|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
149-462 |
1.65e-161 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 462.08 E-value: 1.65e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 149 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQEQGSRTVRqNLEPFFDTYVNDLRRQLDGITAERGRLDAELRN 228
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 229 MQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINFYRMIYEAELSQMQNQVSDTSVVLS 308
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 309 MDNNRSLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRSEIDAVKKQ 388
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789317 389 CSSLQTAISDAEQRGELALKDARAKLMELEDALQKAKQDMARLLREYQELMNVKLALDVEIATYRKLLEGEECR 462
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-146 |
8.90e-32 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 120.14 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 16 GFSTASATTPTAGRSRFSSVSVARSSGNSGGLGRisGIGSGFGSRSLYNLGGTRRVSIGGCAGSGFRGGFGGRTSSGFGG 95
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGG--GGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789317 96 SSGFAYGGGIGGGFGGPGFS---------------------------VCPSGGIQEVTVNQSLLTPLNLQIDPTIQRV 146
Cdd:pfam16208 79 FGGGFGGGGGGGFGGGGGFGggfggggyggggfggggfggrggfggpPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-444 |
5.55e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 150 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQEQGSRTVRQNLEpfFDTYVNDLRRQLDGITAERGRLDAELRN 228
Cdd:TIGR02168 674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 229 MQEVVEDFKVR---YEDEINK----RAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINFYRMIY---EAELSQMQN 298
Cdd:TIGR02168 752 LSKELTELEAEieeLEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 299 QVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDI---ANRSRAEAESWYQtKYEELQVTAGRHGDDLRNTKQEISEMNRMI 375
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 376 QRLRSEIDAVKKQCSSLQTAISDAEQR-----------GELALKDARAKLMELEDALQKAKQDMARLLREYQELMNVKLA 444
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-438 |
7.38e-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: 62.01 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 205 VNDLRRQLDGITAERGRLDAELRNMQEVVEDFKVRYE------DEINKR--AAAENEFVGLKKDVDsaymnkvELEAKVD 276
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKikDLGEEEQLRVKEKIG-------ELEAEIA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 277 SLTDQINFY----------RMIYEAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANR------------ 334
Cdd:TIGR02169 305 SLERSIAEKereledaeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkefaetr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 335 ----SRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQrgelalkda 410
Cdd:TIGR02169 385 delkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW--------- 455
|
250 260
....*....|....*....|....*...
gi 29789317 411 raKLMELEDALQKAKQDMARLLREYQEL 438
Cdd:TIGR02169 456 --KLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
206-431 |
1.43e-07 |
|
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: 54.41 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 206 NDLRRQLDGITAERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLtdqinfy 285
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 286 rmiyEAELSQMQNQVSDTSVVLsmDNNRSL---------DLDSIIAEVK---AQYEDiaNRSRAEAESwyqTKYEELQVT 353
Cdd:pfam01576 572 ----EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 354 AGRHGDDLRNTKQEISEMNRMIQ----RLRSEIDAVKKQCSSLQTAISDAEQrgelALKDARAKLMELEDALQKAKQDMA 429
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKL 716
|
..
gi 29789317 430 RL 431
Cdd:pfam01576 717 RL 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-460 |
1.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 205 VNDLRRQLDGITAERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINf 284
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 285 yrmIYEAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAgrhgdDLRNT 364
Cdd:COG1196 327 ---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-----AAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 365 KQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQ---RGELALKDARAKLMELEDALQKAKQDMARLLREYQELMNV 441
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250
....*....|....*....
gi 29789317 442 KLALDVEIATYRKLLEGEE 460
Cdd:COG1196 479 LAELLEELAEAAARLLLLL 497
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
290-430 |
2.84e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.66 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 290 EAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDI-ANRSRAEAesWYQTKYEELQVTAGRHGD---DLRNTK 365
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789317 366 QEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGelalKDARAKL----MELEDALQKAKQDMAR 430
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIadlgRRLNVALAQRVQELNR 194
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
132-438 |
1.39e-06 |
|
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: 51.17 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 132 LTPLNLQIDPTIQRVRKEERE------QIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQEQgsrtvRQNLEPFFDTYV 205
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVElnklekQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ-----KEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 206 NDL---RRQLDGITAERGRLDAELRNMQEVVEDFKvRYEDEINKraaAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQI 282
Cdd:TIGR04523 180 KEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 283 NfyrmIYEAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRsraEAESWYQTKYEELQvtagRHGDDLR 362
Cdd:TIGR04523 256 N----QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ---KEQDWNKELKSELK----NQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 363 NTKQEISEMNRMIQRLRSEIDAVKKQC-------SSLQTAISDAEQRGELALKDARAKLMELEDaLQKAKQDMARLLREY 435
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQ 403
|
...
