|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
1-89 |
7.30e-41 |
|
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: 154.47 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1 MKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSK-VQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETL 79
Cdd:cd01368 256 SRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETL 335
|
90
....*....|
gi 569007265 80 NVLKFSTTAQ 89
Cdd:cd01368 336 HVMKFSAIAQ 345
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
2-89 |
5.45e-29 |
|
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: 119.60 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:smart00129 241 KTGAEGDRLKEAGNINKSLSALGNVINAL--AQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLST 318
|
....*...
gi 569007265 82 LKFSTTAQ 89
Cdd:smart00129 319 LRFASRAK 326
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
2-91 |
9.37e-27 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 112.67 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQN-EGERLREAGNINTSLLTLGKCINVLknSEKSKvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLN 80
Cdd:pfam00225 239 KTGAaGGQRLKEAANINKSLSALGNVISAL--ADKKS-KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLS 315
|
90
....*....|.
gi 569007265 81 VLKFSTTAQRV 91
Cdd:pfam00225 316 TLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
2-89 |
3.68e-25 |
|
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: 108.11 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd00106 242 KTGAEGDRLKEGGNINKSLSALGKVISAL--ADGQNK-HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLST 318
|
....*...
gi 569007265 82 LKFSTTAQ 89
Cdd:cd00106 319 LRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
2-88 |
3.53e-20 |
|
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: 93.56 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSeKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01370 257 ATNNRGQRLKEGANINRSLLALGNCINALADP-GKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNT 335
|
....*..
gi 569007265 82 LKFSTTA 88
Cdd:cd01370 336 LKYANRA 342
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
2-91 |
7.97e-19 |
|
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: 89.31 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01374 234 QTGAAGVRRKEGSHINKSLLTLGTVISKL--SEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
90
....*....|
gi 569007265 82 LKFSTTAQRV 91
Cdd:cd01374 312 LKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
2-91 |
9.80e-19 |
|
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: 89.19 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNseksKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01366 242 KSGATGDRLKETQAINKSLSALGDVISALRQ----KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
90
....*....|
gi 569007265 82 LKFsttAQRV 91
Cdd:cd01366 318 LRF---ASKV 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-1073 |
1.09e-18 |
|
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: 92.81 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 287 VEDIFHSLQDDVTDIKKQAELA---------------HLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEEL- 350
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAerykelkaelrelelALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLe 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 351 -KNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLIL--VSPPITEEQ 427
Cdd:TIGR02168 271 eLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeLEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 428 NKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASY 507
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 508 -NSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQ-MQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKG 585
Cdd:TIGR02168 431 eEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQaLDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 586 dncLNTSQQLPGGDFSSTWvkeyhtQEISRENSFHASIE-AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKgyreE 664
Cdd:TIGR02168 511 ---LLKNQSGLSGILGVLS------ELISVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFL----P 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 665 NSDLRAQESQGKNRdhQLKEKESLIQQLREELQEKSVSLRV-------QVQLVAEREQALSELSQDVTCYKAKIKDLEVI 737
Cdd:TIGR02168 578 LDSIKGTEIQGNDR--EILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 738 ----VETQKDEckrlvELEQSILEKESAILKLEANLKECEAK-HQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQS 812
Cdd:TIGR02168 656 rpggVITGGSA-----KTNSSILERRREIEELEEKIEELEEKiAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 813 KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVM--------------RD 878
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeelkalrealdelRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 879 EEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK---------MEEAVQQYEKVCKDLSVKEKLVEDMRLTLV 949
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedieslaaeIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 950 EQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSnQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKK 1029
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL-EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 569007265 1030 WLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLT 1073
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
212-266 |
3.16e-18 |
|
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409644 [Multi-domain] Cd Length: 56 Bit Score: 79.45 E-value: 3.16e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569007265 212 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 266
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
2-90 |
2.55e-17 |
|
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: 85.08 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLkNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01372 252 RTGATGDRLKEGISINSGLLALGNVISAL-GDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNT 330
|
....*....
gi 569007265 82 LKFsttAQR 90
Cdd:cd01372 331 LKY---ANR 336
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
5-88 |
2.65e-16 |
|
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: 82.37 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 5 NEGERLREAGNINTSLLTLGKCINVLknSEKSKvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKF 84
Cdd:cd01364 262 AVDKRAREAGNINQSLLTLGRVITAL--VERAP--HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEY 337
|
....
gi 569007265 85 STTA 88
Cdd:cd01364 338 AHRA 341
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
2-91 |
3.47e-16 |
|
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: 82.02 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVL----KNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDE 77
Cdd:cd01365 261 STGATGDRLKEGANINKSLTTLGKVISALadmsSGKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEE 340
|
90
....*....|....
gi 569007265 78 TLNVLKFSTTAQRV 91
Cdd:cd01365 341 TLSTLRYADRAKKI 354
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
2-91 |
5.03e-15 |
|
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: 77.89 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSeksKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01371 248 KTGATGERLKEATKINLSLSALGNVISALVDG---KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLST 324
|
90
....*....|
gi 569007265 82 LKFSTTAQRV 91
Cdd:cd01371 325 LRYANRAKNI 334
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
2-257 |
1.08e-14 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 79.01 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINAL--GDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINT 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 82 LKFSTTAQR----VYVPDTLSSSQ---EKSFASNKSLQDVSLDSNLDNKILNVKRKTVSWENSLEDVLENEDL--VEDLE 152
Cdd:COG5059 327 LKFASRAKSiknkIQVNSSSDSSReieEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLksRIDLI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 153 ENEETQNMETELTDEdsdKSLEECRVSTCHK----KNKELLDLIEKLNKRLINENK-EKLTLELKIREEV---TQEFTQY 224
Cdd:COG5059 407 MKSIISGTFERKKLL---KEEGWKYKSTLQFlrieIDRLLLLREEELSKKKTKIHKlNKLRHDLSSLLSSipeETSDRVE 483
|
250 260 270
....*....|....*....|....*....|...
gi 569007265 225 WSQREaDFKETLLHereILEENAERRLAIFKDL 257
Cdd:COG5059 484 SEKAS-KLRSSAST---KLNLRSSRSHSKFRDH 512
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
3-91 |
4.68e-14 |
|
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: 75.24 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 3 TQNEGERLREAGNINTSLLTLGKCINVLKNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVL 82
Cdd:cd01373 249 THAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTL 328
|
....*....
gi 569007265 83 KFsttAQRV 91
Cdd:cd01373 329 RF---AQRA 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
2-84 |
6.96e-14 |
|
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: 74.46 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01376 236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLST 311
|
...
gi 569007265 82 LKF 84
Cdd:cd01376 312 LNF 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-1093 |
8.66e-14 |
|
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: 76.63 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 447 LKEKNEELKRLLTIGE-----NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVN 521
Cdd:TIGR02168 218 LKAELRELELALLVLRleelrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 522 QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGAKGdNCLNTSQQLpggdfs 601
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE----------ELAELEEKLEELKE-ELESLEAEL------ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 602 stwvKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGK 676
Cdd:TIGR02168 361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 677 NRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiL 756
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-Q 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 757 EKESAILKLEANLKECEAKHQ-----------------------------------------------DHIRTNDLSAKE 789
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 790 ------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSILtq 839
Cdd:TIGR02168 596 niegflgvakdlVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSIL-- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 840 NLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK 919
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 920 MEEAVQQYEKVckdlsVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTM 999
Cdd:TIGR02168 754 KELTELEAEIE-----ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1000 ---------DDLDVLTRKFSKLQ----------DELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRE 1060
Cdd:TIGR02168 829 lerriaateRRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750
....*....|....*....|....*....|...
gi 569007265 1061 RCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1093
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-945 |
1.11e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 141 VLENEDLVEDLEENEETQN-METELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIREEvtq 219
Cdd:TIGR02168 231 VLRLEELREELEELQEELKeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 220 eftqywSQREADFKETLLHEREILEENAERRlaifkdlvgkcdsqdeptnricdIELETEEAHnyvgVEDIFHSLQDDVT 299
Cdd:TIGR02168 308 ------RERLANLERQLEELEAQLEELESKL-----------------------DELAEELAE----LEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 300 DIKKQAElahlyitslvdpqeaiaclqlKFNQVKAELaetkEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTC 379
Cdd:TIGR02168 355 SLEAELE---------------------ELEAELEEL----ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 380 NETSEMPKNSRAQTHSERKRLNEDGLQlgeppakkglilvsppitEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLT 459
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELK------------------ELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 460 IGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRA--DVEQIQASYNSAVAEL-----QTQKAVNQEQRDRILKLS 532
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 533 QEMETAARSIESNVSQIKQMQTKIDELRSLdSPSHISKIDLLNLQDLSSGAK-GDNCLNTSQQLPG--GDFSST--WVKE 607
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFLPLDSI-KGTEIQGNDREILKNIEGFLGvAKDLVKFDPKLRKalSYLLGGvlVVDD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 608 YHT-QEISRENSFHASI----EAIWEECKEIVKASSKKSHQIQG-------LEEQIEKLQVEVKGYREENSDLRAQESQG 675
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIvtldGDLVRPGGVITGGSAKTNSSILErrreieeLEEKIEELEEKIAELEKALAELRKELEEL 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 676 KNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKR-LVELEQS 754
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 755 ILEKESAILKLEANLKECEAKHQdhirtnDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAN 834
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELT------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 835 SILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 914
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830
....*....|....*....|....*....|....
gi 569007265 915 LSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMR 945
Cdd:TIGR02168 945 LSEEyslTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-1122 |
1.11e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 447 LKEKNEELKRL-LTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQR 525
Cdd:TIGR02168 215 YKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 526 DRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSSGAKGDNCLNTSQQLPGGdfsstwV 605
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELES--------KLDELAEELAELEEKLEELKEELESLEAE------L 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 606 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGKNRDH 680
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 681 QLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiLEKES 760
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 761 AILKLEANLKECEAK-----------HQDHIRTNDLSA--KEVKFREE-----VTRLANNLHDTKQLLQSKEEENE---- 818
Cdd:TIGR02168 520 GILGVLSELISVDEGyeaaieaalggRLQAVVVENLNAakKAIAFLKQnelgrVTFLPLDSIKGTEIQGNDREILKnieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 819 ----ISRQETEKLKEELAANSILTQNLKAD-LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL------LRIKI 887
Cdd:TIGR02168 600 flgvAKDLVKFDPKLRKALSYLLGGVLVVDdLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssileRRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 888 NELEKKKNQYSQDLDMKQRTIQQLKEQLSN---------QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQ 958
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 959 DRVLEAKSEEADWLATELDKWKEKFKDLETRSNQrlntgTMDDLDVLTRKFSKLQDELQESEEKYKADRkkwlEEKAVLT 1038
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-----LKEELKALREALDELRAELTLLNEEAANLR----ERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1039 TQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALLSSCKHKDEEIQEL 1118
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELEELSEELREL 906
|
....
