EKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLR---EMN 719
Cdd:pfam17380 403 KVKILEE--ERQRKIQQQKVEMEqiraEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRkklELE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 720 RDLQKLQAAQKEHARLLknqsryERELKKLQAEVAEMKKAKVALMKQMRE------EQQRRRLVETKRNREIAQlkKEQR 793
Cdd:pfam17380 481 KEKRDRKRAEEQRRKIL------EKELEERKQAMIEEERKRKLLEKEMEErqkaiyEEERRREAEEERRKQQEM--EERR 552
|
170 180 190
....*....|....*....|....*....|...
gi 86990454 794 RQEFQIRA-------LESQKRQQEIVLRRKTQE 819
Cdd:pfam17380 553 RIQEQMRKateersrLEAMEREREMMRQIVESE 585
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
643-825 |
9.11e-07 |
|
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: 53.87 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 643 EIEIKQKLIDELENSQRRLQTLKHQYEEKLILL-------QNKIRDTQLERDRVLQNLSTMECYTE-------------E 702
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeklniQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqiselkK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 703 KANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKR 781
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKE 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86990454 782 NREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRR 825
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
645-818 |
1.10e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 51.31 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 645 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnkirdTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQK 724
Cdd:pfam14988 22 KLWNQYVQECEEIERRRQELASRYTQQTAELQ-----TQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 725 LQAA-----QKEHARLLKNQSRYERELKKLQA-EVAEMKKAKVALMKQMREEQQRRRLVETKRN--REIAQLKKEQRRQE 796
Cdd:pfam14988 97 VRAEtaekdREAHLQFLKEKALLEKQLQELRIlELGERATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQLI 176
|
170 180
....*....|....*....|..
gi 86990454 797 FQIRALESQKRQQEivlRRKTQ 818
Cdd:pfam14988 177 QETQALEAIKSKLE---NRKQR 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
709-996 |
1.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 709 ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETkrNREIAQL 788
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS--SDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 789 KKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEvsastTSSEAESGARSVS 868
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-----ERFAAALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 869 SIVRQWNRKIDhflgdrptatvnggrparkkfqkkgasqsfskAARLKWQSLERRIIDIVMQ-----RMTIVNLEADMER 943
Cdd:COG4913 766 ELRENLEERID--------------------------------ALRARLNRAEEELERAMRAfnrewPAETADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 86990454 944 LIKKREEL-FLLQEALRRKRE---HLQAESPEEEKG--LQELAEEIEVLAANIDYINDS 996
Cdd:COG4913 814 LPEYLALLdRLEEDGLPEYEErfkELLNENSIEFVAdlLSKLRRAIREIKERIDPLNDS 872
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
725-1025 |
1.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 725 LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRRLVETkrNREIAQLKKEQRRQEFQIRALES 804
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAAL--ARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 805 QKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPpnmdsgaevsasttsseaesgarsvssivrqwnrkidhflgd 884
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSP------------------------------------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 885 rptatvnggrparkkfqkKGASQSFSKAARLKwQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREH 964
Cdd:COG4942 129 ------------------EDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86990454 965 LQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDSTDTSVVISS 1025
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
651-805 |
1.33e-06 |
|
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: 51.46 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 651 IDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKaDYEKRLrEMNRDLQKLQAAQK 730
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQL-GNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86990454 731 EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQ 805
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
644-832 |
1.54e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 52.37 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 644 IEIKQ---KLIDELENSQRRLQTLKHQyeeklillQNKIRDTQLERDRVLQNLSTMECYTE----EKANKIKADyEKRLr 716
Cdd:pfam15742 62 AELKQaqqKLLDSTKMCSSLTAEWKHC--------QQKIRELELEVLKQAQSIKSQNSLQEklaqEKSRVADAE-EKIL- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 717 emnrDLQKlqaaQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETK-----------RNREi 785
Cdd:pfam15742 132 ----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNvnelqqqvrslQDKE- 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86990454 786 AQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSE 832
Cdd:pfam15742 203 AQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSS 249
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
627-828 |
1.68e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLID-ELENSQRRLQTLKhqyeeklilLQNKIRDTQLERDRVLQNLSTMEcytEEKAN 705
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEkEEEKLAQVLKENK---------EEEKEKKLQEEELKLLAKEEEEL---KSELL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 706 KIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREI 785
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86990454 786 AQLKKEQRRQEFQI-RALESQKRQQEIVLRRKTQEVSALRRLAK 828
Cdd:pfam02463 384 ERLSSAAKLKEEELeLKSEEEKEAQLLLELARQLEDLLKEEKKE 427
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
715-839 |
1.71e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.59 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 715 LREMNRDLQKLQAAQkehARLLKNQSRYERELKKLQAEVAEMKK-------------AKVALMKQMREEQQRRRLvetkr 781
Cdd:COG1842 32 IRDMEEDLVEARQAL---AQVIANQKRLERQLEELEAEAEKWEEkarlalekgredlAREALERKAELEAQAEAL----- 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 86990454 782 NREIAQLKKEQRRQEFQIRALESQKRQqeivLRRKTQEVSALRRLAKpMSERVAGRVG 839
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEE----LKAKKDTLKARAKAAK-AQEKVNEALS 156
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
647-835 |
2.68e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.46 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 647 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLsTMECYTEEKANKIKADYEKRlREMNRDLQKLQ 726
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL-YQEEQERKERQKEREEAEKK-ARQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 727 AAQKEHARLLKnqsryerelkklQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQefqiraLESQK 806
Cdd:pfam13868 242 EEQIELKERRL------------AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ------IEERE 303
|
170 180
....*....|....*....|....*....
gi 86990454 807 RQQEIVLRRKTQEVSALRRLAKPMSERVA 835
Cdd:pfam13868 304 EQRAAEREEELEEGERLREEEAERRERIE 332
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
674-819 |
2.73e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 674 LLQNKIRDTQLERDRVLQNLST-MECYTEEK-------ANKIKADYEKRLREMNRDLQKLQAaqkehaRLLKNQSRYERE 745
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKeAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEK------RLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 746 LKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR------EIAQLKKEQRRQEfQIRALESQKRQQEIVLRRKTQE 819
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqeleRISGLTAEEAKEI-LLEKVEEEARHEAAVLIKEIEE 180
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
653-833 |
2.89e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 653 ELENSQRRLQTLKhqyEEKLILLQNKIRDT---QLER----DRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKL 725
Cdd:pfam17380 354 RQEERKRELERIR---QEEIAMEISRMRELerlQMERqqknERVRQEL--------EAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 726 QA--AQKEHAR---LLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKEQRR----QE 796
Cdd:pfam17380 423 EQirAEQEEARqreVRRLEEERAREMERVRLEEQE-RQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQRRkileKE 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86990454 797 FQIRAL--------------ESQKRQQEIVLRRKTQEVSALRRLAKPMSER 833
Cdd:pfam17380 501 LEERKQamieeerkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEER 551
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
657-833 |
4.34e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 657 SQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQK--EHAR 734
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERkrELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 735 LLKNQSRYE----RELKKLQ-----------AEVAEMKKAKV-------------ALMKQMREEQqrrrlvETKRNREIA 786
Cdd:pfam17380 365 IRQEEIAMEisrmRELERLQmerqqknervrQELEAARKVKIleeerqrkiqqqkVEMEQIRAEQ------EEARQREVR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86990454 787 QLKKEQRRQEFQIRaLESQKRQQEIVLRRKTQEVSALRRLAKPMSER 833
Cdd:pfam17380 439 RLEEERAREMERVR-LEEQERQQQVERLRQQEEERKRKKLELEKEKR 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
713-833 |
5.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 713 KRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK--AKVALMKQMREEQQRRRLVETKRNREIAQLKK 790
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86990454 791 EQRRQEfQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSER 833
Cdd:COG4717 151 LEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
483-1018 |
8.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 483 IREIEELR-----TKLLESEAMNESLRRSlsrASARNPYSLGASPAGPAFGGSPATSMEDASEV-----IRKA--KQDLE 550
Cdd:PTZ00121 1229 VKKAEEAKkdaeeAKKAEEERNNEEIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKkkadeAKKAeeKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 551 RLKKKEVRQRR----KSPEKEAFKKRAKLQAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDP 626
Cdd:PTZ00121 1306 EAKKKAEEAKKadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTmECYTEEKANK 706
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKK 1464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 707 iKADYEKRLREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVAlmKQMREEQQRRRLVETKR 781
Cdd:PTZ00121 1465 -KAEEAKKADEAKKKAEEAKKADEakkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKK 1541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 782 NREIA---QLKK-EQRRQEFQIRALESQKRQQEivlrRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAE----VSA 853
Cdd:PTZ00121 1542 AEEKKkadELKKaEELKKAEEKKKAEEAKKAEE----DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakkAEE 1617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 854 STTSSEAESGARSVSSIVRQWN-------RKIDHFLGDRPTATVNGGRPARKKFQKKGASQSFSKA---ARLKWQSLERR 923
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKkkeaeekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEALKKE 1697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 924 iidiVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEiEVLAANIDYINDSITDCQAT 1003
Cdd:PTZ00121 1698 ----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEE 1772
|
570
....*....|....*..
