|
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 |
8.27e-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: 8.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1 MKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSK-VQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETL 79
Cdd:cd01368 256 SRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETL 335
|
90
....*....|
gi 1720395285 80 NVLKFSTTAQ 89
Cdd:cd01368 336 HVMKFSAIAQ 345
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
2-89 |
6.06e-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: 119.21 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:smart00129 241 KTGAEGDRLKEAGNINKSLSALGNVINAL--AQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLST 318
|
....*...
gi 1720395285 82 LKFSTTAQ 89
Cdd:smart00129 319 LRFASRAK 326
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
2-91 |
9.93e-27 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 112.67 E-value: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQN-EGERLREAGNINTSLLTLGKCINVLknSEKSKvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLN 80
Cdd:pfam00225 239 KTGAaGGQRLKEAANINKSLSALGNVISAL--ADKKS-KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLS 315
|
90
....*....|.
gi 1720395285 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 |
3.94e-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: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd00106 242 KTGAEGDRLKEGGNINKSLSALGKVISAL--ADGQNK-HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLST 318
|
....*...
gi 1720395285 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 |
3.91e-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: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSeKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01370 257 ATNNRGQRLKEGANINRSLLALGNCINALADP-GKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNT 335
|
....*..
gi 1720395285 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 |
8.22e-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: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01374 234 QTGAAGVRRKEGSHINKSLLTLGTVISKL--SEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
90
....*....|
gi 1720395285 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 |
1.13e-18 |
|
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: 88.80 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNseksKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01366 242 KSGATGDRLKETQAINKSLSALGDVISALRQ----KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
90
....*....|
gi 1720395285 82 LKFsttAQRV 91
Cdd:cd01366 318 LRF---ASKV 324
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
212-266 |
4.85e-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: 79.06 E-value: 4.85e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720395285 212 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 266
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-905 |
7.33e-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: 90.12 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 141 VLENEDLVEDLEENEETQN-METELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIRE-EVT 218
Cdd:TIGR02168 231 VLRLEELREELEELQEELKeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 219 QEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDEPTNRICDIELETEEAIACLQLKFNQVKAELAE 298
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 299 TKEELIKAQEELKNRESnslvqalktsskvdtsltsnkstcneTSEMPKNSRAQTHSERKRLNEDglqlgeppakkgliL 378
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--------------------------RLERLEDRRERLQQEIEELLKK--------------L 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 379 VSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRA 458
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 459 --DVEQIQASYNSAVAEL-----QTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLdSPSHISKI 531
Cdd:TIGR02168 511 llKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSI-KGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 532 DLLNLQDLSSGAK-GDNCLNTSQQLPG--GDFSST--WVKEYHT-QEISRENSFHASI----EAIWEECKEIVKASSKKS 601
Cdd:TIGR02168 590 DREILKNIEGFLGvAKDLVKFDPKLRKalSYLLGGvlVVDDLDNaLELAKKLRPGYRIvtldGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 602 HQIQG-------LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAERE 674
Cdd:TIGR02168 670 SSILErrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 675 QALSELSQDVTCYKAKIKDLEVIVETQKDECKR-LVELEQSILEKESAILKLEANLKECEAKHQdhirtnDLSAKEVKFR 753
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQIEQLKEELKALREALDELRAELT------LLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 754 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREV 833
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395285 834 SVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMR 905
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEyslTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| 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 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLkNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01372 252 RTGATGDRLKEGISINSGLLALGNVISAL-GDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNT 330
|
....*....
gi 1720395285 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 |
3.07e-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: 81.99 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 5 NEGERLREAGNINTSLLTLGKCINVLknSEKSKvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKF 84
Cdd:cd01364 262 AVDKRAREAGNINQSLLTLGRVITAL--VERAP--HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEY 337
|
....
gi 1720395285 85 STTA 88
Cdd:cd01364 338 AHRA 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-1045 |
3.53e-16 |
|
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: 84.34 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 244 EENAERRLAI--FKDLVGKCDSQDEPTNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAQEELKNresnslvqa 321
Cdd:TIGR02168 222 LRELELALLVlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA--------- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 322 lktsskvdtsLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLIL--VSPPITEEQNKMGEMQQSVSE 399
Cdd:TIGR02168 293 ----------LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 400 VVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASY-NSAVAELQTQK 478
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 479 AVNQEQRDRILKLSQEMETAARSIESNVSQIKQ-MQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGdncLNTSQQLPG 557
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQaLDAAERELAQLQARLDSLERLQENLEGFSEGVKA---LLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 558 GDFSSTWvkeyhtQEISRENSFHASIE-AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKgyreENSDLRAQESQGK 636
Cdd:TIGR02168 520 GILGVLS------ELISVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFL----PLDSIKGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 637 NRdhQLKEKESLIQQLREELQEKSVSLRV-------QVQLVAEREQALSELSQDVTCYKAKIKDLEVI----VETQKDEc 705
Cdd:TIGR02168 590 DR--EILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggVITGGSA- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 706 krlvELEQSILEKESAILKLEANLKECEAKhqdhirTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETE 785
Cdd:TIGR02168 667 ----KTNSSILERRREIEELEEKIEELEEK------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 786 KLKEELaansiltqnlkadlQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 865
Cdd:TIGR02168 737 RLEAEV--------------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 866 RTIQQLKEQLSNQKMEEAVQQ--YEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKF 943
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 944 KDLETRSNQRLntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCL 1023
Cdd:TIGR02168 883 ASLEEALALLR-----SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
810 820
....*....|....*....|..
gi 1720395285 1024 KLQNEVETLTAQLAEKNSELQK 1045
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLEN 979
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
2-91 |
3.88e-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: 81.63 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVL----KNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDE 77
Cdd:cd01365 261 STGATGDRLKEGANINKSLTTLGKVISALadmsSGKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEE 340
|
90
....*....|....
gi 1720395285 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 |
5.13e-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: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSeksKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01371 248 KTGATGERLKEATKINLSLSALGNVISALVDG---KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLST 324
|
90
....*....|
gi 1720395285 82 LKFSTTAQRV 91
Cdd:cd01371 325 LRYANRAKNI 334
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
2-310 |
1.89e-14 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 78.24 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINAL--GDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINT 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 82 LKFS-------TTAQRVYVPDTLSSSQEKSFASNKSLQDVSLDSNLDNKILNVKRKTVSWENSLEDVLENEDL--VEDLE 152
Cdd:COG5059 327 LKFAsraksikNKIQVNSSSDSSREIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLksRIDLI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 153 ENEETQNMETELTDEdsdKSLEECRVSTCHK----KNKELLDLIEKLNKRLINENK-EKLTLELKIREEVTQEFTQYWSQ 227
Cdd:COG5059 407 MKSIISGTFERKKLL---KEEGWKYKSTLQFlrieIDRLLLLREEELSKKKTKIHKlNKLRHDLSSLLSSIPEETSDRVE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 228 RE--ADFKETLLHereILEENAERRLAIFKDLVGKcdsqdepTNRICDIELETEEAIACLQLKFNQVKAELAETKEELIK 305
Cdd:COG5059 484 SEkaSKLRSSAST---KLNLRSSRSHSKFRDHLNG-------SNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSLNK 553
|
....*
gi 1720395285 306 AQEEL 310
Cdd:COG5059 554 SLSSL 558
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
649-951 |
4.09e-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: 77.79 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 649 IQQLREELQEKSVSLRVQVQLvAEREQALSE---------LSQDVTCYKAKIKDLEVIVETQKDECK----RLVELEQSI 715
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEK-AERYKELKAelrelelalLVLRLEELREELEELQEELKEAEEELEeltaELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 716 LEKESAILKLEANLKECEAKHQDH-IRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAN 794
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 795 SILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 874
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 875 LSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSN 951
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
3-91 |
5.42e-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: 74.85 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 3 TQNEGERLREAGNINTSLLTLGKCINVLKNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVL 82
Cdd:cd01373 249 THAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTL 328
|
....*....
gi 1720395285 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 |
7.43e-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: 74.08 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01376 236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLST 311
|
...
gi 1720395285 82 LKF 84
Cdd:cd01376 312 LNF 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-1053 |
1.94e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 407 LKEKNEELKRLLTIGE-----NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVN 481
Cdd:TIGR02168 218 LKAELRELELALLVLRleelrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 482 QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGAKGdNCLNTSQQLpggdfs 561
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE----------ELAELEEKLEELKE-ELESLEAEL------ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 562 stwvKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGK 636
Cdd:TIGR02168 361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 637 NRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiL 716
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-Q 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 717 EKESAILKLEANLKECEAKHQ-----------------------------------------------DHIRTNDLSAKE 749
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 750 ------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSILtq 799
Cdd:TIGR02168 596 niegflgvakdlVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSIL-- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 800 NLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK 879
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 880 MEEAVQQYEKVckdlsVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTM 959
Cdd:TIGR02168 754 KELTELEAEIE-----ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 960 ---------DDLDVLTRKFSKLQ----------DELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRE 1020
Cdd:TIGR02168 829 lerriaateRRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750
....*....|....*....|....*....|...
gi 1720395285 1021 RCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1053
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-1082 |
2.01e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 407 LKEKNEELKRL-LTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQR 485
Cdd:TIGR02168 215 YKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 486 DRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSSGAKGDNCLNTSQQLPGGdfsstwV 565
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELES--------KLDELAEELAELEEKLEELKEELESLEAE------L 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 566 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGKNRDH 640
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 641 QLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiLEKES 720
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 721 AILKLEANLKECEAK-----------HQDHIRTNDLSA--KEVKFREE-----VTRLANNLHDTKQLLQSKEEENE---- 778
Cdd:TIGR02168 520 GILGVLSELISVDEGyeaaieaalggRLQAVVVENLNAakKAIAFLKQnelgrVTFLPLDSIKGTEIQGNDREILKnieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 779 ----ISRQETEKLKEELAANSILTQNLKAD-LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL------LRIKI 847
Cdd:TIGR02168 600 flgvAKDLVKFDPKLRKALSYLLGGVLVVDdLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssileRRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 848 NELEKKKNQYSQDLDMKQRTIQQLKEQLSN---------QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQ 918
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 919 DRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRlntgtMDDLDVLTRKFSKLQDELQESEEKYKADRkkwlEEKAVLT 998
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----KEELKALREALDELRAELTLLNEEAANLR----ERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 999 TQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALLSSCKHKDEEIQEL 1078
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELEELSEELREL 906
|
....