gi 569007265 1119 RKAA 1122
Cdd:TIGR02168 907 ESKR 910
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
821-1093 |
4.11e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 821 RQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQrevsvmrDEEKLLRIKINELEKKKNQYSQD 900
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 901 LDMKQRTIQQLKEQLS--NQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQtqaeqdRVLEAKSEEADWLATELDK 978
Cdd:COG1196 311 RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 979 WKEKFKDLETRSNQRlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADD 1058
Cdd:COG1196 385 AEELLEALRAAAELA-----------------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*
gi 569007265 1059 RERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1093
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
620-1124 |
1.26e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 620 HASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 699
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 700 SVSLRVQVQLVAEREQALSELSQDVtcyKAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKLEANLKECEAKHQDH 779
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 780 IRtndlsaKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKF 859
Cdd:COG1196 392 LR------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 860 IDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEK 939
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 940 LVEDMRLTLVEQEQTQAEQDRVLEAKSEEAdwlATELDKWKEKFKDLETRSNQRLntgtmddldVLTRKFSKLQDELQES 1019
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGR---ATFLPLDKIRARAALAAALARG---------AIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1020 EEKYKAdrkkwLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVET 1099
Cdd:COG1196 612 DARYYV-----LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500
....*....|....*....|....*
gi 569007265 1100 QMKALLSSCKHKDEEIQELRKAAAK 1124
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAE 711
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
2-85 |
3.75e-12 |
|
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: 69.25 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQ-SFFTGKGKICMIINISQSCSAYDETLN 80
Cdd:cd01367 244 TSSADRQTRMEGAEINKSLLALKECIRALGQNKA----HIPFRGSKLTQVLKdSFIGENSKTCMIATISPGASSCEHTLN 319
|
....*
gi 569007265 81 VLKFS 85
Cdd:cd01367 320 TLRYA 324
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
2-91 |
2.18e-11 |
|
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: 66.97 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSkvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01369 239 KTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT---HIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
90
....*....|
gi 569007265 82 LKFSTTAQRV 91
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
7-91 |
2.48e-11 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 68.81 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 7 GERLREAGNINTSLLTLGKCINVLKN-SEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFS 85
Cdd:PLN03188 349 GDRLKEAGNINRSLSQLGNLINILAEiSQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFA 428
|
....*.
gi 569007265 86 TTAQRV 91
Cdd:PLN03188 429 QRAKAI 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
423-766 |
8.16e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 423 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 502
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 503 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRsldspshiSKIDLLN--LQDLS 580
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTLLNeeAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 581 SGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRE--NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEV 658
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 659 KGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK-----SVSLRVQVQLVAEREQALSELSQDVTCYKAKIKD 733
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350
....*....|....*....|....*....|....*..
gi 569007265 734 LEVI----VETQKDECKRLVELEQSILEKESAILKLE 766
Cdd:TIGR02168 984 LGPVnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
212-266 |
1.11e-10 |
|
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; This family includes kinesin-like proteins KIF20A and KIF20B. KIF20A (also called GG10_2, mitotic kinesin-like protein 2 (MKlp2), Rab6-interacting kinesin-like protein, or rabkinesin-6) is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1 (polo-like kinase 1), it is involved in recruitment of PLK1 to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus-end-directed motility. KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargoes. It participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. This model corresponds to a conserved domain in the KIF20A subfamily, that shows RAB6 binding ability and has been called the RAB6 binding domain (RBD). KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409643 [Multi-domain] Cd Length: 56 Bit Score: 58.23 E-value: 1.11e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569007265 212 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 266
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
612-968 |
1.99e-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: 65.86 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 612 EISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEvKGYREENSDLRA--QESQGKNRDHQLKEKESLI 689
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKekREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 690 QQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdecKRLVELEQSILEKESAILKLEANL 769
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---------EEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 770 KECEAKHQDhirtndLSAKEVKFREEvtrlannLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKE 849
Cdd:TIGR02169 311 AEKERELED------AEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 850 EDCAELKEKFIDAKKQIEQVQREV-SVMRDEEKL-------------LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQL 915
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREInELKRELDRLqeelqrlseeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 569007265 916 SN--QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE-QTQAEQDRVLEAKSEE 968
Cdd:TIGR02169 458 EQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
610-1121 |
2.80e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 610 TQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKG-------YREENSDLRAQ-ESQGKNRDHQ 681
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereeLAEEVRDLRERlEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 682 LKEKE------SLIQQLREELQEKSVSLRvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlvELEQSI 755
Cdd:PRK02224 299 LAEAGlddadaEAVEARREELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA---ELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 756 LEKESAILKLEANLKECEakhqdhirtndlsakevkfrEEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAans 835
Cdd:PRK02224 373 EEAREAVEDRREEIEELE--------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 836 iltqNLKADLQKKEEDCAElKEKFIDAKK---------------QIEQVQREVSVMRDEEKLLRIKINELEKKKNQySQD 900
Cdd:PRK02224 430 ----ELEATLRTARERVEE-AEALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 901 LDMKQRTIQQLKEQLSNqkmeeavqqyekVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWK 980
Cdd:PRK02224 504 LVEAEDRIERLEERRED------------LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 981 EKFKDLETRSNQrlNTGTMDDLDvltrKFSKLQDELQESEEKYKADRKKwLEEKAVLTTQAKE---AENVRNREMRKYAD 1057
Cdd:PRK02224 572 EEVAELNSKLAE--LKERIESLE----RIRTLLAAIADAEDEIERLREK-REALAELNDERRErlaEKRERKRELEAEFD 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 1058 DrERCLKLQNEVETLTAQLAEKNSELQKWREERDQL---VTAVETQMKALlssckhkdEEIQELRKA 1121
Cdd:PRK02224 645 E-ARIEEAREDKERAEEYLEQVEEKLDELREERDDLqaeIGAVENELEEL--------EELRERREA 702
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
748-1123 |
3.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 748 LVELEQSI--LEKESAI----LKLEANLKECEAKHQdHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISR 821
Cdd:COG1196 195 LGELERQLepLERQAEKaeryRELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 822 QETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL 901
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 902 DMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKE 981
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAE-----EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 982 KFKDLEtrsnqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRER 1061
Cdd:COG1196 429 ALAELE-----------------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007265 1062 CLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAA 1123
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
2-91 |
9.30e-10 |
|
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: 61.83 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01375 250 KTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKDR-THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLST 326
|
90
....*....|
gi 569007265 82 LKFsttAQRV 91
Cdd:cd01375 327 LRF---ASRV 333
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
392-1099 |
1.09e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 392 QTHSERKRLNEDGlQLGEppakKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEE 471
Cdd:pfam15921 86 QVKDLQRRLNESN-ELHE----KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 472 KAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAelqtQKAVNQEQRDRI--LKLSQEMETAARSIESNVSQI 549
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG----KKIYEHDSMSTMhfRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 550 KQMQTKI-DELRSLDSPSHiSKIDLLNLQDLSsgakgdnclNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWE 628
Cdd:pfam15921 237 KGRIFPVeDQLEALKSESQ-NKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 629 ECKeivKASSKKSHQIQGLEEQIEKLQVEVKG----YREENSDLRAQ--------ESQGKNRDHQLKEKESLIQQLREEL 696
Cdd:pfam15921 307 QAR---NQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEELEKQlvlanselTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 697 -----QEKSVSL-RVQVQLVAEREQA----LSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLE 766
Cdd:pfam15921 384 adlhkREKELSLeKEQNKRLWDRDTGnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 767 ANLKECEAKHQDHIR--TNDLSAKEVKFREEvtrlANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKAD 844
Cdd:pfam15921 464 SSLTAQLESTKEMLRkvVEELTAKKMTLESS----ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 845 ---LQKKEEDCAELKEKFIDAKKQIEqvqrevsvmrdeekLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKME 921
Cdd:pfam15921 540 gdhLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 922 EAVQQYEKVCKDLSVK--EKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrsnqrlntgtm 999
Cdd:pfam15921 606 LQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS------------ 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1000 DDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREM-------RKYADDRERCLKLQNEVETL 1072
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQIDALQSKIQFL 753
|
730 740
....*....|....*....|....*..
gi 569007265 1073 TAQLAEKNSELQKWREERDQLVTAVET 1099
Cdd:pfam15921 754 EEAMTNANKEKHFLKEEKNKLSQELST 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
683-923 |
1.93e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 683 KEKESLIQQLRE---ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdeckRLVELEQSILEKE 759
Cdd:TIGR02169 688 RELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE----------DLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 760 SAILKLEANLKECEAK-------------HQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEK 826
Cdd:TIGR02169 758 SELKELEARIEELEEDlhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 827 LKEELaansILTQNLKADLQKKEEDC----AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLD 902
Cdd:TIGR02169 838 LQEQR----IDLKEQIKSIEKEIENLngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260
....*....|....*....|.
gi 569007265 903 MKQRTIQQLKEQLSNQKMEEA 923
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELS 934
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
739-1166 |
4.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 739 ETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTND--LSAKEVKFREEVTRLANNLHDTKQLLQSKEEE 816
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 817 NEisRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLlriKINELEKKKNQ 896
Cdd:PTZ00121 1328 KK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 897 YsqdldmKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATEL 976
Cdd:PTZ00121 1403 D------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 977 DKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKfSKLQDELQESEEKYKADRKKWLEEK-----AVLTTQAKEAENVRNRE 1051
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1052 MRKYADDRERCLKLQNEVETLTAQLaEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEE----IQELRKAAAKSTG 1127
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMAL-RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKK 1634
|
410 420 430
....*....|....*....|....*....|....*....
gi 569007265 1128 TENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAED 1166
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
606-1124 |
5.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 606 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEK 685
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 686 ESLIQQLREELQEKSVSLRV------QVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKE 759
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 760 SAILKLEANLKECEAK----HQDHIRTNDLSAKEVKFREEVTRLAN-NLHDTKQLLQSKEEENEISRQETEKLKEELAAN 834
Cdd:PRK03918 338 ERLEELKKKLKELEKRleelEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 835 SILTQNLKADLQK---------------KEEDCAELKEKFidaKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ 899
Cdd:PRK03918 418 KKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 900 DLDMKQ--RTIQQLKEQLSN---QKMEEAVQQYEKVCKD---LSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 971
Cdd:PRK03918 495 LIKLKElaEQLKELEEKLKKynlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 972 LATEL--------DKWKEKFKDLETRSNQRLN-TGTMDDLDVLTRKFSKLQDELQESEEKYkADRKKWLEEkavLTTQAK 1042
Cdd:PRK03918 575 LLKELeelgfesvEELEERLKELEPFYNEYLElKDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEE---LRKELE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1043 EAENVRNREmrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLvtavetqmKALLSSCKHKDEEIQELRKAA 1122
Cdd:PRK03918 651 ELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL--------KEELEEREKAKKELEKLEKAL 720
|
..
gi 569007265 1123 AK 1124
Cdd:PRK03918 721 ER 722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-1043 |
6.14e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 432 EMQQSVSEVVEGNRVLKEKNEELKRLltiGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAV 511
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 512 AELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSSGAKGDNCLNT 591
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 592 SQQLpggdfsstwvkeyhTQEISRensFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ 671
Cdd:TIGR02169 415 LQRL--------------SEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 672 ESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAK-IKDLE---------VIVETQ 741
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEvaagnrlnnVVVEDD 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 742 KDECK---------------------RLVELEQSILEKESAILKLeANLKECEAKHQ--------DHIRTNDL-SAKE-- 789
Cdd:TIGR02169 558 AVAKEaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFA-VDLVEFDPKYEpafkyvfgDTLVVEDIeAARRlm 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 790 ---------------------------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSI 836
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 837 LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL------------DMK 904
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlshsriPEI 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 905 QRTIQQLKEQLSnqKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQ-----EQTQAEQDRVLEAKSEEADwLATELDKW 979
Cdd:TIGR02169 797 QAELSKLEEEVS--RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkEQIKSIEKEIENLNGKKEE-LEEELEEL 873
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007265 980 KEKFKDLETRSnqrlnTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKE 1043
Cdd:TIGR02169 874 EAALRDLESRL-----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
183-1071 |
6.69e-09 |
|
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: 60.76 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 183 KKNKELLDLIEKLNKRLINENKEKLTLE-LKIREEVTQEFTQYWSQ-READFKETLLHEREILEENAERRLAIFKDLVgk 260
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQ-- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 261 cdSQDEPTNRICDIELETEEAHNYVGVEDIfhslqddvTDIKKQAELAHLYITSLVDPQEAIACLQLKFNQVKAELAETK 340
Cdd:pfam02463 251 --EEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 341 EELIKAQEELKNRESNSLVQALKTSSKVDTSLTsnkstcnETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLilvs 420
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREA-------EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA---- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 421 ppITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADV 500
Cdd:pfam02463 390 --AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 501 EQiqasynSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLS 580
Cdd:pfam02463 468 KK------SEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 581 SGAKGDNClntsqqlpgGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKG 660
Cdd:pfam02463 542 KVAISTAV---------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 661 YREENSDLRAQESQGKNRDHQL-KEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVE 739
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELtKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 740 TQKDECKRLVELEQSI--LEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEEN 817
Cdd:pfam02463 693 EILRRQLEIKKKEQREkeELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 818 EISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQY 897
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLA 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 898 SQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELD 977
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE-EAEILL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 978 KWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYAD 1057
Cdd:pfam02463 932 KYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
890
....*....|....