gi 86990454 1004 IVQLEET--KEELDSTD 1018
Cdd:PTZ00121 1773 IRKEKEAviEEELDEED 1789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
912-1094 |
1.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 912 AARLKWQSLERRIIDivmQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANID 991
Cdd:COG1196 229 LLLLKLRELEAELEE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 992 YINDSITDCQATIVQLEETKEELDSTDTSVVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMTGS 1071
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180
....*....|....*....|...
gi 86990454 1072 SQNHLLLDALREKAEAHPELQAL 1094
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEEL 405
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-1095 |
1.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 703 KANKIKAdyEKRLREMNRDLQKLQAAQKEharlLKNQsryereLKKL--QAEVAEmkKAKvALMKQMREEQQRRRLVETK 780
Cdd:COG1196 171 KERKEEA--ERKLEATEENLERLEDILGE----LERQ------LEPLerQAEKAE--RYR-ELKEELKELEAELLLLKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 781 RNReiAQLKKEQRRQEF---QIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERvagrvglkppnmdsgaevsastts 857
Cdd:COG1196 236 ELE--AELEELEAELEEleaELEELEAELAELEAELEELRLELEELELELEEAQAE------------------------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 858 sEAESGARsvssiVRQWNRKIDHflgdrptatvnggrparkkfQKKGASQSFSKAARLKWQ--SLERRIIDIVMQRMT-- 933
Cdd:COG1196 290 -EYELLAE-----LARLEQDIAR--------------------LEERRRELEERLEELEEElaELEEELEELEEELEEle 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 934 --IVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETK 1011
Cdd:COG1196 344 eeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 1012 EELDStdtsvvisscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMTGSSQNHLLLDALREKAEAHPEL 1091
Cdd:COG1196 424 EELEE----------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
....
gi 86990454 1092 QALI 1095
Cdd:COG1196 494 LLLL 497
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
655-834 |
1.25e-05 |
|
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: 48.38 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 655 ENSQRRLQTLkHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyTE-EKANKIKADYEKRLREMNRDLQKLQAAQKEHA 733
Cdd:COG1579 3 PEDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALE--ARlEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 734 RLLkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlVETKRNrEIAQLKKEQRRQEFQIRALESQKRQQEIVL 813
Cdd:COG1579 80 EQL-GNVRNNKEYEALQKEIESLKRRISDLEDEILELMER---IEELEE-ELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|..
gi 86990454 814 RRKTQEVSALR-RLAKPMSERV 834
Cdd:COG1579 155 EAELEELEAEReELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
627-828 |
1.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLID---------ELENSQRRLQTLKHQ-------------YEEKLILLQNKIRDTQL 684
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNleelekkaeEYEKLKEKLIKLKGEikslkkelekleeLKKKLAELEKKLDELEE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 685 ERDRVLQNLstmecytEEKANKIKADYEKRLREMN---RDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 761
Cdd:PRK03918 571 ELAELLKEL-------EELGFESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86990454 762 ALMKQMrEEQQRRRLVETKRN--REIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAK 828
Cdd:PRK03918 644 ELRKEL-EELEKKYSEEEYEElrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-1030 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 532 ATSMEDASEVIRKAkqdlERLKKKEVRQRRKSPE---KEAFKKRA---KLQAENSEETDENEAEEEEEERDESGCEEEEG 605
Cdd:PTZ00121 1380 ADAAKKKAEEKKKA----DEAKKKAEEDKKKADElkkAAAAKKKAdeaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 606 REDEDEDSGSEESLVDSDSDPEEKEVNFQADladltceiEIKQKLidelENSQRRLQTLKHQYEEKLILLQNKirdtQLE 685
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--------EAKKKA----EEAKKKADEAKKAAEAKKKADEAK----KAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 686 RDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVA-EMKKAKVALM 764
Cdd:PTZ00121 1520 EAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEV 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 765 KQMREEQQRRRLVETKRNREiAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRvglkppn 844
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK------- 1669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 845 mdsgaEVSASTTSSEAESGARSVSSIVRQWNRKIDHflgdrptatvnggrpARKKFQ-KKGASQSFSKAARLKWQSLERR 923
Cdd:PTZ00121 1670 -----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEE---------------AKKAEElKKKEAEEKKKAEELKKAEEENK 1729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 924 IidivmqrmTIVNLEADMERLIKKREELFLLQE-----ALRRKREHLQAESPEEEKGL---QELAEEIEVLAANIDYIND 995
Cdd:PTZ00121 1730 I--------KAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIK 1801
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 86990454 996 SITDCQATIVQ--------LEETKEELDSTDTSVVISSCSLAE 1030
Cdd:PTZ00121 1802 DIFDNFANIIEggkegnlvINDSKEMEDSAIKEVADSKNMQLE 1844
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
384-828 |
2.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 384 QQISALRAEIARLQMELMEYKAGKRVIgedgtegySDLFRENAMLQKENGALRLRVKAMQEAIDAINNRvtqlmsQEANL 463
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL--------EELEEELEELEAELEELREELEKLEKLLQLLPLY------QELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 464 LLAKAGDGNEAIGALiQNYIREIEELRTKLLESEAMNESLRRSLSRASARNpyslgaSPAGPAFGGSPATSMEDASEVIR 543
Cdd:COG4717 137 LEAELAELPERLEEL-EERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 544 KAKQDLERLK--KKEVRQRRKS--PEKEAFKKRAKLQAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESL 619
Cdd:COG4717 210 ELEEELEEAQeeLEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 620 VDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECY 699
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 700 TEEKA--NKIKADYEKRLREMNRDLQKLQAAqkeharllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLV 777
Cdd:COG4717 370 QEIAAllAEAGVEDEEELRAALEQAEEYQEL--------------KEELEELEEQLEELLGELEELLEALDEEELEEELE 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 86990454 778 ETKRN-----REIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEvSALRRLAK 828
Cdd:COG4717 436 ELEEEleeleEELEELREELAELEAELEQLEEDGELAELLQELEELK-AELRELAE 490
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
632-819 |
2.63e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 632 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNK---IRDTQLErdrvLQNLSTMECYTEEKANKIK 708
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeIHDLEIQ----LTAIKTSEEHYLKEVEDLK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 709 ADYEK-RLR--EMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvETKRNREI 785
Cdd:pfam05483 478 TELEKeKLKniELTAHCDKLLLENKE---LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----EMNLRDEL 550
|
170 180 190
....*....|....*....|....*....|....*.
