|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-530 |
1.89e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 299 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 375
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 376 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 455
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947853 456 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAK 530
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
334-532 |
1.51e-10 |
|
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: 63.24 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 334 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 413
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 414 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 490
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622947853 491 LKKQVEKLQAQvtlsNAQLKAFKDEEKAREANRQQKRKAKAS 532
Cdd:COG4942 176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAA 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
336-531 |
2.12e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 336 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 415
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 416 EIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 495
Cdd:COG1196 275 ELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622947853 496 EKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 531
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
330-501 |
4.13e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 60.32 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 330 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 409
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 410 REYQ--EKEI---QRLNKALEEALsiqtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErm 484
Cdd:COG1579 89 KEYEalQKEIeslKRRISDLEDEI------------------LELMERIEELEEELAELEAELAELEAELEEKKAELD-- 148
|
170
....*....|....*..
gi 1622947853 485 nEEKEELKKQVEKLQAQ 501
Cdd:COG1579 149 -EELAELEAELEELEAE 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
301-520 |
1.29e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 301 EKKVKMLEQQRSELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLADLQKQVTDLEAERE----QKQRDFDRKLll 370
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 371 aKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS-IQTPPSspptafgspEGAGA 449
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeIEKLKK---------ENQSY 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947853 450 LLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARE 520
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-499 |
1.58e-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: 61.23 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 191 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsNGNKEGASGQPGSPKM 270
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 271 EGAGKKAVAGQQQASVTAGK---VPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYE---QKITELRQKLA 344
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdleEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 345 DLQKQVTDLEAEREQKQRDFDRKL-LLAKSKIEME--ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE-YQEK----- 415
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLnERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAqLELRlegle 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 416 -EIQRLNKALEEALSI--QTPPSSPPTAFGSPEGAgallrKQELvtqnELLKQQVKIF-------EEDFQRERSDRERMN 485
Cdd:TIGR02168 936 vRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEA-----RRRL----KRLENKIKELgpvnlaaIEEYEELKERYDFLT 1006
|
330
....*....|....
gi 1622947853 486 EEKEELKKQVEKLQ 499
Cdd:TIGR02168 1007 AQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-529 |
2.11e-08 |
|
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: 57.76 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 336 ITELRQKLADLQKQVT------DLEAEREQKQ--------RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQD 401
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 402 QLSPLtrqreyqEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR 481
Cdd:TIGR02168 275 EVSEL-------EEEIEELQKELYALANEI---------------SRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947853 482 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 529
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-515 |
2.32e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 328 MKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLS 404
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 405 PLTRQREYQ--------EKEIQRLNKALEE-------------ALSIQTPPSspptafgspegAGALLRKQELVTQN-EL 462
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEErerrrarleallaALGLPLPAS-----------AEEFAALRAEAAALlEA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622947853 463 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 515
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-429 |
2.46e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 191 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgqpgspkm 270
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 271 egAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQ 347
Cdd:COG1196 329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 348 KQVTDLE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 424
Cdd:COG1196 407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
....*
gi 1622947853 425 EEALS 429
Cdd:COG1196 487 AEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
325-531 |
2.66e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 325 FRSMKQQYEQKITELR-QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQL 403
Cdd:COG1196 215 YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEE----LEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 404 SPLTRQREYQEKEIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRER 483
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEE----------------------RLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947853 484 MNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 531
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
295-501 |
3.19e-08 |
|
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: 55.93 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 295 AALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR----- 366
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 367 ---------KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppssp 437
Cdd:COG4942 114 yrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE-------- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947853 438 ptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 501
Cdd:COG4942 186 --------------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-535 |
3.83e-08 |
|
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: 56.61 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 170 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLEL 248
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 249 KKLLMSNGNKegasgqpgspKMEGAGKKAVAGQQQASVTAGKVpEVAALGA--AEKKVKMLEQQRSELLEVNKQWDQHFR 326
Cdd:TIGR02169 747 SSLEQEIENV----------KSELKELEARIEELEEDLHKLEE-ALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 327 SMkqqyEQKITELRQKLADLQKQVTDLEAEREQKQrdfDRKLLLAKsKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPL 406
Cdd:TIGR02169 816 EI----EQKLNRLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 407 TRQREYQEKEIQRLNKALEEA-LSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 485
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELeAQIEK----------------KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622947853 486 EEkEELKKQVEKLQAQV-TLSNAQLKAFKD-EEKAREANRQQKRKAKASGER 535
Cdd:TIGR02169 952 SL-EDVQAELQRVEEEIrALEPVNMLAIQEyEEVLKRLDELKEKRAKLEEER 1002
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
453-501 |
4.06e-08 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 50.81 E-value: 4.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622947853 453 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 501
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
329-531 |
4.98e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 329 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSplTR 408
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 409 QREYQEKeiQRLNKALEEALSIQtppsSPPTAFGSPEGAGALLRKQ-ELVTQNELLKQQVKIFEEDFQRERSDRERMNEE 487
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLGSE----SFSDFLDRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622947853 488 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 531
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-534 |
1.07e-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: 55.45 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 330 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 409
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 410 REYQEKEIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKE 489
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622947853 490 ELKkqVEKLQAQVTLSNAQlkaFKDEEKAREANRQQKRKAKASGE 534
Cdd:TIGR02168 814 LLN--EEAANLRERLESLE---RRIAATERRLEDLEEQIEELSED 853
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-499 |
2.71e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 230 GLEQRDQAAERL-------REENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVTAGKVPEVAA-LGAAE 301
Cdd:PRK03918 156 GLDDYENAYKNLgevikeiKRRIERLEKFIKRTENIEE--------LIKEKEKELEEVLREINEISSELPELREeLEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 302 KKVKMLEQQRSELLEVNKQWDQHFRSMK------QQYEQKITELRQKLADLQKQVTDLE-----AEREQKQRDFDRKLLL 370
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 371 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQTPPSSPPTAFGSpega 447
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTG---- 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622947853 448 galLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 499
Cdd:PRK03918 384 ---LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
191-531 |
3.18e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 191 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKLLMSNGNKEGASGQPGSPKM 270
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 271 EGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQV 350
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE----KKKEEAKKKADAAKKKAEEKKKA 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 351 TDLE--AEREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKylQDQLSPLTRQREYQEKEIQRLNKALEEAL 428
Cdd:PTZ00121 1394 DEAKkkAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 429 SIQTPPSSPPTAFGSPEG---AGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQV 502
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADE 1550
|
330 340
....*....|....*....|....*....
