|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
148-461 |
4.94e-163 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 465.93 E-value: 4.94e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 148 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGSRTVRqNLEPLFDSYTSELRRQLESITTERGRLEAELRN 227
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 228 MQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDAELSQLQTQVGDTSVVLS 307
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 308 MDNNRNLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQ 387
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791158 388 CSSLQTAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEECR 461
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-145 |
1.04e-40 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 144.41 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 16 GFSTTSAITPAAGRSRFSSVSVARSAAGSGGLGRISSAGasFGSRSLYNLGGAKRVSIN----------------GCGSS 79
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGG--FGSRSLYNLGGSKSISISvagggsrpgsgfgfggGGGGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791158 80 CRSGFGGRASNRF----GVNSGFGYGGGVGGGFSGPSF--------PVCPPGGIQEVTVNQSLLTPLHLQIDPTIQRV 145
Cdd:pfam16208 79 FGGGFGGGGGGGFggggGFGGGFGGGGYGGGGFGGGGFggrggfggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-465 |
1.54e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 149 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGsRTVRQNLEPLFDSYtSELRRQLESITTERGRLEAELRN 227
Cdd:TIGR02168 674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 228 MQDVVEDFKVRYEDEINKRTAAENEFVALKKdvdaaymNKVELEAKVKSLPEEINfihsVFDAELSQLQTQVGDTSVVLS 307
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 308 MDNNRNLDLDSIIAEVKAQYEDIANRSRAEAE--SWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVK 385
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 386 KQCSSLQTAIADAEQrgelALKDARAKLVDLEEALQKAKQDMARLLR----EYQELMNIKLALDVEIATYRKLLEGEECR 461
Cdd:TIGR02168 901 EELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
....
gi 153791158 462 LSGE 465
Cdd:TIGR02168 977 LENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-459 |
3.55e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 206 ELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIh 285
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 286 svfDAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRAEAESW--YQTKYEELQVTAGRHGDDLRNT 363
Cdd:COG1196 322 ---EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 364 KQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQ---RGELALKDARAKLVDLEEALQKAKQDMARLLREYQELMNI 440
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250
....*....|....*....
gi 153791158 441 KLALDVEIATYRKLLEGEE 459
Cdd:COG1196 479 LAELLEELAEAAARLLLLL 497
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
289-437 |
3.83e-08 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 55.36 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 289 DAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDI-ANRSRAEAesWYQTKYEELQVTAGRHGD---DLRNTK 364
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791158 365 QEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGelalKDARAKLVDLEEALQKAkqdmarLLREYQEL 437
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVA------LAQRVQEL 192
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-445 |
7.34e-08 |
|
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: 55.41 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 141 TIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKwalLQEQgsrtvrQNLEPLFDSytselrrQLESITTERGR 220
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQ------EKLNQQKDE-------QIKKLQQEKEL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 221 LEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDaaymnkvELEAKVKSLPEEINFIHSvfdaELSQLQTQVG 300
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQ----NLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 301 DTSVVLSMDNNRNLDLDSIIAEVKAQY------EDIANRSRAEAESWYQTKYEELQvtagrhGDDLRNTKQ----EISEM 370
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKIsslkekIEKLESEKKEKESKISDLEDELN------KDDFELKKEnlekEIDEK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 371 NRMIQRLRAEIDSVKKQCSSLQTAIADAEQ-----RGELALKDarAKLVDLEEALQKAKQDMARLLreyQELMNIKLALD 445
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKekkdlIKEIEEKE--KKISSLEKELEKAKKENEKLS---SIIKNIKSKKN 641
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
192-476 |
1.34e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 192 VRQNLEplfdSYTSELRRQLESITTERGRLEAELRNMQDVVEDFKvryedeinkrtaAENEFVALKKDVDAAYMNKVELE 271
Cdd:COG3206 162 LEQNLE----LRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 272 AKVKSLPEEINFIhsvfDAELSQLQTQVGDTSVVLSMDNNrnldlDSIIAEVKAQYEDIanrsraeaeswyQTKYEELQV 351
Cdd:COG3206 226 SQLAEARAELAEA----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAEL------------EAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 352 TAGrhgddlrntkqeisEMNRMIQRLRAEIDSVKKQcssLQTAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLL 431
Cdd:COG3206 285 RYT--------------PNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 153791158 432 REYQELMNIKLALDVEIATYRKLLEG-EECRLSgEGVSPVNISVVT 476
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
151-456 |
1.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 151 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQgsrtvRQNLEPLFDSYTsELRRQLESITTERGRLEAELRNMQD 230
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 231 VVEDFKVRYED------EINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDaELSQLQTQVGDTSV 304
Cdd:PRK03918 267 RIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 305 VLSMDNNRNLDLD------SIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLR 378
Cdd:PRK03918 346 KLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 379 AEIDSVKK---QCSSLQTAIaDAEQRGELaLKDARAKLVDLEEALQKAKQDMARLLREYQELmNIKLALDVEIATYRKLL 455
Cdd:PRK03918 426 KAIEELKKakgKCPVCGREL-TEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELA 502
|
.