gi 86990454 786 AQLKKE--QRRQEFQIRALESQKRQQEIVLRRKTQE 819
Cdd:pfam05483 551 ESVREEfiQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
380-823 |
3.25e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 380 DKTSQQISALRAEIARLQMEL-----------MEYKAGKRVIGEDGTegysdLFRENAMLQKENGALRlrvKAMQEAIDA 448
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELeemtkfknnkeVELEELKKILAEDEK-----LLDEKKQFEKIAEELK---GKEQELIFL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 449 INNRVTQLMSQEANLLLAKAGDgneaigaliQNYIREIEELRTKLLESEAMNESLRRSLSRASARNPyslgaspagpafg 528
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSE---------EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK------------- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 529 gSPATSMEDASEVIRKAKQDLERLKKKEVRQRRkspekeafkkraklQAENSEETDENEAEEEEEERDESGCEEEEGRED 608
Cdd:pfam05483 503 -ELTQEASDMTLELKKHQEDIINCKKQEERMLK--------------QIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 609 EDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDR 688
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 689 VLQNLSTMeCYTEEKANKIKADYEKRLREmnrDLQKLQAAQKEHARLLKNQSryerelKKLQAEVAEMkkakVALMKqmR 768
Cdd:pfam05483 648 AKQKFEEI-IDNYQKEIEDKKISEEKLLE---EVEKAKAIADEAVKLQKEID------KRCQHKIAEM----VALME--K 711
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86990454 769 EEQQRRRLVEtKRNREIAQLKKEQRRQEFQIRALE-----------SQKRQQEI------VLRRKTQEVSAL 823
Cdd:pfam05483 712 HKHQYDKIIE-ERDSELGLYKNKEQEQSSAKAALEielsnikaellSLKKQLEIekeekeKLKMEAKENTAI 782
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
632-817 |
3.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 632 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEE-KANKIKAD 710
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 711 YEKRLREMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreeqqrrrlveTKRNREIAQLKK 790
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----------SSLEKELEKAKK 624
|
170 180
....*....|....*....|....*....
gi 86990454 791 EQRRQEFQIRALESQKR--QQEIVLRRKT 817
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNklKQEVKQIKET 653
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
718-828 |
3.87e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 45.26 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 718 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLKKE-QRRQE 796
Cdd:pfam03938 7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKE-------QELQKKEQElQQLQQ 79
|
90 100 110
....*....|....*....|....*....|..
gi 86990454 797 FQIRALesQKRQQEIVLRRKTQEVSALRRLAK 828
Cdd:pfam03938 80 KAQQEL--QKKQQELLQPIQDKINKAIKEVAK 109
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1578-1615 |
4.03e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 42.30 E-value: 4.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 86990454 1578 NFTPIGEIKGHDSPINAIC--TNSKHIFTASSDLTVKFWS 1615
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
672-824 |
4.10e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.20 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 672 LILLQNKIRDTQLERDRVLQNLstmecytEEKANKIKADYE---KRLREMNRDLQKLQaaQKEHARLLKNQSRYERELKK 748
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDresDRNQELQKRIRLLE--KREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86990454 749 LQAEVAEMKKAKvalmKQMREEQQRRRLVETKRNrEIAQLKKEQRRQEFQIRALESQK---RQQEIVLRRKTQEVSALR 824
Cdd:pfam05557 82 KKYLEALNKKLN----EKESQLADAREVISCLKN-ELSELRRQIQRAELELQSTNSELeelQERLDLLKAKASEAEQLR 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
652-826 |
5.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 652 DELENSQRRLQTLKhqyeeklilLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYEKRLREMNRDLQKLQAAQKE 731
Cdd:COG3206 189 KELEEAEAALEEFR---------QKNGLVDLSEEAKLLLQQLSELE----SQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 732 HARLLKNQ--SRYERELKKLQAEVAEMK-------------KAKVA-LMKQMREEQQrRRLVETKRNREIAQLKK---EQ 792
Cdd:COG3206 256 LPELLQSPviQQLRAQLAELEAELAELSarytpnhpdvialRAQIAaLRAQLQQEAQ-RILASLEAELEALQAREaslQA 334
|
170 180 190
....*....|....*....|....*....|....
gi 86990454 793 RRQEFQIRALESQKRQQEivLRRKTQEVSALRRL 826
Cdd:COG3206 335 QLAQLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
716-820 |
6.49e-05 |
|
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: 47.64 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 716 REMNRDL-QKLQAAQKEHARLLKNQSRYER-ELKKLQAEVAEMKKakvalmkQMREE----QQRR----RLVETKRNREI 785
Cdd:pfam15709 328 REQEKASrDRLRAERAEMRRLEVERKRREQeEQRRLQQEQLERAE-------KMREEleleQQRRfeeiRLRKQRLEEER 400
|
90 100 110
....*....|....*....|....*....|....*
gi 86990454 786 AQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEV 820
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL 435
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
627-1017 |
7.67e-05 |
|
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: 47.48 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRlqtlkhqyeeklilLQNKIRDTQLERDRVLQNLSTME--------C 698
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR--------------LQQELDDLLVDLDHQRQLVSNLEkkqkkfdqM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 699 YTEEKA-------NKIKADYEKRLRE-----MNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKKAKVALMKQ 766
Cdd:pfam01576 610 LAEEKAisaryaeERDRAEAEAREKEtralsLARALEEALEAKEE----------LERTNKQLRAEMEDLVSSKDDVGKN 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 767 MREEQQRRRLVETkrnrEIAQLKKEQRRQEFQIRALESQKRQQEIVLRR-KTQEVSALRRLAKPMSERvaGRVGLKppnm 845
Cdd:pfam01576 680 VHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRLEVNMQAlKAQFERDLQARDEQGEEK--RRQLVK---- 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 846 dsgaEVSASTTSSEAESGARSVSSIVRqwnRKIDHFLGD--RPTATVNGGRPARKKFQKKGASQsfskaarlkWQSLERR 923
Cdd:pfam01576 750 ----QVRELEAELEDERKQRAQAVAAK---KKLELDLKEleAQIDAANKGREEAVKQLKKLQAQ---------MKDLQRE 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 924 IIDIVMQRMTIVNLEADMERLIKKRE-ELFLLQEAL---RRKREHLQAESpeeekglQELAEEIEVLAANIDYINDSITD 999
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEaELLQLQEDLaasERARRQAQQER-------DELADEIASGASGKSALQDEKRR 886
|
410
....*....|....*...
gi 86990454 1000 CQATIVQLEETKEELDST 1017
Cdd:pfam01576 887 LEARIAQLEEELEEEQSN 904
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
712-828 |
8.01e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 712 EKRLREMNRDLQKLQAAQKEHARLLKnqsryeRELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKE 791
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALE------EEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110
....*....|....*....|....*....|....*..
