|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
120-430 |
4.68e-132 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 385.81 E-value: 4.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 279 NSRELDVDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477127 359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
61-116 |
1.21e-11 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 62.75 E-value: 1.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477127 61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-425 |
1.13e-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: 51.60 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLK 254
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 255 S---LYEEEICLLQSQISETSVIVKmdnsrelDVDGIIAEIKAQYDDIASRSKAEAEAWYQcrYEELRVTAGNHCDNLRN 331
Cdd:TIGR02168 316 RqleELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 332 R-----------KNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQG--------EAALNDAKCKLAGLEEALQKA 392
Cdd:TIGR02168 387 KvaqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEELERLEEALEEL 466
|
250 260 270
....*....|....*....|....*....|...
gi 27477127 393 KQDMACLLKEYQEVMNSKLGLDIEIATYRRLLE 425
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
145-406 |
4.52e-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: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 145 NKLLEtkwNFMQQQRccQTNIEPIfEGYISALRRQLDcvsgdrvRLESELCSLQAALEGYKKKyeeelslrpcveNEFVA 224
Cdd:COG3206 155 NALAE---AYLEQNL--ELRREEA-RKALEFLEEQLP-------ELRKELEEAEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 225 LKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSvivkmDNSRELDVDGIIAEIKAQYddiasrsk 304
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQL-------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 305 AEAEAwyqcRYEELRVTAG-NHCD--NLRNRKNEIL-----EMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGeAALN 376
Cdd:COG3206 273 AELEA----ELAELSARYTpNHPDviALRAQIAALRaqlqqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELP 347
|
250 260 270
....*....|....*....|....*....|
gi 27477127 377 DAKCKLAGLEEALQKAKQDMACLLKEYQEV 406
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-428 |
3.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 121 KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRccqTNIEPIFEgYISALRRQLDCVSGDRVRLESELCSLQAA 200
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 201 LEGYKKKYEEelsLRPCVEnEFVALKKDVDTAFLMKADLETNAEALvQEIDFLKSLYEEEICLLQSQISETSvivkMDNS 280
Cdd:PRK03918 268 IEELKKEIEE---LEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELE----EKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 281 RELDVDGIIAEIKAQYDDIASRSKAeaeawyqcrYEELRVTAGNhCDNLRNRK--NEILEMNKLIQRLQQETENVKAQRC 358
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE-LERLKKRLtgLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 359 KLEGAIAEAEQQGE---AALND-----AKCKLAGLE-------EALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRL 423
Cdd:PRK03918 409 KITARIGELKKEIKelkKAIEElkkakGKCPVCGRElteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
....*
gi 27477127 424 LEGEE 428
Cdd:PRK03918 489 LKKES 493
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
120-430 |
4.68e-132 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 385.81 E-value: 4.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 279 NSRELDVDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477127 359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
61-116 |
1.21e-11 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 62.75 E-value: 1.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477127 61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
98-410 |
1.42e-07 |
|
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: 54.34 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 98 NESLLVPLALEIdptvQRVKRDEKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQTNiEPIFEGYISALR 177
Cdd:pfam05483 375 NEDQLKIITMEL----QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK-EQELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 178 RQLDcvsgdrvRLESELCSLQAALEGYKKKYEEelsLRPCVENEfvALKKDVDTAFLMKADLETnaEALVQEI-DFLKSL 256
Cdd:pfam05483 450 KEIH-------DLEIQLTAIKTSEEHYLKEVED---LKTELEKE--KLKNIELTAHCDKLLLEN--KELTQEAsDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 257 YEEEICLLQSQISETSVIVKMDNSRELD------VDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAG-----NH 325
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEmnlrdeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQmkileNK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 326 CDNLRNrknEILEMNKLIQRLQQETENVKAQrcklegAIAEAEQqgeaaLNDAKCKLAGLEEALQKAKQDMACLLKEYQE 405
Cdd:pfam05483 596 CNNLKK---QIENKNKNIEELHQENKALKKK------GSAENKQ-----LNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
....*
gi 27477127 406 VMNSK 410
Cdd:pfam05483 662 EIEDK 666
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-425 |
1.13e-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: 51.60 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLK 254
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 255 S---LYEEEICLLQSQISETSVIVKmdnsrelDVDGIIAEIKAQYDDIASRSKAEAEAWYQcrYEELRVTAGNHCDNLRN 331
Cdd:TIGR02168 316 RqleELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 332 R-----------KNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQG--------EAALNDAKCKLAGLEEALQKA 392
Cdd:TIGR02168 387 KvaqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEELERLEEALEEL 466
|
250 260 270
....*....|....*....|....*....|...