gi 153791158 456 E 456
Cdd:PRK03918 503 E 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
141-461 |
5.72e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 141 TIQRVRAEEREqiKTLNNKFASFIDKVRFLEQQN------------KVLETKWALLQEQGSRTVRQNLEPLF------DS 202
Cdd:pfam15921 485 TAKKMTLESSE--RTVSDLTASLQEKERAIEATNaeitklrsrvdlKLQELQHLKNEGDHLRNVQTECEALKlqmaekDK 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 203 YTSELRRQLESITTERGRLEAELRNMQdvVEdfKVRYEDEINKRTAAENEFVALKKDVDAAYMnkvELEAKVKslpeein 282
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVS------- 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 283 fihsvfDAELSQLQTqVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRAEA--ESWYQTKYEELQVTAGRHGDDL 360
Cdd:pfam15921 629 ------DLELEKVKL-VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEEMETTTNKLKMQL 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 361 RNTKQEISE---------------------MNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELaLKDARAKLVDLEEA 419
Cdd:pfam15921 702 KSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELST 780
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 153791158 420 LQKAKQDMA---RLLREYQELMNIKLAlDVEIATYRKLLEGEECR 461
Cdd:pfam15921 781 VATEKNKMAgelEVLRSQERRLKEKVA-NMEVALDKASLQFAECQ 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-437 |
5.84e-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: 52.76 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 206 ELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIH 285
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 286 SVFD---AELSQLQTQVGdtSVVLSMDNNRNLDLDSIIAEVKAQYEDI-ANRSRAEAeswyqtKYEELQVTAGRHGDDLR 361
Cdd:TIGR02169 758 SELKeleARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791158 362 NTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQ---RGELALKDARAKLVDLEEALQKAKQDMARLLREYQEL 437
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEeleELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-459 |
1.16e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 190 RTVRQNLEPLFDSyTSELRRQLES-------------ITTERGRLEAELRNMQDvvEDFKVRYEDEINKRTAAENEFVAL 256
Cdd:COG1196 182 EATEENLERLEDI-LGELERQLEPlerqaekaeryreLKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 257 KKDVDAAYMNKVELEAKVKSLPEEINfihsVFDAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRA 336
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELE----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 337 EAEswyqtKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQcsslQTAIADAEQRGELALKDARAKLVDL 416
Cdd:COG1196 335 LEE-----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 153791158 417 EEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEE 459
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-465 |
1.69e-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: 51.21 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 316 LDSIIAEVKAQYEDIANRSRAEAESWYQTKYE--ELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQT 393
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791158 394 AIADAEQRGELA---LKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRK---LLEGEECRLSGE 465
Cdd:TIGR02168 324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
187-432 |
2.06e-06 |
|
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: 50.99 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 187 QGSRTVRQNLEPLFDSYTSELRRQLESIT-------TERGRLEAELRNMQDVVEDFKVRYEDEinKRTAAENEFVALKKD 259
Cdd:pfam12128 646 TALKNARLDLRRLFDEKQSEKDKKNKALAerkdsanERLNSLEAQLKQLDKKHQAWLEEQKEQ--KREARTEKQAYWQVV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 260 VDaaymnkvELEAKVKSLPEEINFIHSVFDAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRsRAEAE 339
Cdd:pfam12128 724 EG-------ALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVL 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 340 SWYQTKYEELQVTAGRHGDDLRNTKQEISEMNrmiQRLRAEIDSVKKQCSSLqtaiadaeqrgELALKDARAKLVDLEEA 419
Cdd:pfam12128 796 RYFDWYQETWLQRRPRLATQLSNIERAISELQ---QQLARLIADTKLRRAKL-----------EMERKASEKQQVRLSEN 861
|
250
....*....|...