gi 1720395285 1079 RKAA 1082
Cdd:TIGR02168 907 ESKR 910
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
781-1053 |
5.51e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 781 RQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQrevsvmrDEEKLLRIKINELEKKKNQYSQD 860
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 861 LDMKQRTIQQLKEQLS--NQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQtqaeqdRVLEAKSEEADWLATELDK 938
Cdd:COG1196 311 RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 939 WKEKFKDLETRSNQRlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADD 1018
Cdd:COG1196 385 AEELLEALRAAAELA-----------------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*
gi 1720395285 1019 RERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1053
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
580-1084 |
1.62e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 580 HASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 659
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 660 SVSLRVQVQLVAEREQALSELSQDVtcyKAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKLEANLKECEAKHQDH 739
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 740 IRtndlsaKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKF 819
Cdd:COG1196 392 LR------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 820 IDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEK 899
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 900 LVEDMRLTLVEQEQTQAEQDRVLEAKSEEAdwlATELDKWKEKFKDLETRSNQRLntgtmddldVLTRKFSKLQDELQES 979
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGR---ATFLPLDKIRARAALAAALARG---------AIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 980 EEKYKAdrkkwLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVET 1059
Cdd:COG1196 612 DARYYV-----LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500
....*....|....*....|....*
gi 1720395285 1060 QMKALLSSCKHKDEEIQELRKAAAK 1084
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 |
3.93e-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: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQ-SFFTGKGKICMIINISQSCSAYDETLN 80
Cdd:cd01367 244 TSSADRQTRMEGAEINKSLLALKECIRALGQNKA----HIPFRGSKLTQVLKdSFIGENSKTCMIATISPGASSCEHTLN 319
|
....*
gi 1720395285 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 |
2.35e-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: 66.58 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSkvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01369 239 KTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT---HIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
90
....*....|
gi 1720395285 82 LKFSTTAQRV 91
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-91 |
3.08e-11 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 68.42 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 3 TQNEGERLREAGNINTSLLTLGKCINVLKN-SEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:PLN03188 345 TGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFST 424
|
90
....*....|
gi 1720395285 82 LKFSTTAQRV 91
Cdd:PLN03188 425 LRFAQRAKAI 434
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
183-1031 |
9.30e-11 |
|
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: 66.92 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 183 KKNKELLDLIEKLNKRLINENKEKLTLE-LKIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRL--------AI 253
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLqellrdeqEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 254 FKDLVGKCDSQDEPTNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAqEELKNRESNSLVQALKTSSKVDTSLT 333
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 334 SNKSTCNETSEMPKNSRAQTHSE-------RKRLNEDGLQLGEPPAKKGLILVSPPITEE--QNKMGEMQQSVSEVVEGN 404
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEeeeeeelEKLQEKLEQLEEELLAKKKLESERLSSAAKlkEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 405 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQiqasynSAVAELQTQKAVNQEQ 484
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK------SEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 485 RDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNClntsqqlpgGDFSSTW 564
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---------IVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 565 VKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQL-K 643
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELtK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 644 EKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSI--LEKESA 721
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREkeELKKLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 722 ILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNL 801
Cdd:pfam02463 717 LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 802 KADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKME 881
Cdd:pfam02463 797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 882 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSNQRLNTGTMDD 961
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE-EAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 962 LDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVET 1031
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-726 |
1.22e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 383 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 462
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 463 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRsldspshiSKIDLLN--LQDLS 540
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTLLNeeAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 541 SGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRE--NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEV 618
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 619 KGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK-----SVSLRVQVQLVAEREQALSELSQDVTCYKAKIKD 693
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720395285 694 LEVI----VETQKDECKRLVELEQSILEKESAILKLE 726
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 |
1.70e-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: 57.46 E-value: 1.70e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720395285 212 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 266
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
572-928 |
3.25e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 572 EISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEvKGYREENSDLRA--QESQGKNRDHQLKEKESLI 649
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKekREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 650 QQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdecKRLVELEQSILEKESAILKLEANL 729
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---------EEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 730 KECEAKHQDhirtndLSAKEVKFREEvtrlannLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKE 809
Cdd:TIGR02169 311 AEKERELED------AEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 810 EDCAELKEKFIDAKKQIEQVQREV-SVMRDEEKL-------------LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQL 875
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREInELKRELDRLqeelqrlseeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395285 876 SN--QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE-QTQAEQDRVLEAKSEE 928
Cdd:TIGR02169 458 EQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
708-1083 |
3.69e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 708 LVELEQSI--LEKESAI----LKLEANLKECEAKHQdHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISR 781
Cdd:COG1196 195 LGELERQLepLERQAEKaeryRELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 782 QETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL 861
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 862 DMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKE 941
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAE-----EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 942 KFKDLEtrsnqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRER 1021
Cdd:COG1196 429 ALAELE-----------------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720395285 1022 CLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAA 1083
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
570-1081 |
4.38e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 570 TQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKG-------YREENSDLRAQ-ESQGKNRDHQ 641
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereeLAEEVRDLRERlEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 642 LKEKE------SLIQQLREELQEKSVSLRvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlvELEQSI 715
Cdd:PRK02224 299 LAEAGlddadaEAVEARREELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA---ELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 716 LEKESAILKLEANLKECEakhqdhirtndlsakevkfrEEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAans 795
Cdd:PRK02224 373 EEAREAVEDRREEIEELE--------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 796 iltqNLKADLQKKEEDCAElKEKFIDAKK---------------QIEQVQREVSVMRDEEKLLRIKINELEKKKNQySQD 860
Cdd:PRK02224 430 ----ELEATLRTARERVEE-AEALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 861 LDMKQRTIQQLKEQLSNqkmeeavqqyekVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWK 940
Cdd:PRK02224 504 LVEAEDRIERLEERRED------------LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 941 EKFKDLETRSNQrlNTGTMDDLDvltrKFSKLQDELQESEEKYKADRKKwLEEKAVLTTQAKE---AENVRNREMRKYAD 1017
Cdd:PRK02224 572 EEVAELNSKLAE--LKERIESLE----RIRTLLAAIADAEDEIERLREK-REALAELNDERRErlaEKRERKRELEAEFD 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 1018 DrERCLKLQNEVETLTAQLAEKNSELQKWREERDQL---VTAVETQMKALlssckhkdEEIQELRKA 1081
Cdd:PRK02224 645 E-ARIEEAREDKERAEEYLEQVEEKLDELREERDDLqaeIGAVENELEEL--------EELRERREA 702
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
2-91 |
9.07e-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: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 2 KTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNV 81
Cdd:cd01375 250 KTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKDR-THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLST 326
|
90
....*....|
gi 1720395285 82 LKFsttAQRV 91
Cdd:cd01375 327 LRF---ASRV 333
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-920 |
1.70e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 383 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELkrlltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 462
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 463 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSpshiskidllnlqdlssg 542
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------------------ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 543 akgdnclntsqqlpggdfsstwvkEYHTQEISREnsfhASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR 622
Cdd:COG1196 418 ------------------------RLEEELEELE----EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 623 EENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAER--EQALSELSQDVTCYKAKIKD------L 694
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAALEAalaaalQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 695 EVIVETQKDECKRLVELEQSILEKESAI----LKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLL 770
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 771 QSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 850
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 851 EKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEkvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDR 920
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
352-1059 |
2.43e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 352 QTHSERKRLNEDGlQLGEppakKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEE 431
Cdd:pfam15921 86 QVKDLQRRLNESN-ELHE----KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 432 KAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAelqtQKAVNQEQRDRI--LKLSQEMETAARSIESNVSQI 509
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG----KKIYEHDSMSTMhfRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 510 KQMQTKI-DELRSLDSPSHiSKIDLLNLQDLSsgakgdnclNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWE 588
Cdd:pfam15921 237 KGRIFPVeDQLEALKSESQ-NKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 589 ECKeivKASSKKSHQIQGLEEQIEKLQVEVKG----YREENSDLRAQ--------ESQGKNRDHQLKEKESLIQQLREEL 656
Cdd:pfam15921 307 QAR---NQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEELEKQlvlanselTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 657 -----QEKSVSL-RVQVQLVAEREQA----LSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLE 726
Cdd:pfam15921 384 adlhkREKELSLeKEQNKRLWDRDTGnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 727 ANLKECEAKHQDHIR--TNDLSAKEVKFREEvtrlANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKAD 804
Cdd:pfam15921 464 SSLTAQLESTKEMLRkvVEELTAKKMTLESS----ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 805 ---LQKKEEDCAELKEKFIDAKKQIEqvqrevsvmrdeekLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKME 881
Cdd:pfam15921 540 gdhLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 882 EAVQQYEKVCKDLSVK--EKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrsnqrlntgtm 959
Cdd:pfam15921 606 LQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS------------ 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 960 DDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREM-------RKYADDRERCLKLQNEVETL 1032
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQIDALQSKIQFL 753
|
730 740
....*....|....*....|....*..
gi 1720395285 1033 TAQLAEKNSELQKWREERDQLVTAVET 1059
Cdd:pfam15921 754 EEAMTNANKEKHFLKEEKNKLSQELST 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
643-883 |
3.09e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 643 KEKESLIQQLRE---ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdeckRLVELEQSILEKE 719
Cdd:TIGR02169 688 RELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE----------DLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 720 SAILKLEANLKECEAK-------------HQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEK 786
Cdd:TIGR02169 758 SELKELEARIEELEEDlhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 787 LKEELaansILTQNLKADLQKKEEDC----AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLD 862
Cdd:TIGR02169 838 LQEQR----IDLKEQIKSIEKEIENLngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260
....*....|....*....|.
gi 1720395285 863 MKQRTIQQLKEQLSNQKMEEA 883
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELS 934
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
699-1126 |
8.07e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 699 ETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTND--LSAKEVKFREEVTRLANNLHDTKQLLQSKEEE 776
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 777 NEisRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLlriKINELEKKKNQ 856
Cdd:PTZ00121 1328 KK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 857 YsqdldmKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATEL 936
Cdd:PTZ00121 1403 D------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 937 DKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKfSKLQDELQESEEKYKADRKKWLEEK-----AVLTTQAKEAENVRNRE 1011
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1012 MRKYADDRERCLKLQNEVETLTAQLaEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEE----IQELRKAAAKSTG 1087
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMAL-RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKK 1634
|
410 420 430
....*....|....*....|....*....|....*....