gi 569007265 1058 DRERCLKLQNEVET 1071
Cdd:pfam02463 1012 IEETCQRLKEFLEL 1025
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
605-1093 |
9.18e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 605 VKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgKNRDHQLKE 684
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 685 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILK 764
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 765 LEANLKECEAKHQdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansiltqnlkad 844
Cdd:PRK03918 326 IEERIKELEEKEE---RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL------------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 845 lqkkEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKK-------------------NQYSQDLDMKQ 905
Cdd:PRK03918 390 ----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 906 RTIQQLKEQLSNQKME-EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQdrvLEAKSEEADWLATELDKWKEKFK 984
Cdd:PRK03918 466 KELKEIEEKERKLRKElRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 985 DLETRSNQrlntgtmddLDVLTRKFSKLQDELQESEEKyKADRKKWLEEKAV-----LTTQAKEAENVRNR--EMRKYAD 1057
Cdd:PRK03918 543 SLKKELEK---------LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEK 612
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 569007265 1058 DRERCLK----LQNEVETLTAQLAEKNSELQKWREERDQL 1093
Cdd:PRK03918 613 ELEREEKelkkLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
447-989 |
1.09e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 447 LKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRD 526
Cdd:COG1196 234 LRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 527 RILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLpggdfsSTWVK 606
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------EELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 607 EYHT--QEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKE 684
Cdd:COG1196 384 LAEEllEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 685 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVEtQKDECKRLVELEQSILEKESAILK 764
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 765 LEAnlkeceAKHQDHIRTNDLSAKEV------KFREEVTRLANNLHDTKQLLQSKEEENEISR-------------QETE 825
Cdd:COG1196 543 ALA------AALQNIVVEDDEVAAAAieylkaAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvasdlreadARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 826 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 905
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 906 RTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlateLDKWKEKFKD 985
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELER 771
|
....
gi 569007265 986 LETR 989
Cdd:COG1196 772 LERE 775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
638-1119 |
2.98e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 638 SKKSHQIQGLEEQIEK------------LQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRV 705
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEkeekdlherlngLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 706 QVQLVAEREQALSELSQdvtcykaKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEAnLKECEAKHQDHIRTND 784
Cdd:PRK02224 263 LRETIAETEREREELAE-------EVRDLRERLEELEEERDDLLaEAGLDDADAEAVEARREE-LEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 785 LSAKEvkFREEVTRLANNLHDTkqllqskEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKK 864
Cdd:PRK02224 335 VAAQA--HNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 865 QIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqqyEKVCKdLSVKEKLVEDM 944
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGS----PHVET-IEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 945 RLTLVEQEQTQAEQDRVLEaKSEEADWLATELDKWKEKFKDLETRSNQRlNTGTMDDLDVLTRKFSKLQDELQESEEKYK 1024
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1025 ADRKKWLEEKAVLTTQAKeaenvRNREMRKYADDRERClklqNEVETLTAQLAEKNSELQKWREERDQLvTAVETQMKAL 1104
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAE-----LNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELNDERRER 628
|
490
....*....|....*
gi 569007265 1105 LSSckhKDEEIQELR 1119
Cdd:PRK02224 629 LAE---KRERKRELE 640
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
445-795 |
3.59e-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: 58.16 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 445 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQ 524
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 525 RDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGgdfSSTW 604
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN---RLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 605 VKEYHTQEIsrensfhASIEAIWEECKEIVKASSKKSHQIQG----LEEQIEKLQVEVKGYREENSDLRAQEsqgKNRDH 680
Cdd:TIGR02169 827 EKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDLESRLGDLKKER---DELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 681 QLKEKESLIQQLREELQEKSvslrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlveLEQSILEKES 760
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKR-------KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----VQAELQRVEE 965
|
330 340 350
....*....|....*....|....*....|....*.
gi 569007265 761 AILKLE-ANLKECEAKHQDHIRTNDLSAKEVKFREE 795
Cdd:TIGR02169 966 EIRALEpVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-960 |
7.08e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 287 VEDIFHSLQDDVTDIKKQAELAHLYITslvdpqeaiacLQLKFNQVKAELAETKEELIKAQEELKNRESNSLVQALKtss 366
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERYRE-----------LKEELKELEAELLLLKLRELEAELEELEAELEELEAELE--- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 367 kvdtSLTSNKSTCNETSEmpkNSRAQTHSERKRLNEDGLQLgeppakkglilvsppiTEEQNKMGEMQQSVSEVVEGNRV 446
Cdd:COG1196 257 ----ELEAELAELEAELE---ELRLELEELELELEEAQAEE----------------YELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 447 LKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRD 526
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 527 RILKLSQEMETAARSIESNVSQIKQMQTKIDELRsldspshiskidllnlqdlssgakgdnclntsqqlpggdfsstwvk 606
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELE---------------------------------------------- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 607 eyhtqeisrensfhASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKE 686
Cdd:COG1196 428 --------------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 687 SLIQQLREELQEKSVSLRVQVQLVAER--EQALSELSQDVTCYKAKIKD------LEVIVETQKDECKRLVELEQSILEK 758
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAALEAalaaalQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 759 ESAI----LKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAN 834
Cdd:COG1196 574 ATFLpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 835 SILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 914
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 569007265 915 LSNQKMEEAVQQYEkvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDR 960
Cdd:COG1196 734 REELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREI 776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
689-1123 |
8.34e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 689 IQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVtcYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEAN 768
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELR----------AELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 769 LKECEAKHQDH--IRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQ 846
Cdd:COG4913 325 LDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 847 KKEEDCAELKEKFIDAKKQIEQVQREvsvmrdeekllrikINELEKKKNQYSQDLdmkQRTIQQLKEQLS---------- 916
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAE--------------IASLERRKSNIPARL---LALRDALAEALGldeaelpfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 917 --------NQKMEEAV---------------QQYEKVCK---DLSVKEKLV-EDMRLTLVEQEQTQAEQD---RVLEAKS 966
Cdd:COG4913 465 elievrpeEERWRGAIervlggfaltllvppEHYAAALRwvnRLHLRGRLVyERVRTGLPDPERPRLDPDslaGKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 967 EEA-DWLATELDKWK--------EKFKDLE---TRSNQRLNTGTM---DD-----------------LDVLTRKFSKLQD 1014
Cdd:COG4913 545 HPFrAWLEAELGRRFdyvcvdspEELRRHPraiTRAGQVKGNGTRhekDDrrrirsryvlgfdnrakLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1015 ELQESEEKY---KADRKKWLEEKAVLTTQAKEAENVRN-----REMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKW 1086
Cdd:COG4913 625 ELAEAEERLealEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASSDDLAALEEQLEELEAELEEL 704
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 569007265 1087 REERDQL---VTAVETQMKALLSSCKHKDEEIQELRKAAA 1123
Cdd:COG4913 705 EEELDELkgeIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
623-1119 |
1.44e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 623 IEAIWEECKEIVKASSKKShqiQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVS 702
Cdd:COG4717 48 LERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 703 LRVQvQLVAEREQALSELSQDVTCYKakikdlevivetqkdeckRLVELEQSILEKESAILKLEANLKECEAKHQDHIRT 782
Cdd:COG4717 125 LQLL-PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 783 NDLSAKE--VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFI 860
Cdd:COG4717 186 LSLATEEelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 861 DAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQlsnqkmeeavqQYEKVCKDLSVKEKL 940
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE-----------ELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 941 VEDMRLTLVEQEQTQAEQDRVLEAKSEEADWlateldkwkekfKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDelqese 1020
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQL------------EELEQEIAALLAEAGVEDEEELRAALEQAEE------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1021 ekykadRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRerclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQ 1100
Cdd:COG4717 397 ------YQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAEL----EAE 461
|
490
....*....|....*....
gi 569007265 1101 MKALLSsckhkDEEIQELR 1119
Cdd:COG4717 462 LEQLEE-----DGELAELL 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-868 |
2.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 319 QEAIACLQLKFNQVKAELAETKEELIKAQEELkNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEmpknSRAQTHSERK 398
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 399 RLNEDGLQLGEppAKKGLILVsppITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQ 478
Cdd:COG1196 327 ELEEELEELEE--ELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 479 VVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDE 558
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 559 LRSLDSPSHISKIDLLNLQDLSSGAkgdnclntsqqlpggdfsSTWVKEYHTQEISRENSFHASIEAIWEECKE--IVKA 636
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGF------------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaLEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 637 SSKKSHQI-----QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVA 711
Cdd:COG1196 544 LAAALQNIvveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 712 EReqALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVK 791
Cdd:COG1196 624 GR--TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 792 FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQ 868
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
810-1024 |
4.81e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 810 LQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINE 889
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 890 LEKKKNQYSQDLDMKQRTIQQLKEQ------LSNQKMEEAVqqyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLE 963
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007265 964 AKSEEADWLATELDKWKEKFKDLETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEKYK 1024
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAE 223
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
434-957 |
7.71e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.93 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 434 QQSVSEVVEGNRVLKEKNEELKRLLTIGENEL---RNEKEEKAELNKQVVSLQ------QQLRFFEEKNSSLRADVeqiq 504
Cdd:COG5022 771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLlslLGSRKEYRSYLACIIKLQktikreKKLRETEEVEFSLKAEV---- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 505 aSYNSAVAELQTQKAVNQEQRDRIL-----------KLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDL 573
Cdd:COG5022 847 -LIQKFGRSLKAKKRFSLLKKETIYlqsaqrvelaeRQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEF 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 574 LNlqDLSSGAKgdnclntsQQLPGGDFSSTWVKEYHTQEISRE-NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIE 652
Cdd:COG5022 926 KT--ELIARLK--------KLLNNIDLEEGPSIEYVKLPELNKlHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 653 KLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQvQLVAEREQALSELSqdvtcykAKIK 732
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQ-KLKGLLLLENNQLQ-------ARYK 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 733 DLEVIVETQKDECKRLVELE-QSILEKesailklEANLKECEAKHQDHIrtndLSAKEVKFREEVTRLANNLHDTKQLLQ 811
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLEsTENLLK-------TINVKDLEVTNRNLV----KPANVLQFIVAQMIKLNLLQEISKFLS 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 812 SKEEENEISRQETEKLKEELAANSILTQN--------LKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK-- 881
Cdd:COG5022 1137 QLVNTLEPVFQKLSVLQLELDGLFWEANLealpspppFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFsg 1216
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 882 -LLRIKINELEKKKNQYSQdldmkqrTIQQLKEQLSNQKmEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAE 957
Cdd:COG5022 1217 wPRGDKLKKLISEGWVPTE-------YSTSLKGFNNLNK-KFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPAT 1285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1093 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 845 LQKKEEDCAELKEKFIDAKKQIEQVQREVsvmrdeeKLLRIKINELEKKKNQYSQDLDMK--QRTIQQLKEQL-----SN 917
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 918 QKMEEAVQQYEKVCKDLSVKEKLVEDM--RLTLVEQEQTQAE------QDRVLEAKSEEADWLATELDKWKEKFKDLETR 989
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELkgEIGRLEKELEQAEeeldelQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 990 SNQRLNTGtmDDLDVLTRKFSKLQDELQESEEKYKADrkkWLEEKAVLTTQAKEAENVRNREMRKYADD----RERCLKL 1065
Cdd:COG4913 765 RELRENLE--ERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLDRLEEDGlpeyEERFKEL 839
|
250 260
....*....|....*....|....*....
