|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
24-611 |
0e+00 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 942.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 24 AFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPF 103
Cdd:pfam09726 74 AFSVFFVCIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 104 AAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILiHHN 183
Cdd:pfam09726 154 AAHCIGYPVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQERETSETAKGLSEVDPLAL-NQN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 184 GGIPANKKLSTALPEIEYREKGKEKDKDAKKH-NLGINNNNILQPVDSKIQEIEYMENHINSKRLNND-LVGSTENLLKE 261
Cdd:pfam09726 233 GHSLNKKDSTLQLPELEYREKKNSGTSSGSDSkKSHNHNIHNLNHVDSKLQEKEYMENHSNSKRLNIStSPGSEEDLLVR 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 262 DSC--------TASSKNYKNAS----GVVNSSPRSHSATNGSIPSSSS-KNEKKQRC-TSKGPSAHKDLMENCIPNNQLS 327
Cdd:pfam09726 313 ESVssksssssSSSNKNYKNASggsaNSSNSSPRSHSHNSGSVTSSSSsKNSKKQKGpGGKSGARHKDPAENCIPNNQLS 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 328 KPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEK 407
Cdd:pfam09726 393 KPDALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEK 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 408 RLKAEQEARGFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKV 487
Cdd:pfam09726 473 RLKAEQEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKV 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 488 QELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVM 567
Cdd:pfam09726 553 QELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVM 632
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1958776666 568 AVMPSitysaaTSPLSPVSPHYSSKFVETSPSGLDPNASVYQPL 611
Cdd:pfam09726 633 AVMPS------TSRITPVTPHYSSKFMDTSPSMRDPNASVYPPL 670
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-565 |
4.21e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 323 NNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNI 402
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 403 SQLEKRLKAEQEARGFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECtETLRSRIRELEAEGKKLTMDLKVKEEQI-- 480
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLes 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 481 --RELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFS----ALGDAKRQLEIAQGQILQKDQ 554
Cdd:TIGR02168 829 leRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEELSEELRELES 908
|
250
....*....|.
gi 1958776666 555 EIKDLKQKIAE 565
Cdd:TIGR02168 909 KRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
332-573 |
2.28e-09 |
|
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: 60.46 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 332 LVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKRLKA 411
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 412 EQEARGFVEKQLmEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELR 491
Cdd:TIGR02168 307 LRERLANLERQL-EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 492 -KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAkrQLEIAQGQILQKDQEIKDLKQKIAEVMAVM 570
Cdd:TIGR02168 386 sKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEAL 463
|
...
gi 1958776666 571 PSI 573
Cdd:TIGR02168 464 EEL 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-565 |
5.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 330 DALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRL 409
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 410 KAEQEARGFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTmdlKVKEEQIRELELKVQE 489
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776666 490 ---LRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:COG1196 410 ealLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-565 |
1.42e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 334 RLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKRLKAEQ 413
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-------LAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 414 EARGFVEKQLmeekkrkkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELR-K 492
Cdd:COG1196 309 ERRRELEERL-----------------------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEaE 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776666 493 YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-600 |
1.38e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 326 LSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQL 405
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 406 EKRLKAEQEArgfVEKQLmeekkrkKLEEATAARAVAFAAASRGECTETLRSRIREleaegKKLTMDLKVKEEQIRELEL 485
Cdd:COG4942 96 RAELEAQKEE---LAELL-------RALYRLGRQPPLALLLSPEDFLDAVRRLQYL-----KYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 486 KVQELRKYKENEKDTevLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:COG4942 161 ELAALRAELEAERAE--LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958776666 566 VMAVMPSITYSAATSPLS-PVSPHYSSKFVETSPSG 600
Cdd:COG4942 239 AAERTPAAGFAALKGKLPwPVSGRVVRRFGERDGGG 274
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-565 |
1.88e-07 |
|
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: 54.29 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 330 DALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRL 409
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 410 KAEQEARGFVEKQLmEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQE 489
Cdd:TIGR02168 799 KALREALDELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 490 LRK-YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQK---------------- 552
Cdd:TIGR02168 878 LLNeRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysltleeae 957
|
250 260
....*....|....*....|....*.
gi 1958776666 553 -------------DQEIKDLKQKIAE 565
Cdd:TIGR02168 958 alenkieddeeeaRRRLKRLENKIKE 983
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-587 |
2.00e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 352 VEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKL------HNAVQMKQKDK---QNISQLEKRLKAEQEARGFVEKQ 422
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALeefrqkNGLVDLSEEAKlllQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 423 LmeekkrKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELRKYKENEKDTEV 502
Cdd:COG3206 242 L------AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 503 --LMSALSAMQDKTQHLENSLsAETRIKLDLFSA----LGDAKRQLEIAQG---QILQKDQEIkdlkqKIAEVMAVMPSI 573
Cdd:COG3206 316 asLEAELEALQAREASLQAQL-AQLEARLAELPEleaeLRRLEREVEVARElyeSLLQRLEEA-----RLAEALTVGNVR 389
|
250
....*....|....