gi 153791158 420 LQKAKQDMARLLR 432
Cdd:pfam12128 862 LRGLRCEMSKLAT 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-456 |
2.15e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 182 ALLQEQgsRTVRQNLEPLFDSyTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVD 261
Cdd:TIGR02169 692 SLQSEL--RRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 262 aaymnkvELEAKVKSLPEEINFI-----HSVF---DAELSQLQTQVGDTSVVLSMDN---------------------NR 312
Cdd:TIGR02169 769 -------ELEEDLHKLEEALNDLearlsHSRIpeiQAELSKLEEEVSRIEARLREIEqklnrltlekeylekeiqelqEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 313 NLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTaGRHGD---DLRNTKQEISEMNRMIQRLRAEIDSVKKQCS 389
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-SRLGDlkkERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 390 SLQTAIADAEQR----------------GELALKDARAKLVDLEEALQ-------KAKQDMARLLREYQELMNIKLALDV 446
Cdd:TIGR02169 921 ELKAKLEALEEElseiedpkgedeeipeEELSLEDVQAELQRVEEEIRalepvnmLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
330
....*....|
gi 153791158 447 EIATYRKLLE 456
Cdd:TIGR02169 1001 ERKAILERIE 1010
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
138-459 |
2.21e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 138 IDPT-IQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGSRTV------RQNLEPLFDSYTSELRRQ 210
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgEEKSNHIINHYNEKKSRL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 211 LESITtergRLEAELRNMQDVVEDFKVRYE----DEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHS 286
Cdd:PRK01156 482 EEKIR----EIEIEVKDIDEKIVDLKKRKEylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 287 VFDAELSQLQTQVGDTSVVLSmdnnrNLDLDSIIA---EVKAQYEDIANRSRaEAESWYQTKYEELQVTAGRHGDD---L 360
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannL 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 361 RNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQtAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQELMNI 440
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
330
....*....|....*....
gi 153791158 441 KLALDVEIATYRKLLEGEE 459
Cdd:PRK01156 711 INELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-462 |
3.27e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 191 TVRQNLEpLFDSYTSELRRQLESITTERGRLEaelrnmqdvvedfkvRYeDEINKRTAaENEFVALKKDVDAAYMNKVEL 270
Cdd:TIGR02169 181 EVEENIE-RLDLIIDEKRQQLERLRREREKAE---------------RY-QALLKEKR-EYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 271 EAKVKSLPEEInfihSVFDAELSQLQTQVgdtsvvlsmdNNRNLDLDSIIAEVKAQYEDIANRsraeaeswYQTKYEELQ 350
Cdd:TIGR02169 243 ERQLASLEEEL----EKLTEEISELEKRL----------EEIEQLLEELNKKIKDLGEEEQLR--------VKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 351 VTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSV--------------KKQCSSLQTAIADAEQRGEL----------AL 406
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaeieelereieeeRKRRDKLTEEYAELKEELEDlraeleevdkEF 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791158 407 KDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEECRL 462
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-430 |
3.64e-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: 50.17 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 143 QRVRAEEREQIKTLNNKFASFIDKVRFLEQQN-------KVLETKWALLQEQGSRTVRQNLE------PLFDSYTSeLRR 209
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvSSLESQLQDTQELLQEETRQKLNlstrlrQLEDERNS-LQE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 210 QLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINfihsvfd 289
Cdd:pfam01576 504 QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN------- 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 290 aelsQLQTQVGDTSVVLsmDNNRNL---------DLDSIIAEVK---AQYEDiaNRSRAEAESwyqTKYEELQVTAGRHG 357
Cdd:pfam01576 577 ----RLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALSLARAL 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 358 DDLRNTKQEISEMNRMiqrLRAEI-------DSVKKQCSSLQTAIADAEQrgelALKDARAKLVDLEEALQKAKQDMARL 430
Cdd:pfam01576 646 EEALEAKEELERTNKQ---LRAEMedlvsskDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
151-444 |
9.77e-06 |
|
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: 47.64 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 151 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQgsrtvrqnleplFDSYTSELRRqleSITTeRGRLEAELRNMQ- 229
Cdd:pfam09728 18 EKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKE------------KDQLQSELSK---AILA-KSKLEKLCRELQk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 230 ---DVVEDFKVRYEDEINKRTAAENEFVALKKDVDAaYMNK------------VELEAKVKSLPEEINFIHSVFDAELSQ 294
Cdd:pfam09728 82 qnkKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQD-KMEEkseknnklreenEELREKLKSLIEQYELRELHFEKLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 295 --LQTQVGDTS-VVLSMDNNRNLD--LDSIIAEVKAQYEDIanrSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTK 364
Cdd:pfam09728 161 keLEVQLAEAKlQQATEEEEKKAQekEVAKARELKAQVQTL---SETEKElreqlNLYVEKFEEFQDTLNKSNEVFTTFK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 365 QEISEMNRMIQRLRAEIDSVKKQCSSLQTAIAD-AEQRgelalkdaraklvdleealQKAKQDMARLLREYQELMNIKLA 443
Cdd:pfam09728 238 KEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEmAEER-------------------QKLKEELEKLQKKLEKLENLCRA 298
|
.