gi 29789317 436 QEL 438
Cdd:TIGR04523 404 EKL 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-463 |
3.28e-06 |
|
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: 50.06 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 191 RTVRQNLEPFFDTyVNDLRRQLDGIT-----AERGR-LDAELRNMQEVVedFKVRYEDEINKRAAAENEFVGLKKDVDSA 264
Cdd:TIGR02168 182 ERTRENLDRLEDI-LNELERQLKSLErqaekAERYKeLKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 265 YMNKVELEAKVDSLTDQINFYRM---IYEAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRS---RAE 338
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEeieELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLdelAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 339 AESWyQTKYEELQVtagrhgdDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELA---LKDARAKLM 415
Cdd:TIGR02168 339 LAEL-EEKLEELKE-------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneIERLEARLE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 29789317 416 ELEDALQKAKQDMARLLREYQElmNVKLALDVEIATYRKLLEGEECRL 463
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEEL 456
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
193-477 |
5.79e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 193 VRQNLEpffdTYVNDLRRQLDGITAERGRLDAELRNMQEVVEDFKvryedeinkraaAENEFVGLKKDVDSAYMNKVELE 272
Cdd:COG3206 162 LEQNLE----LRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 273 AKVDSLTDQINfyrmIYEAELSQMQNQVSDTSVVLSMDNNrsldlDSIIAEVKAQYEDIanrsraeaeswyQTKYEELQV 352
Cdd:COG3206 226 SQLAEARAELA----EAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAEL------------EAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 353 TAGrhgddlrntkqeisEMNRMIQRLRSEIDAVKKQcssLQTAISDAEQRGELALKDARAKLMELEDALQKAKQDMARLL 432
Cdd:COG3206 285 RYT--------------PNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29789317 433 REYQELMNVKLALDVEIATYRKLLEG-EECRLSgEGVSPVNISVVT 477
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
139-460 |
7.29e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 139 IDPTIQRVRKEE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQEQGSRTVRQNL--EPFFDTYVNDLRRQLDGI 215
Cdd:PRK01156 402 IDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTlgEEKSNHIINHYNEKKSRL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 216 TAERGRLDAELRNMQEVVEDFKVRYE----DEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINFYRMIYEA 291
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 292 ELSQMQNQVSDTSVVLS---MDNNRSLDldsiiAEVKAQYEDIANRSRaEAESWYQTKYEELQVTAGRHGDD---LRNTK 365
Cdd:PRK01156 562 DLDSKRTSWLNALAVISlidIETNRSRS-----NEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLNNKY 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 366 QEISEMNRMIQRLRSEIDAVKKQCSSLQtAISDAEQRGELALKDARAKLMELEDALQKAKQDMARLLREYQELMNVKLAL 445
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
330
....*....|....*
gi 29789317 446 DVEIATYRKLLEGEE 460
Cdd:PRK01156 715 SDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
208-464 |
1.07e-05 |
|
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: 48.53 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 208 LRRQLDGITAERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQI-NFYR 286
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIeNVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 287 MI--YEAELSQMQNQVSdtSVVLSMDNNRSLDLDSIIAEVKAQYEDI-ANRSRAEAeswyqtKYEELQVTAGRHGDDLRN 363
Cdd:TIGR02169 759 ELkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 364 TKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRgelaLKDARAKLMELEDALQKAKQDMARLLREYQELMNVKL 443
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|.