gi 1622947853 503 TLSNAQLKAFKDEEKAREANRQQKRKAKA 531
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
333-531 |
4.49e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 333 EQKITELRQKLADLQKQVTDLEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVKYLQDQLSPLTRQREY 412
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 413 QEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 485
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622947853 486 EEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 531
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
208-530 |
5.61e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 208 ILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVT 287
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE--------ELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 288 AGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRK 367
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 368 LLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY--QEKEIQRLNKALEEALSIQ---------TPPSS 436
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLliaaallalLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 437 PPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQL-KAFKDE 515
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlELLDRI 346
|
330
....*....|....*
gi 1622947853 516 EKAREANRQQKRKAK 530
Cdd:COG4717 347 EELQELLREAEELEE 361
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
329-495 |
1.09e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 329 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 406
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 407 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 474
Cdd:PRK00409 602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
|
170 180
....*....|....*....|.
gi 1622947853 475 qrerSDRERMNEEKEELKKQV 495
Cdd:PRK00409 677 ----SDLEKIQKPKKKKKKKP 693
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
185-495 |
1.58e-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: 51.61 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 185 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkEGASGQ 264
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL-------EARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 265 PGSPKMEGAGKKAvagQQQASVTAGKVPEV-AALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELR 340
Cdd:TIGR02169 791 SRIPEIQAELSKL---EEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 341 QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRL 420
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL----EEELSEIEDP 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 421 NKALEEalsiqTPPSSPP---------------TAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEdfqreRSDRERMN 485
Cdd:TIGR02169 940 KGEDEE-----IPEEELSledvqaelqrveeeiRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE-----RKAILERI 1009
|
330
....*....|
gi 1622947853 486 EEKEELKKQV 495
Cdd:TIGR02169 1010 EEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-498 |
2.67e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 297 LGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 373
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA----LEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 374 KIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS--IQTPPSSPPTAFGSPEGAGALL 451
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYL 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622947853 452 RKQELVTQNELLKQQVKIFEedFQRERSDRE------RMNEEKEELKKQVEKL 498
Cdd:COG4913 819 ALLDRLEEDGLPEYEERFKE--LLNENSIEFvadllsKLRRAIREIKERIDPL 869
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
461-503 |
3.95e-06 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 45.75 E-value: 3.95e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622947853 461 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 503
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-431 |
4.51e-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: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 191 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENlelKKLLMSNGNKEGasgqpgspkM 270
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE---EKLEELKEELES---------L 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 271 EGAGKKAVAGQQQASvtagkvpevAALGAAEKKvkmLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQV 350
Cdd:TIGR02168 357 EAELEELEAELEELE---------SRLEELEEQ---LETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 351 TDLEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 429
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 1622947853 430 IQ 431
Cdd:TIGR02168 497 LQ 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-545 |
7.28e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 187 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRKENEALK-AKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQP 265
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 266 GSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEK-----KVKMLEQQRSEllEVNKQWDQHFRSMKQQYEQKITELR 340
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 341 QKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEI 417
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 418 QRLNKALEEalsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVkifeedfQRERSDRERMNEEKEELKKQVEK 497
Cdd:PTZ00121 1678 EEAKKAEED----------------EKKAAEALKKEAEEAKKAEELKKKE-------AEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622947853 498 LQAqvtlsnaqlKAFKDEEKAREANRQQKRKAKASGERYHVEPHPEHL 545
Cdd:PTZ00121 1735 AKK---------EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-530 |
7.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 196 ASKVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEGA 273
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 274 GKKAVAGQQQASVTAGKVPEvaALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELRQ--------- 341
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkKADEAKKaaeakkkad 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 342 --KLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 419
Cdd:PTZ00121 1514 eaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 420 LNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNEllkQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQ 499
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAE-EKKKAEELKKAEEENKIKAAEEAKK 1669
|
330 340 350
....*....|....*....|....*....|.
gi 1622947853 500 AQVTLSNAQlKAFKDEEKAREANRQQKRKAK 530
Cdd:PTZ00121 1670 AEEDKKKAE-EAKKAEEDEKKAAEALKKEAE 1699
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
301-525 |
7.68e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 301 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQrdfdrklllakSKIEMEET 380
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 381 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqelvtqn 460
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---------------------------------- 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947853 461 elLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQ 525
Cdd:TIGR04523 466 --LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
185-501 |
8.29e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 185 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQ 264
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 265 PGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLA 344
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 345 DLQKQVTDLEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ--E 414
Cdd:pfam02463 835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleE 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 415 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAG----------------ALLRKQELVTQNELLKQQVKIFEEDFQRER 478
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|...
gi 1622947853 479 SDRERMNEEKEELKKQVEKLQAQ 501
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
163-422 |
8.61e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 163 QRLETTLSVCAEEPDHSQLFTHLGRMALEFNRL----------ASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLDK 229
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrrlfdekqSEKDKKNKALAERKDSANERLNSleaQLKQLDKKHQA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 230 GLEQRDQAAERLREENLELKKLLMSNgnkegASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQ 309
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGA-----LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 310 QRSEL------LEVNK-------QWDQH-FRSMKQQYEQKITELRQKLADLQKQVTDLEAERE------QKQRDFDRKLL 369
Cdd:pfam12128 776 EIRTLerkierIAVRRqevlryfDWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKlrraklEMERKASEKQQ 855
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947853 370 ------LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 422
Cdd:pfam12128 856 vrlsenLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
191-450 |
8.95e-06 |
|
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: 48.22 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 191 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmsngnkegasgqpgspKM 270
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----------------AE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 271 EGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQrsellevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQV 350
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL------------QYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 351 TDLEAEREQKQRDfdrklllakskIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 430
Cdd:COG4942 167 AELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|
gi 1622947853 431 QTPPSSPPTAFGSPEGAGAL 450
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKL 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
203-530 |
1.28e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 203 EQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQaaeRLREENLELKKLLmsnGNKEGASGQpgspKMEGAGKKAVAGQQ 282
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQAL---LKEKREYEGYELL---KEKEALERQ----KEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 283 QASVTAgkvpevaalgAAEKKVKMLEQQRSELLEVNKQwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLE---AEREQ 359
Cdd:TIGR02169 253 LEKLTE----------EISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLErsiAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 360 KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppssppt 439
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE------------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 440 afgspegagallrkqelvTQNELLKQQVKIfeEDFQRERSD----RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 515
Cdd:TIGR02169 383 ------------------TRDELKDYREKL--EKLKREINElkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330
....*....|....*.