gi 1720395285 1088 TENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAED 1126
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-1003 |
1.18e-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: 59.70 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 392 EMQQSVSEVVEGNRVLKEKNEELKRLltiGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAV 471
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 472 AELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSSGAKGDNCLNT 551
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 552 SQQLpggdfsstwvkeyhTQEISRensFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ 631
Cdd:TIGR02169 415 LQRL--------------SEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 632 ESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAK-IKDLE---------VIVETQ 701
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEvaagnrlnnVVVEDD 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 702 KDECK---------------------RLVELEQSILEKESAILKLeANLKECEAKHQ--------DHIRTNDL-SAKE-- 749
Cdd:TIGR02169 558 AVAKEaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFA-VDLVEFDPKYEpafkyvfgDTLVVEDIeAARRlm 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 750 ---------------------------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSI 796
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 797 LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL------------DMK 864
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlshsriPEI 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 865 QRTIQQLKEQLSnqKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQ-----EQTQAEQDRVLEAKSEEADwLATELDKW 939
Cdd:TIGR02169 797 QAELSKLEEEVS--RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkEQIKSIEKEIENLNGKKEE-LEEELEEL 873
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720395285 940 KEKFKDLETRsnqrlNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKE 1003
Cdd:TIGR02169 874 EAALRDLESR-----LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-949 |
1.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 407 LKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRD 486
Cdd:COG1196 234 LRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 487 RILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLpggdfsSTWVK 566
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------EELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 567 EYHT--QEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKE 644
Cdd:COG1196 384 LAEEllEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 645 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVEtQKDECKRLVELEQSILEKESAILK 724
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 725 LEAnlkeceAKHQDHIRTNDLSAKEV------KFREEVTRLANNLHDTKQLLQSKEEENEISR-------------QETE 785
Cdd:COG1196 543 ALA------AALQNIVVEDDEVAAAAieylkaAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvasdlreadARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 786 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 865
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 866 RTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlateLDKWKEKFKD 945
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELER 771
|
....
gi 1720395285 946 LETR 949
Cdd:COG1196 772 LERE 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
566-1084 |
1.47e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 566 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEK 645
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 646 ESLIQQLREELQEKSVSLRVQVQLVAE------REQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKE 719
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKElkelkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 720 SAILKLEANLKECEAK----HQDHIRTNDLSAKEVKFREEVTRLAN-NLHDTKQLLQSKEEENEISRQETEKLKEELAAN 794
Cdd:PRK03918 338 ERLEELKKKLKELEKRleelEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 795 SILTQNLKADLQK---------------KEEDCAELKEKFidaKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ 859
Cdd:PRK03918 418 KKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 860 DLDMKQ--RTIQQLKEQLSN---QKMEEAVQQYEKVCKD---LSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 931
Cdd:PRK03918 495 LIKLKElaEQLKELEEKLKKynlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 932 LATEL--------DKWKEKFKDLETRSNQRLN-TGTMDDLDVLTRKFSKLQDELQESEEKYkADRKKWLEEkavLTTQAK 1002
Cdd:PRK03918 575 LLKELeelgfesvEELEERLKELEPFYNEYLElKDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEE---LRKELE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1003 EAENVRNREmrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLvtavetqmKALLSSCKHKDEEIQELRKAA 1082
Cdd:PRK03918 651 ELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL--------KEELEEREKAKKELEKLEKAL 720
|
..
gi 1720395285 1083 AK 1084
Cdd:PRK03918 721 ER 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
565-1053 |
2.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 565 VKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgKNRDHQLKE 644
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 645 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILK 724
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 725 LEANLKECEAKHQdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansiltqnlkad 804
Cdd:PRK03918 326 IEERIKELEEKEE---RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL------------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 805 lqkkEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKK-------------------NQYSQDLDMKQ 865
Cdd:PRK03918 390 ----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 866 RTIQQLKEQLSNQKME-EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQdrvLEAKSEEADWLATELDKWKEKFK 944
Cdd:PRK03918 466 KELKEIEEKERKLRKElRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 945 DLETRSNQrlntgtmddLDVLTRKFSKLQDELQESEEKyKADRKKWLEEKAV-----LTTQAKEAENVRNR--EMRKYAD 1017
Cdd:PRK03918 543 SLKKELEK---------LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEK 612
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1720395285 1018 DRERCLK----LQNEVETLTAQLAEKNSELQKWREERDQL 1053
Cdd:PRK03918 613 ELEREEKelkkLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
605-1079 |
4.22e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 605 QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQdv 684
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAE-- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 685 tcykaKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEAnLKECEAKHQDHIRTNDLSAKEvkFREEVTRLANNL 763
Cdd:PRK02224 280 -----EVRDLRERLEELEEERDDLLaEAGLDDADAEAVEARREE-LEDRDEELRDRLEECRVAAQA--HNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 764 HDTkqllqskEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLL 843
Cdd:PRK02224 352 DDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 844 RIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqqyEKVCKdLSVKEKLVEDMRLTLVEQEQTQAEQDRVLE 923
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGS----PHVET-IEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 924 aKSEEADWLATELDKWKEKFKDLETRSNQRlNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKe 1003
Cdd:PRK02224 500 -RAEDLVEAEDRIERLEERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE- 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395285 1004 aenvRNREMRKYADDRERClklqNEVETLTAQLAEKNSELQKWREERDQLvTAVETQMKALLSSckhKDEEIQELR 1079
Cdd:PRK02224 577 ----LNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAE---KRERKRELE 640
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-755 |
5.53e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 405 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQ 484
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 485 RDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGgdfSSTW 564
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN---RLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 565 VKEYHTQEIsrensfhASIEAIWEECKEIVKASSKKSHQIQG----LEEQIEKLQVEVKGYREENSDLRAQEsqgKNRDH 640
Cdd:TIGR02169 827 EKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDLESRLGDLKKER---DELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 641 QLKEKESLIQQLREELQEKSvslrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlveLEQSILEKES 720
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKR-------KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----VQAELQRVEE 965
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720395285 721 AILKLE-ANLKECEAKHQDHIRTNDLSAKEVKFREE 755
Cdd:TIGR02169 966 EIRALEpVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-828 |
9.60e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 277 ETEEAIACLQLKFNQVKAELAETKEELIKAQEELkNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEmpknSRAQTHSE 356
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 357 RKRLNEDGLQLgeppaKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELN 436
Cdd:COG1196 325 LAELEEELEEL-----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 437 KQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKI 516
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 517 DELRSLDSPSHISKIDLLNLQDLSSGAkgdnclntsqqlpggdfsSTWVKEYHTQEISRENSFHASIEAIWEECKE--IV 594
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGF------------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 595 KASSKKSHQI-----QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQL 669
Cdd:COG1196 542 AALAAALQNIvveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 670 VAEReqALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKE 749
Cdd:COG1196 622 LLGR--TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720395285 750 VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQ 828
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
649-1083 |
9.95e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 649 IQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVtcYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEAN 728
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELR----------AELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 729 LKECEAKHQDH--IRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQ 806
Cdd:COG4913 325 LDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 807 KKEEDCAELKEKFIDAKKQIEQVQREvsvmrdeekllrikINELEKKKNQYSQDLdmkQRTIQQLKEQLS---------- 876
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAE--------------IASLERRKSNIPARL---LALRDALAEALGldeaelpfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 877 --------NQKMEEAV---------------QQYEKVCK---DLSVKEKLV-EDMRLTLVEQEQTQAEQD---RVLEAKS 926
Cdd:COG4913 465 elievrpeEERWRGAIervlggfaltllvppEHYAAALRwvnRLHLRGRLVyERVRTGLPDPERPRLDPDslaGKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 927 EEA-DWLATELDKWK--------EKFKDLE---TRSNQRLNTGTM---DD-----------------LDVLTRKFSKLQD 974
Cdd:COG4913 545 HPFrAWLEAELGRRFdyvcvdspEELRRHPraiTRAGQVKGNGTRhekDDrrrirsryvlgfdnrakLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 975 ELQESEEKY---KADRKKWLEEKAVLTTQAKEAENVRN-----REMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKW 1046
Cdd:COG4913 625 ELAEAEERLealEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASSDDLAALEEQLEELEAELEEL 704
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1720395285 1047 REERDQL---VTAVETQMKALLSSCKHKDEEIQELRKAAA 1083
Cdd:COG4913 705 EEELDELkgeIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
583-1079 |
2.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 583 IEAIWEECKEIVKASSKKShqiQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVS 662
Cdd:COG4717 48 LERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 663 LRVQvQLVAEREQALSELSQDVTCYKakikdlevivetqkdeckRLVELEQSILEKESAILKLEANLKECEAKHQDHIRT 742
Cdd:COG4717 125 LQLL-PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 743 NDLSAKE--VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFI 820
Cdd:COG4717 186 LSLATEEelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 821 DAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQlsnqkmeeavqQYEKVCKDLSVKEKL 900
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE-----------ELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 901 VEDMRLTLVEQEQTQAEQDRVLEAKSEEADWlateldkwkekfKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDelqese 980
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQL------------EELEQEIAALLAEAGVEDEEELRAALEQAEE------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 981 ekykadRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRerclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQ 1060
Cdd:COG4717 397 ------YQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAEL----EAE 461
|
490
....*....|....*....
gi 1720395285 1061 MKALLSsckhkDEEIQELR 1079
Cdd:COG4717 462 LEQLEE-----DGELAELL 475
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
770-984 |
5.74e-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: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 770 LQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINE 849
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 850 LEKKKNQYSQDLDMKQRTIQQLKEQ------LSNQKMEEAVqqyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLE 923
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395285 924 AKSEEADWLATELDKWKEKFKDLETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEKYK 984
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAE 223
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
394-917 |
1.16e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 394 QQSVSEVVEGNRVLKEKNEELKRLLTIGENEL---RNEKEEKAELNKQVVSLQ------QQLRFFEEKNSSLRADVeqiq 464
Cdd:COG5022 771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLlslLGSRKEYRSYLACIIKLQktikreKKLRETEEVEFSLKAEV---- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 465 aSYNSAVAELQTQKAVNQEQRDRIL-----------KLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDL 533
Cdd:COG5022 847 -LIQKFGRSLKAKKRFSLLKKETIYlqsaqrvelaeRQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEF 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 534 LNlqDLSSGAKgdnclntsQQLPGGDFSSTWVKEYHTQEISRE-NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIE 612
Cdd:COG5022 926 KT--ELIARLK--------KLLNNIDLEEGPSIEYVKLPELNKlHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 613 KLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQvQLVAEREQALSELSqdvtcykAKIK 692
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQ-KLKGLLLLENNQLQ-------ARYK 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 693 DLEVIVETQKDECKRLVELE-QSILEKesailklEANLKECEAKHQDHIrtndLSAKEVKFREEVTRLANNLHDTKQLLQ 771
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLEsTENLLK-------TINVKDLEVTNRNLV----KPANVLQFIVAQMIKLNLLQEISKFLS 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 772 SKEEENEISRQETEKLKEELAANSILTQN--------LKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK-- 841
Cdd:COG5022 1137 QLVNTLEPVFQKLSVLQLELDGLFWEANLealpspppFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFsg 1216
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 842 -LLRIKINELEKKKNQYSQdldmkqrTIQQLKEQLSNQKmEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAE 917
Cdd:COG5022 1217 wPRGDKLKKLISEGWVPTE-------YSTSLKGFNNLNK-KFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPAT 1285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
805-1053 |
1.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 805 LQKKEEDCAELKEKFIDAKKQIEQVQREVsvmrdeeKLLRIKINELEKKKNQYSQDLDMK--QRTIQQLKEQL-----SN 877
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 878 QKMEEAVQQYEKVCKDLSVKEKLVEDM--RLTLVEQEQTQAE------QDRVLEAKSEEADWLATELDKWKEKFKDLETR 949
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELkgEIGRLEKELEQAEeeldelQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 950 SNQRLNTGtmDDLDVLTRKFSKLQDELQESEEKYKADrkkWLEEKAVLTTQAKEAENVRNREMRKYADD----RERCLKL 1025
Cdd:COG4913 765 RELRENLE--ERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLDRLEEDGlpeyEERFKEL 839
|
250 260
....*....|....*....|....*....
