|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
151-464 |
5.38e-157 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 450.53 E-value: 5.38e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 151 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRqNLEPMFEQYISNLRRQLDSIIGERGRLDSELRN 230
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 231 MQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADSLTDDINFLRALYEAELSQMQTHISDTSVVLS 310
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 311 MDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54607171 391 CANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
15-148 |
2.44e-28 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 110.51 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 15 GYSASSARVPGLNRSGFSSVSVCRSRGSGGSSAMCGGAGFGSRSLYGVGSSKRISIGGGSCGIGGGYGSRFGGSFGIGGG 94
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54607171 95 AGSGFGFGGGAGFGG----------------------GYGGAGFPVCPPGGIQEVTINQSLLTPLNLQIDPTIQRV 148
Cdd:pfam16208 81 GGFGGGGGGGFGGGGgfgggfggggyggggfggggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-475 |
8.93e-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: 61.61 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 148 VRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRQNLEpmFEQYISNLRRQLDSIIGERGRLDSE 227
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 228 LRNMQDTVEDYkskyEDEINKRTAAENEFVTLKKDVDAaymNKVELQAKADSLTDDINFLRALY---EAELSQMQTHISD 304
Cdd:TIGR02168 749 IAQLSKELTEL----EAEIEELEERLEEAEEELAEAEA---EIEELEAQIEQLKEELKALREALdelRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 305 TSVVLSMDNNRsldldsiIAEVKAQYEDIAQRSRAEAEswyqtkyeelqvtagrhgdDLRNTKQEIAEINRMIQRLRSEI 384
Cdd:TIGR02168 822 LRERLESLERR-------IAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESEL 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 385 DHVKKQCANLQAAIADAE-----------------QRGEMALKDARGKLEGLEDALQKAKQDMARLLK----EYQELMNV 443
Cdd:TIGR02168 876 EALLNERASLEEALALLRseleelseelreleskrSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEE 955
|
330 340 350
....*....|....*....|....*....|....
gi 54607171 444 KLALDVEIATYRKLLEGEECRLNGE--GVGPVNI 475
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKikELGPVNL 989
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-459 |
8.10e-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: 55.46 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 210 LRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADSLTDDINFLRA 289
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 290 L---YEAELSQMQTHISdtSVVLSMDNNRSLDLDSIIAEVKAQYEDI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 365
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 366 TKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKL 445
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 54607171 446 ALDVEIATYRKLLE 459
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
145-440 |
1.17e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 145 IQRVRTEEREQIKTLNNKFAsfiDKVRFLEQQNKVLDTKWALLQEQGTKTVRQnlepmfeqyISNLRRQLDSIIGERGRL 224
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRRERE---KAERYQALLKEKREYEGYELLKEKEALERQ---------KEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 225 DSELRNMQDTVEDYKSKYEdEINKRTAA--ENEFVTLKKDVDaaymnkvELQAKADSLTDDINFL----------RALYE 292
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLE-ELNKKIKDlgEEEQLRVKEKIG-------ELEAEIASLERSIAEKereledaeerLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 293 AELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIaqRSRAEAESwyqTKYEELQVTAGRHGDDLRNTKQEIAE 372
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD---KEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54607171 373 INRMIQRLRSEIDHVKKQCANLQAAIADAEQR----------GEMALKDARGKLEGLEDALQKAKQDMARLLKEYQEL 440
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-462 |
1.77e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 149 RTEE-REQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgtktvRQNLEPMFEQyISNLRRQLDSIIGERGRLDSE 227
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 228 LRNMQDTVEDYKSKYEdEINKRTAAENEfvtLKKDVDaAYMNKVELQAKADSLTDDINFLRALYEAELSQMQTHISDtsv 307