gi 1622947853 516 -EKAREANRQQKRKAK 530
Cdd:TIGR02169 443 kEDKALEIKKQEWKLE 458
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
322-525 |
1.35e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 322 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 396
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 397 KYLQDQL-------SPLTRQREYQE--KEIQRLNKALEEALSIQTPpsspptafGSPEGAGAllrKQELVTQNELLKQQV 467
Cdd:COG3206 243 AALRAQLgsgpdalPELLQSPVIQQlrAQLAELEAELAELSARYTP--------NHPDVIAL---RAQIAALRAQLQQEA 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947853 468 KifeEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQ 525
Cdd:COG3206 312 Q---RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
194-530 |
1.53e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 194 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEga 273
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 274 gkkavagqqqasvtagkvpEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrSMKQQYEQKITELRQKLADLQKQVTDL 353
Cdd:pfam02463 252 -------------------EIESSKQEIEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 354 EAEREQKQRDfDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQreyQEKEIQRLNKALEEALSIQTP 433
Cdd:pfam02463 310 VDDEEKLKES-EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 434 PSSPPTAFGSpEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 513
Cdd:pfam02463 386 LSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330
....*....|....*..
gi 1622947853 514 DEEKAREANRQQKRKAK 530
Cdd:pfam02463 465 LELKKSEDLLKETQLVK 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-545 |
1.77e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 316 EVNKQWDqhfrSMKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFdrklllAKSKIEMEETDKEQLTAEAKELR 393
Cdd:TIGR02168 197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 394 QKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEA-LSIQTPPSSPPTAFGSPEGAGALLR--KQELVTQNELLKQQVKIF 470
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947853 471 EEDfqrersdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdEEKAREANRQQKRKAKASGERYHVEPHPEHL 545
Cdd:TIGR02168 347 EEL-------KEELESLEAELEELEAELEELESRLEELEEQL--ETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-430 |
1.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 194 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLReenlELKKLLMSNGnkegasgqpgspkmega 273
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNG----------------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 274 gkkavaGQQqasvtagkvpevaaLGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL 353
Cdd:COG4913 337 ------GDR--------------LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947853 354 EAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRqreyqekEIQRLNKALEEALSI 430
Cdd:COG4913 397 EEELEALEEALAEA-----------EAALRDLRRELRELEAEIASLERRKSNIPA-------RLLALRDALAEALGL 455
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
202-427 |
2.22e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 202 NEQRTSILQTLcEQLRKENEALKAKLdkglEQRDQAAERLREENlelkKLLMSNGNKEGASGQpgspkmegagkKAVAGQ 281
Cdd:COG3206 167 ELRREEARKAL-EFLEEQLPELRKEL----EEAEAALEEFRQKN----GLVDLSEEAKLLLQQ-----------LSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 282 QQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEvnkqwDQHFRSMKQQY---EQKITELRQKLAD-------LQKQVT 351
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLaelEAELAELSARYTPnhpdviaLRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947853 352 DLEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL---QDQLSPLTRQREYQEKEIQRLNKALEEA 427
Cdd:COG3206 302 ALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
301-508 |
2.32e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 301 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQKQVTDLEAE---------------REQKQR 362
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 363 DFDRKLLLAKSKIEMEETDKE---------QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQTP 433
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS---DLEDE 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 434 PSSPPTAFGSPEGAGALLRKQELV-----TQNELLKQQVKiFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQ 508
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIeelkqTQKSLKKKQEE-KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
301-534 |
3.09e-05 |
|
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: 47.04 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 301 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQkladlqkqvtDLEAEREQKQRDFDRKLLLAKSKIEMEET 380
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 381 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQEL---- 456
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 457 -----------VTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdeEKAREANRQQ 525
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM---EREREMMRQI 581
|
....*....
gi 1622947853 526 KRKAKASGE 534
Cdd:pfam17380 582 VESEKARAE 590
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
191-510 |
3.76e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 191 EFNRLASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLdkglEQRDQAAERLREENLELKKLLMSNGNKEGA------ 261
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAmqveka 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 262 --SGQPGSPKME-------GAGKKAVAGQQQASVTAGKVPEVAALGAAEKK---VKMLEQQRSELLEVNKQWDQHFRSMK 329
Cdd:pfam15921 594 qlEKEINDRRLElqefkilKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRNELNSLS 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 330 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSkieMEETD----------KEQLTAEAKE---LRQKV 396
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDghamkvamgmQKQITAKRGQidaLQSKI 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 397 KYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqtppSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQR 476
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQEL----------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622947853 477 ERSDR--ERMNEEKEELKKQ----VEKLQAQVTLSNAQLK 510
Cdd:pfam15921 821 AECQDiiQRQEQESVRLKLQhtldVKELQGPGYTSNSSMK 860
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
296-400 |
5.19e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 45.74 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 296 ALGAAEKKVKM-------LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkl 368
Cdd:pfam02841 198 ALTAKEKAIEAerakaeaAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER-- 265
|
90 100 110
....*....|....*....|....*....|..
gi 1622947853 369 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQ 400
Cdd:pfam02841 266 MLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-529 |
5.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 333 EQKITELRQKLADLQKQVTDLEAEREQKQRDFD--RKLLLAKSKIEM---EETDKEQLTAEAKELRQKVKYL---QDQLS 404
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswDEIDVASAEREIAELEAELERLdasSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 405 PLTRQREYQEKEIQRLNKALEealsiqtppsspptafgspegagallrkqELVTQNELLKQQVKIFEEDFQRERSDRERM 484
Cdd:COG4913 689 ALEEQLEELEAELEELEEELD-----------------------------ELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622947853 485 NE-EKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 529
Cdd:COG4913 740 EDlARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
124-517 |
5.91e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 124 EFEVVTPEEQSSPPENSSHANETVLGPLPHEDGNLMLHLQRLETTLSVCAEEPDhsqlfthlGRMALEFNRLASKVHKNE 203
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 204 QRTSI---LQTLCEQLRKENEALKAK-------------LDKGLEQRDQAAERLREE--------NLELKKL--LMSNGN 257
Cdd:pfam15921 462 KVSSLtaqLESTKEMLRKVVEELTAKkmtlessertvsdLTASLQEKERAIEATNAEitklrsrvDLKLQELqhLKNEGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 258 K-EGASGQPGSPKMEGAGKKAVAG---QQQASVT--AGKVPEVAALGAAEKKV--KMLEQQRSELlevnkqwdQHFRSMK 329
Cdd:pfam15921 542 HlRNVQTECEALKLQMAEKDKVIEilrQQIENMTqlVGQHGRTAGAMQVEKAQleKEINDRRLEL--------QEFKILK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 330 QQYEQKITELRQKLADLQKQVTDL---EAEREQKQRDFDRklllakskiemeetDKEQLTAEAKELRQKVKYLQDQLSPL 406
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLvnaGSERLRAVKDIKQ--------------ERDQLLNEVKTSRNELNSLSEDYEVL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 407 TRQREYQEKEIQRLNKALEEAL-SIQTPPSSPPTAFGSPEGAGALLRK-----QELVT----QNELLKQQVKIFEEDFQR 476
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKLKMQLkSAQSELEQTRNTLKSMEGSDGHAMKvamgmQKQITakrgQIDALQSKIQFLEEAMTN 759
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1622947853 477 ERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEK 517
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-535 |
6.73e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 340 RQKLADLQKQVTDLEAEREQkqrdfdrklllakskiemeetdkeqLTAEAKELRQKVKYLQDQLSPLTRQREYQ------ 413
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-------------------------AEERLEALEAELDALQERREALQRLAEYSwdeidv 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 414 ---EKEIQRLNKALEEALSiqtppsspptafGSPEgagalLRKqelvtqnelLKQQVKIFEEDFQRERSDRERMNEEKEE 490
Cdd:COG4913 664 asaEREIAELEAELERLDA------------SSDD-----LAA---------LEEQLEELEAELEELEEELDELKGEIGR 717
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622947853 491 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKASGER 535
Cdd:COG4913 718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
301-528 |
7.07e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 301 EKKVKMLEQQRSELLEvnkqwDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK------ 374
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK-----LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 375 -IEMEETDKEQLTAEAKELRQ---KVKYLQDQLSPLTRQRE--YQEKEiQRLNKALEEALSIQtppsspptafgspegag 448
Cdd:TIGR04523 258 lKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlNNQKE-QDWNKELKSELKNQ----------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 449 allRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAR 519
Cdd:TIGR04523 320 ---EKKLEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
....*....