gi 569007265 1066 QNevETLTAQLAEKNSELQKWREE-RDQL 1093
Cdd:COG4913 840 LN--ENSIEFVADLLSKLRRAIREiKERI 866
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
445-1008 |
1.59e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 445 RVLKEKNEELKRLltigENELRNEKEE-KAELNKQVVSLQQQLRFFEeKNSSLRADVEQIQASYNSAVAELQTQKAVNQE 523
Cdd:pfam15921 419 RELDDRNMEVQRL----EALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 524 QRDRILKLSQEMETAARSIESNVSQIKQMQTKIDelrsldspshiskIDLLNLQDLSSgaKGDNCLNTSQQLPGGDFSST 603
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVD-------------LKLQELQHLKN--EGDHLRNVQTECEALKLQMA 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 604 wvKEYHTQEISRENSfhasieaiwEECKEIVKASSKKSHQIQGLEEQIEKlqvEVKGYREENSDLRAQESQgknRDHQLK 683
Cdd:pfam15921 559 --EKDKVIEILRQQI---------ENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEFKILKDK---KDAKIR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 684 EKESLIQQLREE----LQEKSVSLRVQVQLVAEREQALSE----------LSQDVTCYKAKIKDLEVIVETQKDECKRLV 749
Cdd:pfam15921 622 ELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEvktsrnelnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 750 ELEQSILEKEsailklEANLKECEAKHQDHIRTNDLSAKEVKF-REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK 828
Cdd:pfam15921 702 KSAQSELEQT------RNTLKSMEGSDGHAMKVAMGMQKQITAkRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 829 EELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVS-----VMRDEEKLLRIKINE-LEKKKNQ---YSQ 899
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQRQEQESVRLKLQHtLDVKELQgpgYTS 855
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 900 DLDMKQRTIQ--QLKEQLSNQKMEEAVQQY--EKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEaDWLATE 975
Cdd:pfam15921 856 NSSMKPRLLQpaSFTRTHSNVPSSQSTASFlsHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAED-KGRAPS 934
|
570 580 590
....*....|....*....|....*....|...
gi 569007265 976 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRK 1008
Cdd:pfam15921 935 LGALDDRVRDCIIESSLRSDICHSSSNSLQTEG 967
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
818-1091 |
1.62e-06 |
|
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: 52.76 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 818 EISRQETEKLKEElAANSILTQNLKADLQKKEEdcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQY 897
Cdd:TIGR02169 194 DEKRQQLERLRRE-REKAERYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 898 SQDLDMKQRTIQQLKEQLSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLAT 974
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 975 ELDKWKEKFKDLETRSN---QRL------NTGTMDDLDVLTRKFSKLQDELQESeekyKADRKKWLEEKAVLTTQAKEAE 1045
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEdlrAELeevdkeFAETRDELKDYREKLEKLKREINEL----KRELDRLQEELQRLSEELADLN 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 569007265 1046 NvrnremrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1091
Cdd:TIGR02169 427 A-------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
670-925 |
2.00e-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: 51.69 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 670 AQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEvivetqkdecKRLV 749
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----------AELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 750 ELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLsaKEVKFREEVTRLANNLHDTKQLLQSKeeeneisRQETEKLKE 829
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL--ALLLSPEDFLDAVRRLQYLKYLAPAR-------REQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 830 ELAANSILTQNLKADLQKKEEDCAELKEKfidaKKQIEQVQREVsvmrdeekllRIKINELEKKKNQYSQDLDMKQRTIQ 909
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEE----RAALEALKAER----------QKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*.
gi 569007265 910 QLKEQLSNQKMEEAVQ 925
Cdd:COG4942 224 ELEALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
407-1102 |
2.28e-06 |
|
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: 52.28 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 407 LGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRV-LKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQ 485
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAElLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 486 LRFFEEKNSSLRADVEQIQASYNSA------VAELQTQKAVNQEQRDRIlKLSQEMETAARSIESNVSQIKQMQTKIDEL 559
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLkqlrarIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 560 RS-LDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQ----LPGGDFSSTWVKEYHTQEISRENSFHASIEAIwEECKEIV 634
Cdd:TIGR00618 317 QSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQK-TTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 635 KASSKKSHQIQGLEEQIEKLQVEvkgYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAERE 714
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRTSA---FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 715 QALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECE------AKHQDHIRTNDLSAK 788
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtyAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 789 EVK-----FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----ILTQNLKADLQKKEEDCAELKEKF 859
Cdd:TIGR00618 553 SERkqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 860 IDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLS 935
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 936 VKE--KLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlatELDKWKEKFKDLE-TRSNQRLNTGTMDDldvltRKFSKL 1012
Cdd:TIGR00618 713 IEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTAALQTG-----AELSHL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1013 QDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQLAEKNSELQKWREERDQ 1092
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
730
....*....|
gi 569007265 1093 LVTAVETQMK 1102
Cdd:TIGR00618 861 LAQLTQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
644-930 |
2.34e-06 |
|
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: 52.38 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 644 IQGLEEQIEKlqvevkgYREENSDLRAQESQgknrdHQLKEKESLIQQLREELQEKSVSLRvqvqlvaEREQALSELSQD 723
Cdd:TIGR02169 767 IEELEEDLHK-------LEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLR-------EIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 724 VTCYKAKIKDLEVIVETQKDeckRLVELEQSILEKESAILKLEANLKECEAkhqdhiRTNDLSAKEVKFREEVTRLANNL 803
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEA------ALRDLESRLGDLKKERDELEAQL 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 804 HDTKQLLQSKEEENEISRQETEKLKEEL-AANSILTQNLKADLQKKEEDCAELKEKfiDAKKQIEQVQREVSVMRD---- 878
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLeALEEELSEIEDPKGEDEEIPEEELSLE--DVQAELQRVEEEIRALEPvnml 976
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 879 -----EEKLLRikINELEKKKNQysqdLDMKQRTIQQLKEQLSNQKMEEAVQQYEKV 930
Cdd:TIGR02169 977 aiqeyEEVLKR--LDELKEKRAK----LEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
628-1027 |
2.78e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 628 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREEnSDLRAQESQGKNRDHQLKEKESLIQQLR---EELQEKSVSLR 704
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 705 VQVQLVAEREQALSELSQDVTcyKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTND 784
Cdd:COG4717 167 ELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 785 LSAKEVKFREEVTRLA-----NNLHDTKQ---------------LLQSKEEENEISRQETEKLKEELAANSILTQNLKAD 844
Cdd:COG4717 245 LKEARLLLLIAAALLAllglgGSLLSLILtiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 845 LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKllRIKINELEKKKNQYSQDLDMKqrTIQQLKEQLSN-QKMEEA 923
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVE--DEEELRAALEQaEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 924 VQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDrvLEAKSEEadwLATELDKWKEKFKDLETRSNQRLNTGTmddLD 1003
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEE---LEEELEELREELAELEAELEQLEEDGE---LA 472
|
410 420
....*....|....*....|....
gi 569007265 1004 VLTRKFSKLQDELQESEEKYKADR 1027
Cdd:COG4717 473 ELLQELEELKAELRELAEEWAALK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
481-699 |
4.05e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 481 SLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELR 560
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 561 SLDSpshiskiDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK 640
Cdd:COG4942 104 EELA-------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569007265 641 SHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 699
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
831-1089 |
5.70e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 831 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 910
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 911 LKEQLSNQKmeeavQQYEKVckdLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrs 990
Cdd:COG4942 95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 991 nqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVE 1070
Cdd:COG4942 164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*....
gi 569007265 1071 TLTAQLAEKNSELQKWREE 1089
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
306-549 |
8.16e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 306 ELAHLYITSLVDPQEAIACLQLKFnqVKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKVDTSLTSNKSTCNETse 384
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEF--LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEA-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 385 mpknsRAQTHSERKRLNEDGLQLGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEG---------------NRVLKE 449
Cdd:COG3206 232 -----RAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvialraqiAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 450 KNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLrffeeknsslrADVEQIQASYNsavaELQTQKAVNQEQRDRIL 529
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELR----RLEREVEVARELYESLL 371
|
250 260
....*....|....*....|
gi 569007265 530 KLSQEMETAARSIESNVSQI 549
Cdd:COG3206 372 QRLEEARLAEALTVGNVRVI 391
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
333-1079 |
1.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 333 KAELAETKEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEdgLQLGEPPA 412
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE--KKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 413 KKGlilvsppitEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRlltigENELRNEKEEKAELnkqvvslqqqlrffEEK 492
Cdd:PTZ00121 1309 KKA---------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-----AAEAAKAEAEAAAD--------------EAE 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 493 NSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKqmqtKIDELRSldSPSHISKID 572
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKK--KAEEKKKAD 1434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 573 LLNlQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEaiwEECKEIVKASSKKSHQIQGLEEQIE 652
Cdd:PTZ00121 1435 EAK-KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA---DEAKKKAEEAKKKADEAKKAAEAKK 1510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 653 KLQvEVKGYREENSDLRAQESQGKNRDHQLKEKEsliQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKik 732
Cdd:PTZ00121 1511 KAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE-- 1584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 733 dlevivETQKDECKRLVELEQsiLEKESAILKLEANLKECEAKhqdhirtndLSAKEVKFREEVTRlannlhDTKQLLQS 812
Cdd:PTZ00121 1585 ------EAKKAEEARIEEVMK--LYEEEKKMKAEEAKKAEEAK---------IKAEELKKAEEEKK------KVEQLKKK 1641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 813 KEEEneisRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKlLRIKINELEK 892
Cdd:PTZ00121 1642 EAEE----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKK 1716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 893 KKNQYSQDLDMKQRTIQQLKeqlsnQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwl 972
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED-- 1789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 973 ATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKfsklqdELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREM 1052
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK------EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
730 740
....*....|....*....|....*....