gi 29789317 444 ALDVEIATYRKLLEGEECRLS 464
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLE 927
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
270-466 |
1.25e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 270 ELEAKVDSLTDQinfyrmiyeAELSQ----MQNQVSDTSVVLSMDNNRSLD-----LDSIIAEVKAQYEDIANRSRAEAE 340
Cdd:TIGR02168 197 ELERQLKSLERQ---------AEKAErykeLKAELRELELALLVLRLEELReeleeLQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 341 SWYQTKYE--ELQVTAGRHGDDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELA---LKDARAKLM 415
Cdd:TIGR02168 268 KLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLE 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789317 416 ELEDALQKAKQDMARLLREYQELMNVKLALDVEIATYRK---LLEGEECRLSGE 466
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
210-438 |
1.86e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 210 RQLDGITAERGRLDAELRNMQEVVEDFKVRYEdeinkraAAENEFVGLKKDVDsaymnkvELEAKVDSLTDQInfyrmiy 289
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLE-------AAKTELEDLEKEIK-------RLELEIEEVEARI------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 290 eAELSQMQNQVSdtsvvlsmdNNRslDLDSIIAEVkaqyeDIANRSRAEAEswyqtkyeelqvtagrhgddlrntkQEIS 369
Cdd:COG1579 76 -KKYEEQLGNVR---------NNK--EYEALQKEI-----ESLKRRISDLE-------------------------DEIL 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 370 EMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELALKDARAKLMELEDALQKAKQDM-ARLLREYQEL 438
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERI 183
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-545 |
1.93e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 248 AAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINfyrmIYEAELSQMQNQVSDTSVvlSMDNNRSlDLDSIIAEVKAQ 327
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELE----ELNEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 328 YEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNT---KQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQrge 404
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEA--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 405 lALKDARAKLMELEDALQKAKQDMARLLREYQELMNVKLALDVEIATYRKLLEGEECRLSGEGVSPVNISVVTSTVSSGY 484
Cdd:COG3883 162 -LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789317 485 GGGANIGGGSLGLGGNSGYSFTTSGGHSLGTGLGGSGFTTTSSRGPVGSGSSIKFVSSTSS 545
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASG 301
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-441 |
5.35e-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: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 360 DLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQR---GELALKDARAKLMELEDALQKAKQDMARLLREYQ 436
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 29789317 437 ELMNV 441
Cdd:COG4942 108 ELLRA 112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
205-439 |
5.94e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 205 VNDLRRQLDGITAERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENefvgLKKDVDSAYMNKVELEAKVDSLTDQINF 284
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 285 YRMIYEaELSQMQNQVSDTSVVLSMDNN----RSLDLDSIIAEVKAQYEDI---ANRSRAEAESW------YQTKYEELQ 351
Cdd:PRK02224 284 LRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 352 VTAGRHGDDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELALK---DARAKLMELEDALQKAKQDm 428
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARER- 441
|
250
....*....|.
gi 29789317 429 arlLREYQELM 439
Cdd:PRK02224 442 ---VEEAEALL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-438 |
8.00e-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: 45.14 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 217 AERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINfyrmIYEAELSQM 296
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 297 QNQVSDTSVVLSMDNNRSldldsiIAEVKAQYEDIANRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEISEMNRMIQ 376
Cdd:COG4942 103 KEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789317 377 RLRSEIDAVKKQCSSLQTAISDAEQRGELALKDARAKLMELEDALQKAKQDMARLLREYQEL 438
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
359-438 |
9.79e-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: 44.75 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 359 DDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRgelaLKDARAKLMELEDALQKAKQDMARLLREYQEL 438
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
202-412 |
1.03e-04 |
|
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: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 202 DTYVNDLRRQLDGITAERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDsaymnkvELEAKVDSLTDQ 281
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 282 I-NFYRMIYEAelsqmQNQVSDTSVVLSMDN-----NRSLDLDSIIAEVKAQYEDIaNRSRAEAESwYQTKYEELQVTAG 355
Cdd:COG3883 88 LgERARALYRS-----GGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEEL-KADKAELEA-KKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789317 356 RHGDDLRNTKQE----ISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELALKDARA 412
Cdd:COG3883 161 ALKAELEAAKAEleaqQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-454 |
2.29e-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: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 200 FFDT---YVNDLRRQLdGITAER--------------GRLDAELRNMqeVVEDFKVryEDEInkRAAAENeFvglkKDVD 262
Cdd:COG4913 171 FFDSfsaYLARLRRRL-GIGSEKalrllhktqsfkpiGDLDDFVREY--MLEEPDT--FEAA--DALVEH-F----DDLE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 263 SAYMNKVELEAKVDSLTDQINFYRMIYEAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRsRAEAESW 342
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE-LERLEAR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 343 YQTKYEELQVTAGRH----GDDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELALKDARAKLMELE 418
Cdd:COG4913 318 LDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
250 260 270
....*....|....*....|....*....|....*.