Cdd:PRK03918 261 IRELEERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 308 vLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRS 382
Cdd:PRK03918 333 -LEEKEERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 383 EIDHVKKQCANLQAAIADAEQRGE------MALKDARGKL---------EGLEDALQKAKQDMARLLKEYQELMNVKLAL 447
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330
....*....|....*
gi 54607171 448 DVEIATYRKLLEGEE 462
Cdd:PRK03918 479 RKELRELEKVLKKES 493
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
141-462 |
1.15e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 141 IDPT-IQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQ------GTKTVRQNLEPMFEQY---ISNL 210
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYnekKSRL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 211 RRQLDSIIGERGRLDSELRNmQDTVEDYKSKyeDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADSLTDDINFLRAL 290
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVD-LKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 291 YEAELSQMQTHISDTSVVLS---MDNNRSLDldsiiAEVKAQYEDIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 364
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISlidIETNRSRS-----NEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 365 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDARGKLEGLEDALQKAKQDMARLLKEYQELMNVK 444
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 54607171 445 LALDVEIATYRKLLEGEE 462
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-433 |
4.31e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 146 QRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALL-------QEQGTKTVRQNLE-----PMFEQYISNLRRQ 213
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtQELLQEETRQKLNlstrlRQLEDERNSLQEQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 214 LDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADSLtddinflralyEA 293
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-----------EK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 294 ELSQMQTHISDTSVVLsmDNNRSL---------DLDSIIAEVK---AQYEDiaQRSRAEAESwyqTKYEELQVTAGRHGD 361
Cdd:pfam01576 574 TKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALSLARALE 646
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54607171 362 DLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCANLQAAIADAEQrgemALKDARGKLEGLEDALQKAKQDMARL 433
Cdd:pfam01576 647 EALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
292-440 |
5.22e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 292 EAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 368
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54607171 369 EIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGemalKDARGKLEGLEDALQKAkqdmarLLKEYQEL 440
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVA------LAQRVQEL 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
207-404 |
7.66e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 207 ISNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADSLTDDI-N 285
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 286 FLRALYEAELSqmqthISDTSVVLSMDN-----NRSLDLDSII----AEVKAQYEDIAQRSRAEAEswYQTKYEELQVTA 356
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIAdadaDLLEELKADKAELEAKKAE--LEAKLAELEALK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 54607171 357 GRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR 404
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
168-436 |
1.32e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 168 DKVRFLEQQNKVLDTKWALLQEQgtktvrqnLEpMFEQYISNLRRQLDSIIgergrldSELRNMQDTVEDYKSKYEDEIN 247
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ--------IK-TYNKNIEEQRKKNGENI-------ARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 248 KRTAAENEFVTLKKDVDAAY----MNKVELQAKADSLTDDINFLRALYEAElSQMQThISDTsvvlsmdnnrsldlDSII 323
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCP-TCTQQ-ISEG--------------PDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 324 AEVKAQYEDIAQRSRAEaeswyQTKYEELQVTAGRHgDDLRNTKQE----IAEINRMIQRLRSEIDHVKKQCANLQAAIA 399
Cdd:PHA02562 302 TKIKDKLKELQHSLEKL-----DTAIDELEEIMDEF-NEQSKKLLElknkISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270
....*....|....*....|....*....|....*..