gi 27477127 393 KQDMACLLKEYQEVMNSKLGLDIEIATYRRLLE 425
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-357 |
2.52e-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: 50.45 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 112 TVQRVKRDEKEQIKCLNNRFASfinKVRFLEQKNKLLETKWNfmQQQRCCQTNIEPI------FEGYISALRRQLDCVSG 185
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGE--EEQLRVKEKIGELeaeiasLERSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 186 DRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEidfLKSlYEEEICLLQ 265
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE---LKD-YREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 266 SQISE--TSVIVKMDNSRELDVDGI-----IAEIKAQYDDIASRSKAEAEAWYQCRY--EELRVTAGNHCDNLRNRKNEI 336
Cdd:TIGR02169 399 REINElkRELDRLQEELQRLSEELAdlnaaIAGIEAKINELEEEKEDKALEIKKQEWklEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|.
gi 27477127 337 LEMNKLIQRLQQETENVKAQR 357
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQA 499
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
145-406 |
4.52e-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: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 145 NKLLEtkwNFMQQQRccQTNIEPIfEGYISALRRQLDcvsgdrvRLESELCSLQAALEGYKKKyeeelslrpcveNEFVA 224
Cdd:COG3206 155 NALAE---AYLEQNL--ELRREEA-RKALEFLEEQLP-------ELRKELEEAEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 225 LKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSvivkmDNSRELDVDGIIAEIKAQYddiasrsk 304
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQL-------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 305 AEAEAwyqcRYEELRVTAG-NHCD--NLRNRKNEIL-----EMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGeAALN 376
Cdd:COG3206 273 AELEA----ELAELSARYTpNHPDviALRAQIAALRaqlqqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELP 347
|
250 260 270
....*....|....*....|....*....|
gi 27477127 377 DAKCKLAGLEEALQKAKQDMACLLKEYQEV 406
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
175-430 |
2.25e-05 |
|
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: 47.48 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAflmKADLETNAEAlVQEIDFLK 254
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEKAAA-YDKLEKTK 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 255 SLYEEEIcllqsqiseTSVIVKMDNSREL---------DVDGIIAE---IKAQYDDiaSRSKAEAEAwyqcRYEELRVTA 322
Cdd:pfam01576 576 NRLQQEL---------DDLLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA----REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 323 GNH-CDNLRNRKNEILEMNKLiqrlqqetenvkaQRCKLEGAIAEAEQQGEAALNDAKCKLAgLEEALQKAKQDMACLLK 401
Cdd:pfam01576 641 LARaLEEALEAKEELERTNKQ-------------LRAEMEDLVSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELED 706
|
250 260 270
....*....|....*....|....*....|....*...
gi 27477127 402 EYQEVMNSKLGLDIEI----ATYRRLLE-----GEEHR 430
Cdd:pfam01576 707 ELQATEDAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-428 |
3.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 121 KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRccqTNIEPIFEgYISALRRQLDCVSGDRVRLESELCSLQAA 200
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 201 LEGYKKKYEEelsLRPCVEnEFVALKKDVDTAFLMKADLETNAEALvQEIDFLKSLYEEEICLLQSQISETSvivkMDNS 280
Cdd:PRK03918 268 IEELKKEIEE---LEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELE----EKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 281 RELDVDGIIAEIKAQYDDIASRSKAeaeawyqcrYEELRVTAGNhCDNLRNRK--NEILEMNKLIQRLQQETENVKAQRC 358
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE-LERLKKRLtgLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 359 KLEGAIAEAEQQGE---AALND-----AKCKLAGLE-------EALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRL 423
Cdd:PRK03918 409 KITARIGELKKEIKelkKAIEElkkakGKCPVCGRElteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
....*
gi 27477127 424 LEGEE 428
Cdd:PRK03918 489 LKKES 493
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-428 |
3.52e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 108 EIDPTVQRVKRDE-KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCC--------QTNIEPIFEGY---ISA 175
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 176 LRRQLDCVSGDRVRLESE---LCSLQAALEGYK-KKYEEELSLRPCVENEFVALKKDVDTAflmkADLETNAEALVQE-- 249
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINEL----KDKHDKYEEIKNRyk 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 250 ---IDFLKSLYEEEICLLqSQISetsvIVKMDNSRELDvdgiiAEIKAQYDDIASRSK------AEAEAWYQCRYEELRv 320
Cdd:PRK01156 557 slkLEDLDSKRTSWLNAL-AVIS----LIDIETNRSRS-----NEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE- 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 321 tagNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRCKLEGaIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMAcLL 400
Cdd:PRK01156 626 ---NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRA-RL 700
|
330 340
....*....|....*....|....*....
