|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
307-478 |
1.16e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 307 QSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQI-RLLEDKGTSTQLVRENQVL 385
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 386 KRYLEVEKQKTNSFLNERVTLLEEARVLKRDLERERLTAMALRAELEQLAPRQAQGHAdspsvQRGEKEIVLLQQRLAEL 465
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----EAEEELEELAEELLEAL 392
|
170
....*....|...
gi 672062171 466 EQKLSFEQQRSDL 478
Cdd:COG1196 393 RAAAELAAQLEEL 405
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
329-481 |
4.15e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 329 TQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDKGTSTQLVRENQVLK------RYLEVEKQktnsflne 402
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAElaeltrRLAELETQ-------- 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062171 403 rvtlLEEARVLKRDLERERLTAMALRAELEQLAPRQAQGHADSPSVQRGEKEIvlLQQRLAELEQKLSfeQQRSDLWER 481
Cdd:pfam19220 204 ----LDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEA--LTARAAATEQLLA--EARNQLRDR 274
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-565 |
6.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 277 RKVHEDELNSVKDYLFQCQQEQEcaldfKTQSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEEKTLSSLQ 356
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIE-----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 357 EELRQLKEQIRLLEDKGTSTQLVRENQVLKryLEVEKQKTNSFLNERVTLLEEARVLKRDLERERLT-------AMALRA 429
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEEL--IEELESELEALLNERASLEEALALLRSELEELSEElreleskRSELRR 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 430 ELEQLAPRQAQghadspsvqrgekeivlLQQRLAELEQKLsfEQQRSDLWERLYVEAkDQHGKQEADGRKRGSKGSHRVK 509
Cdd:TIGR02168 916 ELEELREKLAQ-----------------LELRLEGLEVRI--DNLQERLSEEYSLTL-EEAEALENKIEDDEEEARRRLK 975
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672062171 510 S-KSKETFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 565
Cdd:TIGR02168 976 RlENKIKELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-603 |
5.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 270 QKRQQLGRKVHEDELNSVKDYLFQCQQEQECALDFKTQSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEE 349
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 350 KTLSSLQEELRQLKEQIRLLEDKGT-STQLVRENQVLKRYLEVEKQKTNSFLNERVTLLEEARVLKRDLERERLTAMALR 428
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 429 AELEQLAPRQaqghadspsvQRGEKEIVLLQQRLAELEQKLSFEQQRSDLWERLYVEAKDQHGKQEADGRKRGSKGSHRV 508
Cdd:PTZ00121 1751 KDEEEKKKIA----------HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV 1820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 509 KSKSKETFLGTVKETFDA---MKNSTKEFVRHHKEKIKQAKEAVKENlkkfSDSVKSTFrHFKDTTKNIFDEKGSKRFRA 585
Cdd:PTZ00121 1821 INDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKNNENGEDGNKE----ADFNKEKD-LKEDDEEEIEEADEIEKIDK 1895
|
330
....*....|....*...
gi 672062171 586 SKEEaTEKPRTAYSYSSY 603
Cdd:PTZ00121 1896 DDIE-REIPNNNMAGKNN 1912
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
110-260 |
9.01e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 43.06 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 110 TLEPPKLEEMG---IQEVAIIKDDLNLGSSSSSQYTFCQPEPEkwweklwkiPECIRGWDDQLRLRVPSQLALQVFSSQH 186
Cdd:PLN02328 5 TKEPEDPADNVndvVSEASSPETDLSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVSDS 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062171 187 SDEESSSDD-----TSHEPSPAPRRRRNRKKtvsiseseepLLPEPEDEPSkeTSKRHFSGGLNKCIILALVIAISMGF 260
Cdd:PLN02328 76 QGDESSSEQqpqnpNSTEPAPPPKKRRRRKR----------FFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
520-577 |
1.67e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 672062171 520 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 577
Cdd:COG4980 36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
307-478 |
1.16e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 307 QSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQI-RLLEDKGTSTQLVRENQVL 385
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 386 KRYLEVEKQKTNSFLNERVTLLEEARVLKRDLERERLTAMALRAELEQLAPRQAQGHAdspsvQRGEKEIVLLQQRLAEL 465
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----EAEEELEELAEELLEAL 392
|
170
....*....|...