gi 54607171 400 DAEqrgemalkdarGKLEGLEDALQKAKQDMARLLKE 436
Cdd:PHA02562 376 DNA-----------EELAKLQDELDKIVKTKSELVKE 401
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
137-441 |
1.78e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 137 LNLQIDPTIQRVRTEEReQIKTLNNKfasfidKVRFLEQQNKVLDTKWALLQEqgtktvrqnlepmfeqyISNLRRQLdS 216
Cdd:PLN02939 126 SDFQLEDLVGMIQNAEK-NILLLNQA------RLQALEDLEKILTEKEALQGK-----------------INILEMRL-S 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 217 IIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTAAENEFV-TLKKDVDAaymnkveLQAKADSLTDDINFLRAlyeaEL 295
Cdd:PLN02939 181 ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVhSLSKELDV-------LKEENMLLKDDIQFLKA----EL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 296 SQMQThiSDTSVVLsMDNNRSLdLDSIIAEVKAQY----EDIAQRSRAEAESWYQtKYEELQVTAGRhgddLRNTKQEIA 371
Cdd:PLN02939 250 IEVAE--TEERVFK-LEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWWE-KVENLQDLLDR----ATNQVEKAA 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 372 EINRMIQRLRSEIDHVKkqcANLQAAIADAEQRGEMALkdARGKLEGLEDALQKAKQDMARLLKEYQELM 441
Cdd:PLN02939 321 LVLDQNQDLRDKVDKLE---ASLKEANVSKFSSYKVEL--LQQKLKLLEERLQASDHEIHSYIQLYQESI 385
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
204-461 |
2.94e-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: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 204 EQYISNLRRQLDS---IIGERGRLDSELRnmqdtVEdyKSKYEDEINKRTAAENEFVTLKKDVDAAYMnkvELQAKADSL 280
Cdd:pfam15921 561 DKVIEILRQQIENmtqLVGQHGRTAGAMQ-----VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDL 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 281 tddinflralyeaELSQMQThISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAEA--ESWYQTKYEELQVTAGR 358
Cdd:pfam15921 631 -------------ELEKVKL-VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEEMETTTNK 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 359 HGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIadAEQRGEMalkDA-RGKLEGLEDALQKAKQDmARLLKEY 437
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI--TAKRGQI---DAlQSKIQFLEEAMTNANKE-KHFLKEE 770
|
250 260
....*....|....*....|....
gi 54607171 438 QELMNVKLAldvEIATYRKLLEGE 461
Cdd:pfam15921 771 KNKLSQELS---TVATEKNKMAGE 791
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
319-468 |
3.21e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 319 LDSIIAEVKAQYEDIAQRSRAEAESWYQTKYE--ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQA 396
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54607171 397 AIADAEQRGEMA---LKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 468
Cdd:TIGR02168 324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-443 |
5.33e-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: 45.53 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 362 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDARGKLEGLEDALQKAKQDMARLLKEYQ 438
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 54607171 439 ELMNV 443
Cdd:COG4942 108 ELLRA 112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
204-436 |
5.58e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 204 EQYISNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEdeinkrtaaenEFVTLKKDVDAAYMNKVELQAKADSLTDD 283
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 284 INFLRALYEaELSQMQTHISDTSVVLSMDNN----RSLDLDSIIAEVKAQYEDI---AQRSRAEAESW------YQTKYE 350
Cdd:PRK02224 281 VRDLRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 351 ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALK---DARGKLEGLEDALQKAK 427
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTAR 439
|
250
....*....|..
gi 54607171 428 QDMA---RLLKE 436
Cdd:PRK02224 440 ERVEeaeALLEA 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
204-479 |
8.62e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 204 EQYI-SNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDeinkrTAAENEFVTLKKDVDAAYMNKVELQAKADSLTD 282
Cdd:COG3206 159 EAYLeQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 283 DINFLRALYEAELSQMQTHISDTSVVLSmdnnrsldlDSIIAEVKAQYEDiAQRSRAEAESWYQTKYEElqvtagrhgdd 362
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAE-LEAELAELSARYTPNHPD----------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 363 lrntkqeiaeinrmIQRLRSEIDHVKKQcanLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMN 442
Cdd:COG3206 293 --------------VIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
250 260 270
....*....|....*....|....*....|....*...
gi 54607171 443 VKLALDVEIATYRKLLEG-EECRLNgEGVGPVNISVVQ 479
Cdd:COG3206 356 LEREVEVARELYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
252-456 |
9.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 252 AENEFVTLKKDVDAAYMNKVELQAKADSLTDDINFLRALY---EAELSQMQTHISDTSVvlsmdnnrslDLDSIIAEVKA 328
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 329 QYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHV---KKQCANLQAAIADAEQRG 405
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELkadKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 54607171 406 EMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRK 456
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
314-456 |
1.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 314 NRSLDLDSIIAEVKAQYEDIAQRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCA 392
Cdd:COG4913 295 AELEELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54607171 393 NLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRK 456
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
361-440 |
1.65e-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: 43.98 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 361 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLEDALQKAKQDMARLLKEYQEL 440
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
288-465 |
2.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 288 RALYEAELSQMQTHISDtsvvlsmdnnrsldLDSIIAEVKAQYEDIAQRSRA----EAESWY-------QTKYEELQ--- 353
Cdd:COG4913 612 LAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAlqrlAEYSWDeidvasaEREIAELEael 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 354 --VTAGrhGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLEDALQKAKQdmA 431
Cdd:COG4913 678 erLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELR--A 749
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 54607171 432 RLLKEYQELM------NVKLALDVEIATYRKLLEGEECRL 465
Cdd:COG4913 750 LLEERFAAALgdaverELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-442 |
3.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 272 ELQAKADSLTDDINFLRALYE---AELSQMQTHISDTSVVLSMDNNRsLDLDSI---IAEVKAQYEDI---------AQR 336
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEaleAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERLdassddlaaLEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 337 SRAEAESWYQTKYEELQVTAGRHGDdlrnTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKL 416
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGR----LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*.