gi 86990454 792 QRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAK 828
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
370-1061 |
8.47e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 370 NIKNKVVVNQDKTSQQIsALRAEIARLQMElmEYKAGKRVIgEDGTEGYSDLFRENAMLQKENGALRLrvkamqeaidaI 449
Cdd:pfam02463 131 SPEAYNFLVQGGKIEII-AMMKPERRLEIE--EEAAGSRLK-RKKKEALKKLIEETENLAELIIDLEE-----------L 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 450 NNRVTQLMSQEANLL-----LAKAGDGNEAIGALIQNYIRE--IEELRTKLLESEAMNESLRRSLSRA---SARNPYSLG 519
Cdd:pfam02463 196 KLQELKLKEQAKKALeyyqlKEKLELEEEYLLYLDYLKLNEerIDLLQELLRDEQEEIESSKQEIEKEeekLAQVLKENK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 520 ASPAGPAFGGSPATSMEDASEVIRKAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQAENSEETDENEAEEEEEERDESG 599
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 600 CEEEEGREDEDEDSGSEESLVDSDSdpeEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKI 679
Cdd:pfam02463 356 EEEEELEKLQEKLEQLEEELLAKKK---LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-EI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 680 RDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKA 759
Cdd:pfam02463 432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 760 KVALMKQMR------EEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSER 833
Cdd:pfam02463 512 LLALIKDGVggriisAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 834 VAGRVGLKPPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIDH-FLGDRPTATVNGGRPARKKFQKKGASQSFSKA 912
Cdd:pfam02463 592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 913 ARLKWQSLErRIIDIVMQRMTIVNLEADME----RLIKKREELFLLQEALRRK---REHLQAESPEEEKGLQELAEEIEV 985
Cdd:pfam02463 672 TKELLEIQE-LQEKAESELAKEEILRRQLEikkkEQREKEELKKLKLEAEELLadrVQEAQDKINEELKLLKQKIDEEEE 750
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86990454 986 LAANIDYINDSITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEG 1061
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
278-797 |
8.91e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 278 SERLKRTGATGERAKEGISINCGLLALGNVISALGDQSK-KVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRdfm 356
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN--- 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 357 eTLNTLKYANRARNIKNKVVVNQDKTSQQISALRAE-IARLQMELMEYKAGKRVIGEDGTEGYSDL--------FRENAM 427
Cdd:pfam02463 605 -LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKSEVKASLSeltkelleIQELQE 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 428 LQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSL 507
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 508 SRASARNPYSLGASpagpafggspatsmEDASEVIRKAKQDLERLKKKEV---RQRRKSPEKEAFKKRAKLQAENSEETD 584
Cdd:pfam02463 764 EEKSELSLKEKELA--------------EEREKTEKLKVEEEKEEKLKAQeeeLRALEEELKEEAELLEEEQLLIEQEEK 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 585 ENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDpEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTL 664
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ-ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 665 KHQYEEKLILLQNKIrdtQLERDRVLQNLStmECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYER 744
Cdd:pfam02463 909 LNLLEEKENEIEERI---KEEAEILLKYEE--EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 86990454 745 ELKKLQAEVAEMKKAKvalMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEF 797
Cdd:pfam02463 984 EEKEERYNKDELEKER---LEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
652-799 |
1.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 652 DELENSQRRLQTLKHQYEEKLILLQNKIRDTqlerDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK-LQAAQK 730
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEA----EKLKEEL-------EEKKEKLQEEEDKLLEEAEKEAQQaIKEAKK 584
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86990454 731 EHARLLknqsryeRELKKLQAEVAEMKKAKVAlmkqmreEQQRRRLVETKRNREIAQLKKEQRRQEFQI 799
Cdd:PRK00409 585 EADEII-------KELRQLQKGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1301-1336 |
1.34e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.79 E-value: 1.34e-04
10 20 30
....*....|....*....|....*....|....*...
gi 86990454 1301 QCISMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1336
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
627-820 |
1.54e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 627 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstMECYTEEKANK 706
Cdd:pfam13868 41 EERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV--ERIQEEDQAEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 707 IKADYEKR-----LREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQR--- 773
Cdd:pfam13868 119 EEKLEKQRqlreeIDEFNEEQAEWKELEKeeereEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKaqd 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 86990454 774 -----------RRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEV 820
Cdd:pfam13868 199 ekaerdelrakLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA 256
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
720-1085 |
1.55e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 720 RDLQKLQAAQKEHARLLKNQSRYErELKKLQAEVAEMKKAKVALMKQMREEQQRRrlvetkrnreiaqlKKEQRRQEFQI 799
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFN-TLESAELRLSHLHFGYKSDETLIASRQEER--------------QETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 800 RALESQKRQqeiVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEvsasTTSSEAESgARSVSSIVRQWNRKID 879
Cdd:pfam12128 293 RTLDDQWKE---KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE----TAAADQEQ-LPSWQSELENLEERLK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 880 HFLGDRPTATvnggrparKKFQK---KGASQSFSKAARLKwQSLERriidivmQRMTIVNLEADMERLIKKreelflLQE 956
Cdd:pfam12128 365 ALTGKHQDVT--------AKYNRrrsKIKEQNNRDIAGIK-DKLAK-------IREARDRQLAVAEDDLQA------LES 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 957 ALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLD 1036
Cdd:pfam12128 423 ELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 86990454 1037 NFLkasidkglqVAQKEAQIRLLE--GRLRQTDMTGSSQNHLLLDALREKA 1085
Cdd:pfam12128 503 QAS---------EALRQASRRLEErqSALDELELQLFPQAGTLLHFLRKEA 544
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
646-789 |
1.67e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 646 IKQKLIDELENSQRRLQTLKhQYEEKL--ILLQNKIRDTQLERD-RVLQNLstmecytEEKANKIKADYEKRLREmnrdl 722
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLM-KELELLnsIKPKLRDRKDALEEElRQLKQL-------EDELEDCDPTELDRAKE----- 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86990454 723 qKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLK 789
Cdd:smart00787 212 -KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLK 277
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
647-827 |
1.75e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.10 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 647 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNlstmecyTEEKANKIKADYEK---------RLR- 716
Cdd:pfam15709 321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQE-------QLERAEKMREELELeqqrrfeeiRLRk 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 717 -------------EMNRDLQkLQAAQkEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR 783
Cdd:pfam15709 394 qrleeerqrqeeeERKQRLQ-LQAAQ-ERARQ--QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLM 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 86990454 784 EIAqlkkEQRRQEFQIRALESQ-KRQQEIVLRRKTQEVSAlrRLA 827
Cdd:pfam15709 470 EMA----EEERLEYQRQKQEAEeKARLEAEERRQKEEEAA--RLA 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
363-1016 |
1.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 363 KYANRARNIKNKVVVNQDK---TSQQISALRAEIARLQMELMEYKAGKRVIgEDGTEGYSDLFRENAMLQKENGALRLRV 439
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 440 KAMQEAIDAINNRVTQLMSQEANLL-LAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARNpysl 518
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE---- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 519 gaspagpafggspaTSMEDASEVIRKAKQDLERLKKK-EVRQRRKSPEKEAFKKRAKLQAENSEETDENEaeeeeeerde 597
Cdd:PRK03918 338 --------------ERLEELKKKLKELEKRLEELEERhELYEEAKAKKEELERLKKRLTGLTPEKLEKEL---------- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 598 sgceeeegredededsgseESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKlillqn 677
Cdd:PRK03918 394 -------------------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE------ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 678 kirdtqlERDRVlqnlstMECYTEEKAN--KIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYErELKKLQAEVAE 755
Cdd:PRK03918 449 -------HRKEL------LEEYTAELKRieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 756 MKKAKValmkqmreeqqrrrlveTKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSE--R 833
Cdd:PRK03918 515 YNLEEL-----------------EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllK 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 834 VAGRVGLKppnmdsgaevsastTSSEAESGARSVSSIVRQWNRKidhflgdrptatvnggRPARKKFQkkgasqsfskaA 913
Cdd:PRK03918 578 ELEELGFE--------------SVEELEERLKELEPFYNEYLEL----------------KDAEKELE-----------R 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 914 RLKWQSLERRiiDIVMQRMTIVNLEADMERLIKKREELfllqealrrKREHLQAESPEEEKGLQELAEEIEVLAANIDYI 993
Cdd:PRK03918 617 EEKELKKLEE--ELDKAFEELAETEKRLEELRKELEEL---------EKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
650 660
....*....|....*....|...