gi 1622947853 520 EANRQQKRK 528
Cdd:TIGR04523 397 ESKIQNQEK 405
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
290-420 |
7.73e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 290 KVPEVAALGAAEKKVKMLEQQRSE--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVtdleaerEQKQ 361
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRL-------LQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947853 362 RDFDRKLLLAKSKiemeetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 420
Cdd:PRK12704 96 ENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
311-514 |
7.75e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 311 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKqvtdleaeREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 390
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ--------RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 391 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQTPpsspptAFGSPEGAGALLRKQ---ELVTQNEL--LKQ 465
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAP------AWLAAQDALARLREQsgeEFEDSQDVteYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622947853 466 QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 514
Cdd:PRK04863 635 QLLERERELTVE---RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
162-545 |
8.60e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 162 LQRLETTLsVCAEEPDHSQLFTHLGRMALEFNRLASKVHKneqrtsilqtLCEQLRKENEALKAKLdkgLEQRDQAAERL 241
Cdd:pfam15921 186 LQEIRSIL-VDFEEASGKKIYEHDSMSTMHFRSLGSAISK----------ILRELDTEISYLKGRI---FPVEDQLEALK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 242 REENLELKKLLMSNGNKEGASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQW 321
Cdd:pfam15921 252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLESTVSQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 322 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR------DFDRKLLLAKSKIEME-ETDKEQltaeAKELRQ 394
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLEKEQ----NKRLWD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 395 KVKYLQDQLSPLTRQREYQEKEIQRLNkaleealsiqtppsspptafgspegagALLRKQELVTQNELLKQQVKI--FEE 472
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLE---------------------------ALLKAMKSECQGQMERQMAAIqgKNE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 473 DFQRERSDRERMNEEKEELKKQVEKLQA-QVTLSNAQ------LKAFKDEEKAREANRQQKRKAKAS-----GERYHVEP 540
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKN 538
|
....*
gi 1622947853 541 HPEHL 545
Cdd:pfam15921 539 EGDHL 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-449 |
8.76e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 197 SKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngNKEGASGQPGSPKMEGAGKK 276
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 277 AVAGQQQASVTAGKVPEV-------AALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQ 349
Cdd:COG3883 91 RARALYRSGGSVSYLDVLlgsesfsDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 350 VTDLEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 429
Cdd:COG3883 163 KAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
250 260
....*....|....*....|
gi 1622947853 430 IQTPPSSPPTAFGSPEGAGA 449
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAA 244
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
283-385 |
8.98e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 283 QASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR 362
Cdd:PRK11448 140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
|
90 100
....*....|....*....|...
gi 1622947853 363 DFDRKlllAKSKIEMEETDKEQL 385
Cdd:PRK11448 220 EITDQ---AAKRLELSEEETRIL 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
193-497 |
1.27e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 193 NRLASKVHKNEQRTSILQTLCEQLRKENEALkakldkgleqrDQAAERLREENLELKKLLMSNGNKEGASgqpgSPKMEG 272
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELL-----------EKEIERLKETIIKNNSEIKDLTNQDSVK----ELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 273 AGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTD 352
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKLNEE--------KKELEEKVKDLTKKISSLKEKIEK 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 353 LEAER---EQKQRDFDRKLL-----LAKSKIEME-----------ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 413
Cdd:TIGR04523 529 LESEKkekESKISDLEDELNkddfeLKKENLEKEideknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 414 EKEIQRLNKALEEAlsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 493
Cdd:TIGR04523 609 EKKISSLEKELEKA---------------KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
....
gi 1622947853 494 QVEK 497
Cdd:TIGR04523 674 KIDD 677
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-449 |
1.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 175 EPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMS 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 255 NgNKEGASGQPGSpkmegagkkAVAGQQQASVTAGKVPEVAALGAAEKkvKMLEQQRSELLEVNKQwdqhfrsmKQQYEQ 334
Cdd:COG3883 95 L-YRSGGSVSYLD---------VLLGSESFSDFLDRLSALSKIADADA--DLLEELKADKAELEAK--------KAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 335 KITELRQKLADLQKQVTDLEAEREQKQrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQE 414
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQE----ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1622947853 415 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGA 449
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
214-486 |
1.86e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 214 EQLRKENEALKAKLDKGLEQRDQAaERLREENLELKKLLmsngnkegasgqpgspkmegagkkAVAGQQQASVTAgkvpE 293
Cdd:PRK11281 52 KLLEAEDKLVQQDLEQTLALLDKI-DRQKEETEQLKQQL------------------------AQAPAKLRQAQA----E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 294 VAALGAAEKKVKmleQQRSELLEVnkqwdqhfrsmkQQYEQKITELRQKLADLQKQVTDLEA---------EREQK---- 360
Cdd:PRK11281 103 LEALKDDNDEET---RETLSTLSL------------RQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtqpERAQAalya 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 361 --QRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVKYLQ------DQLSPL-TRQREYQEKEIQRLNK---ALE 425
Cdd:PRK11281 168 nsQRLQQIRNLLKGGKVGgkaLRPSQRVLLQAEQALLNAQNDLQRkslegnTQLQDLlQKQRDYLTARIQRLEHqlqLLQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947853 426 EALSIQTPPSSPPTA--FGSPEGAGAllrkqelVTQNELLKQqvkifEEDFQRERSDR-----ERMNE 486
Cdd:PRK11281 248 EAINSKRLTLSEKTVqeAQSQDEAAR-------IQANPLVAQ-----ELEINLQLSQRllkatEKLNT 303
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
297-537 |
1.96e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 297 LGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFdRKLLLAKSKIE 376
Cdd:PHA02562 190 IDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 377 MEetdKEQLTAEAKELRQ----------------KVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppssppta 440
Cdd:PHA02562 269 SK---IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK-------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 441 fgspegagallRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARe 520
Cdd:PHA02562 338 -----------KLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI- 391
|
250
....*....|....*..