gi 569007265 1053 RKYADD--RERCLKLQNEVETLTAQLAEK 1079
Cdd:PTZ00121 1864 GNKEADfnKEKDLKEDDEEEIEEADEIEK 1892
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
482-1138 |
1.51e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 482 LQQQLRFFEEKNSSLRADVE----QIQASYNSAVA----ELQTQKAVNQEQRDRILKLSQEMETaarSIESNVSQIKQMQ 553
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDikesKLGSSMNSIKTfwspELKKERALRKEEAARISVLKEQYRV---TQEENQHLQLTIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 554 TKIDELRsldspSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEIS-----------RENSFHAS 622
Cdd:pfam10174 78 ALQDELR-----AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFllrktleemelRIETQKQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 623 IEAIWEECKEIV-----KASSKKS--------HQIQGLEEQIEKLQVEVKGYREENSDLRaQESQGKNRDHQLKEKESLI 689
Cdd:pfam10174 153 LGARDESIKKLLemlqsKGLPKKSgeedwertRRIAEAEMQLGHLEVLLDQKEKENIHLR-EELHRRNQLQPDPAKTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 690 QQLREELQEKSVSL-RVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEAN 768
Cdd:pfam10174 232 QTVIEMKDTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 769 LKECEAKHQD---HIRT--NDLSAKEVK-------------------------------FREEVTRLANNLHDTKQLLQS 812
Cdd:pfam10174 312 LETLTNQNSDckqHIEVlkESLTAKEQRaailqtevdalrlrleekesflnkktkqlqdLTEEKSTLAGEIRDLKDMLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 813 KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDC-------AELKEKFIDAKKQIE----QVQREVSVMRDEEK 881
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIErlkeQREREDRERLEELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 882 LLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQ------------KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLV 949
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 950 EQEQTqAEQDRVLEA----KSEEADWLATELDKWKEKFKDLETRSNQRlnTGTMDDLDVLTRKFSKLQD----ELQESEE 1021
Cdd:pfam10174 552 TNPEI-NDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDK--DKKIAELESLTLRQMKEQNkkvaNIKHGQQ 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1022 KYKADRKKWLEEkaVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQ-------LAEKNSELQKWR-EERDQL 1093
Cdd:pfam10174 629 EMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALE---KTRQELDATKARlsstqqsLAEKDGHLTNLRaERRKQL 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 569007265 1094 VTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPE 1138
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
615-760 |
1.66e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 615 RENSFHASIEAIWEECKEIVK-----ASSKKSHQIQGLEEQIEKLQVEV-KGYREENSDLRAQESQGKNRDHQLKEKESL 688
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEeakkeAEAIKKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007265 689 IQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcYKAKIKDLEVIVETQKDECKRLVeLEQsiLEKES 760
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAKEIL-LEK--VEEEA 167
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
622-1070 |
1.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 622 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLraqeSQGKNRDHQLKEKESLIQQLREELQEKSV 701
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 702 SLRVQVQLVAEREQALSELS-QDVTCYKAKIKDLEVIVETQKDECK----RLVELEQSILEKESAILKLEANLKEC---- 772
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISkitaRIGELKKEIKELKKAIEELKKAKGKCpvcg 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 773 ---EAKHQDHIrTNDLSAKEVKFREEVTRLANNLHDTKQLLqsKEEENEISRQET----EKLKEEL-AANSILTQNLKAD 844
Cdd:PRK03918 443 relTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKEL--RELEKVLKKESEliklKELAEQLkELEEKLKKYNLEE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 845 LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK---LLRIKINELEKKKNQYSQDLDMKQ-RTIQQLKEQLsnQKM 920
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKklaELEKKLDELEEELAELLKELEELGfESVEELEERL--KEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 921 EEAVQQY---EKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLntg 997
Cdd:PRK03918 598 EPFYNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRE--- 674
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007265 998 tmddldvLTRKFSKLQdELQESEEKYKADRKKWLEEKAVLTTQAKEAENVrNREMRKYADDRERCLKLQNEVE 1070
Cdd:PRK03918 675 -------LAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
658-926 |
2.13e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 658 VKGYREENSDLRAQESqgknrdhqlkekESLIQQLREELQEksvsLRVQVQlvaEREQALSELSQdvtcyKAKIKDLEvi 737
Cdd:COG3206 158 AEAYLEQNLELRREEA------------RKALEFLEEQLPE----LRKELE---EAEAALEEFRQ-----KNGLVDLS-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 738 vETQKDECKRLVELEQSILEKESAILKLEANLKECEAKhqdhIRTNDLSAKEVKFREEVTRLANnlhdtkQLLQSKEEEN 817
Cdd:COG3206 212 -EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ----LGSGPDALPELLQSPVIQQLRA------QLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 818 EISRQETEK------LKEELAAnsiltqnLKADLQkkeedcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELE 891
Cdd:COG3206 281 ELSARYTPNhpdviaLRAQIAA-------LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
250 260 270
....*....|....*....|....*....|....*...
gi 569007265 892 KKKNQYSQ---DLDMKQRTIQQLKEQLSNQKMEEAVQQ 926
Cdd:COG3206 348 ELEAELRRlerEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
730-1345 |
2.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 730 KIKDLEVIVETQKDECKRLVELEQSILE--KESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLannlHDTK 807
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEER----KAEEARKAEDAKKA----EAVK 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 808 QLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEdcAELKEKfIDAKKQIEQVQREVSVMRDEEKLlriKI 887
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARK-ADELKKAEEKKKADEAKKAEEKK---KA 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 888 NELEKKKNQYSQDLDMKQrtiqqlKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRltlvEQEQTQAEQDRVLEAKSE 967
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKK------KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA----DEAEAAEEKAEAAEKKKE 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 968 EADWLATELDK-WKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADR-KKWLEEKAVLTTQAKEAE 1045
Cdd:PTZ00121 1375 EAKKKADAAKKkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAE 1454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1046 NVRNRE-MRKYADDRERCLKLQNEVETltaqlAEKNSELQKWREER----DQLVTAVETQMKALLSSCKHKDEEIQELRK 1120
Cdd:PTZ00121 1455 EAKKAEeAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEAkkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1121 AAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTPLQP 1200
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1201 NKMAVKHPGcptpvtiKIPKARKRKSGEVEEDLVKCENKKNSTPRSNVKFPVSEHRNSPVKKEQKVSVGPSSKKTYSLRS 1280
Cdd:PTZ00121 1610 EEAKKAEEA-------KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007265 1281 QASTVSANIASKKREGTLQKFGDFLQHSPTILQSKAKKIIETMSSPKLSTVEVSKENVSQPKKAK 1345
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
742-1091 |
2.55e-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: 48.81 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 742 KDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFRE------EVTRLANNLHDTKQLLQSKEE 815
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 816 ENEISRQETEKLKEELAansilTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKn 895
Cdd:pfam02463 252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 896 qysqdldmkqrtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATE 975
Cdd:pfam02463 326 -------------AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS-SAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 976 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKY 1055
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 569007265 1056 ADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1091
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
474-1104 |
2.61e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 474 ELNKQVVSLQQQL----RFFEEKNSSLRADVEQIQASYNS------AVAELQTQKAVNQEQ-RDRILKLSQEMEtAARSI 542
Cdd:pfam15921 82 EYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEmqmerdAMADIRRRESQSQEDlRNQLQNTVHELE-AAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 543 ESNVsqIKQMQTKIDELRSLdSPSHISKidllnLQDLSSGAKgdnclntsqqlpggDFSSTWVKEYHTQEISRENSFHAS 622
Cdd:pfam15921 161 KEDM--LEDSNTQIEQLRKM-MLSHEGV-----LQEIRSILV--------------DFEEASGKKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 623 IEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREensdLRAQESQgkNRDHQL-KEKESLIQQLREELQE-KS 700
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIE----LLLQQHQ--DRIEQLiSEHEVEITGLTEKASSaRS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 701 VSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIV---ETQKDECKRLVELEQSILEKESAIlkleANLKECEAKhq 777
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSM----YMRQLSDLESTVsqlRSELREAKRMYEDKIEELEKQLVL----ANSELTEAR-- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 778 dhirtndlsAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKE 857
Cdd:pfam15921 363 ---------TERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 858 KFIDAKKQIE-QVQREVSVMRDEekllrikiNELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMeeAVQQYEKVCKDLSV 936
Cdd:pfam15921 434 LLKAMKSECQgQMERQMAAIQGK--------NESLEKVSSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDLTA 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 937 ----KEKLVE-------------DMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDletrsnqrlntgTM 999
Cdd:pfam15921 504 slqeKERAIEatnaeitklrsrvDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQ------------QI 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1000 DDLDVLTRKFSKLQDELQESE---EKYKADRKKWLEEKAVLttqaKEAENVRNREMRKYADDrerclkLQNEVETLTAQL 1076
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKaqlEKEINDRRLELQEFKIL----KDKKDAKIRELEARVSD------LELEKVKLVNAG 641
|
650 660
....*....|....*....|....*...
gi 569007265 1077 AEKNSELQKWREERDQLVTAVETQMKAL 1104
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
899-1127 |
3.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 899 QDLDMKQRTIQQLKEQLSN-QKMEEAVQQYEKVCKDLSVKEKLVEdmRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD 977
Cdd:COG4913 235 DDLERAHEALEDAREQIELlEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 978 KWKEKFKDLETR----SNQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYK--ADRKKWLEEKAVLTTQA-KEAENVRNR 1050
Cdd:COG4913 313 RLEARLDALREEldelEAQIRGNGG-DRLEQLEREIERLERELEERERRRArlEALLAALGLPLPASAEEfAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 1051 EMRKYADDRERclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALlssckhkDEEIQELRKAAAKSTG 1127
Cdd:COG4913 392 LLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNI-------PARLLALRDALAEALG 454
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
448-1141 |
4.30e-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: 48.04 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 448 KEKNEELKRLLTIGENELRNEKEEKAELNKQvvslqqqlrffEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQrdr 527
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELKLLAKE-----------EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 528 ILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSgakgdnclntsqqlpggDFSSTWVKE 607
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-----------------ERLSSAAKL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 608 YHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKES 687
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 688 LIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELeqsILEKESAILKLEA 767
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV---AVENYKVAISTAV 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 768 NLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLkadLQK 847
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK---VVE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 848 KEEDCAELKEKFIDAKKQIEQVQREVSVMRDE-EKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK-MEEAVQ 925
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLeIKKKEQ 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 926 QYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQ------RLNTGTM 999
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEkelaeeREKTEKL 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1000 DDLDVLTRKFSKLQDELQE--SEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCL-KLQNEVETLTAQL 1076
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeEELERLEEEITKE 866
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007265 1077 AEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYND 1141
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
844-1115 |
5.69e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 844 DLQKKEEDCAELKEK--------FIDAKKQIEQVQREVSVMRDeekllrikineLEKKKNQYSQDL-DMKQRTIQQLK-- 912
Cdd:pfam15921 89 DLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMERDAMAD-----------IRRRESQSQEDLrNQLQNTVHELEaa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 913 EQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQA----EQD---------------RVLEAKSEEADWLA 973
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGkkiyEHDsmstmhfrslgsaisKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 974 TELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMR 1053
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007265 1054 KYADDRERCLKLQNE-----------VETLTAQLAEKNSELQKWREERDQLVTA---VETQMKALLSSCKHKDEEI 1115
Cdd:pfam15921 318 QLSDLESTVSQLRSElreakrmyedkIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKEL 393
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
641-893 |
5.87e-05 |
|
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: 47.07 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 641 SHQIQGLEEQIEKLQVEVKgyrEENSDLRAQESQGKNRDHQLKEKESLIQQLREELQeksvslrvqvqlvaEREQALSEL 720
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIR--------------ALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 721 SQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANlkeceaKHQDHIRTNDLSAKEVKFREEvtrLA 800
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARRE---QA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 801 NNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRevsvmrdEE 880
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ-------EA 222
|
250
....*....|...
gi 569007265 881 KLLRIKINELEKK 893
Cdd:COG4942 223 EELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
892-1124 |
6.93e-05 |
|
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: 46.68 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 892 KKKNQYSQDLDMKQRTIQQLKEQLSNQKmeeavQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 971
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK-----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 972 LATELDKWKEKFKDLeTRSNQR----------LNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQa 1041
Cdd:COG4942 95 LRAELEAQKEELAEL-LRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1042 keaenvrnremrkyaddrerclklQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKA 1121
Cdd:COG4942 173 ------------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
...
gi 569007265 1122 AAK 1124
Cdd:COG4942 229 IAR 231
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
464-561 |
7.14e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 464 ELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAE---LQTQKAVNQEQRD----RILKLSQEME 536
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAaaegRAGELAQELD 126
|
90 100
....*....|....*....|....*
gi 569007265 537 TAARSIESNVSQIKQMQTKIDELRS 561
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRR 151
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
683-919 |
1.18e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 683 KEKESLIQQLRE-------ELQEKSVSLRVQ--VQLVAEREQALSELSQDV--------TCYKAKIKDLEVIVETQKDEc 745
Cdd:PRK05771 16 SYKDEVLEALHElgvvhieDLKEELSNERLRklRSLLTKLSEALDKLRSYLpklnplreEKKKVSVKSLEELIKDVEEE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 746 krLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREE--VTRLANNLHDTKQLLQSKEEENEISrQE 823
Cdd:PRK05771 95 --LEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVENV-EY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 824 TEKLKEEL---------AANSILTQNLKADLQKKE-EDCAELKEKFIDAKKQIEQVQREvsvmrdEEKLlrikINELEKK 893
Cdd:PRK05771 172 ISTDKGYVyvvvvvlkeLSDEVEEELKKLGFERLElEEEGTPSELIREIKEELEEIEKE------RESL----LEELKEL 241
|
250 260
....*....|....*....|....*.