gi 29789317 419 DALQKAKQDMARLLREYQELMNVKLALDVEIATYRK 454
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
123-442 |
2.52e-04 |
|
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: 43.94 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 123 QEVTVNQSLLTPLNLQIdptiQRVRKEEREQIKTLNNKFASfidkvrfLEQQNKVLETKWNLLQE-----------QGSR 191
Cdd:pfam05483 370 QRLEKNEDQLKIITMEL----QKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 192 TVRQNLEPFFDTYVNDLRRQLDGITAERGRLDAELRNMQEVVEDFKVRyedeiNKRAAAENEFVGLKKDVDSAYMNKVEL 271
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK-----NIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 272 EAKvdSLTDQINFYRMIYEAELSQMQNqvsdtsvVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQ 351
Cdd:pfam05483 514 ELK--KHQEDIINCKKQEERMLKQIEN-------LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 352 VTAGRHGDDLR--NTKQEISEMNRMIQRLRSEIDAVKKQcsslqtaiSDAEQRgELALKDARAKLMELEdaLQKAKQDMA 429
Cdd:pfam05483 585 KEKQMKILENKcnNLKKQIENKNKNIEELHQENKALKKK--------GSAENK-QLNAYEIKVNKLELE--LASAKQKFE 653
|
330
....*....|...
gi 29789317 430 RLLREYQELMNVK 442
Cdd:pfam05483 654 EIIDNYQKEIEDK 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
321-454 |
2.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 321 IAEVKAQYEDIANRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAE 400
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 29789317 401 QRGELAlkdaraklmELEDALQKAKQDMARLLREYQELMNVKLALDVEIATYRK 454
Cdd:COG4717 467 EDGELA---------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-440 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 209 RRQLDGITAERGRLDAELRNMQEVVEDFKVRYeDEINKRAAAENEFVGLK-KDVDSAymnkvELEAKVDSLTDQInfyrm 287
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSwDEIDVA-----SAEREIAELEAEL----- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 288 iyeaelsqmqnqvsdtsvvlsmdnnRSLDLDS-IIAEVKAQYEDiANRSRAEAESwyqtKYEELQVTAGRHgddlrntKQ 366
Cdd:COG4913 678 -------------------------ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EK 720
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789317 367 EISEMNRMIQRLRSEIDAVKKQCSSLQTAISDaEQRGELALKDARAKLME-LEDALQKAKQDMARLLREYQELMN 440
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERELREnLEERIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-458 |
4.34e-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: 43.13 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 192 TVRQNLEPFfDTYVNDLRRQLDgiTAERGRLDAElrnmqevvedfkvRYeDEINKRAAaENEFVGLKKDVDSAYMNKVEL 271
Cdd:TIGR02169 181 EVEENIERL-DLIIDEKRQQLE--RLRREREKAE-------------RY-QALLKEKR-EYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 272 EAKVDSLtdqinfyrmiyEAELSQMQNQVSDTSVVLsmdNNRSLDLDSIIAEVKAQYEDIANRsraeaeswYQTKYEELQ 351
Cdd:TIGR02169 243 ERQLASL-----------EEELEKLTEEISELEKRL---EEIEQLLEELNKKIKDLGEEEQLR--------VKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 352 VTAGRHGDDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAIsdAEQRGElalkdaRAKLMEledALQKAKQDMARL 431
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI--EEERKR------RDKLTE---EYAELKEELEDL 369
|
250 260
....*....|....*....|....*..