gi 153791158 444 L 444
Cdd:pfam09728 299 L 299
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-453 |
1.59e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 142 IQRVRAEEREQIKTLNNKFASF---IDKVRFLEQQNKVLETKWALLQEQGSRTVRQNLEPLFDSYtSELRRQLESITTER 218
Cdd:COG4717 137 LEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 219 GRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVAL------------------------------------------ 256
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllar 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 257 KKDVDAAYMNKVEL--------EAKVKSLPEEINFIHSVFDAELSQLQTQVGDTSVVLS--MDNNRNLDLDSIIAEVKAQ 326
Cdd:COG4717 296 EKASLGKEAEELQAlpaleeleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaEELEEELQLEELEQEIAAL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 327 YEDIANRSRAEAESWYQT--KYEELQVTAGRHGDDLRNTKQEI---------SEMNRMIQRLRAEIDSVKKQCSSLQTAI 395
Cdd:COG4717 376 LAEAGVEDEEELRAALEQaeEYQELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEELEEELEELREEL 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791158 396 ADAEQRGELALKDARakLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRK 453
Cdd:COG4717 456 AELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
249-453 |
2.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 249 AENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFD---AELSQLQTQVGDTsvvlsmdnnrNLDLDSIIAEVKA 325
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 326 QYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNT---KQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQrg 402
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEA-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791158 403 elALKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRK 453
Cdd:COG3883 162 --LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
359-435 |
4.01e-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: 45.91 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 359 DLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQR-----GELA-----LKDARAKLVDLEEALQKAKQDMA 428
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleQELAaleaeLAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 153791158 429 RLLREYQ 435
Cdd:COG4942 108 ELLRALY 114
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-437 |
6.54e-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: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 358 DDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRgelaLKDARAKLVDLEEALQKAKQDMARLLREYQEL 437
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
208-439 |
6.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 208 RRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAEN--EFVALKKDVDAAymnkveleakvkslpeeinfih 285
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASA---------------------- 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 286 svfDAELSQLQTQVgdtsvvlsmdnnRNLDLDS-IIAEVKAQYEDiANRSRAEAESwyqtKYEELQVTAGRHgddlrntK 364
Cdd:COG4913 667 ---EREIAELEAEL------------ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------E 719
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791158 365 QEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADaEQRGELALKDARAKLVD-LEEALQKAKQDMARLLREYQELMN 439
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERELREnLEERIDALRARLNRAEEELERAMR 794
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
142-441 |
7.97e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 142 IQRVRAEEREQIKTLNNKFASfidkvrfLEQQNKVLETKWALLQEQGS--------RTVRQNLEPLFDSYTSE---LRRQ 210
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEKKQfekiaeelKGKEQELIFLLQAREKEihdLEIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 211 LESITTERGRLEAELRNMQDVVEDFKVRyedeiNKRTAAENEFVALKKDVDAAYMNKVELEakVKSLPEEINFIHSVFDA 290
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLK-----NIELTAHCDKLLLENKELTQEASDMTLE--LKKHQEDIINCKKQEER 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 291 ELSQLQTqvgdtsvVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLR--NTKQEIS 368
Cdd:pfam05483 532 MLKQIEN-------LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIE 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791158 369 EMNRMIQRLRAEIDSVKKQCSslqtaiADAEQrgelaLKDARAKLVDLEEALQKAKQDMARLLREYQELMNIK 441
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGS------AENKQ-----LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
315-418 |
8.13e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 315 DLDSIIAEVKAQYEDIANRSRAEAESW--YQTKYE-ELQvtagRHGDD---LRNTKQEISEMNRMIQRLRAEIDSVKKQC 388
Cdd:pfam07926 12 RLKEEAADAEAQLQKLQEDLEKQAEIAreAQQNYErELV----LHAEDikaLQALREELNELKAEIAELKAEAESAKAEL 87
|
90 100 110
....*....|....*....|....*....|
gi 153791158 389 SSLQTAIADAEQRGELALKDARAKLVDLEE 418
Cdd:pfam07926 88 EESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-441 |
8.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 151 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQgsrtvRQNLEPLFDSYTSELRRQLESITT---ERGRLEAELRN 227
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ-----KEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 228 MQDVVEDFKvRYEDEINKrtaAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDAELSQLQTQVGDtsvvLS 307
Cdd:TIGR04523 206 LKKKIQKNK-SLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 308 MDNNRNLDLDSIIAEVKAQYEDIANRsraEAESWYQTKYEELQvtagRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQ 387
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQ---KEQDWNKELKSELK----NQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791158 388 C-------SSLQTAIADAEQRGELALKDARAKLVDLEEaLQKAKQDMARLLREYQELMNIK 441
Cdd:TIGR04523 351 LtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQK 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
205-437 |