gi 569007265 894 KNQYSQDldmkqrtIQQLKEQLSNQK 919
Cdd:PRK05771 242 AKKYLEE-------LLALYEYLEIEL 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
423-929 |
1.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 423 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 502
Cdd:TIGR04523 70 INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 503 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarSIESNVSQIKQmQTKIDELRSLDSPSHISKIDLLNLQDLSSG 582
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKL----NIQKNIDKIKN-KLLKLELLLSNLKKKIQKNKSLESQISELK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 583 AKGDNCLNTSQQLpggdfsstwvKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR 662
Cdd:TIGR04523 225 KQNNQLKDNIEKK----------QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 663 EENSDLRAQESQGKNRD--HQLKEKESLIQQLREEL---QEKSVSLRVQV-QLVAEREQALSELSQDVTCYKAKIKDLEV 736
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKElkSELKNQEKKLEEIQNQIsqnNKIISQLNEQIsQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 737 IVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVK-FREEVTRLANNLHDTKQLLQSKEE 815
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErLKETIIKNNSEIKDLTNQDSVKEL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 816 ENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKN 895
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
490 500 510
....*....|....*....|....*....|....
gi 569007265 896 QYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEK 929
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEKNK 568
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
643-929 |
1.62e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 643 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKeslIQQLREELQEKSVSLRVQVQLVAEREQALSELsq 722
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 723 dvtcyKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEanlkeceakhqDHIRTNDLS-AKEVKFREEVTRLAN 801
Cdd:COG1340 84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE-----------WRQQTEVLSpEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 802 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK 881
Cdd:COG1340 148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 569007265 882 LLRIKINELEKKKNQYSQDLD-MKQRTIQQLKEQLSNQKMEEAVQQYEK 929
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKkLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
643-824 |
1.69e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 643 QIQGLEEQIEKLQVEVKGYREENSDLRAQEsQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQ 722
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 723 D--VTCYKAKIKDLE-----------------VIVETQKDECKRLV--ELEQSILEKESAILKLEANLKECEAKHQDH-I 780
Cdd:COG3206 262 SpvIQQLRAQLAELEaelaelsarytpnhpdvIALRAQIAALRAQLqqEAQRILASLEAELEALQAREASLQAQLAQLeA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569007265 781 RTNDLSAKEVKFReEVTRLANNLHDTKQLLQSKEEENEISRQET 824
Cdd:COG3206 342 RLAELPELEAELR-RLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
757-1124 |
1.89e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 757 EKESAILKLEANLKECEAKhQDHIRTNDLSAKEVKFREEVTRLANN---LHDTKQLLQSKEEENEISRQETEKLKEELAa 833
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEK-DLHERLNGLESELAELDEEIERYEEQreqARETRDEADEVLEEHEERREELETLEAEIE- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 834 nsiltqNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL-------LRIKINELEKKKNQYSQDLDMKQR 906
Cdd:PRK02224 262 ------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 907 TIQQLKEQLSNqkMEEAVQQYEKVCKDLSVK----EKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEK 982
Cdd:PRK02224 336 AAQAHNEEAES--LREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 983 FKDLEtrsnqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQ-AKEAENVRNREmrkyaDDRER 1061
Cdd:PRK02224 414 LEELR------------EERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQpVEGSPHVETIE-----EDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1062 CLKLQNEVETLTAQ-------------LAEKNSELQKWREERDQLV-------TAVETQMKALLSSCKHKDE---EIQEL 1118
Cdd:PRK02224 477 VEELEAELEDLEEEveeveerleraedLVEAEDRIERLEERREDLEeliaerrETIEEKRERAEELRERAAEleaEAEEK 556
|
....*.
gi 569007265 1119 RKAAAK 1124
Cdd:PRK02224 557 REAAAE 562
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
335-917 |
2.02e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 335 ELAETKEELIKAQEELKNRE-------------------SNSLVQALKTSSK-VDTSLTSNKSTCNETSEMPKNSRAQTH 394
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEkelknldknlnkdeekinnSNNKIKILEQQIKdLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 395 SERKRLNEDGLQLGEppAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAE 474
Cdd:TIGR04523 114 NDKEQKNKLEVELNK--LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 475 LNKQVVSLQQQLRFFEEKN----------SSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 544
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 545 NVSQIKQMQTKIDELRSLdspshISKIDlLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIE 624
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQ-----LNQLK-SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 625 AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ----ESQGKNRDHQLKEKESLIQQLREELQEKS 700
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindlESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 701 VSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECK-----------RLVELEQSILEKESAILKLEANL 769
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 770 KECEAKHQDHIRTNDLS-AKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK--EELAANSILTQNLKADLQ 846
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLkEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEELKQTQKSLKKKQE 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007265 847 KKEEDCAELKEKFIDAKKQIE-------QVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSN 917
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
633-1140 |
2.11e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 633 IVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAE 712
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 713 REQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKF 792
Cdd:TIGR00606 620 QLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 793 REEVTRLA-NNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQR 871
Cdd:TIGR00606 700 LQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 872 EVSVMRD---EEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDmrltl 948
Cdd:TIGR00606 780 EEESAKVcltDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD----- 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 949 vEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSN--QRLNTGTMDDLDVLTRKFSKLQDELQESEE---KY 1023
Cdd:TIGR00606 855 -QQEQIQHLKSKTNELKSEKLQ-IGTNLQRRQQFEEQLVELSTevQSLIREIKDAKEQDSPLETFLEKDQQEKEElisSK 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1024 KADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLK-LQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQ-- 1100
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQki 1012
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 569007265 1101 ----MKALLSSCKHKDE--EIQELRKAAAKSTGtENQTMNPKPEYN 1140
Cdd:TIGR00606 1013 qerwLQDNLTLRKRENElkEVEEELKQHLKEMG-QMQVLQMKQEHQ 1057
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
643-833 |
3.17e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 643 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNR----DHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALS 718
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 719 ELSQ------------------DVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKEceakhqdhi 780
Cdd:COG4942 115 RLGRqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE--------- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569007265 781 RTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAA 833
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
635-1105 |
3.27e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 635 KASSKKSHQIQGLEEQIEKLQVE--VKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSvslrvqvqlvaE 712
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPcmPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-----------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 713 REQALSELSQDVTCYKAKIKDLEVIVETQKDECK--RLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEV 790
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRARKaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 791 KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAE---------------- 854
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilqreqatidtrts 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 855 ----LKEKFIDAKKQIEQVQREVSVMR-------DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKE--QLSNQKME 921
Cdd:TIGR00618 418 afrdLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 922 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSnqrlnTGTMDD 1001
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQM-----QEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1002 LDVLTRKFSKLQDELqESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNS 1081
Cdd:TIGR00618 572 FSILTQCDNRSKEDI-PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
490 500
....*....|....*....|....
gi 569007265 1082 ELQKWREERDQLVTAVETQMKALL 1105
Cdd:TIGR00618 651 LQLTLTQERVREHALSIRVLPKEL 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
854-1104 |
3.75e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 854 ELKEKFIDAKKQIEQVQREVS---------VMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAV 924
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRgsldqlkaqIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR--DEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 925 QQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEqdrvleakseeadwLATELDKWKEKFKDLETRSNQRLNTGTMDDLDV 1004
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREE--------------LAEEVRDLRERLEELEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1005 LTrkFSKLQDELQESEEKYkadRKKWLEEKAVLTTQAKEAENVRNRemrkyADDRE-RCLKLQNEVETLTAQLAEKNSEL 1083
Cdd:PRK02224 310 EA--VEARREELEDRDEEL---RDRLEECRVAAQAHNEEAESLRED-----ADDLEeRAEELREEAAELESELEEAREAV 379
|
250 260
....*....|....*....|.
gi 569007265 1084 QKWREERDQLVTAVETQMKAL 1104
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERF 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1125 |
3.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 677 NRDHQLKEKEsLIQQLREELQEKSVSLRVQVQlvAEREQALSELSQDVTCYKAKIKDlevivETQKDECKRLVELEQSIL 756
Cdd:PTZ00121 1037 NNDDVLKEKD-IIDEDIDGNHEGKAEAKAHVG--QDEGLKPSYKDFDFDAKEDNRAD-----EATEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 757 EK-ESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS 835
Cdd:PTZ00121 1109 GKaEEARKAEEAKKKAEDARKAEEAR----KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 836 ILTQnlKADLQKKEEDCaelkeKFIDAKKQIEQVQR--EVSVMRDEEKLLRIKINELEKKKNQYSQDLDmKQRTIQQLKE 913
Cdd:PTZ00121 1185 EEVR--KAEELRKAEDA-----RKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 914 QLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSE-EADWLATELDKWKEKFKDLETRSNQ 992
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 993 RLNTGTMDDlDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRN-REMRKYADDRErclKLQNEVET 1071
Cdd:PTZ00121 1337 KAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDK---KKADELKK 1412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 1072 LTAQlAEKNSELQKWREER---DQLVTAVETQMKAllSSCKHKDEEIQELRKAAAKS 1125
Cdd:PTZ00121 1413 AAAA-KKKADEAKKKAEEKkkaDEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKA 1466
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
309-536 |
3.99e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 309 HLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKV--DTSLTSNKSTCNETSEM 385
Cdd:COG3096 825 HLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQlKEQLQLLNKLLPQANLlaDETLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 386 PKNSRA--QTHSERKRLNEDGLQlgeppakkglILVSPPITEEQnkmgeMQQSVSEVVEGNRVLKEKNEELK----RLLT 459
Cdd:COG3096 905 AQEAQAfiQQHGKALAQLEPLVA----------VLQSDPEQFEQ-----LQADYLQAKEQQRRLKQQIFALSevvqRRPH 969
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 460 IGENELRNEKEEKAELNKQvvsLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEME 536
Cdd:COG3096 970 FSYEDAVGLLGENSDLNEK---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
462-1072 |
4.06e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 462 ENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAvnqeQRDRILKLSQEMETAA-- 539
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEIKTAEsd 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 540 -RSIESNVSQIKQMQTKIDELRSldSPSHISKIDLLNLQDLssgaKGDnCLNTSQQLPGGDfsstwvkeyhtQEISRENS 618
Cdd:PRK01156 265 lSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINDYFKY----KND-IENKKQILSNID-----------AEINKYHA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 619 FHASIEAIWEECKEIVKASSKKshqiqgleEQIEKLQVEVKGYREE-NSDLRAQESQGKNRDHQLKEKESLIQQLREELQ 697
Cdd:PRK01156 327 IIKKLSVLQKDYNDYIKKKSRY--------DDLNNQILELEGYEMDyNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 698 EKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLevivETQKDECKRLVEleqsILEKESAILKLEANLKECEAKHQ 777
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAL----RENLDELSRNME----MLNGQSVCPVCGTTLGEEKSNHI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 778 DHIRTNDLSAKEVKFRE---EVTRLANNLHDTKQLLQSKEEEnEISRQETEKLKEElaansiltqNLKADLQKKEEDCAE 854
Cdd:PRK01156 471 INHYNEKKSRLEEKIREieiEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNKIE---------SARADLEDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 855 LKEKFIDAKKQIEQVQrevsvmrdeekllRIKINELEKKKNQY--------SQDLDMKQRTIQQLKEQLSNqkMEEAVQQ 926
Cdd:PRK01156 541 LKDKHDKYEEIKNRYK-------------SLKLEDLDSKRTSWlnalavisLIDIETNRSRSNEIKKQLND--LESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 927 YEKVCKDL-SVKEKLVEDMRltlveqeqtqaEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRlnTGTMDDLDVL 1005
Cdd:PRK01156 606 IEIGFPDDkSYIDKSIREIE-----------NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI--DSIIPDLKEI 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1006 TRKFSKLQDELQESE---EKYKADRKKWLEEKAVLTTQAKEAeNVRNREMRKYADDRERCLKLQNEVETL 1072