gi 672062171 466 EQKLSFEQQRSDL 478
Cdd:COG1196 393 RAAAELAAQLEEL 405
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
324-496 |
4.43e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 324 KVTFETQNNNLAAE------NKYLRLSLEKE----EKTLSSLQEELRQLKEQIRLLEDKgtstqlvrenqvLKRYleveK 393
Cdd:COG3206 139 EISYTSPDPELAAAvanalaEAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEAA------------LEEF----R 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 394 QKTNSF-LNERVTLLEEARV-LKRDLERERLTAMALRAELEQLAPRQAQGH------ADSPSVQRGEKEIVLLQQRLAEL 465
Cdd:COG3206 203 QKNGLVdLSEEAKLLLQQLSeLESQLAEARAELAEAEARLAALRAQLGSGPdalpelLQSPVIQQLRAQLAELEAELAEL 282
|
170 180 190
....*....|....*....|....*....|....*....
gi 672062171 466 EQKL--------SFEQQRSDLWERLYVEAKDQHGKQEAD 496
Cdd:COG3206 283 SARYtpnhpdviALRAQIAALRAQLQQEAQRILASLEAE 321
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
329-481 |
4.15e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 329 TQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDKGTSTQLVRENQVLK------RYLEVEKQktnsflne 402
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAElaeltrRLAELETQ-------- 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062171 403 rvtlLEEARVLKRDLERERLTAMALRAELEQLAPRQAQGHADSPSVQRGEKEIvlLQQRLAELEQKLSfeQQRSDLWER 481
Cdd:pfam19220 204 ----LDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEA--LTARAAATEQLLA--EARNQLRDR 274
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-565 |
6.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 277 RKVHEDELNSVKDYLFQCQQEQEcaldfKTQSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEEKTLSSLQ 356
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIE-----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 357 EELRQLKEQIRLLEDKGTSTQLVRENQVLKryLEVEKQKTNSFLNERVTLLEEARVLKRDLERERLT-------AMALRA 429
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEEL--IEELESELEALLNERASLEEALALLRSELEELSEElreleskRSELRR 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 430 ELEQLAPRQAQghadspsvqrgekeivlLQQRLAELEQKLsfEQQRSDLWERLYVEAkDQHGKQEADGRKRGSKGSHRVK 509
Cdd:TIGR02168 916 ELEELREKLAQ-----------------LELRLEGLEVRI--DNLQERLSEEYSLTL-EEAEALENKIEDDEEEARRRLK 975
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672062171 510 S-KSKETFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 565
Cdd:TIGR02168 976 RlENKIKELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
336-495 |
2.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 336 AENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDKGTSTQLVRENQVLKRYLEVEKQKTNSFLN---ERVTLLEEARV 412
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 413 LKRDLERERLTAMALRAELEQLAPRQAQGHADspSVQRGEKEIVLLQQRLAELEQKLSFEQQRSDLWERLYVEAKDQHGK 492
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEELQDLAE--ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
...
gi 672062171 493 QEA 495
Cdd:COG4717 246 KEA 248
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-475 |
3.16e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 334 LAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEdkgtstqlvRENQVLKRYLEVEKQKTNSFLNERVTLLEEARVL 413
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELE---------AELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672062171 414 KRDLERERLTAMALRAELEQLAPR----QAQGHADSPSVQRGEKEIVLLQQRLAELEQKLSFEQQR 475
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEElaelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-489 |
3.94e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 344 SLEKE-EKTLS--SLQEELRQLKEQIRLLEDKGTSTQLVRENQVLKRyLEVEKQKtnsflnervtLLEEARVLKRDLERE 420
Cdd:COG1196 204 PLERQaEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEE-LEAELEE----------LEAELAELEAELEEL 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062171 421 RLTAMALRAELEQLapRQAQGHADSpSVQRGEKEIVLLQQRLAELEQKLSFEQQRSDLWERLYVEAKDQ 489
Cdd:COG1196 273 RLELEELELELEEA--QAEEYELLA-ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-603 |
5.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 270 QKRQQLGRKVHEDELNSVKDYLFQCQQEQECALDFKTQSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEE 349
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 350 KTLSSLQEELRQLKEQIRLLEDKGT-STQLVRENQVLKRYLEVEKQKTNSFLNERVTLLEEARVLKRDLERERLTAMALR 428
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 429 AELEQLAPRQaqghadspsvQRGEKEIVLLQQRLAELEQKLSFEQQRSDLWERLYVEAKDQHGKQEADGRKRGSKGSHRV 508
Cdd:PTZ00121 1751 KDEEEKKKIA----------HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV 1820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 509 KSKSKETFLGTVKETFDA---MKNSTKEFVRHHKEKIKQAKEAVKENlkkfSDSVKSTFrHFKDTTKNIFDEKGSKRFRA 585
Cdd:PTZ00121 1821 INDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKNNENGEDGNKE----ADFNKEKD-LKEDDEEEIEEADEIEKIDK 1895
|
330
....*....|....*...