9.21e-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: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 205 SELRRQLESittERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFI 284
Cdd:COG4942 19 ADAAAEAEA---ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 285 HsvfdAELSQLQTQVGDTSVVLSMDNNRNldldsiIAEVKAQYEDIANRSRAEAesWYQTKYEELQvtagRHGDDLRNTK 364
Cdd:COG4942 96 R----AELEAQKEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791158 365 QEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQEL 437
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
166-410 |
1.99e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 166 KVRFL---EQQNKVLETkwalLQEQGSRTVRQNLEPLFDSYTSELRR----------QLESITTERGRLEAELRNMQDV- 231
Cdd:PRK05771 8 KVLIVtlkSYKDEVLEA----LHELGVVHIEDLKEELSNERLRKLRSlltklsealdKLRSYLPKLNPLREEKKKVSVKs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 232 VEDFKVRYEDEINKrtaAENEFVALKKDVDaaymnkvELEAKVKSLPEEINFIHSV--FDAELSQLQTQvGDTSVVLSMD 309
Cdd:PRK05771 84 LEELIKDVEEELEK---IEKEIKELEEEIS-------ELENEIKELEQEIERLEPWgnFDLDLSLLLGF-KYVSVFVGTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 310 NNRNLDLDSIIAEVKAQYED----------IANRSRAEAESWYQTK---YEELQVTAGRHGDD-LRNTKQEISEMNRMIQ 375
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgFERLELEEEGTPSElIREIKEELEEIEKERE 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 153791158 376 RLRAEIDSVKKQCSSLQTAIADA----EQRGELALKDAR 410
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALYEYleieLERAEALSKFLK 271
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
269-453 |
2.85e-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: 42.60 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 269 ELEAKVKSLPEEINFIhsvfDAELSQLQTQVGDTSVVLSmdnnrnlDLDSIIAEVKAQYEDIANRsraeaeswyQTKYEE 348
Cdd:COG1579 21 RLEHRLKELPAELAEL----EDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEAR---------IKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 349 LQVTAgrhgddlRNTKQeisemnrmIQRLRAEIDSVKKQCSSLQTAIADAEQRgelaLKDARAKLVDLEEALQKAKQDMA 428
Cdd:COG1579 81 QLGNV-------RNNKE--------YEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELE 141
|
170 180
....*....|....*....|....*
gi 153791158 429 RLLREYQELMNiklALDVEIATYRK 453
Cdd:COG1579 142 EKKAELDEELA---ELEAELEELEA 163
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-470 |
3.07e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 122 QEVTVNQSLLTPLHL-----QIDPTIQRVRAEEREQIKTLNNKFasfiDKVRFLEQQNKVLET---KWALLQEQGSRTVR 193
Cdd:pfam17380 263 QTMTENEFLNQLLHIvqhqkAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLEEAekaRQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 194 QnleplfDSYTSELRRQLESITTERGRLEAE-LRNMQDVVEDFKVRYEDEINKRTAAENEFValKKDVDAAYMNKVELEA 272
Cdd:pfam17380 339 Q------ERMAMERERELERIRQEERKRELErIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 273 KVKSLPEEINFIHSVFDAELSQLQTQVGdtsvvlSMDNNRNLDLDSIIAEVKAQYEDIaNRSRAEAESWYQTKYEElqvt 352
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVR------RLEEERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLEL---- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 353 agrhgDDLRNTKQEISEMNRMI------QRLRAEIDS------VKKQCSSLQTAIADAEQRGElaLKDARAKLVDLEEAl 420
Cdd:pfam17380 480 -----EKEKRDRKRAEEQRRKIlekeleERKQAMIEEerkrklLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEER- 551
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 153791158 421 QKAKQDMARLLREYQELMniklALDVEIATYRKLLEGEECRLSGEGVSPV 470
Cdd:pfam17380 552 RRIQEQMRKATEERSRLE----AMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
315-458 |
3.48e-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: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 315 DLDSIIAEVKAQYEDIANRSRA----EAESWYQTKYEELQVTAGRHGD---DLRNTKQEISEMNRMIQRLRAEIDSVKKQ 387
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791158 388 CSSLQTAIADAEQRgelaLKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGE 458
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
218-425 |
3.68e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 218 RGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDV----------DAA----YMNKVELEAKVKSLPEEINF 283
Cdd:pfam01576 63 RARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIqdleeqldeeEAArqklQLEKVTTEAKIKKLEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 284 I---HSVFDAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRAEAESWyqtkyEELQVTAgrhgddl 360
Cdd:pfam01576 143 LedqNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGR-----QELEKAK------- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791158 361 RNTKQEISEMNRMIQRLRAEIDSVKKQCS----SLQTAIADAE----QRGEL--ALKDARAKLVDLEEALQKAKQ 425
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAkkeeELQAALARLEeetaQKNNAlkKIRELEAQISELQEDLESERA 285
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
141-467 |
4.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 141 TIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVletkWALLQEQgsRTVRQNLEPLFDSYTsELRRQLESITtergR 220
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQL----LPLYQEL--EALEAELAELPERLE-ELEERLEELR----E 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 221 LEAELRNMQDVVEDFKVRYEDEINKRT-AAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDA--------- 290
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleneleaaa 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 291 ---ELSQLQTQVGDTSVVLSMDNNRNLDLDSI----------------IAEVKAQYEDIANRSRAEAESWYQTK---YEE 348
Cdd:COG4717 241 leeRLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEeleEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 349 LQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELalkdARAKLVDLEEALQKAKQdma 428
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL----AEAGVEDEEELRAALEQ--- 393
|
330 340 350
....*....|....*....|....*....|....*....