Cdd:PRK01156 673 TSRINDIEDNLKKSRkalDDAKANRARLESTIEILRTRINEL-SDRINDINETLESMKKIKKAIGDLKRL 741
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
783-998 |
7.96e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 783 NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiltqnLKADLQKKEEdcaELKEKFIDA 862
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERRE---ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 863 KKQ-------------------IEQVQREVSVMRDEEKLLRiKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK--ME 921
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdfLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKaeLE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 922 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGT 998
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
466-695 |
8.27e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 466 RNEKEEKAELNKQVVSLQQQL----RFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarS 541
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIktynKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE----D 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 542 IESNVSQIKQMQTKIDelrsldspshiSKIDLLNlQDLSSGAKGDNCLNTSQQLPGGDfsstwvkeyhtqeisrensfhA 621
Cdd:PHA02562 253 PSAALNKLNTAAAKIK-----------SKIEQFQ-KVIKMYEKGGVCPTCTQQISEGP---------------------D 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007265 622 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREE 695
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
442-988 |
8.75e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 442 EGNRVLKEKNEELKRLLTIGE--NELRNEKE----EKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQ 515
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAeiEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 516 TQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskidllNLQDLSSGAKgdnclNTSQQL 595
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-------------EAAELESELE-----EAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 596 pggdfsstwvkeyhtqeisreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQG 675
Cdd:PRK02224 380 ---------------------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 676 KNRdhqLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckrLVELE--- 752
Cdd:PRK02224 439 RER---VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED----LVEAEdri 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 753 QSILEKESAILKLEANLKEceakhqdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELA 832
Cdd:PRK02224 512 ERLEERREDLEELIAERRE---------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 833 ANsiltqnlkadlqkKEEdcaelkekfIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLK 912
Cdd:PRK02224 583 EL-------------KER---------IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007265 913 EQLSNQKMEEAVQQYEKVCKDLsvkEKLVEDMRLTLVEQEQTQAEQDRVlEAKSEEADWLATELDKWKEKFKDLET 988
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYL---EQVEEKLDELREERDDLQAEIGAV-ENELEELEELRERREALENRVEALEA 712
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
469-707 |
9.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 469 KEEKAELNKQVVSLQQQLRFFEEKNSSLRAD-----VEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIE 543
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 544 SN------VSQIKQMQTKIDELRSLDSPSHISKIDLLnlqdlssgakgdnclntsqqlpggdfsstwvkeyhtQEIsren 617
Cdd:COG3206 261 QSpviqqlRAQLAELEAELAELSARYTPNHPDVIALR------------------------------------AQI---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 618 sfhASIEAIWEEckEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGK--NRDHQLKEK--ESLIQQLR 693
Cdd:COG3206 301 ---AALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElyESLLQRLE 375
|
250
....*....|....*
gi 569007265 694 E-ELQEKSVSLRVQV 707
Cdd:COG3206 376 EaRLAEALTVGNVRV 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
675-926 |
9.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 675 GKNRDHQLKEKESLIQQLREEL---QEKSVSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIVEtqkdeckRLVEL 751
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAE----YSWDEIDVASAER-------EIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 752 EQSI--LEKESAILK-LEANLKECEAKHQDHIRT-NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQET--E 825
Cdd:COG4913 674 EAELerLDASSDDLAaLEEQLEELEAELEELEEElDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 826 KLKEELAANSI--LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRD---------EEKLLRIKINELEKKK 894
Cdd:COG4913 754 RFAAALGDAVEreLRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslpeyLALLDRLEEDGLPEYE 833
|
250 260 270
....*....|....*....|....*....|..
gi 569007265 895 NQYsqdLDMKQRTIQQLKEQLsNQKMEEAVQQ 926
Cdd:COG4913 834 ERF---KELLNENSIEFVADL-LSKLRRAIRE 861
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
687-913 |
1.12e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 687 SLIQQLREELQEKSVSLRVQVQLVAEREQALSEL----SQDVTCYKAKIKDLeviVETQKDECKRLVELEQSILEKESAI 762
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDEL---VEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 763 LKLEANLKECEAKHQDHIRTNDLSAKEVKFREE-----------------VTRLANNLHDtkqlLQSKEEENEISRQETE 825
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDELE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 826 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 905
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
....*...
gi 569007265 906 RTIQQLKE 913
Cdd:PHA02562 407 IVTDLLKD 414
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
457-927 |
1.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 457 LLTIGENELRNEKEE-------KAELN-KQVVSLQQQLRFFEEKNSSLRADVEQIQaSYNSAVAELQTQKAVNQEQRDRI 528
Cdd:COG4717 43 IRAMLLERLEKEADElfkpqgrKPELNlKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 529 LKLSQ------EMETAARSIESNVSQIKQMQTKIDELRSLdspshISKIDLLNLQdlssgakgdnclntsqqlpggdfss 602
Cdd:COG4717 122 EKLLQllplyqELEALEAELAELPERLEELEERLEELREL-----EEELEELEAE------------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 603 twVKEYHTQEISRENSFHASIEAIWEECKEivkasskkshQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQL 682
Cdd:COG4717 172 --LAELQEELEELLEQLSLATEEELQDLAE----------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 683 KEKESLIQQLRE--------ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQS 754
Cdd:COG4717 240 ALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 755 ILEKESAILKLEANLKECEAKHQ-DHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAA 833
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELlDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 834 NSILTQNLKADLQKKEE---------DCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKkknqySQDLDMK 904
Cdd:COG4717 400 LKEELEELEEQLEELLGeleellealDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAEL 474
|
490 500
....*....|....*....|...
gi 569007265 905 QRTIQQLKEQLSNQKMEEAVQQY 927
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKL 497
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
625-1107 |
1.27e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 625 AIWEECKEIVKASSKKSHQIQGLEEQIE-------KLQVEVKGYREensDLRAQESQGKNRDHQLKEKESLIQQLREELQ 697
Cdd:pfam12128 224 EHWIRDIQAIAGIMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKS---DETLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 698 EKSVSLR------------VQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKL 765
Cdd:pfam12128 301 EKRDELNgelsaadaavakDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 766 EANLKEceakhQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSK-----EEENEISRQETEKLKEELA------AN 834
Cdd:pfam12128 381 RSKIKE-----QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElreqlEAGKLEFNEEEYRLKSRLGelklrlNQ 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 835 SILTQNLKADLQKKEEDCAELKEKfidakkqIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 914
Cdd:pfam12128 456 ATATPELLLQLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 915 LSNQK-------MEEAVQQYEKVCKDLSVKEKLVEDMRLTLVE---------------------------QEQTQAEQDR 960
Cdd:pfam12128 529 LFPQAgtllhflRKEAPDWEQSIGKVISPELLHRTDLDPEVWDgsvggelnlygvkldlkridvpewaasEEELRERLDK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 961 VLEA------KSEEADWLATELDKWKEKFKDLETRSNQRLNtGTMDDLDVLTRKFSKLQDELQESEEKYKA----DRKKW 1030
Cdd:pfam12128 609 AEEAlqsareKQAAAEEQLVQANGELEKASREETFARTALK-NARLDLRRLFDEKQSEKDKKNKALAERKDsaneRLNSL 687
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 1031 LEEKAVLTTQAKEAENVRNREMRKYAddRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSS 1107
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1069-1355 |
1.48e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1069 VETLTAQLAEKNSELQK---------WREERDQLVTAVETQMKALLssckhkdEEIQELRKAAAKSTGTENQTMNPKPEY 1139
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALEEQEEVEE-------KEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1140 NDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTplqpnKMAVKHPGCPTPVTIKIP 1219
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1220 KARKRKSGEVEEDLVKCENKKNSTPRSNvkfpvsehrnspvkkeqkvSVGPSSKKTyslrSQASTVSANIASKKREGTLQ 1299
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVS-------------------AVQYSPPPP----SKRPDGESNGGSKPSSPTKK 1308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 569007265 1300 KFGDFLQHSPTILQSKAKKIIETMSSPKLST--VEVSKENVSQPKKAKRKLYRNEISS 1355
Cdd:PTZ00108 1309 KVKKRLEGSLAALKKKKKSEKKTARKKKSKTrvKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
918-1134 |
1.57e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 918 QKMEEAVQQYEKVCKDLSVKEKLVEDMR--LTLVEQEQTQAEQDRVLEAKSEEADWLA-----TELDKWKEKFKDLETRS 990
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELErqLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 991 NQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE---EKAVLTTQ---AKEAENVRNREMRKYADDRERCLK 1064
Cdd:TIGR02168 252 EEELEELT-AELQELEEKLEELRLEVSELEEEIEELQKELYAlanEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1065 LQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMN 1134
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
647-963 |
1.85e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 647 LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREEL-------------------------QEKSV 701
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrekheeleekykelsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 702 SLRVQvqlvAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEANLKECEAKHQDHI 780
Cdd:pfam07888 120 LLAQR----AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 781 RTNDLSAKE----VKFREEVTRLANNLHDTKQllqsKEEENEISRQETEKLKEELAANSILTQNLKADLQkkeedcaelk 856
Cdd:pfam07888 196 ELRNSLAQRdtqvLQLQDTITTLTQKLTTAHR----KEAENEALLEELRSLQERLNASERKVEGLGEELS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 857 ekfiDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSN-----QKMEEAVQQ- 926
Cdd:pfam07888 262 ----SMAAQRDRTQAELHQARLQAAQLTLQLADaslaLREGRARWAQERETLQQSAEADKDRIEKlsaelQRLEERLQEe 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 569007265 927 ------------YEKVCKDLSVKEKLVE------DMRLTLVEQEQTQAEQDRVLE 963
Cdd:pfam07888 338 rmereklevelgREKDCNRVQLSESRRElqelkaSLRVAQKEKEQLQAEKQELLE 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
423-945 |
1.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 423 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 502
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 503 IQA----------------SYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPS 566
Cdd:PRK03918 285 LKElkekaeeyiklsefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 567 HISKIDLLNLQDLSSGAKGDNCLNTSQQLPggdfSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKA--SSKKSHQI 644
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELE----ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkKAKGKCPV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 645 QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQ----ALSEL 720
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkyNLEEL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 721 SQDVTCY---KAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECeakhqdHIRTNDLSAKEVKFREEVT 797
Cdd:PRK03918 521 EKKAEEYeklKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFESVEELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 798 RLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansiltqnlkadlQKKEEDCAELKEKFIDAKKQIEQVQREVSVMR 877
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEEL--------------DKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007265 878 DEEKL-----LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAVQQYEKVCKDLSVKEKLVEDMR 945
Cdd:PRK03918 661 YEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVK 731
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
690-973 |
2.05e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 690 QQLREELQE-KSVSLRVQVQLVAEREQALSELS------QDVTCYKAKIKDLEVI-------VETQKDECKRL------V 749
Cdd:PRK10929 26 KQITQELEQaKAAKTPAQAEIVEALQSALNWLEerkgslERAKQYQQVIDNFPKLsaelrqqLNNERDEPRSVppnmstD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 750 ELEQSILEKESAILKLEANLKEceakHQDHIRtndlsakevkfreEVTRLANNLhdTKQLLQSKEEENEISRQetekLKE 829
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAR-------------EISDSLSQL--PQQQTEARRQLNEIERR----LQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 830 ELAANSILTQNLKADLQkkeedcAELKEKfidaKKQIEQVQREVSVMRDEEKLLRIKInELEKKKnqySQDLDMKqrtIQ 909
Cdd:PRK10929 163 LGTPNTPLAQAQLTALQ------AESAAL----KALVDELELAQLSANNRQELARLRS-ELAKKR---SQQLDAY---LQ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 910 QLKEQLSNQKMEEAVQQYEKVckdlsvkEKLVE---DMRLTLVEQEQTQAEQDRVLEAKSEEADWLA 973
Cdd:PRK10929 226 ALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIA 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
844-1100 |
2.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 844 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQkmeeA 923
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 924 VQQYEkvckdlsvkeklvEDMRLTLVEQeqtqaeqdrVLEAKSeeadwlateldkwkekFKDLETRsnqrlntgtMDDLD 1003
Cdd:COG3883 93 RALYR-------------SGGSVSYLDV---------LLGSES----------------FSDFLDR---------LSALS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1004 VLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSEL 1083
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250
....*....|....*..