gi 1958776666 574 TYSAATSPLSPVSP 587
Cdd:COG3206 390 VIDPAVVPLKPVSP 403
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
332-567 |
2.85e-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: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 332 LVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNaVQMKQKD------KQNISQL 405
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK-LEEALNDlearlsHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 406 EKRLKAEQEARGFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTEtLRSRIRELEAEGKKLTMDLKVKEEQIRELEL 485
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 486 KVQELRK-YKENEKDTEVLMSALSAMQDKTQHLENSLSaetriklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIA 564
Cdd:TIGR02169 876 ALRDLESrLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
...
gi 1958776666 565 EVM 567
Cdd:TIGR02169 949 EEL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-565 |
3.85e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 334 RLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRLKAEQ 413
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 414 EARGFVEKQLMEEKKRKkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELRKY 493
Cdd:COG1196 379 EELEELAEELLEALRAA----------------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776666 494 KENEKDTEvlmsaLSAMQDKTQHLENSLSAETRIKLDLFSALGdAKRQLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:COG1196 437 EEEEEEAL-----EEAAEEEAELEEEEEALLELLAELLEEAAL-LEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-562 |
7.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 330 DALVRLEQDIKKLkADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQEneLLQNKLHNAVQMKQKDKQNISQLEKRL 409
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 410 KAEQEARGFVEKQLMEekkrkkleeataaravafaaaSRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQE 489
Cdd:COG4913 319 DALREELDELEAQIRG---------------------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776666 490 LRKykenekdtevlmsALSAMQDKTQHLENSLSAETRiklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQK 562
Cdd:COG4913 378 SAE-------------EFAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
335-565 |
1.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 335 LEQDIKKLKADLQASRQVEQELRSQ----------ISSLSSTERGIRSEMGQLR---QENELLQNKLHNAVQMKQKDKQN 401
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 402 ISQLEKRLKAEQEARGFVEKQLMEEKKRKKLEEATAARAVAFAAASrgECTETLRSRIRELEAEGKKLTMDLKVKEEQIR 481
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 482 ELELKVQELR----KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDlfsALGDAKRQLEIAQGQILQKDQEIK 557
Cdd:PRK03918 332 ELEEKEERLEelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEIS 408
|
....*...
gi 1958776666 558 DLKQKIAE 565
Cdd:PRK03918 409 KITARIGE 416
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
316-564 |
5.22e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 316 LMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERgIRSEMGQLRQENELLQNKLhnAVQMK 395
Cdd:TIGR00618 205 LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQE--AVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 396 QKDKQNISQLEKRLKAEQEARGFVEKQlmeekkrkkleeataaravafaaasRGECTETLRSRIRELEAEGKKLTMDLKV 475
Cdd:TIGR00618 282 TQERINRARKAAPLAAHIKAVTQIEQQ-------------------------AQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 476 KEEQIRELELKVQELRKYKENEKDTEVLMSALsAMQDKTQHLENSLSAETRIK---LDLFSALGDAKRQLEIAQGQILQK 552
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-EISCQQHTLTQHIHTLQQQKttlTQKLQSLCKELDILQREQATIDTR 415
|
250
....*....|..
gi 1958776666 553 DQEIKDLKQKIA 564
Cdd:TIGR00618 416 TSAFRDLQGQLA 427
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
342-566 |
3.99e-04 |
|
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: 43.67 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 342 LKADLQA-----SRQVEQELRSQISSLSST-------ERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRL 409
Cdd:pfam12128 583 VKLDLKRidvpeWAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 410 KAEQEArgfVEKQLMEEKKRKKLeeataaravafaaasrgectetlrsRIRELEAEGKKLTMDLKVKEEQIRE--LELKV 487
Cdd:pfam12128 663 QSEKDK---KNKALAERKDSANE-------------------------RLNSLEAQLKQLDKKHQAWLEEQKEqkREART 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 488 QELRKYKENEKDTEVLMSALSAMQDK--TQHLENSLSAETRIKLDLFSalgdakrqLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:pfam12128 715 EKQAYWQVVEGALDAQLALLKAAIAArrSGAKAELKALETWYKRDLAS--------LGVDPDVIAKLKREIRTLERKIER 786
|
.