gi 1622947853 521 anrqQKRKAKASGERYH 537
Cdd:PHA02562 392 ----VKTKSELVKEKYH 404
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
215-252 |
2.09e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 43.43 E-value: 2.09e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1622947853 215 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 252
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
173-501 |
2.77e-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: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 173 AEEPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKaKLDKGLEQRDQAAERLREEnlelkkll 252
Cdd:pfam17380 327 AEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQE-------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 253 msngnkegasgqpgspkMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSEllEVNKQWDQHFRSMKQQY 332
Cdd:pfam17380 398 -----------------LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 333 EQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllakskieMEETDKEQLTAEAKELRQKVkyLQDQlspltRQREY 412
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----RKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 413 QEKEIQRLNKALEEALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEKEELK 492
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE--------------AEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMR 579
|
....*....
gi 1622947853 493 KQVEKLQAQ 501
Cdd:pfam17380 580 QIVESEKAR 588
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-396 |
3.55e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 215 QLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQpgspkmeGAGKKAVAGQQQASVTAGKvpEV 294
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-------VEARIKKYEEQLGNVRNNK--EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 295 AALgaaEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK 374
Cdd:COG1579 92 EAL---QKEIESLKRRISDL------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1622947853 375 IEMEETDKEQLTAEAKELRQKV 396
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
316-426 |
3.66e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.03 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 316 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 394
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 1622947853 395 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 426
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-488 |
3.83e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 187 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERlreENLELKKLLMSNGNKEGASGQPG 266
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVM 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 267 SPKMEGAGKKAvagqQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADL 346
Cdd:PTZ00121 1599 KLYEEEKKMKA----EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 347 QKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 424
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947853 425 EEALSIQTppsspptafgspegagalLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 488
Cdd:PTZ00121 1754 EEKKKIAH------------------LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-426 |
4.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 185 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQ 264
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 265 PGSPKMEGAGKKAVAGQQQASVtAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLA 344
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 345 DLQKQVTDLEA------EREQKQRDFDRKL--------LLAKSKIEMEETDK----------EQLTAEAKELRQKVKYLQ 400
Cdd:PRK03918 325 GIEERIKELEEkeerleELKKKLKELEKRLeeleerheLYEEAKAKKEELERlkkrltgltpEKLEKELEELEKAKEEIE 404
|
250 260
....*....|....*....|....*.
gi 1622947853 401 DQLSPLTRQREYQEKEIQRLNKALEE 426
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEE 430
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
195-541 |
4.85e-04 |
|
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: 43.42 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 195 LASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSngnkegasgQPGSPKMEGAG 274
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA---------QEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 275 KKAVAGQQQASVTAGKVPEV-AALGAAEKKVKMLEQQRSeLLEVNKQWDQHFRSMKQQyEQKITELRQKLADLQKQVTDL 353
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETqERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 354 EAEREQKQRDFDRKLLLAKSKiEMEETDKEQLTaEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkalEEALSIQTP 433
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAH-EVATSIREISC-QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ---REQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 434 PSSpptaFGSPEGAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSnaQLKAFK 513
Cdd:TIGR00618 416 TSA----FRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH--LQETRK 488
|
330 340
....*....|....*....|....*...
gi 1622947853 514 DEEKAREANRQQKRKAKASGERYHVEPH 541
Cdd:TIGR00618 489 KAVVLARLLELQEEPCPLCGSCIHPNPA 516
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
295-422 |
5.07e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 295 AALGAAEKKVKMLEQQRSELL-EVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR-KLLLAK 372
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQaELDRL--QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrRVLAPI 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947853 373 SKIEMEETDKEQltAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 422
Cdd:pfam00529 136 GGISRESLVTAG--ALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR 183
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-500 |
5.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 198 KVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmSNGNKEGASGQPGSPKMEgagkka 277
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLA------ 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 278 vagqqqasvtagkvpevaalgAAEKKVKMLEQQRSELLevNKQWDQHFRSMKQqYEQKITELR---QKLADLQKQVTDLE 354
Cdd:PRK03918 560 ---------------------ELEKKLDELEEELAELL--KELEELGFESVEE-LEERLKELEpfyNEYLELKDAEKELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 355 AEREqkqrdfdrKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQdqlspltrqREYQEKEIQRLNKALEEAlsiqtpp 434
Cdd:PRK03918 616 REEK--------ELKKLEEELDKAFEELAETEKRLEELRKELEELE---------KKYSEEEYEELREEYLEL------- 671
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947853 435 sspptafgSPEGAGALLRKQELvtqnELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQA 500
Cdd:PRK03918 672 --------SRELAGLRAELEEL----EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
303-535 |
5.80e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 303 KVKMLEQQRSELLEVNKQWDQHF----RSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEME 378
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 379 ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAgallRKQELVT 458
Cdd:pfam00038 95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAA----RKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 459 QNELLKQQvkiFEEDFQRERSDRErmneekEELKKQVEKLQAQVTLSNAQLKAFKDEEK-------AREANRQQKRKAKA 531
Cdd:pfam00038 171 ALAEIRAQ---YEEIAAKNREEAE------EWYQSKLEELQQAAARNGDALRSAKEEITelrrtiqSLEIELQSLKKQKA 241
|
....