gi 54607171 417 EGLEDALQKAKQDMARLLKEYQELMN 442
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMR 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
207-432 |
3.69e-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: 42.83 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 207 ISNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADSLTDDINF 286
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 287 LRALYEAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAevkaQYEDIAQRSRAEAESwYQTKYEELQVTAGRHGDDLRNT 366
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEE-LRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54607171 367 KQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDARGKLEGLEDALQKAKQDMAR 432
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
193-460 |
6.52e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 193 KTVRQNLEpMFEQYISNLRRQLDSIIGERGRLDsELRNMQDTVEDYKskYEDEINKRTAAENEFVTLKKDVDAAYMNKVE 272
Cdd:TIGR02169 180 EEVEENIE-RLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 273 LQAKADSLTDDINFLralyEAELSQMQTHISDtsvvlsMDNNRSLDLDSIIAEVKAQyedIAQRSRAEAESwyqtkyeel 352
Cdd:TIGR02169 256 LTEEISELEKRLEEI----EQLLEELNKKIKD------LGEEEQLRVKEKIGELEAE---IASLERSIAEK--------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 353 qvtagrhgddlrntKQEIAEINRMIQRLRSEIDHVKKQCANLqaaiadaeqrgEMALKDARGKLEGLEDALQKAKQDMAR 432
Cdd:TIGR02169 314 --------------ERELEDAEERLAKLEAEIDKLLAEIEEL-----------EREIEEERKRRDKLTEEYAELKEELED 368
|
250 260
....*....|....*....|....*...
gi 54607171 433 LLKEYQELMNVKLALDVEIATYRKLLEG 460
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEK 396
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-467 |
9.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 361 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANL----------------QAAIADAEQRGEmALKDARGKLEGLEDALQ 424
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 54607171 425 KAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 467
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
323-456 |
1.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 323 IAEVKAQYEDIAQRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 402
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 54607171 403 QRGEmalkdargkLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRK 456
Cdd:COG4717 467 EDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
190-421 |
1.64e-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: 41.36 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 190 QGTKTVRQNLEPMFEQYiSNLRRQLDSIIGERGRLDSELRN---MQDTVEDYKSKYEDEINKRTAAENEFVTLkkdvdaA 266
Cdd:pfam12128 646 TALKNARLDLRRLFDEK-QSEKDKKNKALAERKDSANERLNsleAQLKQLDKKHQAWLEEQKEQKREARTEKQ------A 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 267 YMNKVE--LQAKADSLTDDINFLRALYEAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRsRAEAESW 344
Cdd:pfam12128 719 YWQVVEgaLDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRY 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 345 YQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEidhVKKQCANLQA---AIADAEQRGEMALKDARGKLEGLED 421
Cdd:pfam12128 798 FDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD---TKLRRAKLEMerkASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
325-462 |
1.69e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 325 EVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR 404
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 54607171 405 gemaLKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEE 462
Cdd:COG1196 297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
145-444 |
1.81e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 145 IQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTK---WALLQE-QGTKTVRQNLEPMFEQYISNLRRQLDSIIGE 220
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKkqfEKIAEElKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 221 RGRLDSELRNMQDTVEDYKSKyedeiNKRTAAENEFVTL--KKDVDAAYMNKVELQAKadslTDDINFLRALYEAELSQM 298
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLK-----NIELTAHCDKLLLenKELTQEASDMTLELKKH----QEDIINCKKQEERMLKQI 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 299 QThisdtsvVLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLR--NTKQEIAEINRM 376
Cdd:pfam05483 537 EN-------LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIENKNKN 609
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54607171 377 IQRLRSEIDHVKKQcanlqaAIADAEQrgemaLKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVK 444
Cdd:pfam05483 610 IEELHQENKALKKK------GSAENKQ-----LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-440 |