gi 86990454 994 NDSITDCQATIVQLEETKEELDS 1016
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREK 708
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
644-815 |
2.28e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 42.97 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 644 IEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteekankikadyekRLREMNRDLQ 723
Cdd:COG2882 11 LDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAA----------------QLRNYQQFIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 724 KLQAAQKEHARLLKN-QSRYERELKKLQaevaemkkakvalmkqmrEEQQRRRLVETKRNREIAQLKKEQRRQEfqiral 802
Cdd:COG2882 75 RLDEAIEQQQQQVAQaEQQVEQARQAWL------------------EARQERKALEKLKERRREEERQEENRRE------ 130
|
170
....*....|...
gi 86990454 803 esQKRQQEIVLRR 815
Cdd:COG2882 131 --QKELDELASRR 141
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
643-810 |
2.47e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.71 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 643 EIEIKQKLIDELENSQRR----LQTLKHQYEEKlillqnKIRDTQLERDRVLQnlstmECYTEEKANKIKADYEKRLREM 718
Cdd:pfam15709 367 QLERAEKMREELELEQQRrfeeIRLRKQRLEEE------RQRQEEEERKQRLQ-----LQAAQERARQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 719 NRDLQKlQAAQKEHARllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnreiAQLKKEQRRQ--E 796
Cdd:pfam15709 436 QRKKQQ-EEAERAEAE--------KQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK----ARLEAEERRQkeE 502
|
170
....*....|....*
gi 86990454 797 FQIR-ALESQKRQQE 810
Cdd:pfam15709 503 EAARlALEEAMKQAQ 517
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1299-1336 |
2.69e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.99 E-value: 2.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 86990454 1299 PLQCISMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1336
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
634-803 |
3.01e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 634 QADLADLTCEIEIKQKLIDELENSQ---RRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIkAD 710
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLeelRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL-AD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 711 YEKRLREMNRDLQK-----LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQ-----MREEQQRRRLVETK 780
Cdd:pfam07888 291 ASLALREGRARWAQeretlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELK 370
|
170 180
....*....|....*....|....*...
gi 86990454 781 RNREIAQLKKEQRRQEFQ-----IRALE 803
Cdd:pfam07888 371 ASLRVAQKEKEQLQAEKQelleyIRQLE 398
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
545-1065 |
3.30e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 545 AKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQAENSEETDENEAEE--EEEERDESGCEEEEGREDEDedsgSEESLVDS 622
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKklQEEELKLLAKEEEELKSELL----KLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 623 DSDPEEKEVNfqadladltcEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEE 702
Cdd:pfam02463 312 DEEKLKESEK----------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 703 KANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRN 782
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 783 REIAQLKKEqRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEVSAST--TSSEA 860
Cdd:pfam02463 462 KDELELKKS-EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlgVAVEN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 861 ESGARSVSSIVRqwnrkiDHFLGDRPTATVNGGRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIvNLEAD 940
Cdd:pfam02463 541 YKVAISTAVIVE------VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATL 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 941 MERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDSTDTS 1020
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 86990454 1021 VVISSCSLAEARL---LLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1065
Cdd:pfam02463 694 ILRRQLEIKKKEQrekEELKKLKLEAEELLADRVQEAQDKINEELKLL 741
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
624-862 |
3.45e-04 |
|
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: 45.55 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 624 SDPEEKEVNFQADLADLTCEIEIKQkliDELENSQRRL---QTLKHQYEEKLILLQNKIRDTQ--LERDRVLQNlstmec 698
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKE---EELQAALARLeeeTAQKNNALKKIRELEAQISELQedLESERAARN------ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 699 yteeKANKIKADYEKRLREMNRDLQKLQ---AAQKEHarllknQSRYERELKKLQAEVAEMKKAKVALMKQMRE------ 769
Cdd:pfam01576 289 ----KAEKQRRDLGEELEALKTELEDTLdttAAQQEL------RSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqal 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 770 EQQRRRLVETKRNR---EIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAK-PMSERVAGRVGLKPPNM 845
Cdd:pfam01576 359 EELTEQLEQAKRNKanlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARlSESERQRAELAEKLSKL 438
|
250
....*....|....*..
gi 86990454 846 DSGAEvSASTTSSEAES 862
Cdd:pfam01576 439 QSELE-SVSSLLNEAEG 454
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
718-828 |
3.72e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.90 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 718 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvetKRNREIAQLKKE--QRRQ 795
Cdd:COG2825 31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQ------KKERELQKKQQElqRKQQ 104
|
90 100 110
....*....|....*....|....*....|....*
gi 86990454 796 EFQiRALesQKRQQEIV--LRRKTQEvsALRRLAK 828
Cdd:COG2825 105 EAQ-QDL--QKRQQELLqpILEKIQK--AIKEVAK 134
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1544-1575 |
3.75e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.60 E-value: 3.75e-04
10 20 30
....*....|....*....|....*....|..
gi 86990454 1544 NAHKDWVCALAFVPGRPMLLSACRAGFIKVWN 1575
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
683-948 |
3.78e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 683 QLERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVA 762
Cdd:COG3064 38 EAEEERLAELEAKRQ--AEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 763 LMKQMREEQQRRRLVETKRN-----REIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGR 837
Cdd:COG3064 116 AAEKEKAEEAKRKAEEEAKRkaeeeRKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 838 VGLKPPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIDHFLGDRPTATVNGGRPARKKFQKKGASQSFSKAARLKW 917
Cdd:COG3064 196 AAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275
|
250 260 270
....*....|....*....|....*....|.
gi 86990454 918 QSLERRIIDIVMQRMTIVNLEADMERLIKKR 948
Cdd:COG3064 276 SGLVVVAAALAGLAAAAAGLVLDDSAALAAE 306
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
645-810 |
3.82e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 45.21 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 645 EIKQKLIDELENSQRRLQTL--KHQY-EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKI--KADYEKRLRemn 719
Cdd:pfam15066 318 EVLQKLKHTNRKQQMQIQDLqcSNLYlEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVIleKNDINKTLQ--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 720 rDLQKLQAAQKEHARllknQSRYERELkkLQAEVAEMKKAKVALMKQ-MREEQQRRRLVE---------TKRNREIAQLK 789
Cdd:pfam15066 395 -NLQEILANTQKHLQ----ESRKEKET--LQLELKKIKVNYVHLQERyITEMQQKNKSVSqclemdktlSKKEEEVERLQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 86990454 790 --------------------KEQRRQEFQIRALESQKRQQE 810
Cdd:pfam15066 468 qlkgelekattsaldllkreKETREQEFLSLQEEFQKHEKE 508
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1579-1615 |
4.86e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 4.86e-04
10 20 30
....*....|....*....|....*....|....*....