gi 1622947853 532 SGER 535
Cdd:pfam00038 242 SLER 245
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
307-428 |
5.85e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 307 LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLT 386
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPELE 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 387 AEAKELRQKVKYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEEAL 428
Cdd:COG0542 492 KELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEEEL 547
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
309-526 |
7.64e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 309 QQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKSKIEMEETDK 382
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 383 EQL-TAEAKELRQKVKYLQDQLspltrqreyqekeiQRLNKALEEA----LSIQTPPSSPPTA---------------FG 442
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQL--------------QNAQNDLAEYnsqlVSLQTQPERAQAAlyansqrlqqirnllKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 443 SPEGAGALL--RKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAqvTLSNAQ 508
Cdd:PRK11281 182 GKVGGKALRpsQRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKR 254
|
250
....*....|....*...
gi 1622947853 509 LKAFkdEEKAREANRQQK 526
Cdd:PRK11281 255 LTLS--EKTVQEAQSQDE 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
305-427 |
7.87e-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: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 305 KMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllaksKIEMEEtdkEQ 384
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----------RIERLE---RE 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622947853 385 LTAEAKELRQKVKylqdqlspltRQREYQ--EKEIQRLNKALEEA 427
Cdd:COG2433 450 LSEARSEERREIR----------KDREISrlDREIERLERELEEE 484
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
316-426 |
9.03e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 316 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 395
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
|
90 100 110
....*....|....*....|....*....|.
gi 1622947853 396 VKYLQDQLSplTRQREYQEKEIQRLNKALEE 426
Cdd:pfam03938 78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
295-411 |
9.74e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 295 AALGAAEKKVKMLEQ----QRSELLEVNKQWDQHfRSMKQQYEQKITELRQKLADLQKQVTD-LEAEREQKQRDFDRKLL 369
Cdd:COG1842 16 ALLDKAEDPEKMLDQairdMEEDLVEARQALAQV-IANQKRLERQLEELEAEAEKWEEKARLaLEKGREDLAREALERKA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622947853 370 LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE 411
Cdd:COG1842 95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKD 136
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
209-526 |
1.06e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 209 LQTLCEQLRKENEALKAKLdKGLEQRDQAAERLREENLELKKllmsnGNKEGASGQP--GSPKMEGAGKK---------- 276
Cdd:PRK02224 410 AEDFLEELREERDELRERE-AELEATLRTARERVEEAEALLE-----AGKCPECGQPveGSPHVETIEEDrerveeleae 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 277 -AVAGQQQASVTAgKVPEVAALGAAEKKVKMLEQQRSELLEvnkqwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLEA 355
Cdd:PRK02224 484 lEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEE-----------LIAERRETIEEKRERAEELRERAAELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 356 EREQKqRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQTpps 435
Cdd:PRK02224 552 EAEEK-REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELND--- 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 436 spptafgspegagalLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLSNA 507
Cdd:PRK02224 624 ---------------ERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAVEN 688
|
330 340
....*....|....*....|.
gi 1622947853 508 QLKAFKD--EEKAREANRQQK 526
Cdd:PRK02224 689 ELEELEElrERREALENRVEA 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-426 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 187 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPg 266
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL- 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 267 SPKMEGAGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQWDQHFRSMK-------------QQYE 333
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAA--EIEELEELIEELESELEALLNERASLEEALAllrseleelseelRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 334 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL--LLAKSKIEMEETDKEQ--------------------------- 384
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEAEALEnkieddeeearrrlkrlenkikelgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622947853 385 -LTA--EAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 426
Cdd:TIGR02168 988 nLAAieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
307-527 |
1.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 307 LEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 383
Cdd:COG4372 40 LDKLQEELEQLREELEQ-AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQaelAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 384 QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQ 459
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLeslqEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947853 460 NELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKR 527
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
299-400 |
1.41e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 299 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkLLLAKSKiEME 378
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 1622947853 379 ETDKEQLTAEAKELRQKVKYLQ 400
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-519 |
1.49e-03 |
|
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: 41.63 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 198 KVHKNEQRTSILqtLCEQLRKENEaLKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMegagkka 277
Cdd:pfam05483 234 EINDKEKQVSLL--LIQITEKENK-MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 278 vagQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQH-----------------FRSMKQQYEQKITELR 340
Cdd:pfam05483 304 ---SLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvvtefeattcsleelLRTEQQRLEKNEDQLK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 341 QKLADLQKQVTDLEAE---REQKQRDFD--RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL-----------QDQLS 404
Cdd:pfam05483 381 IITMELQKKSSELEEMtkfKNNKEVELEelKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarekeihdlEIQLT 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 405 PLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFgspegagaLLRKQELVTQNELLKQQVKIFEEDFQRERSDRERM 484
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--------LLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
330 340 350
....*....|....*....|....*....|....*
gi 1622947853 485 NEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAR 519
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
330-534 |
1.93e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 330 QQYEQKIT-------ELRQKLADLQKQVTDLEAerEQKQRDFDRKLLLAKSkiemeetdkeQLTAEAKELRQ---KVKYL 399
Cdd:PRK10929 68 KQYQQVIDnfpklsaELRQQLNNERDEPRSVPP--NMSTDALEQEILQVSS----------QLLEKSRQAQQeqdRAREI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 400 QDQLSPLTRQREyqekEIQRLNKALEEALSIQTPPSSPptafgspegagaLLRKQELVTQNELLKQQVKIFEEDF-QRER 478
Cdd:PRK10929 136 SDSLSQLPQQQT----EARRQLNEIERRLQTLGTPNTP------------LAQAQLTALQAESAALKALVDELELaQLSA 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947853 479 SDRERMNEEKEEL-KKQVEKLQAQVTLSNAQLKAFKDEEkAREANRQQKRKAKASGE 534
Cdd:PRK10929 200 NNRQELARLRSELaKKRSQQLDAYLQALRNQLNSQRQRE-AERALESTELLAEQSGD 255
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
385-505 |
2.10e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 385 LTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQTPPSSPPTAFgspegAGALLRKQELVTQNELL 463
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQL-----ATERSARREAEAELERL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622947853 464 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQVTLS 505
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQLTSK 158
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-515 |
2.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 157 NLMLHLQRLETTLSVCAEEPDHSQLFTHLgRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKglEQRDQ 236