2.01e-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: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 319 LDSIIAEVKAQYEDI-AQRSRAEAEswyqtkYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAA 397
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 54607171 398 IADAEQRgemaLKDARGKLEGLEDALQKAKQDMARLLKEYQEL 440
Cdd:COG1196 318 LEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEA 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
212-440 |
2.10e-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: 39.91 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 212 RQLDSIIGERGRLDSELRNMQDTVEdykskyedeinkrtAAENEFVTLKKDVDaaymnkvELQAKADSLTDDINFLRAL- 290
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELA--------------ALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 291 --YEAELSQMQthisdtsvvlsmdNNRslDLDSIIAEVkaqyeDIAQRSRAEAEswyqtkyeelqvtagrhgddlrntkQ 368
Cdd:COG1579 76 kkYEEQLGNVR-------------NNK--EYEALQKEI-----ESLKRRISDLE-------------------------D 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54607171 369 EIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQDM-ARLLKEYQEL 440
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERI 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-453 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 323 IAEVKAQYEDIAQRSRAEAEswyqtKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 402
Cdd:COG1196 262 LAELEAELEELRLELEELEL-----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 54607171 403 QR---GEMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIAT 453
Cdd:COG1196 337 EEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
347-468 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 347 TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGE------MALKDARgKLEGLE 420
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlGNVRNNK-EYEALQ 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 54607171 421 DALQKAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGE 468
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
286-462 |
3.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 286 FLRALYEAELSQMQTHISDTSVVLSMDNNRSLD-LDSIIAEVKAQYEDIAQ---------RSRAEAESWYQTKYEEL--- 352
Cdd:COG4717 42 FIRAMLLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAElqeeleeleEELEELEAELEELREELekl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 353 --QVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK---KQCANLQAAIADAEQRGEMALKD----ARGKLEGLEDAL 423
Cdd:COG4717 122 ekLLQLLPLYQELEALEAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQlslaTEEELQDLAEEL 201
|
170 180 190
....*....|....*....|....*....|....*....
gi 54607171 424 QKAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEE 462
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-390 |
4.07e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 149 RTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgTKTVRQNLEPMfEQYISNLRRQLDSIIGERGRLDSEL 228
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS-INKIKQNLEQK-QKELKSKEKELKKLNEEKKELEEKV 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 229 RNMQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDaaymnkvelqakadslTDDINFLRALYEAELSQMQTHISDtsvv 308
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN----------------KDDFELKKENLEKEIDEKNKEIEE---- 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 309 LSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESwYQTKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVK 388
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-KEKKISSLE-------KELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
..
gi 54607171 389 KQ 390
Cdd:TIGR04523 645 QE 646
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-459 |
9.58e-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: 38.59 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 318 DLDSIIAEVKAQYEDIAQRSRAEAESwyQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAA 397
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 398 IA-------------------------DAEQRGEM-------------ALKDARGKLEGLEDALQKAKQDMARLLKEYQE 439
Cdd:COG4942 106 LAellralyrlgrqpplalllspedflDAVRRLQYlkylaparreqaeELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180
....*....|....*....|
gi 54607171 440 LmnvKLALDVEIATYRKLLE 459
Cdd:COG4942 186 E---RAALEALKAERQKLLA 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
315-462 |
9.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54607171 315 RSLDLDSIIAEVKAQYEDIAQRSRAEAESwyQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANL 394
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEEL--EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54607171 395 QAAIADAEQRG---EMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEE 462
Cdd:COG1196 301 EQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| |