gi 29789317 432 LREYQELMNVKLALDVEIATYRKLLEG 458
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEK 396
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-431 |
4.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 220 GRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINFYRMIYEaELSQMQNQ 299
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 300 VSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDI-ANRSRAEAESWYQTKYEELqvtagrhGDDLRNTKQEISEMNRMIQRL 378
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELeEKVKELKELKEKAEEYIKL-------SEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789317 379 RSEIDAVKKQCSSLQtaiSDAEQRGELA--LKDARAKLMELED---ALQKAKQDMARL 431
Cdd:PRK03918 320 EEEINGIEERIKELE---EKEERLEELKkkLKELEKRLEELEErheLYEEAKAKKEEL 374
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
317-457 |
5.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 317 LDSIIAEVKAQYEDIANRSRAeaeswYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRS---------EIDAVKK 387
Cdd:COG1579 22 LEHRLKELPAELAELEDELAA-----LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 388 QCSSLQTAISDAEQRgelaLKDARAKLMELEDALQKAKQDMARLLREYQELmnvKLALDVEIATYRKLLE 457
Cdd:COG1579 97 EIESLKRRISDLEDE----ILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-459 |
5.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 316 DLDSIIAEVKAQYEDIANRSRA----EAESWYQTKYEELQVTAGRHGD---DLRNTKQEISEMNRMIQRLRSEIDAVKKQ 388
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789317 389 CSSLQTAISDAEQRgelaLKDARAKLMELEDALQKAKQDMARLLREYQELMNVKLALDVEIATYRKLLEGE 459
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-468 |
6.95e-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: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 359 DDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELALKD----------ARAKLMELEDALQKAKQDM 428
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleqeeekLKERLEELEEDLSSLEQEI 753
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 29789317 429 ARLLREYQELMNVKLALDVEIATYRKLLEGEECRLSGEGV 468
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-457 |
8.41e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 147 RKEE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQEQgsrtvRQNLEPFFDTyVNDLRRQLDGITAERGRLDAE 225
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 226 LRNMQEVVEDFKVRYEdEINKRAAAENEfvgLKKDVDsAYMNKVELEAKVDSLTDQINFYRMIYEAELSQMQNQVSDtsv 305
Cdd:PRK03918 261 IRELEERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 306 vLSMDNNRSLDLDSIIAEVKAQYEDIANRSRAEAESwyQTKYEELQVTAGRHG-----------DDLRNTKQE----ISE 370
Cdd:PRK03918 333 -LEEKEERLEELKKKLKELEKRLEELEERHELYEEA--KAKKEELERLKKRLTgltpeklekelEELEKAKEEieeeISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 371 MNRMIQRLRSEIDAVKKQCSSLQTAIS---------DAEQRGELaLKDARAKLMELEDALQKAKQDMARLLREYQELMNV 441
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
330
....*....|....*.
gi 29789317 442 kLALDVEIATYRKLLE 457
Cdd:PRK03918 489 -LKKESELIKLKELAE 503
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
268-457 |
9.05e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 268 KVELEAKVDSLTDQINFYRMIYEAELSQMQNQVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRAEAE-SWYQTK 346
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 347 YEELQVTAGRHGDDL--------RNTKQEISEMNRMIQR-------LRSEIDAVKKQCSSLQTAISDAEQRGE------L 405
Cdd:pfam05557 84 YLEALNKKLNEKESQladareviSCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQnlekqqS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789317 406 ALKDARAKLMELEDALQKAKQDMARLLREYQELMNV------KLALDVEIATYRKLLE 457
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIpelekeLERLREHNKHLNENIE 221
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
152-436 |
1.21e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.09 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 152 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQEQgsrtvRQNLEPFFDTYVNdLRRQLDGitaergrLDAEL-RNMQ 230
Cdd:pfam09728 18 EKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKE-----KDQLQSELSKAIL-AKSKLEK-------LCRELqKQNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 231 EVVEDFKVRYEDEINKRAAAENEFVGLKKDVdSAYMNK------------VELEAKVDSLTDQINFYRMIYEAELSQM-- 296
Cdd:pfam09728 85 KLKEESKKLAKEEEEKRKELSEKFQSTLKDI-QDKMEEkseknnklreenEELREKLKSLIEQYELRELHFEKLLKTKel 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 297 QNQVSDTS-VVLSMDNNRSLD--LDSIIAEVKAQYEDIanrSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTKQEI 368
Cdd:pfam09728 164 EVQLAEAKlQQATEEEEKKAQekEVAKARELKAQVQTL---SETEKElreqlNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789317 369 SEMNRMIQRLRSEIDAVKKQCSSLQTAIsdaeqrgeLALKDARAKLMELEDALQKAKQDMARLLREYQ 436
Cdd:pfam09728 241 EKMSKKIKKLEKENLTWKRKWEKSNKAL--------LEMAEERQKLKEELEKLQKKLEKLENLCRALQ 300
