|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-526 |
9.16e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 3 ASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQE---ERTQ 79
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 80 RQDLELRLEETREALAGrayAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQ 159
Cdd:COG1196 311 RRELEERLEELEEELAE---LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 160 EMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDS 239
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 240 HGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKlcDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQ 319
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG--FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 320 VVLKSKNTKDgnlgkeLEAAQEQLAELKEKYIS--LRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRT 397
Cdd:COG1196 546 AALQNIVVED------DEVAAAAIEYLKAAKAGraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 398 LKLEEELHKQRDRALAVLTEKDLElEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAE 477
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLA-GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 193787412 478 QLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIE 526
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-535 |
1.89e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 14 QDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLELRLEETREa 93
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 94 lagrayAAEQMEGFELQTKQLTREVEELKSELQAIRDEknqpdprLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQ 173
Cdd:COG1196 314 ------LEERLEELEEELAELEEELEELEEELEELEEE-------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 174 QSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDlenktlALAASSRSPLDSHGEESSLDVNVLKD 253
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE------ALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 254 KMEKLKRLLQVAARKSQVTLDVEKLcdleimpssEAADGEKATALYYQQELKQLKEEFERYkmrAQVVLKSKNTKDGNLG 333
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAAL---------AELLEELAEAAARLLLLLEAEADYEGF---LEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 334 KELEAAQEQLAELKEKYISLRLScEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALA 413
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALA-AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 414 VLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQK 493
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 193787412 494 HRLEVEVHQLQDRLLEEGERHREEVAALQSHIEKNIRDQSRE 535
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
|
| GRIP |
pfam01465 |
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ... |
536-579 |
4.18e-13 |
|
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Pssm-ID: 460221 [Multi-domain] Cd Length: 44 Bit Score: 63.53 E-value: 4.18e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 193787412 536 GANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVI 579
Cdd:pfam01465 1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
|
|
| Grip |
smart00755 |
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245; |
536-581 |
2.11e-10 |
|
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
Pssm-ID: 197860 Cd Length: 46 Bit Score: 56.07 E-value: 2.11e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 193787412 536 GANLEYLKNIIYRFLTLPDSLgRQQTLTAILTILHFSPEEKQVIMR 581
Cdd:smart00755 1 EANFEYLKNVLLQFLTLRESE-RETLLPVISTVLQLSPEEMQKLLE 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-353 |
6.72e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 26 ERARLEGELKGLQEQIAETKARLIT--QQHDRAQEQ------------SDHASMLRELQKLLQEERTQRQDLELRLEETR 91
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAElrKELEELEEEleqlrkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 92 EALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQqemrktalAEDQL 171
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE--------RLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 172 RQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKErilQLDLENKTLALAASSRSPLDSHGEESSLDVNVL 251
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 252 KDKMEKLKRLLQVA-ARKSQVTLDVEKLcdleimpsseaadgekatalyyQQELKQLKEEF-ERYKMRAQVVLKSKNTKD 329
Cdd:TIGR02168 907 ESKRSELRRELEELrEKLAQLELRLEGL----------------------EVRIDNLQERLsEEYSLTLEEAEALENKIE 964
|
330 340
....*....|....*....|....
gi 193787412 330 GnlgkELEAAQEQLAELKEKYISL 353
Cdd:TIGR02168 965 D----DEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-520 |
2.88e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLEL 85
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 86 RLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSE---------------LQAIRDEknqpdprlQELQEEAARLK 150
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaeaeeeleelaeelLEALRAA--------AELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 151 SHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALA 230
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 231 ASSRSPLDshgeessldvnvLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEE 310
Cdd:COG1196 487 AEAAARLL------------LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 311 FERYKMRAQVVLKSKntKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQ 390
Cdd:COG1196 555 DDEVAAAAIEYLKAA--KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 391 LDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAAnep 470
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL--- 709
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 193787412 471 tfflyAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAA 520
Cdd:COG1196 710 -----AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
12-205 |
1.82e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 12 MKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLIT--QQH---DRAQEQSDHASMLRELQKLLQEERTQRQDLELR 86
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 87 LEETREALAGRAYAAEQMEGfELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTAL 166
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190
....*....|....*....|....*....|....*....