gi 569007265 1084 QKWREERDQLVTAVETQ 1100
Cdd:COG3883 206 AAAEAAAAAAAAAAAAA 222
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
686-829 |
2.65e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 686 ESLIQQLREELQEKSVSLRVQVQLVAEREQALSElsqdvtcykAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKL 765
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEE---------EEIRRLEEQVERLEAE---VEELEAELEEKDERIERL 446
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007265 766 EANLKEceakhqdhIRTNdlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKE 829
Cdd:COG2433 447 ERELSE--------ARSE--ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
301-518 |
3.10e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 301 IKKQAELAHLYITSLVDPQ-EAIACLQLKFNQVKAELAETKEELIKAQEELKN--RESNSLVQALKTSSKVDTSLTSNKS 377
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNgENIARKQNKYDELVEEAKTIKAEIEELTDELLNlvMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 378 TCNETSEMpknsraqthserkrlNEDGlqlGEPPAkkglilVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRL 457
Cdd:PHA02562 273 QFQKVIKM---------------YEKG---GVCPT------CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007265 458 ltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQAS---YNSAVAELQTQK 518
Cdd:PHA02562 329 ----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDEL 388
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
794-1079 |
3.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 794 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREV 873
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 874 SVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQ 953
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 954 TQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEE 1033
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 569007265 1034 KAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEK 1079
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
425-833 |
3.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 425 EEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGE--NELRNEKEEKAELNKQVVSLQQQLRFFEE---KNSSLRAD 499
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELREleeELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 500 VEQIQASYNSAVAELQTQKAVN-QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQD 578
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 579 LSSGA-------KGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHAsieaiwEECKEIVKASSKKSHQIQGLEEQI 651
Cdd:COG4717 252 LLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG------KEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 652 EKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcykaki 731
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA----------- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 732 kdlevivETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEvkfrEEVTRLANNLHDTKQLLQ 811
Cdd:COG4717 395 -------EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE----EELEELREELAELEAELE 463
|
410 420
....*....|....*....|....
gi 569007265 812 SKEEENEIS--RQETEKLKEELAA 833
Cdd:COG4717 464 QLEEDGELAelLQELEELKAELRE 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
863-1124 |
4.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 863 KKQIEQVQREVsvmRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVE 942
Cdd:COG1196 199 ERQLEPLERQA---EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE-----AELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 943 DMRLTLVEQEQT-QAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRsnqrlntgtmddldvltrkfsklQDELQESEE 1021
Cdd:COG1196 271 ELRLELEELELElEEAQAEEYELLAELAR-LEQDIARLEERRRELEER-----------------------LEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1022 KYKADRKKWLEEKAVLTTQAKEAEnvrnremrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAvETQM 1101
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAA 395
|
250 260
....*....|....*....|...
gi 569007265 1102 KALLSSCKHKDEEIQELRKAAAK 1124
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER 418
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-962 |
5.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 643 QIQGLEEQIEKLQVEVKGYREENSDLRAQESqgknrdhQLKEKESLIQQLrEELQEKSVSLRVQVQLVAEREQALSEL-- 720
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELD-------ALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 721 -SQDVTCYKAKIKDLEVIVETQKDECKRLVE----LEQSILEKESAILKLEANLKECEAKHQDHIRTN-DLSAKEVKFRE 794
Cdd:COG4913 683 sSDDLAALEEQLEELEAELEELEEELDELKGeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 795 EVTRLANNLHDtkQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL-----------QKKEEDCAELKEKFIDAK 863
Cdd:COG4913 763 VERELRENLEE--RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpeylalldRLEEDGLPEYEERFKELL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 864 KQ--IEQVQREVSVMRDEEKLLRIKINELEK--KKNQYSQD----LDMKQRTIQQLKE------QLSNQKMEEAVQQYEK 929
Cdd:COG4913 841 NEnsIEFVADLLSKLRRAIREIKERIDPLNDslKRIPFGPGrylrLEARPRPDPEVREfrqelrAVTSGASLFDEELSEA 920
|
330 340 350
....*....|....*....|....*....|...
gi 569007265 930 VCKDLsvkEKLVEdmRLTLVEQEQTQAEQDRVL 962
Cdd:COG4913 921 RFAAL---KRLIE--RLRSEEEESDRRWRARVL 948
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
463-761 |
5.29e-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: 40.90 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 463 NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSI 542
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 543 ESNVSQIKQMqtkideLRSLDSPSHISKIDLLnlqdLSSgakgdnclntsqqlpggdfsstwvkeyhtqeisrensfhas 622
Cdd:COG4942 100 EAQKEELAEL------LRALYRLGRQPPLALL----LSP----------------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 623 ieaiwEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgknrdhqLKEKESLIQQLREELQEKSvs 702
Cdd:COG4942 129 -----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----------RAELEALLAELEEERAALE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569007265 703 lrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESA 761
Cdd:COG4942 192 -----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
647-959 |
5.63e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 647 LEEQIEKLQVEVkgyreensdLRAQESQGKNRDHQLKEK-ESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVT 725
Cdd:PLN03229 434 LEGEVEKLKEQI---------LKAKESSSKPSELALNEMiEKLKKEIDLEYTEAVIAMGLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 726 CYKAKIKDLEVIVE---------------TQKDECKRLVELEQSILEKESAILKLEAnlkECEAKHQDHIRTNDLSAKEV 790
Cdd:PLN03229 505 MHPVLMEKIEKLKDefnkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKA---EINKKFKEVMDRPEIKEKME 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 791 KFREEVtrlannlhdTKQLLQSKEEENEISRQETEKLKEELA---ANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIE 867
Cdd:PLN03229 582 ALKAEV---------ASSGASSGDELDDDLKEKVEKMKKEIElelAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 868 QVQREVS-----VMRDEEKLLRIKINELEKKKNQYSQDLDMKQrTIQQLKEQLsNQKMEEAVQQYEkvckdlsVKEKLvE 942
Cdd:PLN03229 653 SLNEEINkkierVIRSSDLKSKIELLKLEVAKASKTPDVTEKE-KIEALEQQI-KQKIAEALNSSE-------LKEKF-E 722
|
330
....*....|....*..
gi 569007265 943 DMRLTLVEQEQTQAEQD 959
Cdd:PLN03229 723 ELEAELAAARETAAESN 739
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
860-1120 |
6.10e-03 |
|
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: 40.88 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 860 IDAKKQIEQVQREVSVMRDEeklLRIKINELEKKKNQYSQDL---DMKQRTIQQLKEQLSNQKMEEAV--QQYEKVCKDL 934
Cdd:pfam17380 236 MERRKESFNLAEDVTTMTPE---YTVRYNGQTMTENEFLNQLlhiVQHQKAVSERQQQEKFEKMEQERlrQEKEEKAREV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 935 SVKEKLVEDMRLTLVE---QEQTQAEQDRVLEAKSEEADWLATEldkwkEKFKDLETRSNQRL--NTGTMDDLDVLT--- 1006
Cdd:pfam17380 313 ERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEIamEISRMRELERLQmer 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 1007 -RKFSKLQDELqESEEKYK---ADRKKWLEEKAVLTTQA-KEAENVRNREMRKYADDRERCL--------KLQNEVETLT 1073
Cdd:pfam17380 388 qQKNERVRQEL-EAARKVKileEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREMervrleeqERQQQVERLR 466
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569007265 1074 AQLAE-KNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRK 1120
Cdd:pfam17380 467 QQEEErKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK 514
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
793-1061 |
6.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 793 REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRE 872
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 873 VSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE 952
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 953 QTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE 1032
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260
....*....|....*....|....*....
gi 569007265 1033 EKAVLTTQAKEAENVRNREMRKYADDRER 1061
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
844-989 |
7.82e-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: 39.52 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 844 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEA 923
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007265 924 VQQYEKVCKDLSVKEKLVEDMRLTLVEQ-EQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETR 989
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
669-1093 |
7.95e-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: 40.93 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 669 RAQESQGKNrDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckRL 748
Cdd:pfam01576 16 KVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEE---RS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 749 VELEQSILEKESAILKLEANLKECEAKHQD-HIRTNDLSAKEVKFREEVTRLA---NNLHDTKQLLQSKEEENEISRQET 824
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEKVTTEAKIKKLEEDILLLEdqnSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 825 EK------------------LKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIK 886
Cdd:pfam01576 172 EEkakslsklknkheamisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 887 INELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqQYEKVCKDLS-----VKEKLVEDMRLTLVEQE---QTQAEQ 958
Cdd:pfam01576 252 LEEETAQKNNALKKIRELEAQISELQEDLESERAARN--KAEKQRRDLGeeleaLKTELEDTLDTTAAQQElrsKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 959 DRVLEAKSEEADWLATELDKWKEK-FKDLETRSNQ-----RLNTGTMDDLDVLTRKFSKLQDELQE-SEEKYKADRKKWL 1031
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKhTQALEELTEQleqakRNKANLEKAKQALESENAELQAELRTlQQAKQDSEHKRKK 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007265 1032 EEKAVLTTQAKEAENVRNRemrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1093
Cdd:pfam01576 410 LEGQLQELQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
794-914 |
8.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 794 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDcaELKEKFIDAKKQIEQVQREV 873
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKKEADEIIKEL 593
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 569007265 874 SVMRDEEKlLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 914
Cdd:PRK00409 594 RQLQKGGY-ASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
831-1001 |
9.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 831 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKqiEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 910
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK--ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 911 LKEQLSnqKMEEAVQQYEkvcKDLSVKEKLVED--MRLTLVEQEQTQAEQDRVLEAKSEEAdwLATELDKWKEKFKDLET 988
Cdd:PRK12705 103 LENQLE--EREKALSARE---LELEELEKQLDNelYRVAGLTPEQARKLLLKLLDAELEEE--KAQRVKKIEEEADLEAE 175
|
170
....*....|...
gi 569007265 989 RSNQRLNTGTMDD 1001
Cdd:PRK12705 176 RKAQNILAQAMQR 188
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
811-970 |
9.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 811 QSKEEENEISRQETEKLKEELaansiltQNLKADLQKkeedcaELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 890
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEI-------HKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007265 891 EKKKNQYSQ---DLDMKQRTIQQLK-------EQLSNQKMEEAVQQYEKvckdlSVKEKLVEDMRLTLVEQEQtqaeqdr 960
Cdd:PRK12704 113 EKKEKELEQkqqELEKKEEELEELIeeqlqelERISGLTAEEAKEILLE-----KVEEEARHEAAVLIKEIEE------- 180
|
170
....*....|
gi 569007265 961 vlEAKsEEAD 970
Cdd:PRK12704 181 --EAK-EEAD 187
|
|
| |