gi 1720395285 1026 QNevETLTAQLAEKNSELQKWREE-RDQL 1053
Cdd:COG4913 840 LN--ENSIEFVADLLSKLRRAIREiKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
778-1051 |
2.36e-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: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 778 EISRQETEKLKEElAANSILTQNLKADLQKKEEdcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQY 857
Cdd:TIGR02169 194 DEKRQQLERLRRE-REKAERYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 858 SQDLDMKQRTIQQLKEQLSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLAT 934
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 935 ELDKWKEKFKDLETRSN---QRL------NTGTMDDLDVLTRKFSKLQDELQESeekyKADRKKWLEEKAVLTTQAKEAE 1005
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEdlrAELeevdkeFAETRDELKDYREKLEKLKREINEL----KRELDRLQEELQRLSEELADLN 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720395285 1006 NvrnremrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1051
Cdd:TIGR02169 427 A-------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
630-885 |
2.60e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 630 AQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEvivetqkdecKRLV 709
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----------AELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 710 ELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLsaKEVKFREEVTRLANNLHDTKQLLQSKeeeneisRQETEKLKE 789
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL--ALLLSPEDFLDAVRRLQYLKYLAPAR-------REQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 790 ELAANSILTQNLKADLQKKEEDCAELKEKfidaKKQIEQVQREVsvmrdeekllRIKINELEKKKNQYSQDLDMKQRTIQ 869
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEE----RAALEALKAER----------QKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*.
gi 1720395285 870 QLKEQLSNQKMEEAVQ 885
Cdd:COG4942 224 ELEALIARLEAEAAAA 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
405-968 |
2.90e-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: 52.04 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 405 RVLKEKNEELKRLltigENELRNEKEE-KAELNKQVVSLQQQLRFFEeKNSSLRADVEQIQASYNSAVAELQTQKAVNQE 483
Cdd:pfam15921 419 RELDDRNMEVQRL----EALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 484 QRDRILKLSQEMETAARSIESNVSQIKQMQTKIDelrsldspshiskIDLLNLQDLSSgaKGDNCLNTSQQLPGGDFSST 563
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVD-------------LKLQELQHLKN--EGDHLRNVQTECEALKLQMA 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 564 wvKEYHTQEISRENSfhasieaiwEECKEIVKASSKKSHQIQGLEEQIEKlqvEVKGYREENSDLRAQESQgknRDHQLK 643
Cdd:pfam15921 559 --EKDKVIEILRQQI---------ENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEFKILKDK---KDAKIR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 644 EKESLIQQLREE----LQEKSVSLRVQVQLVAEREQALSE----------LSQDVTCYKAKIKDLEVIVETQKDECKRLV 709
Cdd:pfam15921 622 ELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEvktsrnelnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 710 ELEQSILEKEsailklEANLKECEAKHQDHIRTNDLSAKEVKF-REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK 788
Cdd:pfam15921 702 KSAQSELEQT------RNTLKSMEGSDGHAMKVAMGMQKQITAkRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 789 EELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVS-----VMRDEEKLLRIKINE-LEKKKNQ---YSQ 859
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQRQEQESVRLKLQHtLDVKELQgpgYTS 855
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 860 DLDMKQRTIQ--QLKEQLSNQKMEEAVQQY--EKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEaDWLATE 935
Cdd:pfam15921 856 NSSMKPRLLQpaSFTRTHSNVPSSQSTASFlsHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAED-KGRAPS 934
|
570 580 590
....*....|....*....|....*....|...
gi 1720395285 936 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRK 968
Cdd:pfam15921 935 LGALDDRVRDCIIESSLRSDICHSSSNSLQTEG 967
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
604-890 |
3.40e-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: 51.61 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 604 IQGLEEQIEKlqvevkgYREENSDLRAQESQgknrdHQLKEKESLIQQLREELQEKSVSLRvqvqlvaEREQALSELSQD 683
Cdd:TIGR02169 767 IEELEEDLHK-------LEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLR-------EIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 684 VTCYKAKIKDLEVIVETQKDeckRLVELEQSILEKESAILKLEANLKECEAkhqdhiRTNDLSAKEVKFREEVTRLANNL 763
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEA------ALRDLESRLGDLKKERDELEAQL 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 764 HDTKQLLQSKEEENEISRQETEKLKEEL-AANSILTQNLKADLQKKEEDCAELKEKfiDAKKQIEQVQREVSVMRD---- 838
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLeALEEELSEIEDPKGEDEEIPEEELSLE--DVQAELQRVEEEIRALEPvnml 976
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 839 -----EEKLLRikINELEKKKNQysqdLDMKQRTIQQLKEQLSNQKMEEAVQQYEKV 890
Cdd:TIGR02169 977 aiqeyEEVLKR--LDELKEKRAK----LEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
588-987 |
3.62e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 588 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREEnSDLRAQESQGKNRDHQLKEKESLIQQLR---EELQEKSVSLR 664
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 665 VQVQLVAEREQALSELSQDVTcyKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTND 744
Cdd:COG4717 167 ELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 745 LSAKEVKFREEVTRLA-----NNLHDTKQ---------------LLQSKEEENEISRQETEKLKEELAANSILTQNLKAD 804
Cdd:COG4717 245 LKEARLLLLIAAALLAllglgGSLLSLILtiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 805 LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKllRIKINELEKKKNQYSQDLDMKqrTIQQLKEQLSN-QKMEEA 883
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVE--DEEELRAALEQaEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 884 VQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDrvLEAKSEEadwLATELDKWKEKFKDLETRSNQRLNTGTmddLD 963
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEE---LEEELEELREELAELEAELEQLEEDGE---LA 472
|
410 420
....*....|....*....|....
gi 1720395285 964 VLTRKFSKLQDELQESEEKYKADR 987
Cdd:COG4717 473 ELLQELEELKAELRELAEEWAALK 496
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
367-1062 |
4.29e-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: 51.51 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 367 LGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRV-LKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQ 445
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAElLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 446 LRFFEEKNSSLRADVEQIQASYNSA------VAELQTQKAVNQEQRDRIlKLSQEMETAARSIESNVSQIKQMQTKIDEL 519
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLkqlrarIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 520 RS-LDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQ----LPGGDFSSTWVKEYHTQEISRENSFHASIEAIwEECKEIV 594
Cdd:TIGR00618 317 QSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQK-TTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 595 KASSKKSHQIQGLEEQIEKLQVEvkgYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAERE 674
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRTSA---FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 675 QALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECE------AKHQDHIRTNDLSAK 748
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtyAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 749 EVK-----FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----ILTQNLKADLQKKEEDCAELKEKF 819
Cdd:TIGR00618 553 SERkqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 820 IDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLS 895
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 896 VKE--KLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlatELDKWKEKFKDLE-TRSNQRLNTGTMDDldvltRKFSKL 972
Cdd:TIGR00618 713 IEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTAALQTG-----AELSHL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 973 QDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQLAEKNSELQKWREERDQ 1052
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
730
....*....|
gi 1720395285 1053 LVTAVETQMK 1062
Cdd:TIGR00618 861 LAQLTQEQAK 870
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
441-659 |
4.83e-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: 50.53 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 441 SLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELR 520
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 521 SLDSpshiskiDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK 600
Cdd:COG4942 104 EELA-------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720395285 601 SHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 659
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1049 |
7.61e-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: 49.76 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 791 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 870
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 871 LKEQLSNQKmeeavQQYEKVckdLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrs 950
Cdd:COG4942 95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 951 nqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVE 1030
Cdd:COG4942 164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*....