gi 27477127 401 KEYQEVMNSKLG-LDIEIATYRRLLEGEE 428
Cdd:PRK01156 701 ESTIEILRTRINeLSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-416 |
9.51e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 222 FVALK--KDVDTAF----LMKADLETNAEALVQEIDFLKSLYEEeicllqsqisetsvIVKMDNSRELdvdgiIAEIKAQ 295
Cdd:COG4913 200 TQSFKpiGDLDDFVreymLEEPDTFEAADALVEHFDDLERAHEA--------------LEDAREQIEL-----LEPIREL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 296 YDDIAsRSKAEAEAWYQCRyEELRVTAGNHCDNLRnrKNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQ----G 371
Cdd:COG4913 261 AERYA-AARERLAELEYLR-AALRLWFAQRRLELL--EAELEELRAELARLEAELERLEARLDALREELDELEAQirgnG 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27477127 372 EAALNDAKCKLAGLEEALQKAKQDmaclLKEYQEVMNSkLGLDIE 416
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERR----RARLEALLAA-LGLPLP 376
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
327-396 |
2.55e-04 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 40.65 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 327 DNLRNRKNEILEMNKLIQ------RLQQETENVKAQRCKLEGAIAEAEQQGE------AALNDAKCKLAGLEEALQKAKQ 394
Cdd:pfam02403 16 ESLKKRGVDVLDVDELLEldekrrELQVELEELQAERNELSKEIGQAKKKKEdadaliAEVKELKDELKALEAELKELEA 95
|
..
gi 27477127 395 DM 396
Cdd:pfam02403 96 EL 97
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
173-511 |
3.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 173 ISALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEelslrpcVENEFVALKKDVDTAflmKADLETNAEALV--QEI 250
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKL---QAEIAEAEAEIEerREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 251 --DFLKSLYEE-------EIcLLQSQ-----ISETSVIVK-MDNSREldvdgIIAEIKAQYDDIASRsKAEAEAwyqcRY 315
Cdd:COG3883 88 lgERARALYRSggsvsylDV-LLGSEsfsdfLDRLSALSKiADADAD-----LLEELKADKAELEAK-KAELEA----KL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 316 EELRVTAgnhcDNLRNRKNEIL----EMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGEAALNDAKCKLAGLEEALQK 391
Cdd:COG3883 157 AELEALK----AELEAAKAELEaqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 392 AKQDMAcllKEYQEVMNSKLGLDIEIATYRRLLEGEEHRLCEGIGPVniSVSSSKGAFLYEPCGVSTPVLSTGVLRSNGG 471
Cdd:COG3883 233 AAAAAA---AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA--AAASAAGGGAGGAGGGGGGGGAASGGSGGGS 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 27477127 472 CSIVGTGELYVPCEPQGLLSCGSGRKSSMTLGAGGSSPSH 511
Cdd:COG3883 308 GGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGG 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
196-422 |
3.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 196 SLQAALEGYKKKYEEelslrpcVENEFVALKKDVDTAFLMKADLETNAEALVQEIDflksLYEEEICLLQSQISETsviv 275
Cdd:COG4942 24 EAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAELAEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 276 kmdnsrELDVDGIIAEIKAQYDDIASRSKAeAEAWYQCRYEELRVTAGNHCDNLRN----------RKNEILEMNKLIQR 345
Cdd:COG4942 89 ------EKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEDFLDAVRRlqylkylapaRREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 346 LQQETENVKAQRCKLEGAIAEAEQQG---EAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRR 422
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
252-408 |
7.08e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.54 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 252 FLKSLYEEEICLLQSQISETSVIVKMDNSREldVDGIIAEIKAQYDDIASRSKAEAEAwyqcryEELRVTAgnhcdnlrn 331
Cdd:PRK06669 26 RFKVLSIKEKERLREEEEEQVEQLREEANDE--AKEIIEEAEEDAFEIVEAAEEEAKE------ELLKKTD--------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477127 332 rkneilEMNKLIQRLQQETENvkaqrcklegAIAEAEQQGEAALNDAKCKlaGLEEALQKAKQDMaclLKEYQEVMN 408
Cdd:PRK06669 89 ------EASSIIEKLQMQIER----------EQEEWEEELERLIEEAKAE--GYEEGYEKGREEG---LEEVRELIE 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
331-430 |
1.85e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 331 NRKNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGEAA----------LNDAKCKLAGLEEALQKAKQDMACLL 400
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleelsrqISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110
....*....|....*....|....*....|.