gi 86990454 1579 FTPIGEIKGHDSPINAIC--TNSKHIFTASSDLTVKFWS 1615
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
709-837 |
5.57e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.13 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 709 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEVAEM-KKAKVALMKQmrEEQQRRRLVETKRNRE-- 784
Cdd:pfam04012 21 EDPEKMLEQAIRDMQSeLVKARQALAQTIARQKQLERRLEQQTEQAKKLeEKAQAALTKG--NEELAREALAEKKSLEkq 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86990454 785 --------------IAQLKKEQRRQEFQIRALESQKR-----------QQEIVLRRKTQEVSALRRLAKPMSERVAGR 837
Cdd:pfam04012 99 aealetqlaqqrsaVEQLRKQLAALETKIQQLKAKKNllkarlkaakaQEAVQTSLGSLSTSSATDSFERIEEKIEER 176
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
645-829 |
6.33e-04 |
|
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: 44.72 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 645 EIKQ---KLIDELENSQRRLQTLKHQYE----------EKLILLQNK----IRDTQLERDRVLQNLSTMECyTEEKANKI 707
Cdd:pfam15921 650 DIKQerdQLLNEVKTSRNELNSLSEDYEvlkrnfrnksEEMETTTNKlkmqLKSAQSELEQTRNTLKSMEG-SDGHAMKV 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 708 KADYEKRLREMNRDLQKLQA-----------AQKEHARLLKNQSRYERELkklqAEVAEMKKAKVALMKQMReeQQRRRL 776
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSkiqfleeamtnANKEKHFLKEEKNKLSQEL----STVATEKNKMAGELEVLR--SQERRL 802
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 86990454 777 VETKRNREIAQLKKEQRRQEFQiralESQKRQQEIVLRRKTQEVSALRRLAKP 829
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQ----DIIQRQEQESVRLKLQHTLDVKELQGP 851
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
701-823 |
6.49e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 701 EEKANKIKADYEKRLREMNRDlqKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKaKValmkQMREEQQRRRLVE-T 779
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKE--ALLEAKEE---IHKLRNEFEKELRERRNELQKLEK-RL----LQKEENLDRKLELlE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 86990454 780 KRNREIAQLKK--EQRRQEFQIRALESQKRQQEivLRRKTQEVSAL 823
Cdd:PRK12704 107 KREEELEKKEKelEQKQQELEKKEEELEELIEE--QLQELERISGL 150
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1016 |
6.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 685 ERDRVLQNLSTMECYteEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQsryERELKKLQAEVAEMKKAKVALM 764
Cdd:PRK03918 146 SREKVVRQILGLDDY--ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK---EKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 765 KQMRE-EQQRRRLVETKRnrEIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSErvagrvgLKPp 843
Cdd:PRK03918 221 EELEKlEKEVKELEELKE--EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-------LKE- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 844 nmDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIdhflgdrptatvnggrparKKFQKKGASQSfSKAARLKWqsLERR 923
Cdd:PRK03918 291 --KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI-------------------NGIEERIKELE-EKEERLEE--LKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 924 iidivmqrmtIVNLEADMERLiKKREELF----LLQEALRRKREHLQAESPEE-EKGLQELAEEIEVLAANIDYINDSIT 998
Cdd:PRK03918 347 ----------LKELEKRLEEL-EERHELYeeakAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIG 415
|
330
....*....|....*...
gi 86990454 999 DCQATIVQLEETKEELDS 1016
Cdd:PRK03918 416 ELKKEIKELKKAIEELKK 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
625-828 |
7.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 625 DPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEeklillqnKIRDTQLERDRVLQnlstmecyTEEKA 704
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVAS--------AEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 705 nkikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAkvalMKQMREEQQR-RRLVETKRNR 783
Cdd:COG4913 671 ----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDElQDRLEAAEDL 742
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86990454 784 EIAQLKK--EQRRQEFQIRALESQKRQQeiVLRRKTQEVSALRRLAK 828
Cdd:COG4913 743 ARLELRAllEERFAAALGDAVERELREN--LEERIDALRARLNRAEE 787
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
702-810 |
1.17e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 702 EKANKIKADYEKRLREMNRDLQKLQAAQK--EHARLLKNQSRYERELK-------KLQAEVAEMKKAKVALMKQMREEQQ 772
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKakqaaeaKAKAEAEAERKAKEEAAKQAEEEAK 157
|
90 100 110
....*....|....*....|....*....|....*...
gi 86990454 773 RRRLVETKRNREIAQLKKEQRRQEfqiRALESQKRQQE 810
Cdd:TIGR02794 158 AKAAAEAKKKAEEAKKKAEAEAKA---KAEAEAKAKAE 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
713-843 |
1.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 713 KRLREMNRDLQKLQAAQKEHARL--LKNQSRY---ERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVEtkrnREIAQ 787
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELeyLRAALRLwfaQRRLELLEAELEELRAELARLEAELERLEARLDALR----EELDE 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 86990454 788 LKKEQRRQEFQ-IRALESQKRQQEIVLRRKTQEVSALRRLAKpmservagRVGLKPP 843
Cdd:COG4913 328 LEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLA--------ALGLPLP 376
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
712-835 |
1.52e-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: 42.22 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 712 EKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKE 791
Cdd:COG1579 23 EHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEA-RIKKYEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 86990454 792 QRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVA 835
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
645-833 |
1.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 645 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKIRDTQLERDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK 724
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR-ELETHIEEYDREFNEI-------ENASSSLGSDLAAREDALNQSLKE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 725 LQAAQKEHARLLKNqsryERELKKLQAEVAEMKKAKVALMKQmrEEQQRRRLVETkRNREIAQLKKE---QRRQEFQIRA 801
Cdd:TIGR00618 748 LMHQARTVLKARTE----AHFNNNEEVTAALQTGAELSHLAA--EIQFFNRLREE-DTHLLKTLEAEigqEIPSDEDILN 820
|
170 180 190
....*....|....*....|....*....|....*..
gi 86990454 802 LESQKRQQEI-----VLRRKTQEVSALRRLAKPMSER 833
Cdd:TIGR00618 821 LQCETLVQEEeqflsRLEEKSATLGEITHQLLKYEEC 857
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
711-816 |
1.77e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 711 YEKRLREMNRDLQKLQAAQKEharllknQSRYERELKKLQAEVAEMK-----------KAKVALMKQMREEQQRRRLVET 779
Cdd:pfam13904 57 YENWLAAKQRQRQKELQAQKE-------EREKEEQEAELRKRLAKEKyqewlqrkarqQTKKREESHKQKAAESASKSLA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 86990454 780 KRNREIAQ-----------LKKEQRRQEFQIRALESQKRQQEIVLRRK 816
Cdd:pfam13904 130 KPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
645-819 |
2.03e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 42.33 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 645 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNlstmecytEEKANKIKADYEKRLREMNRDLQK 724
Cdd:pfam15558 77 EERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQC--------QEQRLKEKEEELQALREQNSLQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 725 LQAAQKEHARLLKN-QSRYERELKKLqAEVAEMKKAKVALMKQMREEQQRRRL-VETK--RNREIAQLKKEQRRQEFQIR 800
Cdd:pfam15558 149 ERLEEACHKRQLKErEEQKKVQENNL-SELLNHQARKVLVDCQAKAEELLRRLsLEQSlqRSQENYEQLVEERHRELREK 227
|
170
....*....|....*....
gi 86990454 801 ALESQKRQQEIVLRRKTQE 819
Cdd:pfam15558 228 AQKEEEQFQRAKWRAEEKE 246
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1544-1575 |
2.40e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|..