gi 153791158 429 rlLREYQELMNIKLALDVEIATYRKLLEGEECRLSGEGV 467
Cdd:COG4717 394 --AEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
316-456 |
4.21e-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: 42.22 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 316 LDSIIAEVKAQYEDIANRSRAeaeswYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVK--KQCSSLQT 393
Cdd:COG1579 22 LEHRLKELPAELAELEDELAA-----LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791158 394 AIADAEQRGELA---LKDARAKLVDLEEALQKAKQDMARLLREYQELmniKLALDVEIATYRKLLE 456
Cdd:COG1579 97 EIESLKRRISDLedeILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
312-467 |
4.69e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 312 RNLDLDSIIAEVKAQY------EDIANRSRAEAEswyqtkyEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVK 385
Cdd:COG2433 361 PDVDRDEVKARVIRGLsieealEELIEKELPEEE-------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 386 KQCSSLQTAIADAEQRGELALKDARAKlVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEEcrlSGE 465
Cdd:COG2433 434 AELEEKDERIERLERELSEARSEERRE-IRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH---SGE 509
|
..
gi 153791158 466 GV 467
Cdd:COG2433 510 LV 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-446 |
6.16e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 147 AEEREQIKTLN---NKFASFI----DKVRFLEQQNKVLETKWALLQEQGSRTVRQnleplfdsyTSELRRQLESITTERG 219
Cdd:pfam01576 169 AEEEEKAKSLSklkNKHEAMIsdleERLKKEEKGRQELEKAKRKLEGESTDLQEQ---------IAELQAQIAELRAQLA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 220 RLEAELRNMQDvvedfkvRYEDEINKRTAA-------ENEFVALKKDVDAAYMNKVELEAKVKSLPEeinfihsvfdaEL 292
Cdd:pfam01576 240 KKEEELQAALA-------RLEEETAQKNNAlkkirelEAQISELQEDLESERAARNKAEKQRRDLGE-----------EL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 293 SQLQTQVGDTsvvlsmdnnrnldLDSIIA--EVKAQYE-DIANRSRAEAEswyQTKYEELQVTAGR--HG-------DDL 360
Cdd:pfam01576 302 EALKTELEDT-------------LDTTAAqqELRSKREqEVTELKKALEE---ETRSHEAQLQEMRqkHTqaleeltEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 361 RNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQR---GELALKDARAKLVDLEEALQKAKQDMARLLREYQ-- 435
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELEsv 445
|
330
....*....|....*...
gi 153791158 436 -------ELMNIKLALDV 446
Cdd:pfam01576 446 ssllneaEGKNIKLSKDV 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-331 |
7.58e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 147 AEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQgSRTVRQNLeplfdsytSELRRQLESITTERGRLEAELR 226
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-LETLRSKV--------AQLELQIASLNNEIERLEARLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 227 NMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVE-----LEAKVKSLPEEINFIHSVFDAELSQLQTQVGD 301
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQeelerLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190
....*....|....*....|....*....|
gi 153791158 302 TSVVLSMDNNrNLDLDSIIAEVKAQYEDIA 331
Cdd:TIGR02168 491 LDSLERLQEN-LEGFSEGVKALLKNQSGLS 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
315-453 |
7.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 315 DLDSIIAEVKAQYEDIANRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQT 393
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 394 AIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRK 453
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
168-438 |
7.78e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 168 RFLEQQNKVLETKWALLQEQGSRTVRQNLEPLfDSYTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYED------ 241
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLNGL-ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletlea 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 242 EINK----RTAAENEFVALKKDVDaaymnkvELEAKVKSLPEEINfiHSVFDAELSQLQtqvgDTSVVLSMDnnrnlDLD 317
Cdd:PRK02224 259 EIEDlretIAETEREREELAEEVR-------DLRERLEELEEERD--DLLAEAGLDDAD----AEAVEARRE-----ELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 318 SIIAEVKAQYEDI---ANRSRAEAESW------YQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQC 388
Cdd:PRK02224 321 DRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 153791158 389 SSLQTAIADAEQRGELALK---DARAKLVDLEEALQKAKQDmarlLREYQELM 438
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREerdELREREAELEATLRTARER----VEEAEALL 449
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-423 |
8.39e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 201 DSYTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSL--- 277
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 278 ----PEEINFIHSVFDAE-LSQLQTQVGDTSVVLSMDNNrnldldsIIAEVKAQYEDIANRsRAEAESwyqtKYEELQVT 352
Cdd:COG3883 95 lyrsGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADAD-------LLEELKADKAELEAK-KAELEA----KLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791158 353 AGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELALKDARAKLVDLEEALQKA 423
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
219-459 |
9.25e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 219 GRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDaELSQLQTQ 298
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 299 VGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDI-ANRSRAEAESWYQTKYEELqvtagrhGDDLRNTKQEISEMNRMIQRL 377
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELeEKVKELKELKEKAEEYIKL-------SEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 378 RAEIDSVKKQcsslqtaIADAEQRGElALKDARAKLVDLEEALQKAKQDmarlLREYQELMniklALDVEIATYRKLLEG 457
Cdd:PRK03918 320 EEEINGIEER-------IKELEEKEE-RLEELKKKLKELEKRLEELEER----HELYEEAK----AKKEELERLKKRLTG 383
|
..