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSL-ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ--LENEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 237 AAERLREENLELKKLLMSNG---NKEGASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSe 313
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 314 lLEvNKQWDQHFRSMKQQYEQKITELR------QKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET--DKEQL 385
Cdd:COG4717 316 -LE-EEELEELLAALGLPPDLSPEELLelldriEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 386 TAEAKELRQKVKYLQDQLSPLTRQREYQ---------EKEIQRLNKALEEalsiqtppsspptafgspegagalLRKQEL 456
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELlealdeeelEEELEELEEELEE------------------------LEEELE 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947853 457 VTQNEL--LKQQVKIFEED--FQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 515
Cdd:COG4717 450 ELREELaeLEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
328-535 |
2.62e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 328 MKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLT 407
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 408 RQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNElLKQQVKIFEEDFQRERSDRERMNEE 487
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE-EEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947853 488 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKASGER 535
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
302-498 |
3.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 302 KKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQK------ITELRQKLADLQKQ----VTDLEAERE------------- 358
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRqqteVLSPEEEKElvekikelekele 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 359 --QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqtppss 436
Cdd:COG1340 151 kaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA--------- 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622947853 437 pptafgspEGAGALLRKQELVTQNELLKQQVKIFEedfQRERSDRERMNEEKEELKKQVEKL 498
Cdd:COG1340 222 --------QEKADELHEEIIELQKELRELRKELKK---LRKKQRALKREKEKEELEEKAEEI 272
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
335-524 |
3.10e-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: 39.12 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 335 KITELRQKLADLQKQVTDLEAErEQKQRDFDRKLLLAKSKIEMEETDKEQL----TAEAKELRQKVKYLQDQLSPLTRQR 410
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKE-NRLLKRLQKRQEKALGKYEGTESELPQLiarhNEEVRVLRERLRRLQEKERDLERKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 411 EYQEKEIQRLNKALE--EALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQR-----ERSDRER 483
Cdd:pfam15619 91 KEKEAELLRLRDQLKrlEKLSEDK----------------NLAEREELQKKLEQLEAKLEDKDEKIQDlerklELENKSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622947853 484 MNEEKEELKKQVEklqAQVTLSNAQLKAFKDEEKAREANRQ 524
Cdd:pfam15619 155 RRQLAAEKKKHKE---AQEEVKILQEEIERLQQKLKEKERE 192
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-502 |
3.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 187 RMALEFNRLASKVHKNEQRTSilqtlCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKllmSNGNKEGASGQPG 266
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKK---AEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 267 SPKMEGAGKKAVAGQQqasVTAGKVPEVAALGAAEKKVKM-----LEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQ 341
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAeeakkAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 342 KLADLQK--QVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 419
Cdd:PTZ00121 1648 KAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 420 LNKALEEAlsiqtppsspptafgsPEGAGALLRKQELVTQNELLKQQVK--IFEEDFQRERSDRERMNEEKEELKKQVEK 497
Cdd:PTZ00121 1728 NKIKAEEA----------------KKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
....*
gi 1622947853 498 LQAQV 502
Cdd:PTZ00121 1792 RRMEV 1796
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
365-511 |
3.90e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 365 DRKLLLAKSKIEMEETDKE------QLTAEAKELRQKVKYLQDQlspltrQREYQEKEIQRLNKAlEEALSIQtppsspp 438
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEarqalaQVIANQKRLERQLEELEAE------AEKWEEKARLALEKG-REDLARE------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947853 439 tafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA 511
Cdd:COG1842 89 ----------ALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
311-514 |
3.96e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 311 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKQVTDLEAEREQkQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 390
Cdd:COG3096 490 RSQAWQTARELLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 391 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIF 470
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD----------------ALERLREQSGEALADSQEVTAA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947853 471 -EEDFQRERS---DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 514
Cdd:COG3096 632 mQQLLEREREatvERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
307-428 |
4.87e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 39.96 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 307 LEQQRSELLEVNKQWD----QHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLL-------AKSKI 375
Cdd:pfam14643 243 VEEWWASLEALNEQLDqyhdQCMTKLRAEYEEVWQECLARVQKLKQELLDYKVCSEEEAEALVNEEFLplvgklqRDAED 322
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622947853 376 EMEETDK--EQLtaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL 428
Cdd:pfam14643 323 ELEKLDKflEEL---AKQTEAQSEDLFKFFREAAQLWDVHQTELAKQELELEKKL 374
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
331-511 |
4.94e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 39.33 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 331 QYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKskiemeetDKEQLTAEAKELRQKVKYLQDQLSPLTRQR 410
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ--------DYDGATAQLRAAQAAVKAAQAQLAQAQIDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 411 EYQEkeiQRLNKALEEALSIQTppsspptafgspegAGALLRKQE-----LVTQNELLKQQVKIFEEDFQRE-RSDRERM 484
Cdd:pfam00529 127 ARRR---VLAPIGGISRESLVT--------------AGALVAQAQanllaTVAQLDQIYVQITQSAAENQAEvRSELSGA 189
|
170 180
....*....|....*....|....*..
gi 1622947853 485 NEEKEELKKQVEklQAQVTLSNAQLKA 511
Cdd:pfam00529 190 QLQIAEAEAELK--LAKLDLERTEIRA 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
214-535 |
5.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 214 EQLRKENEALKAKLDKGLEQRDQAAERLREENL----ELKKLLMSNG-----------NKEGASGQPGSPKMEGAGKKAV 278
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEArkaeDAKKAEAARKaeevrkaeelrKAEDARKAEAARKAEEERKAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 279 AGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQklADLQKQVTDLEAERE 358
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK--ADELKKAEEKKKADE 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 359 QKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALsiQTPPSSPP 438
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE--EKAEAAEK 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 439 TAFGSPEGAGALLRKQELVTQNELLKQQVkifEEDFQRERSDRERMNEEK--EELKKQVEKLQAQVTLSNAQLKAFKDEE 516
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKA---EEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
330 340
....*....|....*....|..
gi 1622947853 517 ---KAREANRQQKRKAKASGER 535
Cdd:PTZ00121 1449 akkKAEEAKKAEEAKKKAEEAK 1470
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-528 |
5.72e-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: 39.77 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 290 KVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQyeqkITELRQKLADLQKQVTDLEAEREQKQrdfDRKLL 369
Cdd:pfam01576 126 KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN----LAEEEEKAKSLSKLKNKHEAMISDLE---ERLKK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 370 LAKSKIEMEETdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspEGAga 449
Cdd:pfam01576 199 EEKGRQELEKA-KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE------------------ETA-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 450 llRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV--TL--SNAQL--------------KA 511
Cdd:pfam01576 258 --QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELedTLdtTAAQQelrskreqevtelkKA 335
|
250
....*....|....*..