gi 86990454 1544 NAHKDWVCALAFVPGRPMLLSACRAGFIKVWN 1575
Cdd:pfam00400 8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
718-820 |
2.45e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 718 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQqrrrlvETKRNREIAQLKKEQRRQeF 797
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA------REKKEKELQKKVQEFQRK-Q 78
|
90 100
....*....|....*....|....*
gi 86990454 798 QIRALESQKRQQEIV--LRRKTQEV 820
Cdd:smart00935 79 QKLQQDLQKRQQEELqkILDKINKA 103
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
645-774 |
2.48e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 645 EIKQKLIDELENSQRRLQTLKH-QYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA---NKIKADYEKRLRE-MN 719
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghlTNLRAERRKQLEEiLE 708
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 86990454 720 RDLQKLQAAQKEH----ARLLKNQSRYerelKKLQAEVAEMKKAKVALMKQMREEQQRR 774
Cdd:pfam10174 709 MKQEALLAAISEKdaniALLELSSSKK----KKTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
616-825 |
2.58e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 616 EESLVDSDSDPEEKE---VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLK-------HQYEEKLILLQNKIRDTQLE 685
Cdd:pfam01576 74 EEILHELESRLEEEEersQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteakiKKLEEDILLLEDQNSKLSKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 686 RDRVLQNLSTMECY---TEEKA---NKIK-------ADYEKRLREMNRDLQKLQAA-----------QKEHARL------ 735
Cdd:pfam01576 154 RKLLEERISEFTSNlaeEEEKAkslSKLKnkheamiSDLEERLKKEEKGRQELEKAkrklegestdlQEQIAELqaqiae 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 736 LKNQ-SRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKRNREIAQLKKEQRRQEF--QIRAL--------E 803
Cdd:pfam01576 234 LRAQlAKKEEELQAALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAEKQRRDLgeELEALkteledtlD 313
|
250 260
....*....|....*....|..
gi 86990454 804 SQKRQQEIVLRRKtQEVSALRR 825
Cdd:pfam01576 314 TTAAQQELRSKRE-QEVTELKK 334
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1445-1485 |
2.63e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 36.91 E-value: 2.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 86990454 1445 FQPIGKLTGHIGPVMCLTVtqtSNQHDLVVTGSKDHYVKMF 1485
Cdd:smart00320 2 GELLKTLKGHTGPVTSVAF---SPDGKYLASGSDDGTIKLW 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
653-1017 |
2.79e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 653 ELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKaDYEKRLREMNRDLQKLQAAQKEH 732
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 733 ARLLKNQSRYERELKKLQAEVAEMKKAKVALMK-QMREEQQRRRLVETKRNREIAQLKKEQrrqefqiralesQKRQQEi 811
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEK------------QEKQHE- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 812 vLRRKTQEVSALRRLAKPMSERVAgrvGLKPPNMDSGAE-VSASTTSSEA---ESGARSVSSIVRQWNRKI-DHFLGDRP 886
Cdd:TIGR00606 838 -LDTVVSKIELNRKLIQDQQEQIQ---HLKSKTNELKSEkLQIGTNLQRRqqfEEQLVELSTEVQSLIREIkDAKEQDSP 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 887 TATvnggrpARKKFQKK-----GASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLlqealrrk 961
Cdd:TIGR00606 914 LET------FLEKDQQEkeeliSSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETEL-------- 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 86990454 962 rEHLQAESPEEEKGLQELAEEIEVLAANID--YINDSITDCQATIVQLEETKEELDST 1017
Cdd:TIGR00606 980 -NTVNAQLEECEKHQEKINEDMRLMRQDIDtqKIQERWLQDNLTLRKRENELKEVEEE 1036
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1445-1485 |
2.98e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 2.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 86990454 1445 FQPIGKLTGHIGPVMCLTVtqtSNQHDLVVTGSKDHYVKMF 1485
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAF---SPDGKLLASGSDDGTVKVW 38
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
728-820 |
3.64e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 728 AQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR---EIAQLKKEQRRQEFQIRALES 804
Cdd:pfam20492 4 AEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEaeeEKERLEESAEMEAEEKEQLEA 83
|
90
....*....|....*.
gi 86990454 805 QKRQQEIVLRRKTQEV 820
Cdd:pfam20492 84 ELAEAQEEIARLEEEV 99
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
768-1066 |
3.78e-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: 41.98 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 768 REEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSA---LRRLAKPMSERVAGRVGLkppn 844
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGyelLKEKEALERQKEAIERQL---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 845 mdSGAEVSASTTSSEAESGARSVSSIVR---QWNRKIDHFLGDRPTAtvnggrparkkFQKKGASQSfSKAARLkwqsle 921
Cdd:TIGR02169 247 --ASLEEELEKLTEEISELEKRLEEIEQlleELNKKIKDLGEEEQLR-----------VKEKIGELE-AEIASL------ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 922 RRIIDIVMQRM-----TIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDS 996
Cdd:TIGR02169 307 ERSIAEKERELedaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86990454 997 ITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQ----KEAQIRLLEGRLRQT 1066
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEekedKALEIKKQEWKLEQL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
379-576 |
4.08e-03 |
|
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: 41.29 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 379 QDKTSQQISALRAEIARLQMELMEYKAGKRvigedgtegysDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLms 458
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEK-----------ALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 459 qeanlllakagdgneaigaliqnyIREIEELRTKLLESEAMNESLRRSLSRASARNPYSLGASPAGPAFGGSPATSMEDA 538
Cdd:COG4942 89 ------------------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 86990454 539 SEVIRKA----KQDLERLKKKEVRQRRKSPEKEAFKKRAKLQ 576
Cdd:COG4942 145 APARREQaeelRADLAELAALRAELEAERAELEALLAELEEE 186
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
723-809 |
4.08e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 40.30 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 723 QKLQAAQKEHARL-LKN---QSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRR--------------------LVE 778
Cdd:pfam06391 68 KKIEQYEKENKDLiLKNkmkLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKekakqelidelmtsnkdaeeIIA 147
|
90 100 110
....*....|....*....|....*....|.
gi 86990454 779 TKRNReIAQLKKEQRRQEFQIRALESQKRQQ 809
Cdd:pfam06391 148 QHKKT-AKKRKSERRRKLEELNRVLEQKPTQ 177
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
703-815 |
4.13e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 38.80 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 703 KANKIKADYEKRLREMNRDLQKLQAAQKEH-----ARLLKNQSRY----ERELKKLQAEVAEMKKAKVALMKQMREEQQR 773
Cdd:pfam02050 9 EAQRELQQAEEKLEELQQYRAEYQQQLSGAgqgisAAELRNYQAFisqlDEAIAQQQQELAQAEAQVEKAREEWQEARQE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 86990454 774 RRLVETKRNREIAQLKKEQRRQEfqiralesQKRQQEIVLRR 815
Cdd:pfam02050 89 RKSLEKLREREKKEERKEQNRRE--------QKQLDELAARL 122
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
536-825 |
4.44e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 536 EDASEVIRKAKQDLERLKKKE-----VRQRRKSPEKEAFKKRAKLQAENSEETDENEAEEEEEERDESGCEEEEGREDED 610
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEepsgqVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 611 EDSGSEESLVDSDSDPEEKEVNFQADLADLT---------CEIEIKQKLIDELENSQRRLQTLKHQYEEKLillqNKIRD 681
Cdd:pfam02029 86 QKEFDPTIADEKESVAERKENNEEEENSSWEkeekrdsrlGRYKEEETEIREKEYQENKWSTEVRQAEEEG----EEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 682 TQLERDRVLQNLSTMECYTEEKANKIKADYEKRL----REMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEmk 757
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKvfldQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE-- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86990454 758 kAKVALMKQMREEQQRRRLVEtKRNREIAQLKkeQRRQEFQIRALESQKRQQEivlRRKTQEVSALRR 825
Cdd:pfam02029 240 -AEVFLEAEQKLEELRRRRQE-KESEEFEKLR--QKQQEAELELEELKKKREE---RRKLLEEEEQRR 300
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
535-809 |
4.83e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 535 MEDASEVIRKAKQDLER-LKKKEVRQRRKSPEKEAFKKRAKLQAENSEETDENEAEEEEEerdesgceeeegredededs 613
Cdd:pfam13868 39 KEEERRLDEMMEEERERaLEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ-------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 614 gsEESLVDSDSDPEEKEvnfqaDLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLqnl 693
Cdd:pfam13868 99 --EREQMDEIVERIQEE-----DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAERE--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 694 stmecytEEKANKIKADYEKRLREMNRDLQKLQAAQKEHA-----RLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMR 768
Cdd:pfam13868 169 -------EEREAEREEIEEEKEREIARLRAQQEKAQDEKAerdelRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 86990454 769 EEQ----QRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQ 809
Cdd:pfam13868 242 EEQielkERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM 286
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
633-798 |
6.12e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.12 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 633 FQADLADLTCEIE----IKQKLIDEL----ENSQRRLQTLKHQYEEKLILLQNkiRDTQLERDRVLQNLST----MECYT 700
Cdd:cd00176 45 LEAELAAHEERVEalneLGEQLIEEGhpdaEEIQERLEELNQRWEELRELAEE--RRQRLEEALDLQQFFRdaddLEQWL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 701 EEKANKIKADyekrlrEMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALmkqmREEQQRRRLVETK 780
Cdd:cd00176 123 EEKEAALASE------DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD----ADEEIEEKLEELN 192
|
170
....*....|....*...