gi 1720395285 1031 TLTAQLAEKNSELQKWREE 1049
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
575-720 |
1.78e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 575 RENSFHASIEAIWEECKEIVK-----ASSKKSHQIQGLEEQIEKLQVEV-KGYREENSDLRAQESQGKNRDHQLKEKESL 648
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEeakkeAEAIKKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720395285 649 IQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcYKAKIKDLEVIVETQKDECKRLVeLEQsiLEKES 720
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAKEIL-LEK--VEEEA 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
618-886 |
2.27e-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: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 618 VKGYREENSDLRAQESqgknrdhqlkekESLIQQLREELQEksvsLRVQVQlvaEREQALSELSQdvtcyKAKIKDLEvi 697
Cdd:COG3206 158 AEAYLEQNLELRREEA------------RKALEFLEEQLPE----LRKELE---EAEAALEEFRQ-----KNGLVDLS-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 698 vETQKDECKRLVELEQSILEKESAILKLEANLKECEAKhqdhIRTNDLSAKEVKFREEVTRLANnlhdtkQLLQSKEEEN 777
Cdd:COG3206 212 -EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ----LGSGPDALPELLQSPVIQQLRA------QLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 778 EISRQETEK------LKEELAAnsiltqnLKADLQkkeedcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELE 851
Cdd:COG3206 281 ELSARYTPNhpdviaLRAQIAA-------LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720395285 852 KKKNQYSQ---DLDMKQRTIQQLKEQLSNQKMEEAVQQ 886
Cdd:COG3206 348 ELEAELRRlerEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-1087 |
3.81e-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: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 859 QDLDMKQRTIQQLKEQLSN-QKMEEAVQQYEKVCKDLSVKEKLVEdmRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD 937
Cdd:COG4913 235 DDLERAHEALEDAREQIELlEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 938 KWKEKFKDLETR----SNQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYK--ADRKKWLEEKAVLTTQA-KEAENVRNR 1010
Cdd:COG4913 313 RLEARLDALREEldelEAQIRGNGG-DRLEQLEREIERLERELEERERRRArlEALLAALGLPLPASAEEfAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 1011 EMRKYADDRERclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALlssckhkDEEIQELRKAAAKSTG 1087
Cdd:COG4913 392 LLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNI-------PARLLALRDALAEALG 454
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
442-1098 |
4.09e-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: 48.28 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 442 LQQQLRFFEEKNSSLRADVE----QIQASYNSAVA----ELQTQKAVNQEQRDRILKLSQEMETaarSIESNVSQIKQMQ 513
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDikesKLGSSMNSIKTfwspELKKERALRKEEAARISVLKEQYRV---TQEENQHLQLTIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 514 TKIDELRsldspSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEIS-----------RENSFHAS 582
Cdd:pfam10174 78 ALQDELR-----AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFllrktleemelRIETQKQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 583 IEAIWEECKEIV-----KASSKKS--------HQIQGLEEQIEKLQVEVKGYREENSDLRaQESQGKNRDHQLKEKESLI 649
Cdd:pfam10174 153 LGARDESIKKLLemlqsKGLPKKSgeedwertRRIAEAEMQLGHLEVLLDQKEKENIHLR-EELHRRNQLQPDPAKTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 650 QQLREELQEKSVSL-RVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEAN 728
Cdd:pfam10174 232 QTVIEMKDTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 729 LKECEAKHQD---HIRT--NDLSAKEVK-------------------------------FREEVTRLANNLHDTKQLLQS 772
Cdd:pfam10174 312 LETLTNQNSDckqHIEVlkESLTAKEQRaailqtevdalrlrleekesflnkktkqlqdLTEEKSTLAGEIRDLKDMLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 773 KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDC-------AELKEKFIDAKKQIE----QVQREVSVMRDEEK 841
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIErlkeQREREDRERLEELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 842 LLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQ------------KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLV 909
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 910 EQEQTqAEQDRVLEA----KSEEADWLATELDKWKEKFKDLETRSNQRlnTGTMDDLDVLTRKFSKLQD----ELQESEE 981
Cdd:pfam10174 552 TNPEI-NDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDK--DKKIAELESLTLRQMKEQNkkvaNIKHGQQ 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 982 KYKADRKKWLEEkaVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQ-------LAEKNSELQKWR-EERDQL 1053
Cdd:pfam10174 629 EMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALE---KTRQELDATKARlsstqqsLAEKDGHLTNLRaERRKQL 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1720395285 1054 VTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPE 1098
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
588-952 |
4.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 588 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQV 667
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 668 QLV--AEREQALSELSQDVTCYKAKIKDLEVIVETQK--DECKRLVELEqsileKESAILKLEANLKECEAKHQDHIRtn 743
Cdd:PTZ00121 1474 EAKkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAK-----KADEAKKAEEAKKADEAKKAEEKK-- 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 744 dlSAKEVKFREEVtRLANNLHDTKQLLQSKEEEN------EISRQETEKLKEELAANSILTQNLKADLQKKEEDC----- 812
Cdd:PTZ00121 1547 --KADELKKAEEL-KKAEEKKKAEEAKKAEEDKNmalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikae 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 813 -----AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQ-------YSQDLDMKQRTIQQLKEQLSNQKM 880
Cdd:PTZ00121 1624 elkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkaeeAKKAEEDEKKAAEALKKEAEEAKK 1703
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720395285 881 EEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQD--RVLEAKSEEADWLATELDKWKEKFKDLETRSNQ 952
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
702-1051 |
4.72e-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: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 702 KDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFRE------EVTRLANNLHDTKQLLQSKEE 775
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 776 ENEISRQETEKLKEELAansilTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKn 855
Cdd:pfam02463 252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 856 qysqdldmkqrtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATE 935
Cdd:pfam02463 326 -------------AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS-SAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 936 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKY 1015
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720395285 1016 ADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1051
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
292-509 |
4.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 292 VKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKVDTSLTSNKSTCNETsempknsRAQTHSERKRLNEDGLQLGEP 370
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEA-------RAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 371 PAKKGLILVSPPITEEQNKMGEMQQSVSEVVEG---------------NRVLKEKNEELKRLLTIGENELRNEKEEKAEL 435
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvialraqiAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720395285 436 NKQVVSLQQQLrffeeknsslrADVEQIQASYNsavaELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQI 509
Cdd:COG3206 333 QAQLAQLEARL-----------AELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-1305 |
5.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 690 KIKDLEVIVETQKDECKRLVELEQSILE--KESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLannlHDTK 767
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEER----KAEEARKAEDAKKA----EAVK 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 768 QLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEdcAELKEKfIDAKKQIEQVQREVSVMRDEEKLlriKI 847
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARK-ADELKKAEEKKKADEAKKAEEKK---KA 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 848 NELEKKKNQYSQDLDMKQrtiqqlKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRltlvEQEQTQAEQDRVLEAKSE 927
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKK------KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA----DEAEAAEEKAEAAEKKKE 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 928 EADWLATELDK-WKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADR-KKWLEEKAVLTTQAKEAE 1005
Cdd:PTZ00121 1375 EAKKKADAAKKkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAE 1454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1006 NVRNRE-MRKYADDRERCLKLQNEVETltaqlAEKNSELQKWREER----DQLVTAVETQMKALLSSCKHKDEEIQELRK 1080
Cdd:PTZ00121 1455 EAKKAEeAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEAkkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1081 AAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTPLQP 1160
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1161 NKMAVKHPGcptpvtiKIPKARKRKSGEVEEDLVKCENKKNSTPRSNVKFPVSEHRNSPVKKEQKVSVGPSSKKTYSLRS 1240
Cdd:PTZ00121 1610 EEAKKAEEA-------KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395285 1241 QASTVSANIASKKREGTLQKFGDFLQHSPTILQSKAKKIIETMSSPKLSTVEVSKENVSQPKKAK 1305
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
434-1064 |
6.85e-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: 47.42 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 434 ELNKQVVSLQQQL----RFFEEKNSSLRADVEQIQASYNS------AVAELQTQKAVNQEQ-RDRILKLSQEMEtAARSI 502
Cdd:pfam15921 82 EYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEmqmerdAMADIRRRESQSQEDlRNQLQNTVHELE-AAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 503 ESNVsqIKQMQTKIDELRSLdSPSHISKidllnLQDLSSGAKgdnclntsqqlpggDFSSTWVKEYHTQEISRENSFHAS 582
Cdd:pfam15921 161 KEDM--LEDSNTQIEQLRKM-MLSHEGV-----LQEIRSILV--------------DFEEASGKKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 583 IEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREensdLRAQESQgkNRDHQL-KEKESLIQQLREELQE-KS 660
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIE----LLLQQHQ--DRIEQLiSEHEVEITGLTEKASSaRS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 661 VSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIV---ETQKDECKRLVELEQSILEKESAIlkleANLKECEAKhq 737
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSM----YMRQLSDLESTVsqlRSELREAKRMYEDKIEELEKQLVL----ANSELTEAR-- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 738 dhirtndlsAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKE 817
Cdd:pfam15921 363 ---------TERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 818 KFIDAKKQIE-QVQREVSVMRDEekllrikiNELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMeeAVQQYEKVCKDLSV 896
Cdd:pfam15921 434 LLKAMKSECQgQMERQMAAIQGK--------NESLEKVSSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDLTA 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 897 ----KEKLVE-------------DMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTM 959
Cdd:pfam15921 504 slqeKERAIEatnaeitklrsrvDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 960 DDLDVLTRKfSKLQDELQeseekykaDRKKWLEEKAVLttqaKEAENVRNREMRKYADDrerclkLQNEVETLTAQLAEK 1039
Cdd:pfam15921 584 TAGAMQVEK-AQLEKEIN--------DRRLELQEFKIL----KDKKDAKIRELEARVSD------LELEKVKLVNAGSER 644
|
650 660
....*....|....*....|....*
gi 1720395285 1040 NSELQKWREERDQLVTAVETQMKAL 1064
Cdd:pfam15921 645 LRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
424-521 |
7.09e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 424 ELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAE---LQTQKAVNQEQRD----RILKLSQEME 496
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAaaegRAGELAQELD 126
|
90 100
....*....|....*....|....*
gi 1720395285 497 TAARSIESNVSQIKQMQTKIDELRS 521
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRR 151
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
601-853 |
7.50e-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: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 601 SHQIQGLEEQIEKLQVEVKgyrEENSDLRAQESQGKNRDHQLKEKESLIQQLREELQeksvslrvqvqlvaEREQALSEL 680
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIR--------------ALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 681 SQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANlkeceaKHQDHIRTNDLSAKEVKFREEvtrLA 760
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARRE---QA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 761 NNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRevsvmrdEE 840
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ-------EA 222
|
250
....*....|...
gi 1720395285 841 KLLRIKINELEKK 853
Cdd:COG4942 223 EELEALIARLEAE 235
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
804-1075 |
8.68e-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: 47.04 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 804 DLQKKEEDCAELKEK--------FIDAKKQIEQVQREVSVMRDeekllrikineLEKKKNQYSQDL-DMKQRTIQQLK-- 872
Cdd:pfam15921 89 DLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMERDAMAD-----------IRRRESQSQEDLrNQLQNTVHELEaa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 873 EQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQA----EQD---------------RVLEAKSEEADWLA 933
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGkkiyEHDsmstmhfrslgsaisKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 934 TELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMR 1013
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395285 1014 KYADDRERCLKLQNE-----------VETLTAQLAEKNSELQKWREERDQLVTA---VETQMKALLSSCKHKDEEI 1075
Cdd:pfam15921 318 QLSDLESTVSQLRSElreakrmyedkIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKEL 393
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
852-1084 |
9.73e-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: 46.30 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 852 KKKNQYSQDLDMKQRTIQQLKEQLSNQKmeeavQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 931
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK-----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 932 LATELDKWKEKFKDLeTRSNQR----------LNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQa 1001
Cdd:COG4942 95 LRAELEAQKEELAEL-LRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1002 keaenvrnremrkyaddrerclklQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKA 1081
Cdd:COG4942 173 ------------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
...
gi 1720395285 1082 AAK 1084
Cdd:COG4942 229 IAR 231
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
408-1101 |
9.77e-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: 46.89 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 408 KEKNEELKRLLTIGENELRNEKEEKAELNKQvvslqqqlrffEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQrdr 487
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELKLLAKE-----------EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 488 ILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSgakgdnclntsqqlpggDFSSTWVKE 567
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-----------------ERLSSAAKL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 568 YHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKES 647
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 648 LIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELeqsILEKESAILKLEA 727
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV---AVENYKVAISTAV 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 728 NLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLkadLQK 807
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK---VVE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 808 KEEDCAELKEKFIDAKKQIEQVQREVSVMRDE-EKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK-MEEAVQ 885
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLeIKKKEQ 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 886 QYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQ------RLNTGTM 959
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEkelaeeREKTEKL 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 960 DDLDVLTRKFSKLQDELQE--SEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCL-KLQNEVETLTAQL 1036
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeEELERLEEEITKE 866
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395285 1037 AEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYND 1101
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
643-879 |
1.07e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 643 KEKESLIQQLRE-------ELQEKSVSLRVQ--VQLVAEREQALSELSQDV--------TCYKAKIKDLEVIVETQKDEc 705
Cdd:PRK05771 16 SYKDEVLEALHElgvvhieDLKEELSNERLRklRSLLTKLSEALDKLRSYLpklnplreEKKKVSVKSLEELIKDVEEE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 706 krLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREE--VTRLANNLHDTKQLLQSKEEENEISrQE 783
Cdd:PRK05771 95 --LEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVENV-EY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 784 TEKLKEEL---------AANSILTQNLKADLQKKE-EDCAELKEKFIDAKKQIEQVQREvsvmrdEEKLlrikINELEKK 853
Cdd:PRK05771 172 ISTDKGYVyvvvvvlkeLSDEVEEELKKLGFERLElEEEGTPSELIREIKEELEEIEKE------RESL----LEELKEL 241
|
250 260
....*....|....*....|....*.