gi 153791158 458 EE 459
Cdd:PRK03918 384 LT 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-459 |
1.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 283 FIHSVFDAELSQLQTQVGDTSVVLSMDNNRNLD-LDSIIAEVKAQYEDIA---------NRSRAEAESWYQTKYEEL--- 349
Cdd:COG4717 42 FIRAMLLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAelqeeleelEEELEELEAELEELREELekl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 350 --QVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVK---KQCSSLQTAIADAEQRGELALKD----ARAKLVDLEEAL 420
Cdd:COG4717 122 ekLLQLLPLYQELEALEAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQlslaTEEELQDLAEEL 201
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791158 421 QKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEE 459
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-467 |
1.45e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 131 LTPLHLQIDPTIQRVRaEEREQIKTLNNKFASFIDKV-----RFLEQQNKVLETKWALLQEQGSR-TVRQNLEPLFDSYt 204
Cdd:TIGR02169 401 INELKRELDRLQEELQ-RLSEELADLNAAIAGIEAKIneleeEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEY- 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 205 SELRRQLESITTERGRLEAELRNMQDVVEDFKvRYEDEINKR-----------------------TAAEN--EFVALKKD 259
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGR-AVEEVLKASiqgvhgtvaqlgsvgeryataieVAAGNrlNNVVVEDD 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 260 VDAAY-----------------MNKVELEAKVKSLPEE-------INFIHsvFDAELSQLQTQV-GDTSVVLSMDNNRNL 314
Cdd:TIGR02169 558 AVAKEaiellkrrkagratflpLNKMRDERRDLSILSEdgvigfaVDLVE--FDPKYEPAFKYVfGDTLVVEDIEAARRL 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 315 ----DLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHgddlrntkqEISEMNRMIQRLRAEIDSVKKQCSS 390
Cdd:TIGR02169 636 mgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRE---------RLEGLKRELSSLQSELRRIENRLDE 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 391 LQTAIADAEQRGELALKD----------ARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEEC 460
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEieqleqeeekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA 786
|
....*..
gi 153791158 461 RLSGEGV 467
Cdd:TIGR02169 787 RLSHSRI 793
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
202-286 |
1.84e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 202 SYTSELRRQLESITTERGRLEAELRNMQDVVEDfKVRYEDEINKRtaaENEFVALKKDVDAAYMNKVELEAKVKSLPEEI 281
Cdd:COG2433 427 AEVEELEAELEEKDERIERLERELSEARSEERR-EIRKDREISRL---DREIERLERELEEERERIEELKRKLERLKELW 502
|
....*
gi 153791158 282 NFIHS 286
Cdd:COG2433 503 KLEHS 507
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
364-471 |
2.77e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 38.60 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 364 KQEISEMNRMIQRLRAEIDSVKKQcsslqtaiadAEQRGELALKDARAKLV--------DLEEALQKAKQDmarllreyQ 435
Cdd:COG0576 5 EAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLAedllpvldNLERALAAAEED--------E 66
|
90 100 110
....*....|....*....|....*....|....*.
gi 153791158 436 ELMNIKLALDveiATYRKLLEGeecrLSGEGVSPVN 471
Cdd:COG0576 67 DVKSLLEGVE---MTLKQLLDV----LEKHGVEEIE 95
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
165-429 |
3.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 165 DKVRFLEQQNKVLETKWALLQEQ---------GSRTV-RQNLEPLFDSYTsELRRQLESITTERGRLEAELRNMQDVVED 234
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQiktynknieEQRKKnGENIARKQNKYD-ELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 235 fkvrYEDEINKRTaaenefvalkkdvdaayMNKVELEAKVKSLPEEINFIHS--VFDAELSQLQTQvgdtsvvlsmdNNR 312
Cdd:PHA02562 253 ----PSAALNKLN-----------------TAAAKIKSKIEQFQKVIKMYEKggVCPTCTQQISEG-----------PDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 313 NLDLDSIIAEVKAQYEDIANRSRAEAESwyQTKYEELQVTagrhgddLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQ 392
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEEI--MDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
|
250 260 270
....*....|....*....|....*....|....*..