gi 86990454 781 RNREIAQLKKEQRRQEFQ 798
Cdd:cd00176 193 ERWEELLELAEERQKKLE 210
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
647-873 |
6.53e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 647 KQKLIDELENSQRRLQT----LKHQYEEKLILlqNKIRDTQLERDRVLQNLSTMECYTEEKANKIKA------------- 709
Cdd:PTZ00108 997 KEYLLGKLERELARLSNkvrfIKHVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAeeeegaeeddead 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 710 ------------DYEKRLR--------EMNRDLQK-LQAAQKEHARLLKN--QSRYERELKKLQAEVAEMKKAKVALMKQ 766
Cdd:PTZ00108 1075 deddeeelgaavSYDYLLSmpiwsltkEKVEKLNAeLEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAK 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 767 MREEQQRRRLVETKRNREIAQLKKEQRRQefqirALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMD 846
Cdd:PTZ00108 1155 EQRLKSKTKGKASKLRKPKLKKKEKKKKK-----SSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDE 1229
|
250 260
....*....|....*....|....*..
gi 86990454 847 SGAEVSASTTSSEAESGARSVSSIVRQ 873
Cdd:PTZ00108 1230 EQKTKPKKSSVKRLKSKKNNSSKSSED 1256
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
652-823 |
6.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 652 DELENSQRRLQ-TLKHQYEEklILLQNKirDTQLER-DRVLQNLS-TME---------------CYTEEKaNKIKADYEK 713
Cdd:cd16269 86 DEDQKFQKKLMeQLEEKKEE--FCKQNE--EASSKRcQALLQELSaPLEekisqgsysvpggyqLYLEDR-EKLVEKYRQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 714 RLR---EMNRDLQK-LQAAQKEHARLLK-NQSRYERELKKLqaevAEMKKAKVALMKQMREEQQRRRLVETKRNRE---- 784
Cdd:cd16269 161 VPRkgvKAEEVLQEfLQSKEAEAEAILQaDQALTEKEKEIE----AERAKAEAAEQERKLLEEQQRELEQKLEDQErsye 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 86990454 785 --IAQLKKE-----QRRQEFQIRALESQKRQQEIVLRRKTQEVSAL 823
Cdd:cd16269 237 ehLRQLKEKmeeerENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
304-561 |
6.91e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 304 LGNVISALgDQSKKVVHVPYRDSKLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQ 379
Cdd:COG3206 96 LERVVDKL-NLDEDPLGEEASREAAIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 380 DKTS---QQISALRAEIARLQMELMEYKAGKRVIgeDGTEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQL 456
Cdd:COG3206 175 KALEfleEQLPELRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 457 MSQEANLLlakagdGNEAIGALIQNYI---REIEELRTKLLES-------EAMNESLRRSLSRASARNPYSLGASPAGpa 526
Cdd:COG3206 253 PDALPELL------QSPVIQQLRAQLAeleAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRILASLEAELEA-- 324
|
250 260 270
....*....|....*....|....*....|....*.
gi 86990454 527 fggspATSMEDA-SEVIRKAKQDLERLKKKEVRQRR 561
Cdd:COG3206 325 -----LQAREASlQAQLAQLEARLAELPELEAELRR 355
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-820 |
8.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 381 KTSQQISALRAEIARLQMELMEYKAGKRVIGEdgTEGYSDLFRENAM--LQKENGALRLRVKAMQEAIDAINNRVTQLMS 458
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYEEAKAKKEE--LERLKKRLTGLTPekLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 459 QEANLLLA----KAGDG----------NEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRA-SARNpyslgaspa 523
Cdd:PRK03918 420 EIKELKKAieelKKAKGkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELeKVLK--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 524 gpafGGSPATSMEDASEVIRKAKQDLERLKKKEVRqrRKSPEKEAFKKRA-KLQAENSEETDENEaeeeeeerdesgcee 602
Cdd:PRK03918 491 ----KESELIKLKELAEQLKELEEKLKKYNLEELE--KKAEEYEKLKEKLiKLKGEIKSLKKELE--------------- 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 603 eegredededsgSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQ-KLIDELEnsqRRLQTLKHQYEEKLIL------- 674
Cdd:PRK03918 550 ------------KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELE---ERLKELEPFYNEYLELkdaekel 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 675 --LQNKIRDTQLERDRVLQNLSTME---------------CYTEEKANKIkadyEKRLREMNRDLQKLQAAQKEHARLLK 737
Cdd:PRK03918 615 erEEKELKKLEEELDKAFEELAETEkrleelrkeleelekKYSEEEYEEL----REEYLELSRELAGLRAELEELEKRRE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 738 NqsrYERELKKLQAEVAEMKKAK--VALMKQMREEQQRRRlvetKRNREIAQLKKEQRRQEFQIRALE-----SQKRQQE 810
Cdd:PRK03918 691 E---IKKTLEKLKEELEEREKAKkeLEKLEKALERVEELR----EKVKKYKALLKERALSKVGEIASEifeelTEGKYSG 763
|
490
....*....|
gi 86990454 811 IVLRRKTQEV 820
Cdd:PRK03918 764 VRVKAEENKV 773
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
643-811 |
9.92e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 643 EIEIKQKLIDELENSQRRLQTLKHQYEEklilLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKAdyEKRLREMNRD- 721
Cdd:pfam05667 326 EEELQQQREEELEELQEQLEDLESSIQE----LEKEIKKLESSIKQVEEELEELKEQNEELEKQYKV--KKKTLDLLPDa 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86990454 722 ---LQKLQAAQKEHA-RLLKNQSRYE----------RELKKLQAEVAEMKKAKVALMKQMRE------------EQQRRR 775
Cdd:pfam05667 400 eenIAKLQALVDASAqRLVELAGQWEkhrvplieeyRALKEAKSNKEDESQRKLEEIKELREkikevaeeakqkEELYKQ 479
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 86990454 776 LVEtkrnrEIAQLKKEQRRQEFQIRALES----QKRQQEI 811
Cdd:pfam05667 480 LVA-----EYERLPKDVSRSAYTRRILEIvkniKKQKEEI 514
|
|
| |