gi 672062171 586 SKEEaTEKPRTAYSYSSY 603
Cdd:PTZ00121 1896 DDIE-REIPNNNMAGKNN 1912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-582 |
5.33e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 328 ETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDKGTSTQLVREN-----QVLKRYLEVEKQKTNSFLNE 402
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeiEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 403 RVTLLEEARVLKRDLERERLTAMALRAELEQLAPRQAQGHADSPSVQRG----EKEIVLLQQRLAELEQKLSF-EQQRSD 477
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaatERRLEDLEEQIEELSEDIESlAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 478 LWERL---------YVEAKDQHGKQEADGRKRGSKGSHRVKSKSKEtflgtVKETFDAMKNSTKEFVrHHKEKIKQAKEA 548
Cdd:TIGR02168 864 LEELIeeleseleaLLNERASLEEALALLRSELEELSEELRELESK-----RSELRRELEELREKLA-QLELRLEGLEVR 937
|
250 260 270
....*....|....*....|....*....|....*
gi 672062171 549 VKENLKKFSDSVKSTFRHFKDTTKNI-FDEKGSKR 582
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEAEALENKIeDDEEEARR 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-500 |
1.74e-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: 44.75 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 328 ETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDK--GTSTQLVRENQVLKRyLEVEKQKTNSFLNERVT 405
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAE-LEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 406 LLEE-ARVLKRDLERERLTAMALRAELEQLAPRQAQGHADSPSVQRGEKEIVLLQQRLAELEQKLsfEQQRSDLwERLYV 484
Cdd:COG4942 105 ELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL--EAERAEL-EALLA 181
|
170
....*....|....*.
gi 672062171 485 EAKDQHGKQEADGRKR 500
Cdd:COG4942 182 ELEEERAALEALKAER 197
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
341-485 |
3.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 341 LRLSLEKEEKTLSSLQ--------EELRQLKEQIRLLEDK-GTSTQLVRENQVLKRYLEvEKQKTNSFLNERVTLLEEAR 411
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKeEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672062171 412 VLKRDLERERltamALRAELEQLAPRQAQGHADSPSVQRGEKEIVLLQQRLAELEQKLSFEQQRSDLWERLYVE 485
Cdd:COG4717 126 QLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
350-488 |
4.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 350 KTLSSLQEELRQLKEQIRLLE---DKGTSTQLVRENQVLKRYL------EVEKQKTNSFLNERVTLLEEARVLKRDLERE 420
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirELAERYAAARERLAELEYLraalrlWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 421 RLTAMALRAELEQL-APRQAQGHADspsVQRGEKEIVLLQQRLAELEQKLS-FEQQRSDLWERLYVEAKD 488
Cdd:COG4913 315 EARLDALREELDELeAQIRGNGGDR---LEQLEREIERLERELEERERRRArLEALLAALGLPLPASAEE 381
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
295-547 |
4.62e-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: 43.96 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 295 QQEQECALDFKTQSSKEnLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLlEDKGT 374
Cdd:pfam17380 295 KMEQERLRQEKEEKARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ-EEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 375 STQLVREnqvLKRyLEVEKQKTNsflnERVTL-LEEARVLK-RDLERERLTAMALRaELEQLapRQAQGHADSPSVQRGE 452
Cdd:pfam17380 373 EISRMRE---LER-LQMERQQKN----ERVRQeLEAARKVKiLEEERQRKIQQQKV-EMEQI--RAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 453 KEivllqqRLAELEQKLSFEQQRSDLWERLYVEAKDQHGKQ-EADGRKRGSKGSHRVKSKSKETFLGTVKETFDAMKNST 531
Cdd:pfam17380 442 EE------RAREMERVRLEEQERQQQVERLRQQEEERKRKKlELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR 515
|
250
....*....|....*.
gi 672062171 532 KEFVRHHKEKIKQAKE 547
Cdd:pfam17380 516 KLLEKEMEERQKAIYE 531
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-497 |
5.50e-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: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 305 KTQSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDK------------ 372
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkeelaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 373 ------------------GTSTQLVRENQVLKRYLEVEKQKTNSFLNErvtlLEEARVLKRDLERERLTAMALRAELEQL 434
Cdd:COG4942 111 ralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672062171 435 APRQAQGHADSPS-VQRGEKEIVLLQQRLAELEQKlsfEQQRSDLWERLYVEAKDQHGKQEADG 497
Cdd:COG4942 187 RAALEALKAERQKlLARLEKELAELAAELAELQQE---AEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
295-478 |
5.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 295 QQEQECALDF---KTQSSKENLERcwttTESEKVTFETQNN--NLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLL 369
Cdd:COG3206 170 REEARKALEFleeQLPELRKELEE----AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 370 EDkgtstQLVRENQVLKRYLEvekqktNSFLNERVTLLEEARvLKRDLERERLTA-----MALRAELEQLapRQAQGHAD 444
Cdd:COG3206 246 RA-----QLGSGPDALPELLQ------SPVIQQLRAQLAELE-AELAELSARYTPnhpdvIALRAQIAAL--RAQLQQEA 311
|
170 180 190
....*....|....*....|....*....|....