gi 193787412 167 AEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQK 205
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-417 |
3.46e-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: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 23 AEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERtqrqdLELRLEETREALAgrayaae 102
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYE-----GYELLKEKEALER------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 103 QMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRV 182
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 183 AALENQIsevsellgtyekakQKDQLAIQKLKERILQLDLENKTLALAassrspLDSHGEEssldVNVLKDKMEKLKRLL 262
Cdd:TIGR02169 318 EDAEERL--------------AKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEE----YAELKEELEDLRAEL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 263 QVAARKSQVTLDVEKlcdleimpsseaadgekatalYYQQELKQLKEEFE---RYKMRAQVVLKSKNTKDGNLGKELEAA 339
Cdd:TIGR02169 374 EEVDKEFAETRDELK---------------------DYREKLEKLKREINelkRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787412 340 QEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLhRQELERCQldfrDRTLKLEEELHKQRDRALAVLTE 417
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-KEEYDRVE----KELSKLQRELAEAEAQARASEER 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-209 |
4.14e-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: 55.54 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLEL 85
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 86 RL------------------EETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAA 147
Cdd:COG4942 109 LLralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787412 148 RLKSHFQ------AQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLA 209
Cdd:COG4942 189 ALEALKAerqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
7-419 |
4.56e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 7 ADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLELR 86
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 87 LEETREALAGRAYAAEQMEGFELQTK-QLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTA 165
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 166 LAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESS 245
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 246 LDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADgEKATALYYQQELKQLKEEFEryKMRAQVVLKSK 325
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK-IKAEELKKAEEEKKKVEQLK--KKEAEEKKKAE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 326 NTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELAR-LQQLHRQELERCQldfRDRTLKLEEEL 404
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKK---KAEELKKAEEE 1727
|
410
....*....|....*
gi 193787412 405 HKQRDRALAVLTEKD 419
Cdd:PTZ00121 1728 NKIKAEEAKKEAEED 1742
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-258 |
2.38e-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: 53.91 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 14 QDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQeertQRQDLELRLEETREA 93
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----KLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 94 LAGrayAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQaqlQQEMRKTALAEDQLRQ 173
Cdd:TIGR02168 346 LEE---LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE---RLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 174 QSQVEEQRVAALENQISEVSELLGTYEKAKQKdqlAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKD 253
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
....*
gi 193787412 254 KMEKL 258
Cdd:TIGR02168 497 LQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-217 |
2.55e-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: 53.91 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQhdraqeqsdhaSMLRELQKLLQEERTQRQDLEL 85
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----------EALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 86 RLEETREALagrAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEaarlkshfQAQLQQEMRKTA 165
Cdd:TIGR02168 825 RLESLERRI---AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE--------RASLEEALALLR 893
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 193787412 166 LAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERI 217
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-359 |
5.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 2 EASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQ 81
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 82 DLELRLEETREALAGRAyAAEQMEGFELQTKQLTREVEELKSELQAIRDE--KNQPDPRLQELQ-------EEAARLKSH 152
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKK-AEEKKKADELKKAEELKKAEEKKKAEEAKKAEedKNMALRKAEEAKkaeeariEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 153 FQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERilQLDLENKTLALAAS 232
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA--KKAEEDKKKAEEAK 1681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 233 SRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATAlyyqQELKQLKEEfe 312
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA----EEAKKDEEE-- 1755
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 193787412 313 ryKMRAQVVLKSKNTKDGNLGKELEAAQEQlaELKEKYISLRLSCEE 359
Cdd:PTZ00121 1756 --KKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDK 1798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-407 |
1.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 2 EASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQ--EERTQ 79
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKK 1458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 80 RQDLELRLEETREALAGRAYAAEQMEGFELQTK--QLTREVEELKSELQAirdEKNQPDPRLQELQEEAARLKSHFQAQL 157
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 158 QQEMRKTALAE--DQLRQQSQVEE-QRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSR 234
Cdd:PTZ00121 1536 ADEAKKAEEKKkaDELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 235 SPLDSHGEESSLDVNVlKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERY 314
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 315 KMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQ-QEADDWKQELARLQQLHRQELERCQLDF 393
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
410
....*....|....
gi 193787412 394 RDRTLKLEEELHKQ 407
Cdd:PTZ00121 1775 KEKEAVIEEELDEE 1788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-151 |
1.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 16 LEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLELRLEETREALA 95
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 193787412 96 GRAYAAEqmEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKS 151
Cdd:COG4913 373 LPLPASA--EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-434 |
3.02e-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: 50.44 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 52 QHDRAQEQSDHASMLRELQKllQEERTQRQDLELRLEETRealagrayaaEQMEGFELQTKQLTREVEELKSELQAIRDE 131
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKA--ELRELELALLVLRLEELR----------EELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 132 KNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTalaedqlrQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQ 211
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 212 KLKERILQL--DLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMpssea 289
Cdd:TIGR02168 341 ELEEKLEELkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR----- 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 290 adgekatalyyQQELKQLKEEFERYKMRAQvvLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEAD 369
Cdd:TIGR02168 416 -----------RERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193787412 370 DWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGL 434
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-260 |
8.41e-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: 48.91 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 15 DLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQ-EQSDHASMLRELQKLLQEERTQRQDLELRLEETREA 93
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 94 LAGRAYAAE-----------QMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQaQLQQEMR 162
Cdd:TIGR02169 821 LNRLTLEKEylekeiqelqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD-ELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 163 KTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQ------LAIQKLKERILQLDLENKTLAlAASSRSP 236
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeeLSLEDVQAELQRVEEEIRALE-PVNMLAI 978
|
250 260
....*....|....*....|....