gi 1720395285 854 KNQYSQDldmkqrtIQQLKEQLSNQK 879
Cdd:PRK05771 242 AKKYLEE-------LLALYEYLEIEL 260
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
603-784 |
1.90e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 603 QIQGLEEQIEKLQVEVKGYREENSDLRAQEsQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQ 682
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 683 D--VTCYKAKIKDLE-----------------VIVETQKDECKRLV--ELEQSILEKESAILKLEANLKECEAKHQDH-I 740
Cdd:COG3206 262 SpvIQQLRAQLAELEaelaelsarytpnhpdvIALRAQIAALRAQLqqEAQRILASLEAELEALQAREASLQAQLAQLeA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720395285 741 RTNDLSAKEVKFReEVTRLANNLHDTKQLLQSKEEENEISRQET 784
Cdd:COG3206 342 RLAELPELEAELR-RLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
717-1084 |
2.29e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 717 EKESAILKLEANLKECEAKhQDHIRTNDLSAKEVKFREEVTRLANN---LHDTKQLLQSKEEENEISRQETEKLKEELAa 793
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEK-DLHERLNGLESELAELDEEIERYEEQreqARETRDEADEVLEEHEERREELETLEAEIE- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 794 nsiltqNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL-------LRIKINELEKKKNQYSQDLDMKQR 866
Cdd:PRK02224 262 ------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 867 TIQQLKEQLSNqkMEEAVQQYEKVCKDLSVK----EKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEK 942
Cdd:PRK02224 336 AAQAHNEEAES--LREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 943 FKDLEtrsnqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQ-AKEAENVRNREmrkyaDDRER 1021
Cdd:PRK02224 414 LEELR------------EERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQpVEGSPHVETIE-----EDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1022 CLKLQNEVETLTAQ-------------LAEKNSELQKWREERDQLV-------TAVETQMKALLSSCKHKDE---EIQEL 1078
Cdd:PRK02224 477 VEELEAELEDLEEEveeveerleraedLVEAEDRIERLEERREDLEeliaerrETIEEKRERAEELRERAAEleaEAEEK 556
|
....*.
gi 1720395285 1079 RKAAAK 1084
Cdd:PRK02224 557 REAAAE 562
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
383-889 |
2.54e-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: 45.40 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 383 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 462
Cdd:TIGR04523 70 INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 463 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarSIESNVSQIKQmQTKIDELRSLDSPSHISKIDLLNLQDLSSG 542
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKL----NIQKNIDKIKN-KLLKLELLLSNLKKKIQKNKSLESQISELK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 543 AKGDNCLNTSQQLpggdfsstwvKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR 622
Cdd:TIGR04523 225 KQNNQLKDNIEKK----------QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 623 EENSDLRAQESQGKNRD--HQLKEKESLIQQLREEL---QEKSVSLRVQV-QLVAEREQALSELSQDVTCYKAKIKDLEV 696
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKElkSELKNQEKKLEEIQNQIsqnNKIISQLNEQIsQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 697 IVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVK-FREEVTRLANNLHDTKQLLQSKEE 775
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErLKETIIKNNSEIKDLTNQDSVKEL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 776 ENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKN 855
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
490 500 510
....*....|....*....|....*....|....
gi 1720395285 856 QYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEK 889
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEKNK 568
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
582-1030 |
2.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 582 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLraqeSQGKNRDHQLKEKESLIQQLREELQEKSV 661
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 662 SLRVQVQLVAEREQALSELS-QDVTCYKAKIKDLEVIVETQKDECK----RLVELEQSILEKESAILKLEANLKEC---- 732
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISkitaRIGELKKEIKELKKAIEELKKAKGKCpvcg 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 733 ---EAKHQDHIrTNDLSAKEVKFREEVTRLANNLHDTKQLLqsKEEENEISRQET----EKLKEEL-AANSILTQNLKAD 804
Cdd:PRK03918 443 relTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKEL--RELEKVLKKESEliklKELAEQLkELEEKLKKYNLEE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 805 LQKKEEDCAELKEKFIDAKKQIEQVQREVSvmrdeekllriKINELEKKKnqysQDLDMKQRTIQQLKEQLSNQKMEEAV 884
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELE-----------KLEELKKKL----AELEKKLDELEEELAELLKELEELGF 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 885 QQYEKVCKDLSVKEKLVEDMrLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDV 964
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395285 965 LTRKFSKLQDE----------LQESEEKYKADRKKWLEEKAVLTTQAKEAENVrNREMRKYADDRERCLKLQNEVE 1030
Cdd:PRK03918 664 LREEYLELSRElaglraeleeLEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
603-889 |
3.41e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 603 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKeslIQQLREELQEKSVSLRVQVQLVAEREQALSELsq 682
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 683 dvtcyKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEanlkeceakhqDHIRTNDLS-AKEVKFREEVTRLAN 761
Cdd:COG1340 84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE-----------WRQQTEVLSpEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 762 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK 841
Cdd:COG1340 148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720395285 842 LLRIKINELEKKKNQYSQDLD-MKQRTIQQLKEQLSNQKMEEAVQQYEK 889
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKkLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
593-1100 |
3.66e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 593 IVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAE 672
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 673 REQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKF 752
Cdd:TIGR00606 620 QLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 753 REEVTRLA-NNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQR 831
Cdd:TIGR00606 700 LQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 832 EVSVMRD---EEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDmrltl 908
Cdd:TIGR00606 780 EEESAKVcltDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD----- 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 909 vEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSN--QRLNTGTMDDLDVLTRKFSKLQDELQESEE---KY 983
Cdd:TIGR00606 855 -QQEQIQHLKSKTNELKSEKLQ-IGTNLQRRQQFEEQLVELSTevQSLIREIKDAKEQDSPLETFLEKDQQEKEElisSK 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 984 KADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLK-LQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQ-- 1060
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQki 1012
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720395285 1061 ----MKALLSSCKHKDE--EIQELRKAAAKSTGtENQTMNPKPEYN 1100
Cdd:TIGR00606 1013 qerwLQDNLTLRKRENElkEVEEELKQHLKEMG-QMQVLQMKQEHQ 1057
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
603-793 |
3.84e-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: 44.37 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 603 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNR----DHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALS 678
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 679 ELSQ------------------DVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKEceakhqdhi 740
Cdd:COG4942 115 RLGRqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE--------- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720395285 741 RTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAA 793
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
595-1065 |
4.58e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 595 KASSKKSHQIQGLEEQIEKLQVE--VKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSvslrvqvqlvaE 672
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPcmPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-----------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 673 REQALSELSQDVTCYKAKIKDLEVIVETQKDECK--RLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEV 750
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRARKaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 751 KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAE---------------- 814
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilqreqatidtrts 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 815 ----LKEKFIDAKKQIEQVQREVSVMR-------DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKE--QLSNQKME 881
Cdd:TIGR00618 418 afrdLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 882 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSnqrlnTGTMDD 961
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQM-----QEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 962 LDVLTRKFSKLQDELqESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNS 1041
Cdd:TIGR00618 572 FSILTQCDNRSKEDI-PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
490 500
....*....|....*....|....
gi 1720395285 1042 ELQKWREERDQLVTAVETQMKALL 1065
Cdd:TIGR00618 651 LQLTLTQERVREHALSIRVLPKEL 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
814-1064 |
4.64e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 814 ELKEKFIDAKKQIEQVQREVS---------VMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAV 884
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRgsldqlkaqIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR--DEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 885 QQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEqdrvleakseeadwLATELDKWKEKFKDLETRSNQRLNTGTMDDLDV 964
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREE--------------LAEEVRDLRERLEELEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 965 LTrkFSKLQDELQESEEKYkadRKKWLEEKAVLTTQAKEAENVRNREmrkyADDRERCLKLQNEVETLTAQLAEKNSELQ 1044
Cdd:PRK02224 310 EA--VEARREELEDRDEEL---RDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREEAAELESELEEAREAVE 380
|
250 260
....*....|....*....|
gi 1720395285 1045 KWREERDQLVTAVETQMKAL 1064
Cdd:PRK02224 381 DRREEIEELEEEIEELRERF 400
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
295-877 |
5.11e-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: 44.63 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 295 ELAETKEELIKAQEELKNRE-------------------SNSLVQALKTSSK-VDTSLTSNKSTCNETSEMPKNSRAQTH 354
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEkelknldknlnkdeekinnSNNKIKILEQQIKdLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 355 SERKRLNEDGLQLGEppAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAE 434
Cdd:TIGR04523 114 NDKEQKNKLEVELNK--LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 435 LNKQVVSLQQQLRFFEEKN----------SSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 504
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 505 NVSQIKQMQTKIDELRSLdspshISKIDlLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIE 584
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQ-----LNQLK-SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 585 AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ----ESQGKNRDHQLKEKESLIQQLREELQEKS 660
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindlESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 661 VSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECK-----------RLVELEQSILEKESAILKLEANL 729
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 730 KECEAKHQDHIRTNDLS-AKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK--EELAANSILTQNLKADLQ 806
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLkEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEELKQTQKSLKKKQE 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720395285 807 KKEEDCAELKEKFIDAKKQIE-------QVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSN 877
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
637-1085 |
7.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 637 NRDHQLKEKEsLIQQLREELQEKSVSLRVQVQlvAEREQALSELSQDVTCYKAKIKDlevivETQKDECKRLVELEQSIL 716
Cdd:PTZ00121 1037 NNDDVLKEKD-IIDEDIDGNHEGKAEAKAHVG--QDEGLKPSYKDFDFDAKEDNRAD-----EATEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 717 EK-ESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS 795
Cdd:PTZ00121 1109 GKaEEARKAEEAKKKAEDARKAEEAR----KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 796 ILTQnlKADLQKKEEDCaelkeKFIDAKKQIEQVQR--EVSVMRDEEKLLRIKINELEKKKNQYSQDLDmKQRTIQQLKE 873
Cdd:PTZ00121 1185 EEVR--KAEELRKAEDA-----RKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 874 QLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSE-EADWLATELDKWKEKFKDLETRSNQ 952
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 953 RLNTGTMDDlDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRN-REMRKYADDRErclKLQNEVET 1031
Cdd:PTZ00121 1337 KAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDK---KKADELKK 1412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 1032 LTAQlAEKNSELQKWREER---DQLVTAVETQMKAllSSCKHKDEEIQELRKAAAKS 1085
Cdd:PTZ00121 1413 AAAA-KKKADEAKKKAEEKkkaDEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKA 1466
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
743-958 |
8.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 743 NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiltqnLKADLQKKEEdcaELKEKFIDA 822
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERRE---ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 823 KKQ-------------------IEQVQREVSVMRDEEKLLRiKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK--ME 881
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdfLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKaeLE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 882 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGT 958
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
426-655 |
8.78e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 426 RNEKEEKAELNKQVVSLQQQL----RFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarS 501
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIktynKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE----D 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 502 IESNVSQIKQMQTKIDelrsldspshiSKIDLLNlQDLSSGAKGDNCLNTSQQLPGGDfsstwvkeyhtqeisrensfhA 581
Cdd:PHA02562 253 PSAALNKLNTAAAKIK-----------SKIEQFQ-KVIKMYEKGGVCPTCTQQISEGP---------------------D 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720395285 582 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREE 655
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
635-886 |
1.05e-03 |
|
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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 635 GKNRDHQLKEKESLIQQLREEL---QEKSVSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIVEtqkdeckRLVEL 711
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAE----YSWDEIDVASAER-------EIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 712 EQSI--LEKESAILK-LEANLKECEAKHQDHIRT-NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQET--E 785
Cdd:COG4913 674 EAELerLDASSDDLAaLEEQLEELEAELEELEEElDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 786 KLKEELAANSI--LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRD---------EEKLLRIKINELEKKK 854
Cdd:COG4913 754 RFAAALGDAVEreLRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslpeyLALLDRLEEDGLPEYE 833
|
250 260 270
....*....|....*....|....*....|..