gi 672062171 445 SPSVQRGEKEIVLLQQRLAELEQKLsfEQQRSDL 478
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQL--AQLEARL 343
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
328-413 |
5.80e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 328 ETQNNNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDKGTS-TQLVRENQVLKRYLEvEKQKTNSFLNERVTL 406
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREiSRLDREIERLERELE-EERERIEELKRKLER 497
|
....*..
gi 672062171 407 LEEARVL 413
Cdd:COG2433 498 LKELWKL 504
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-434 |
8.10e-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: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 334 LAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLED-----KGTSTQLVRENQVLKRYLEVEKQKTNSFLNER--VTL 406
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeveelEAELEEKDERIERLERELSEARSEERREIRKDreISR 469
|
90 100
....*....|....*....|....*....
gi 672062171 407 LE-EARVLKRDLERERLTAMALRAELEQL 434
Cdd:COG2433 470 LDrEIERLERELEEERERIEELKRKLERL 498
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
110-260 |
9.01e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 43.06 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 110 TLEPPKLEEMG---IQEVAIIKDDLNLGSSSSSQYTFCQPEPEkwweklwkiPECIRGWDDQLRLRVPSQLALQVFSSQH 186
Cdd:PLN02328 5 TKEPEDPADNVndvVSEASSPETDLSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVSDS 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062171 187 SDEESSSDD-----TSHEPSPAPRRRRNRKKtvsiseseepLLPEPEDEPSkeTSKRHFSGGLNKCIILALVIAISMGF 260
Cdd:PLN02328 76 QGDESSSEQqpqnpNSTEPAPPPKKRRRRKR----------FFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
270-544 |
1.49e-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: 42.35 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 270 QKRQQLGRKVHE--DELNSVKDYLFQCQQEQECALDFKTQSS------KENLERcwTTTESEKVTFETQNNN-----LAA 336
Cdd:TIGR02168 684 EKIEELEEKIAEleKALAELRKELEELEEELEQLRKELEELSrqisalRKDLAR--LEAEVEQLEERIAQLSkelteLEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 337 ENKYLRLSLEKEEKTLSSLQEELRQLKEQI-----RLLEDKGTSTQLVRENQVLKRYLEVEKQKTNSFLNERVTLLEEAR 411
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 412 VLKRDLERERLTAMALRAELEQL--APRQAQGHADSPSVQRGEKE--IVLLQQRLAELEQKL-SFEQQRSDLwERLYVEA 486
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEeaLALLRSELEELSEELrELESKRSEL-RRELEEL 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672062171 487 KDQHGK-----QEADGRKRGSKGSHRVKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQ 544
Cdd:TIGR02168 921 REKLAQlelrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-555 |
1.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 332 NNLAAENKYLRLSLEKEEKTLSSLQEELRQLKEQIRLLEDKgtstqlVRENQVLKRYLEvEKQKTNSFLNErvtLLEEAR 411
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK------VKELKELKEKAE-EYIKLSEFYEE---YLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 412 VLKRDLERerltamaLRAELEQLAPRQAQGHADSPSVQRGEKEIVLLQQRLAELEQklsfeqqrsdlWERLYVEAKDQHG 491
Cdd:PRK03918 311 EIEKRLSR-------LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----------RHELYEEAKAKKE 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672062171 492 KQEADGRKRGSKGSHRVKSKSKEtfLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKEnLKK 555
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKK 433
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
520-577 |
1.67e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 672062171 520 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 577
Cdd:COG4980 36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-490 |
2.58e-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: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 342 RLSLEKEEKTLSSLQEELRQLKEQIRLLEDkgtstqlvRENQVLKRYLEVEKQKTNSFLNErvtlLEEARVLKRDLERER 421
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEA--------RLDALREELDELEAQIRGNGGDR----LEQLEREIERLEREL 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062171 422 LTAMALRAELEQLAprQAQGHADSPSVQRGEKEIVLLQQRLAELEQKLSFEQQRSDLWERLYVEAKDQH 490