gi 153791158 393 TAIADAeqrgelalKDARAKLVDLEEALQKAKQDMAR 429
Cdd:PHA02562 372 AEFVDN--------AEELAKLQDELDKIVKTKSELVK 400
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
369-430 |
4.34e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.07 E-value: 4.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791158 369 EMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELA---LKDARAKLVDLEEALQKAKQDMARL 430
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLqakERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
140-436 |
5.80e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 140 PTIQRV---RAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQeqGSRTVRQNLEPLFDSYTSELRRQLESITT 216
Cdd:TIGR00606 681 PVCQRVfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML--GLAPGRQSIIDLKEKEIPELRNKLQKVNR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 217 ERGRLEAELRNMQDVVEdfKVRYEDEINKrtaaenefvALKKDV---DAAYMNKVELEAKVKSLPEEINFIHsvFDAELS 293
Cdd:TIGR00606 759 DIQRLKNDIEEQETLLG--TIMPEEESAK---------VCLTDVtimERFQMELKDVERKIAQQAAKLQGSD--LDRTVQ 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 294 QLQTQVGDtsvvlsmdnnRNLDLDSIIAEVKAQYEDIANRSraEAESWYQTKYEELQV----------TAGRHGDDLRNT 363
Cdd:TIGR00606 826 QVNQEKQE----------KQHELDTVVSKIELNRKLIQDQQ--EQIQHLKSKTNELKSeklqigtnlqRRQQFEEQLVEL 893
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791158 364 KQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQE 436
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
319-436 |
6.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 319 IIAEVKAQYEDIanrsRAEAESWYQTKYEELQVTAGR---HGDDLRNTKQEI----SEMNRMIQRLRAEIDSVKKQCSSL 391
Cdd:PRK12704 58 ALLEAKEEIHKL----RNEFEKELRERRNELQKLEKRllqKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 153791158 392 QTAIADAEQRGE----LALKDARAKLvdLEEALQKAKQDMARLLREYQE 436
Cdd:PRK12704 134 EELIEEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
191-382 |
8.63e-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: 37.98 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 191 TVRQNLEPLFDsyTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDaaymnkvEL 270
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 271 EAKVKSLPEEINfihSVFDA-ELSQLQTQvgdtsvvLSMDNNRNLDLDSIIAEVKAQYEDIANRsRAEAESWYQTKYEEL 349
Cdd:COG1579 72 EARIKKYEEQLG---NVRNNkEYEALQKE-------IESLKRRISDLEDEILELMERIEELEEE-LAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|...
gi 153791158 350 QVTAGRHGDDLRNTKQEISEMNRMIQRLRAEID 382
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-448 |
8.69e-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: 38.85 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 151 EQIKTL----NNKFASFIDKVRFLEQQNKVLETKWALLQEQGSRTVRQNLEPLFDsYTSELRRQLESITTERGRLEAELR 226
Cdd:TIGR04523 253 TQLNQLkdeqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD-WNKELKSELKNQEKKLEEIQNQIS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 227 NMQDVVEDFKvryeDEINK----RTAAENEFVALKKdvdaaymnkvELEAKVKSLPEEINFIHSVFDaELSQLQTQVGDT 302
Cdd:TIGR04523 332 QNNKIISQLN----EQISQlkkeLTNSESENSEKQR----------ELEEKQNEIEKLKKENQSYKQ-EIKNLESQINDL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 303 SVVLSMDNNRNLDLDSIIAEVKAQYEDIanrsraeaeswyQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEID 382
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELL------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791158 383 SVKKQCSSLQTAIADAEQ-----RGELALKDARAKLV-----DLEEALQKAKQDMARLLREYQELMNIKLALDVEI 448
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQnleqkQKELKSKEKELKKLneekkELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-284 |
9.59e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 143 QRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKwalLQEQGSRTVR------QNLEPLFDSYT------SELRRQ 210
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEeleerlKELEPFYNEYLelkdaeKELERE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 211 LESITTERGRLEAELRNMQDV----------VEDFKVRYEDEINKRtaAENEFVALKKDVDAAYMNKVELEAKVKSLPEE 280
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETekrleelrkeLEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
....
gi 153791158 281 INFI 284
Cdd:PRK03918 696 LEKL 699
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
125-292 |
9.88e-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: 37.98 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 125 TVNQSLLTPLHLQ-IDPTIQRVRAEERE----------QIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGSR--- 190
Cdd:COG1579 1 AMPEDLRALLDLQeLDSELDRLEHRLKElpaelaeledELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791158 191 ---TVRQNLEplfdsYTSeLRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAymnK 267
Cdd:COG1579 81 qlgNVRNNKE-----YEA-LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---L 151
|
170 180
....*....|....*....|....*
gi 153791158 268 VELEAKVKSLPEEINFIHSVFDAEL 292
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPEL 176
|
|
| |