gi 1720395285 855 NQYsqdLDMKQRTIQQLKEQLsNQKMEEAVQQ 886
Cdd:COG4913 834 ERF---KELLNENSIEFVADL-LSKLRRAIRE 861
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
429-667 |
1.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 429 KEEKAELNKQVVSLQQQLRFFEEKNSSLRAD-----VEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIE 503
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 504 SN------VSQIKQMQTKIDELRSLDSPSHISKIDLLnlqdlssgakgdnclntsqqlpggdfsstwvkeyhtQEIsren 577
Cdd:COG3206 261 QSpviqqlRAQLAELEAELAELSARYTPNHPDVIALR------------------------------------AQI---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 578 sfhASIEAIWEEckEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGK--NRDHQLKEK--ESLIQQLR 653
Cdd:COG3206 301 ---AALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElyESLLQRLE 375
|
250
....*....|....*
gi 1720395285 654 E-ELQEKSVSLRVQV 667
Cdd:COG3206 376 EaRLAEALTVGNVRV 390
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
647-873 |
1.23e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 647 SLIQQLREELQEKSVSLRVQVQLVAEREQALSEL----SQDVTCYKAKIKDLeviVETQKDECKRLVELEQSILEKESAI 722
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDEL---VEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 723 LKLEANLKECEAKHQDHIRTNDLSAKEVKFREE-----------------VTRLANNLHDtkqlLQSKEEENEISRQETE 785
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDELE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 786 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 865
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
....*...
gi 1720395285 866 RTIQQLKE 873
Cdd:PHA02562 407 IVTDLLKD 414
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
402-948 |
1.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 402 EGNRVLKEKNEELKRLLTIGE--NELRNEKE----EKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQ 475
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAeiEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 476 TQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskidllNLQDLSSGAKgdnclNTSQQL 555
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-------------EAAELESELE-----EAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 556 pggdfsstwvkeyhtqeisreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQG 635
Cdd:PRK02224 380 ---------------------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 636 KNRdhqLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckrLVELE--- 712
Cdd:PRK02224 439 RER---VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED----LVEAEdri 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 713 QSILEKESAILKLEANLKEceakhqdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELA 792
Cdd:PRK02224 512 ERLEERREDLEELIAERRE---------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 793 ANsiltqnlkadlqkKEEdcaelkekfIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLK 872
Cdd:PRK02224 583 EL-------------KER---------IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395285 873 EQLSNQKMEEAVQQYEKVCKDLsvkEKLVEDMRLTLVEQEQTQAEQDRVlEAKSEEADWLATELDKWKEKFKDLET 948
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYL---EQVEEKLDELREERDDLQAEIGAV-ENELEELEELRERREALENRVEALEA 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
417-887 |
1.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 417 LLTIGENELRNEKEE-------KAELN-KQVVSLQQQLRFFEEKNSSLRADVEQIQaSYNSAVAELQTQKAVNQEQRDRI 488
Cdd:COG4717 43 IRAMLLERLEKEADElfkpqgrKPELNlKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 489 LKLSQ------EMETAARSIESNVSQIKQMQTKIDELRSLdspshISKIDLLNLQdlssgakgdnclntsqqlpggdfss 562
Cdd:COG4717 122 EKLLQllplyqELEALEAELAELPERLEELEERLEELREL-----EEELEELEAE------------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 563 twVKEYHTQEISRENSFHASIEAIWEECKEivkasskkshQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQL 642
Cdd:COG4717 172 --LAELQEELEELLEQLSLATEEELQDLAE----------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 643 KEKESLIQQLRE--------ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQS 714
Cdd:COG4717 240 ALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 715 ILEKESAILKLEANLKECEAKHQ-DHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAA 793
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELlDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 794 NSILTQNLKADLQKKEE---------DCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKkknqySQDLDMK 864
Cdd:COG4717 400 LKEELEELEEQLEELLGeleellealDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAEL 474
|
490 500
....*....|....*....|...
gi 1720395285 865 QRTIQQLKEQLSNQKMEEAVQQY 887
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKL 497
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1029-1315 |
1.58e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1029 VETLTAQLAEKNSELQK---------WREERDQLVTAVETQMKALLssckhkdEEIQELRKAAAKSTGTENQTMNPKPEY 1099
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALEEQEEVEE-------KEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1100 NDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTplqpnKMAVKHPGCPTPVTIKIP 1179
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1180 KARKRKSGEVEEDLVKCENKKNSTPRSNvkfpvsehrnspvkkeqkvSVGPSSKKTyslrSQASTVSANIASKKREGTLQ 1259
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVS-------------------AVQYSPPPP----SKRPDGESNGGSKPSSPTKK 1308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720395285 1260 KFGDFLQHSPTILQSKAKKIIETMSSPKLST--VEVSKENVSQPKKAKRKLYRNEISS 1315
Cdd:PTZ00108 1309 KVKKRLEGSLAALKKKKKSEKKTARKKKSKTrvKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
585-1067 |
1.66e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 585 AIWEECKEIVKASSKKSHQIQGLEEQIE-------KLQVEVKGYREensDLRAQESQGKNRDHQLKEKESLIQQLREELQ 657
Cdd:pfam12128 224 EHWIRDIQAIAGIMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKS---DETLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 658 EKSVSLR------------VQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKL 725
Cdd:pfam12128 301 EKRDELNgelsaadaavakDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 726 EANLKEceakhQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSK-----EEENEISRQETEKLKEELA------AN 794
Cdd:pfam12128 381 RSKIKE-----QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElreqlEAGKLEFNEEEYRLKSRLGelklrlNQ 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 795 SILTQNLKADLQKKEEDCAELKEKfidakkqIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 874
Cdd:pfam12128 456 ATATPELLLQLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 875 LSNQK-------MEEAVQQYEKVCKDLSVKEKLVEDMRLTLVE---------------------------QEQTQAEQDR 920
Cdd:pfam12128 529 LFPQAgtllhflRKEAPDWEQSIGKVISPELLHRTDLDPEVWDgsvggelnlygvkldlkridvpewaasEEELRERLDK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 921 VLEA------KSEEADWLATELDKWKEKFKDLETRSNQRLNtGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE-- 992
Cdd:pfam12128 609 AEEAlqsareKQAAAEEQLVQANGELEKASREETFARTALK-NARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNsl 687
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 993 --EKAVLTTQAKEAENVRNREMRKYAddRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSS 1067
Cdd:pfam12128 688 eaQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
878-1094 |
2.01e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 878 QKMEEAVQQYEKVCKDLSVKEKLVEDMR--LTLVEQEQTQAEQDRVLEAKSEEADWLA-----TELDKWKEKFKDLETRS 950
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELErqLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 951 NQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE---EKAVLTTQ---AKEAENVRNREMRKYADDRERCLK 1024
Cdd:TIGR02168 252 EEELEELT-AELQELEEKLEELRLEVSELEEEIEELQKELYAlanEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 1025 LQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMN 1094
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
650-933 |
2.12e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 650 QQLREELQE-KSVSLRVQVQLVAEREQALSELS------QDVTCYKAKIKDLEVI-------VETQKDECKRL------V 709
Cdd:PRK10929 26 KQITQELEQaKAAKTPAQAEIVEALQSALNWLEerkgslERAKQYQQVIDNFPKLsaelrqqLNNERDEPRSVppnmstD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 710 ELEQSILEKESAILKLEANLKEceakHQDHIRtndlsakevkfreEVTRLANNLhdTKQLLQSKEEENEISRQetekLKE 789
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAR-------------EISDSLSQL--PQQQTEARRQLNEIERR----LQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 790 ELAANSILTQNLKADLQkkeedcAELKEKfidaKKQIEQVQREVSVMRDEEKLLRIKInELEKKKnqySQDLDMKqrtIQ 869
Cdd:PRK10929 163 LGTPNTPLAQAQLTALQ------AESAAL----KALVDELELAQLSANNRQELARLRS-ELAKKR---SQQLDAY---LQ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 870 QLKEQLSNQKMEEAVQQYEKVckdlsvkEKLVE---DMRLTLVEQEQTQAEQDRVLEAKSEEADWLA 933
Cdd:PRK10929 226 ALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIA 285
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
268-478 |
2.29e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 268 TNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAQEELKN--RESNSLVQALKTSSKVDTSLTSNKSTCNETSEM 345
Cdd:PHA02562 201 NKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNlvMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 346 pknsraqthserkrlNEDGlqlGEPPAkkglilVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLltigENEL 425
Cdd:PHA02562 281 ---------------YEKG---GVCPT------CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI----MDEF 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395285 426 RNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQAS---YNSAVAELQTQK 478
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDEL 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
804-1060 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 804 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQkmeeA 883
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 884 VQQYEkvckdlsvkeklvEDMRLTLVEQeqtqaeqdrVLEAKSeeadwlateldkwkekFKDLETRsnqrlntgtMDDLD 963
Cdd:COG3883 93 RALYR-------------SGGSVSYLDV---------LLGSES----------------FSDFLDR---------LSALS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 964 VLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSEL 1043
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250
....*....|....*..