gi 1958776666 566 V 566
Cdd:pfam12128 787 I 787
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
455-524 |
6.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 6.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776666 455 LRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELRK--YKENEKDTEVlmsalSAMQDKTQHLENSLSAE 524
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREI-----SRLDREIERLERELEEE 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
327-506 |
8.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 327 SKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTER--GIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQ 404
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 405 LEKRLKAEQEARGFVEKQLMEEKKRKKLEEATAARAVafaaasrgectETLRSRIRELEAEGKKLTMDLKVKEEQIRELE 484
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-----------EELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180
....*....|....*....|..
gi 1958776666 485 LKVQELRKYKENEKDTEVLMSA 506
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
456-569 |
1.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 456 RSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELRK----------YKENEKDTEVLMSALSAMQDKTQHLENSLS--- 522
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeYSWDEIDVASAEREIAELEAELERLDASSDdla 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958776666 523 -AETRIKlDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAV 569
Cdd:COG4913 689 aLEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
332-566 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 332 LVRLEQDIKKLKADLQASRQVEQ-ELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRLK 410
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 411 AEQEARgfveKQLMEEkkrkkleeataaravafaAASRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQEL 490
Cdd:TIGR02169 347 EERKRR----DKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776666 491 RKYKENEKDTEV-LMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEV 566
Cdd:TIGR02169 405 KRELDRLQEELQrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-568 |
1.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 330 DALVRLEQDIKKLKADLQASRQVEQELRSQISSLSstergirsemgQLRQENELLQNKLHNAVQMKQKDKQnISQLEKRL 409
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQ-----------ERREALQRLAEYSWDEIDVASAERE-IAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 410 KAEQEARGFVekqlmeekkrkkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQE 489
Cdd:COG4913 678 ERLDASSDDL---------------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 490 LRkykenekdtevlmSALSAMQDKTQHLENSLSAETRIKLD-LFSALGDAKRQLEIA---QGQILQKDQEIKDLKQKIAE 565
Cdd:COG4913 725 AE-------------EELDELQDRLEAAEDLARLELRALLEeRFAAALGDAVERELRenlEERIDALRARLNRAEEELER 791
|
...
gi 1958776666 566 VMA 568
Cdd:COG4913 792 AMR 794
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
335-566 |
2.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 335 LEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRLKAEQE 414
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 415 ARGFVEKQLMEEKKRKKLEEATAARAVAFAAASRGEcTETLRSRIRE---LEAEGK------------------------ 467
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEAT-LRTARERVEEaeaLLEAGKcpecgqpvegsphvetieedrerv 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 468 -KLTMDLKVKEEQIRELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLS------AETRIKLDLFSALGDAKR 540
Cdd:PRK02224 478 eELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEekreraEELRERAAELEAEAEEKR 557
|
250 260
....*....|....*....|....*....
gi 1958776666 541 qlEIAQGQILQKD---QEIKDLKQKIAEV 566
Cdd:PRK02224 558 --EAAAEAEEEAEearEEVAELNSKLAEL 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-565 |
2.96e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 335 LEQDIKKLKadlqasRQVEQ-----ELRSQISSLSSTERGIRSEmgQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRl 409
Cdd:COG1196 198 LERQLEPLE------RQAEKaeryrELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAE- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 410 kaEQEARgfvEKQLMEEKKRKKLEEATAARAVAFAAASRGEctETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQE 489
Cdd:COG1196 269 --LEELR---LELEELELELEEAQAEEYELLAELARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776666 490 LR-KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:COG1196 342 LEeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
339-599 |
9.50e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.29 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 339 IKKLKADLQASRQVEQELRSQI-----SSLSSTERgiRSEMGQLRQENELLQNKLHNAVQMKQKDKQ--------NISQL 405
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRLfiklqPLLSLLGS--RKEYRSYLACIIKLQKTIKREKKLRETEEVefslkaevLIQKF 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 406 EKRLKAEQEARGFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLrsriRELEAEGKKLTMDLkvKEEQIRELEL 485
Cdd:COG5022 852 GRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN----LELESEIIELKKSL--SSDLIENLEF 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776666 486 KVQELRKYKENeKDTEVLMSALSAMQDKTQHLENSLSAETRIKlDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 565
Cdd:COG5022 926 KTELIARLKKL-LNNIDLEEGPSIEYVKLPELNKLHEVESKLK-ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAE 1003
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958776666 566 VMAVMPSITYSAATSPLSPVSP---HYSSKFVETSPS 599
Cdd:COG5022 1004 LSKQYGALQESTKQLKELPVEVaelQSASKIISSEST 1040
|
|
| |