Cdd:COG4913 355 EERERRRARLEALL--AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-476 |
2.88e-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: 41.21 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 270 QKRQQLGRKVH---EDELNSVKDYLFQCQQEQEcaldfKTQSSKENLERCWTTTESEKVTFETQNNNLAAENKYLRLSLE 346
Cdd:TIGR02169 272 QLLEELNKKIKdlgEEEQLRVKEKIGELEAEIA-----SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 347 KEEKTLSSLQEELRQLKEQIRLL----EDKGTSTQLVRENQV-LKRYLEVEKQKTNSFLNERVTLLEEARVLKRDLE--- 418
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETRDELKdYREKLEKLKREINELKRELDRLQEELQRLSEELAdln 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 419 ------RERLTAMALRAELEQLAPRQAQGHADSPSVQRG----------------EKEIVLLQQRLAELEQKLSFEQQRS 476
Cdd:TIGR02169 427 aaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSkyeqelydlkeeydrvEKELSKLQRELAEAEAQARASEERV 506
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
327-469 |
3.80e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 327 FETQNNNLAaenkylRLsLEKEEKTLSSLQEELRQLKEQIRLLED--KGTSTQLVRENQVLKRYLEVEKQKTnsfLNERV 404
Cdd:pfam15619 51 YEGTESELP------QL-IARHNEEVRVLRERLRRLQEKERDLERklKEKEAELLRLRDQLKRLEKLSEDKN---LAERE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672062171 405 TLLEEARVLKRDLE--RERLTAMALRAELE------QLAPRQAQGHADSPSVQRGEKEIVLLQQRLAELEQKL 469
Cdd:pfam15619 121 ELQKKLEQLEAKLEdkDEKIQDLERKLELEnksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
272-482 |
6.07e-03 |
|
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: 40.16 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 272 RQQLGRKvhEDELNSVKDYLfqcqqEQECALdfKTQSSKENLErcwtttesekvtFETQNNNLAAENKYLRLSLEKEEKT 351
Cdd:pfam01576 235 RAQLAKK--EEELQAALARL-----EEETAQ--KNNALKKIRE------------LEAQISELQEDLESERAARNKAEKQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 352 LSSLQEELRQLKEQirlLEDKGTST------QLVRENQV--LKRYLEVE-----------KQKTNSFLNERVTLLEEARV 412
Cdd:pfam01576 294 RRDLGEELEALKTE---LEDTLDTTaaqqelRSKREQEVteLKKALEEEtrsheaqlqemRQKHTQALEELTEQLEQAKR 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672062171 413 LKRDLERERLTAMALRAELEQLAPRQAQGHADSpsvQRGEKEivlLQQRLAELEQKLS-FEQQRSDLWERL 482
Cdd:pfam01576 371 NKANLEKAKQALESENAELQAELRTLQQAKQDS---EHKRKK---LEGQLQELQARLSeSERQRAELAEKL 435
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
336-478 |
6.82e-03 |
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Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 336 AENKYLRLSLEKEEKTLSSLQEELRQLKEqirLLEDKGTSTQLVREN-QVLKRYLEVEKQKTNsflnERVTLLEEARVLK 414
Cdd:pfam07888 171 AERKQLQAKLQQTEEELRSLSKEFQELRN---SLAQRDTQVLQLQDTiTTLTQKLTTAHRKEA----ENEALLEELRSLQ 243
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672062171 415 RDLERERLTAMALRAELEQLAPRQAQGHAD--SPSVQRGEKEIVLLQQRLAELEQKLSFEQQRSDL 478
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAQRDRTQAElhQARLQAAQLTLQLADASLALREGRARWAQERETL 309
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| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
282-485 |
8.68e-03 |
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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: 39.70 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 282 DELNSVKDYLFQCQQEQECALDfKTQSSKENLERCWTTTESEKVTFETQNNNlaaenkyLRLSLEKEEKTLSSLQEELRQ 361
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLD-KSEENARSIEYEVLKKEKQMKILENKCNN-------LKKQIENKNKNIEELHQENKA 619
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062171 362 LKEQiRLLEDKGTSTQLVRENQvLKRYLEVEKQKTNSFLNERVTLLEEARVLKRDL--ERERLTAMALRA-ELEQLAPRQ 438
Cdd:pfam05483 620 LKKK-GSAENKQLNAYEIKVNK-LELELASAKQKFEEIIDNYQKEIEDKKISEEKLleEVEKAKAIADEAvKLQKEIDKR 697
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 672062171 439 AQgHADSPSVQRGEKEI----VLLQQRLAELEQKLSFEQQRSDLWERLYVE 485
Cdd:pfam05483 698 CQ-HKIAEMVALMEKHKhqydKIIEERDSELGLYKNKEQEQSSAKAALEIE 747
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