gi 1720395285 1044 QKWREERDQLVTAVETQ 1060
Cdd:COG3883 206 AAAEAAAAAAAAAAAAA 222
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
646-789 |
2.99e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 646 ESLIQQLREELQEKSVSLRVQVQLVAEREQALSElsqdvtcykAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKL 725
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEE---------EEIRRLEEQVERLEAE---VEELEAELEEKDERIERL 446
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720395285 726 EANLKEceakhqdhIRTNdlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKE 789
Cdd:COG2433 447 ERELSE--------ARSE--ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
607-923 |
3.28e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 607 LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREEL-------------------------QEKSV 661
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrekheeleekykelsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 662 SLRVQvqlvAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEANLKECEAKHQDHI 740
Cdd:pfam07888 120 LLAQR----AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 741 RTNDLSAKE----VKFREEVTRLANNLHDTKQllqsKEEENEISRQETEKLKEELAANSILTQNLKADLQkkeedcaelk 816
Cdd:pfam07888 196 ELRNSLAQRdtqvLQLQDTITTLTQKLTTAHR----KEAENEALLEELRSLQERLNASERKVEGLGEELS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 817 ekfiDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSN-----QKMEEAVQQ- 886
Cdd:pfam07888 262 ----SMAAQRDRTQAELHQARLQAAQLTLQLADaslaLREGRARWAQERETLQQSAEADKDRIEKlsaelQRLEERLQEe 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720395285 887 ------------YEKVCKDLSVKEKLVE------DMRLTLVEQEQTQAEQDRVLE 923
Cdd:pfam07888 338 rmereklevelgREKDCNRVQLSESRRElqelkaSLRVAQKEKEQLQAEKQELLE 392
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
392-925 |
3.41e-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: 42.13 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 392 EMQQSVSEVVEGNRVLKEKNEELKRLL---TIGENELRNE----------KEEKAELNKQVVSLQQQLRffeeknsslra 458
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLnqaTATPELLLQLenfderieraREEQEAANAEVERLQSELR----------- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 459 dveQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSqiKQMQTKIDELRSLDSPSHISKIDLLNLQD 538
Cdd:pfam12128 496 ---QARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR--KEAPDWEQSIGKVISPELLHRTDLDPEVW 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 539 LSSGAKGDNCLNTSQQLPGGDFsstwvkeyhtqeisreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEV 618
Cdd:pfam12128 571 DGSVGGELNLYGVKLDLKRIDV----------------PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 619 KGYREENSDLR-----AQESQGKNRDHQLKEKESLIQQLREELQ---EKSVSLRVQVQLVAEREQALSELSQD--VTCYK 688
Cdd:pfam12128 635 EKASREETFARtalknARLDLRRLFDEKQSEKDKKNKALAERKDsanERLNSLEAQLKQLDKKHQAWLEEQKEqkREART 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 689 AKIKDLEVIVETQKDECKRLVEleqsilEKESAILKLEANLKECE--------AKHQDHIRTNDLSAKEVKFREEVTRLA 760
Cdd:pfam12128 715 EKQAYWQVVEGALDAQLALLKA------AIAARRSGAKAELKALEtwykrdlaSLGVDPDVIAKLKREIRTLERKIERIA 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 761 NNLHDTKQLLQSKEEENEISRQeteKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEE 840
Cdd:pfam12128 789 VRRQEVLRYFDWYQETWLQRRP---RLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 841 KLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYekVCKDLSVKEKLvedMRLTLVEQEQTQAEQDR 920
Cdd:pfam12128 866 RCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKY--VEHFKNVIADH---SGSGLAETWESLREEDH 940
|
....*
gi 1720395285 921 VLEAK 925
Cdd:pfam12128 941 YQNDK 945
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
754-1039 |
3.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 754 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREV 833
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 834 SVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQ 913
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 914 TQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEE 993
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720395285 994 KAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEK 1039
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
603-922 |
5.28e-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: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 603 QIQGLEEQIEKLQVEVKGYREENSDLRAQESqgknrdhQLKEKESLIQQLrEELQEKSVSLRVQVQLVAEREQALSEL-- 680
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELD-------ALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 681 -SQDVTCYKAKIKDLEVIVETQKDECKRLVE----LEQSILEKESAILKLEANLKECEAKHQDHIRTN-DLSAKEVKFRE 754
Cdd:COG4913 683 sSDDLAALEEQLEELEAELEELEEELDELKGeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 755 EVTRLANNLHDtkQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL-----------QKKEEDCAELKEKFIDAK 823
Cdd:COG4913 763 VERELRENLEE--RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpeylalldRLEEDGLPEYEERFKELL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 824 KQ--IEQVQREVSVMRDEEKLLRIKINELEK--KKNQYSQD----LDMKQRTIQQLKE------QLSNQKMEEAVQQYEK 889
Cdd:COG4913 841 NEnsIEFVADLLSKLRRAIREIKERIDPLNDslKRIPFGPGrylrLEARPRPDPEVREfrqelrAVTSGASLFDEELSEA 920
|
330 340 350
....*....|....*....|....*....|...
gi 1720395285 890 VCKDLsvkEKLVEdmRLTLVEQEQTQAEQDRVL 922
Cdd:COG4913 921 RFAAL---KRLIE--RLRSEEEESDRRWRARVL 948
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
385-793 |
5.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 385 EEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGE--NELRNEKEEKAELNKQVVSLQQQLRFFEE---KNSSLRAD 459
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELREleeELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 460 VEQIQASYNSAVAELQTQKAVN-QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQD 538
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 539 LSSGA-------KGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHAsieaiwEECKEIVKASSKKSHQIQGLEEQI 611
Cdd:COG4717 252 LLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG------KEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 612 EKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcykaki 691
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA----------- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 692 kdlevivETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEvkfrEEVTRLANNLHDTKQLLQ 771
Cdd:COG4717 395 -------EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE----EELEELREELAELEAELE 463
|
410 420
....*....|....*....|....
gi 1720395285 772 SKEEENEIS--RQETEKLKEELAA 793
Cdd:COG4717 464 QLEEDGELAelLQELEELKAELRE 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
823-1084 |
5.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 823 KKQIEQVQREVsvmRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVE 902
Cdd:COG1196 199 ERQLEPLERQA---EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE-----AELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 903 DMRLTLVEQEQT-QAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRsnqrlntgtmddldvltrkfsklQDELQESEE 981
Cdd:COG1196 271 ELRLELEELELElEEAQAEEYELLAELAR-LEQDIARLEERRRELEER-----------------------LEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 982 KYKADRKKWLEEKAVLTTQAKEAEnvrnremrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAvETQM 1061
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAA 395
|
250 260
....*....|....*....|...
gi 1720395285 1062 KALLSSCKHKDEEIQELRKAAAK 1084
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
277-504 |
6.24e-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: 40.52 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 277 ETEEAIACLQLKFNQVKAELAETKEELIKAQEELKNREsNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSE 356
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 357 RKRLNE--DGLQ-LGEPPAKKglILVSPPITEEQNKMGEMQQSVsevvegNRVLKEKNEELKRLLTIGENELRNEKEEKA 433
Cdd:COG4942 103 KEELAEllRALYrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395285 434 ELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 504
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
753-1021 |
6.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 753 REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRE 832
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 833 VSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE 912
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 913 QTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE 992
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260
....*....|....*....|....*....
gi 1720395285 993 EKAVLTTQAKEAENVRNREMRKYADDRER 1021
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
607-919 |
6.51e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 607 LEEQIEKLQVEVkgyreensdLRAQESQGKNRDHQLKEK-ESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVT 685
Cdd:PLN03229 434 LEGEVEKLKEQI---------LKAKESSSKPSELALNEMiEKLKKEIDLEYTEAVIAMGLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 686 CYKAKIKDLEVIVE---------------TQKDECKRLVELEQSILEKESAILKLEAnlkECEAKHQDHIRTNDLSAKEV 750
Cdd:PLN03229 505 MHPVLMEKIEKLKDefnkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKA---EINKKFKEVMDRPEIKEKME 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 751 KFREEVtrlannlhdTKQLLQSKEEENEISRQETEKLKEELA---ANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIE 827
Cdd:PLN03229 582 ALKAEV---------ASSGASSGDELDDDLKEKVEKMKKEIElelAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 828 QVQREVS-----VMRDEEKLLRIKINELEKKKNQYSQDLDMKQrTIQQLKEQLsNQKMEEAVQQYEkvckdlsVKEKLvE 902
Cdd:PLN03229 653 SLNEEINkkierVIRSSDLKSKIELLKLEVAKASKTPDVTEKE-KIEALEQQI-KQKIAEALNSSE-------LKEKF-E 722
|
330
....*....|....*..
gi 1720395285 903 DMRLTLVEQEQTQAEQD 919
Cdd:PLN03229 723 ELEAELAAARETAAESN 739
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
279-496 |
7.03e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 279 EEAIACLQLKFNQVKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKV--DTSLTSNKSTCNETSEMPKNSRA--QT 353
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQlKEQLQLLNKLLPQANLlaDETLADRLEELREELDAAQEAQAfiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 354 HSERKRLNEDGLQlgeppakkglILVSPPITEEQnkmgeMQQSVSEVVEGNRVLKEKNEELK----RLLTIGENELRNEK 429
Cdd:COG3096 915 HGKALAQLEPLVA----------VLQSDPEQFEQ-----LQADYLQAKEQQRRLKQQIFALSevvqRRPHFSYEDAVGLL 979
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 430 EEKAELNKQvvsLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEME 496
Cdd:COG3096 980 GENSDLNEK---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
423-721 |
7.30e-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: 40.52 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 423 NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSI 502
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 503 ESNVSQIKQMqtkideLRSLDSPSHISKIDLLnlqdLSSgakgdnclntsqqlpggdfsstwvkeyhtqeisrensfhas 582
Cdd:COG4942 100 EAQKEELAEL------LRALYRLGRQPPLALL----LSP----------------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 583 ieaiwEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgknrdhqLKEKESLIQQLREELQEKSvs 662
Cdd:COG4942 129 -----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----------RAELEALLAELEEERAALE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720395285 663 lrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESA 721
Cdd:COG4942 192 -----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
754-874 |
8.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 754 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDcaELKEKFIDAKKQIEQVQREV 833
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKKEADEIIKEL 593
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720395285 834 SVMRDEEKlLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 874
Cdd:PRK00409 594 RQLQKGGY-ASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
804-949 |
9.14e-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: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395285 804 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEA 883
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395285 884 VQQYEKVCKDLSVKEKLVEDMRLTLVEQ-EQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETR 949
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| |