gi 1622947853 512 FKDEEKAREANRQQKRK 528
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQ 352
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
207-494 |
6.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 207 SILQTLCEQL-RKEN--EALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEGAGKKAVAGQQQ 283
Cdd:pfam10174 436 TALTTLEEALsEKERiiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 284 ASvtagkvpevaalgaaekKVKMLE---QQRSEllEVNKQWDQHFRSMKQQYEQKIT-ELRQKLADLQKQVTDLEAEREQ 359
Cdd:pfam10174 516 DS-----------------KLKSLEiavEQKKE--ECSKLENQLKKAHNAEEAVRTNpEINDRIRLLEQEVARYKEESGK 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 360 KQRDFDRkLLLAKSKIEMEETDKEQLTAEAKELrqKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPT 439
Cdd:pfam10174 577 AQAEVER-LLGILREVENEKNDKDKKIAELESL--TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947853 440 AFGSPEGAGALLR-KQEL-VTQNELLKQQVKIFEED--FQRERSDRERMNEEKEELKKQ 494
Cdd:pfam10174 654 QLQLEELMGALEKtRQELdATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMKQE 712
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
315-531 |
6.28e-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: 39.77 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 315 LEVNKQwdqhfrSMKQQYEQKIT----ELRQKLADLQKQVTDLEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QLTA 387
Cdd:pfam01576 718 LEVNMQ------ALKAQFERDLQardeQGEEKRRQLVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQIDA 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 388 EAK---ELRQKVKYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQTPPSSPPTAFG---------SP 444
Cdd:pfam01576 789 ANKgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdelAD 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 445 EGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTlsnAQLKAFKDEEKAREANRQ 524
Cdd:pfam01576 869 EIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQLER 945
|
....*..
gi 1622947853 525 QKRKAKA 531
Cdd:pfam01576 946 QNKELKA 952
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
295-429 |
7.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 295 AALGAAEKKVKMLEQQ----RSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAERE----QKQRDFDR 366
Cdd:COG1579 24 HRLKELPAELAELEDElaalEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947853 367 KLLLAKSKIEMEETDK-EQLTAEAKELRQKVKYLQDQLSPLTRQRE----YQEKEIQRLNKALEEALS 429
Cdd:COG1579 103 RRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
307-404 |
7.57e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 36.78 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 307 LEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 383
Cdd:pfam13863 1 LLEKKREMFLVQLALDA----KREEIERLEELLKQREEELEKKEQELKEDLIKFDkflKENDAKRRRALKKAEEETKLKK 76
|
90 100
....*....|....*....|.
gi 1622947853 384 QLTAEAKELRQKVKYLQDQLS 404
Cdd:pfam13863 77 EKEKEIKKLTAQIEELKSEIS 97
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
301-524 |
7.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 301 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdrkllLAKSKIEMEET 380
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE----------LEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 381 DKE--QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAleealsiqtppsspptafgspegagallrKQELVT 458
Cdd:COG4372 79 EEEleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-----------------------------RQDLEQ 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947853 459 QNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQ 524
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
214-529 |
8.81e-03 |
|
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: 39.44 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 214 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGN-KEGASGQPGS---------PKMEGAGKKAVAGQQ- 282
Cdd:pfam12128 481 EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAGTllhflrkeaPDWEQSIGKVISPELl 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 283 -----QASVTAGKVPEVAALGAAEKKVKML--------EQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQ 349
Cdd:pfam12128 561 hrtdlDPEVWDGSVGGELNLYGVKLDLKRIdvpewaasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 350 VTD----LEAEREQKQRDFD--RKLLLAKSKIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN 421
Cdd:pfam12128 641 ETFartaLKNARLDLRRLFDekQSEKDKKNKALAERKDSanERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYW 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 422 KALEEALSIQTPPSSPPTAfGSPEGAGALLRKQELVTQNEL------------LKQQVKIFE---EDFQRERSD------ 480
Cdd:pfam12128 721 QVVEGALDAQLALLKAAIA-ARRSGAKAELKALETWYKRDLaslgvdpdviakLKREIRTLErkiERIAVRRQEvlryfd 799
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622947853 481 --RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 529
Cdd:pfam12128 800 wyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKA 850
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
275-427 |
8.83e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.92 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 275 KKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQK 348
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQldaraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947853 349 QVTDLEAEREQKQRDFDRKLLlakskiemeetDKEQLTAEakELRQKVkylqdqLSPLtrQREYQEKEIQRLNKALEEA 427
Cdd:PRK12705 113 ALSARELELEELEKQLDNELY-----------RVAGLTPE--QARKLL------LKLL--DAELEEEKAQRVKKIEEEA 170
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
289-415 |
9.15e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 38.87 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 289 GKVPE-VAALGAAEKKVKML-EQQRSelleVNKQwdqHFRSMkQQYEQKITELRQKLADLQKQVTDLEAEREQKqRDFDR 366
Cdd:smart00435 245 GNVAEkILAYNRANREVAILcNHQRT----VSKT---HEKSM-EKLQEKIKALKYQLKRLKKMILLFEMISDLK-RKLKS 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947853 367 KLLLAKSKIEME-ETDKEQLTAEAKELRQkVKYLQDQLSPLTRQREYQEK 415
Cdd:smart00435 316 KFERDNEKLDAEvKEKKKEKKKEEKKKKQ-IERLEERIEKLEVQATDKEE 364
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-391 |
9.42e-03 |
|
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: 39.32 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 198 KVHKNEQRTSILQTLCEQLRKEnealkakldkgLEQRDQAAERLREENLELKKLLMSNGNKEGASG-QPGSPKMEGAGKK 276
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQ-----------IENKNKNIEELHQENKALKKKGSAENKQLNAYEiKVNKLELELASAK 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 277 AVAGQQ----QASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSM-------KQQYEQKITELRQKLA- 344
Cdd:pfam05483 650 QKFEEIidnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMvalmekhKHQYDKIIEERDSELGl 729
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622947853 345 --DLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKE 391
Cdd:pfam05483 730 ykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-528 |
9.44e-03 |
|
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: 39.18 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 193 NRLASKVHKNEQRTSILQTLCEQLRKENE--ALKAKLDKGLEQRDQAAERLREEnLELKKLLMSNGNKEGASGQPGSPKM 270
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLA-AHIKAVTQIEQQAQRIHTELQSKMR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 271 EGAG---KKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRS--ELLEVNKQWDQHFRSMKQQYE---QKITELRQK 342
Cdd:TIGR00618 322 SRAKllmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTtltQKLQSLCKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 343 LADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLTA--------------EAKELRQKVKYLQDQLSPLT- 407
Cdd:TIGR00618 402 LDILQREQATIDT-RTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitctaqceklekiHLQESAQSLKEREQQLQTKEq 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 408 ---RQREYQEKEIQRLNKALEE---------------ALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKI 469
Cdd:TIGR00618 481 ihlQETRKKAVVLARLLELQEEpcplcgscihpnparQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947853 470 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA-FKDEEKAREANRQQKRK 528
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKlSEAEDMLACEQHALLRK 620
|
|
| |