gi 27477127 401 KEYQEVMNSKLGLDIEIATYR-RLLEGEEHR 430
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEeELAEAEAEI 784
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
219-508 |
5.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 219 ENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSVivKMDNSRElDVDGIIAEIKAQYDD 298
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQA--EIDKLQA-EIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 299 IASRSKAEAEAWYQCRYEELRVTAGNHCDNLRN---------RKNEILEmnkLIQRLQQETENVKAQrckLEGAIAEAEQ 369
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRlsalskiadADADLLE---ELKADKAELEAKKAE---LEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 370 QgeaaLNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEI-ATYRRLLEGEEHRLCEGIGPVNISVSSSKGA 448
Cdd:COG3883 162 L----KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELaAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 449 FLYEPCGVSTPVLSTGVLRSNGGCSIVGTGELYVPCEPQGLLSCGSGRKSSMTLGAGGSS 508
Cdd:COG3883 238 AAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGG 297
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-405 |
7.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 117 KRDEKEQIKCLNNRFASFINKVRFLEQKNKLL-ETKW---------NFMQQQRCCQTNIEPIFEGY---ISALRRQLDCV 183
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELkELKEkaeeyiklsEFYEEYLDELREIEKRLSRLeeeINGIEERIKEL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 184 SGDRVRLE------SELCSLQAALEGYKKKYEEELSLrpcvENEFVALKKDvdtaflmKADLET-NAEALVQEIDFLKSL 256
Cdd:PRK03918 334 EEKEERLEelkkklKELEKRLEELEERHELYEEAKAK----KEELERLKKR-------LTGLTPeKLEKELEELEKAKEE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 257 YEEEICLLQSQISETSVIVKMDNS----------------RELDVD---GIIAEIKAQYDDIASRSKAEAEAWYQCRYEE 317
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgRELTEEhrkELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 318 LRVtagnhcDNLRNRKNEILEMNKLIQRLQ------------------QETENVKAQRCKLEGAIAEAEQQGEAaLNDAK 379
Cdd:PRK03918 483 REL------EKVLKKESELIKLKELAEQLKeleeklkkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEK-LEELK 555
|
330 340
....*....|....*....|....*.
gi 27477127 380 CKLAGLEEALQKAKQDMACLLKEYQE 405
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEE 581
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
302-427 |
8.40e-03 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 38.16 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 302 RSKAEAEAWyqcryEELRVTAGNHCDNLRN---------RKNEILemNKLIQRLQQETE-----NVKAQRCKLEGAIAEA 367
Cdd:pfam14992 44 RSLAEDEER-----EELNFTIMEKEDALQEleletakleKKNEIL--VKSVMELQRKLSrksdkNTGLEQETLKQMLEEL 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477127 368 E---QQGEAALNDAKCKLAGLEEALQKAKQ---DMACLLKEYQEVMNSklgldIEIATYRRLLEGE 427
Cdd:pfam14992 117 KvklQQSEESCADQEKELAKVESDYQSVHQlceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
331-405 |
8.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 331 NRKNEILE-----MNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGE--AALN--DAKCKLagLEEALQKAKQDMACLLK 401
Cdd:PRK12704 99 DRKLELLEkreeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIK 176
|
....
gi 27477127 402 EYQE 405
Cdd:PRK12704 177 EIEE 180
|
|
| |