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-278 |
2.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 144 QRVRKEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKwnlLQEQGSRTVR------QNLEPFFDTYVN----------- 206
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEeleerlKELEPFYNEYLElkdaekelere 617
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789317 207 -----DLRRQLDGITAERGRLDAELRNMQEVVEDFKVRYEDEINKRaaAENEFVGLKKDVDSAYMNKVELEAKVDSL 278
Cdd:PRK03918 618 ekelkKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEI 692
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
359-465 |
2.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 359 DDLRNTKQEISEMNRMIQRLRSEIDAVKKQCS----------------SLQTAISDAEQRGElALKDARAKLMELEDALQ 422
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswdeidvaSAEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 29789317 423 KAKQDMARLLREYQELMNVKLALDVEIATYRKLLEGEECRLSG 465
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
166-434 |
3.84e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 166 DKVRFLEQQNKVLETKWNLLQEQgsrtvrqnlepfFDTYvNDLRRQLDGITAERgrlDAELRNM-QEVVEDFKvRYEDEI 244
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ------------IKTY-NKNIEEQRKKNGEN---IARKQNKyDELVEEAK-TIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 245 NKRAAAENEFVGLKKDVDSAY----MNKVELEAKVDSLTDQINFYRmiyeaelsqmQNQVSDT-SVVLSMDNNRSLDLDS 319
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE----------KGGVCPTcTQQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 320 IIAEVKAQYEDIANRSRAEAESwyQTKYEELQVTagrhgddLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDA 399
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEI--MDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
250 260 270
....*....|....*....|....*....|....*
gi 29789317 400 EqrGELAlkdaraklmELEDALQKAKQDMARLLRE 434
Cdd:PHA02562 378 A--EELA---------KLQDELDKIVKTKSELVKE 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
316-460 |
3.92e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 316 DLDSIIAEVKAQYEDIANRSRAEaeswyQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTA 395
Cdd:COG1196 236 ELEAELEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789317 396 ISDAEQRgelaLKDARAKLMELEDALQKAKQDMARLLREYQELMNVKLALDVEIATYRKLLEGEE 460
Cdd:COG1196 311 RRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
135-439 |
4.68e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 135 LNLQIDPTIQRVRKEEReQIKTLNNKfasfidKVRFLEQQNKVLETKWNLLQEqgsrtvrqnlepffdtyVNDLRRQLDG 214
Cdd:PLN02939 126 SDFQLEDLVGMIQNAEK-NILLLNQA------RLQALEDLEKILTEKEALQGK-----------------INILEMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 215 iTAERGRLDAELRNMQEVVEDFKVRYEDEINKRAAAENEFV-GLKKDVDSAYMNKVeleakvdSLTDQINFYRmiyeAEL 293
Cdd:PLN02939 182 -TDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVhSLSKELDVLKEENM-------LLKDDIQFLK----AEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 294 SQMQNqvSDTSVVLsMDNNRSLdLDSIIAEVKAQY----EDIANRSRAEAESWYQtKYEELQVTAGRhgddlrnTKQEIS 369
Cdd:PLN02939 250 IEVAE--TEERVFK-LEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWWE-KVENLQDLLDR-------ATNQVE 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 370 EMNRMIQRLRSEIDAVKKQCSSLQTAISDAEQRGELALKDARAKLmeLEDALQKAKQDMARLLREYQELM 439
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKL--LEERLQASDHEIHSYIQLYQESI 385
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
359-464 |
5.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 359 DDLRNTKQEISEMNRMIQRLRSEIDAVKKQCSSLQTAISDAE---QRGELALKDARAKLMELEDALQKAKQDMARLLREY 435
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100
....*....|....*....|....*....
gi 29789317 436 QELMNVKLALDVEIATYRKLLEGEECRLS 464
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
156-453 |
7.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 156 TLNNKFASFIDKVRFLEQQnkvletkwnllqeqgsrtvrqnlepffdtyVNDLRRQLDgitaergrlDAELRnmqevVED 235
Cdd:COG3206 165 NLELRREEARKALEFLEEQ------------------------------LPELRKELE---------EAEAA-----LEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 236 FKvryedeinkraaAENEFVGLKKDVDSAYMNKVELEAKVDSLTDQINfyrmIYEAELSQMQNQVSDTSVVLSMDNNrsl 315
Cdd:COG3206 201 FR------------QKNGLVDLSEEAKLLLQQLSELESQLAEARAELA----EAEARLAALRAQLGSGPDALPELLQ--- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789317 316 dlDSIIAEVKAQYEDiANRSRAEAESWYQTKYEELQVTAGRhgddLRNTKQEI-SEMNRMIQRLRSEIDAVKKQCSSLQT 394
Cdd:COG3206 262 --SPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQ----IAALRAQLqQEAQRILASLEAELEALQAREASLQA 334
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789317 395 AISDAEQRGeLALKDARAKLMELEDALQKAKQDMARLLREYQELmnvKLALDVEIATYR 453
Cdd:COG3206 335 QLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEA---RLAEALTVGNVR 389
|
|
| |