gi 193787412 237 LDShgEESSLDVNVLKDKMEKLKR 260
Cdd:TIGR02169 979 QEY--EEVLKRLDELKEKRAKLEE 1000
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
19-205 |
8.79e-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: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 19 ASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASM-----------------LRELQKLLQEERTQRQ 81
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriaalarriraleqeLAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 82 DLELRLEETREALAGRAYAAEQMEG----------------------FELQTKQLTREVEELKSELQAIRDEKNQPDPRL 139
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193787412 140 QELQEEAARLKSHfQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQK 205
Cdd:COG4942 174 AELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
303-427 |
1.29e-05 |
|
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: 47.45 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 303 ELKQLKEEFERYKMRAQVVLKSK-----NTKDGN-----------------LGKELEAAQEQLAELKEKYISLRLSCEEL 360
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKekliaSLKEGSgvegldsstaltleleeLRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787412 361 EHQHQQEADDWKQELARLQ----------QLHRQELERCQLDFRdrtlKLEEELHKQRDRALAVLTEKDLELEQLRS 427
Cdd:pfam09787 81 EAQQQEEAESSREQLQELEeqlatersarREAEAELERLQEELR----YLEEELRRSKATLQSRIKDREAEIEKLRN 153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-189 |
1.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASNKAEEERARLEGELKGLQEQiaetkARLITQQHDRAQEQSDHASMLRELQKLlqeeRTQRQDLEL 85
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQRLAEYSWDEIDVASAEREIAEL----EAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 86 RLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEA-ARLKSHFQAQLQQEMRKT 164
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*..
gi 193787412 165 ALAE--DQLRQQSQVEEQRVAALENQI 189
Cdd:COG4913 763 VERElrENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-253 |
1.99e-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: 47.76 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 10 KKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLELRLEE 89
Cdd:TIGR02169 279 KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 90 TREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKShfqAQLQQEMRKTALAED 169
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE---ELADLNAAIAGIEAK 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 170 QLRQQSQVEEQR--VAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLEnktLALAASSRSPLDSHGEESSLD 247
Cdd:TIGR02169 436 INELEEEKEDKAleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE---LAEAEAQARASEERVRGGRAV 512
|
....*.
gi 193787412 248 VNVLKD 253
Cdd:TIGR02169 513 EEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-194 |
9.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 22 KAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQsdhasmLRELQKLLQEERTQRQDLELRLEETREALAGRAYAA 101
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE------LARLEAELERLEARLDALREELDELEAQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 102 EQmegfelqtkQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHF---QAQLQQEMRKTALAEDQLRQQSQVE 178
Cdd:COG4913 340 LE---------QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFaalRAEAAALLEALEEELEALEEALAEA 410
|
170
....*....|....*.
gi 193787412 179 EQRVAALENQISEVSE 194
Cdd:COG4913 411 EAALRDLRRELRELEA 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
6-157 |
1.11e-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: 44.15 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLitqqhDRAQEQSDHASMLRELQKLLQEERTQRQDLEL 85
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-----KKYEEQLGNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193787412 86 RLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQpdpRLQELQEEAARLKSHFQAQL 157
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA---ELEELEAEREELAAKIPPEL 176
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
117-360 |
1.36e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 117 EVEELKSELQAIRDEKnqPDPRLQELQEEAARLKSHFqaqlqqEMRKTALAEdqlrqqsqVEEQRVAALENQISEVSELL 196
Cdd:PRK05771 32 HIEDLKEELSNERLRK--LRSLLTKLSEALDKLRSYL------PKLNPLREE--------KKKVSVKSLEELIKDVEEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 197 GTYEKAkqkdqlaIQKLKERILQLDLENKTLALAASSRSPLdshgeeSSLDVnvlkdKMEKLKRLLQVAARKSQVTLDVE 276
Cdd:PRK05771 96 EKIEKE-------IKELEEEISELENEIKELEQEIERLEPW------GNFDL-----DLSLLLGFKYVSVFVGTVPEDKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 277 KLCDLEIMPS---SEAADGEKATAL------YYQQELKQLKE-EFERYKM----RAQVVLKSKNTKDGNLGKELEAAQEQ 342
Cdd:PRK05771 158 EELKLESDVEnveYISTDKGYVYVVvvvlkeLSDEVEEELKKlGFERLELeeegTPSELIREIKEELEEIEKERESLLEE 237
|
250
....*....|....*...
gi 193787412 343 LAELKEKYISLRLSCEEL 360
Cdd:PRK05771 238 LKELAKKYLEELLALYEY 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3-510 |
2.01e-04 |
|
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: 44.34 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 3 ASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQD 82
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 83 LELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDE-KNQPDPRLQELQEEAARLK--SHFQAQLQ- 158
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEkvSSLTAQLEs 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 159 -QEMRKTALAEDQLRQQSQVEEQRVaalenqISEVSELLGTYEKAKQKDQLAIQKLKERIlqlDLENKTLALAASSrspl 237
Cdd:pfam15921 473 tKEMLRKVVEELTAKKMTLESSERT------VSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQELQHLKNE---- 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 238 DSHGEESSLDVNVLKDKMEKLKRLLQVAARKsqvtldveklcdLEIMPSSEAADGEKATALyyQQELKQLKEEFERYKMR 317
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVIEILRQQ------------IENMTQLVGQHGRTAGAM--QVEKAQLEKEINDRRLE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 318 AQVVLKSKNTKDGNLgKELEAAQEQLAELKEKYI---SLRL-SCEELEHQHQQEADDWKQELARLQQLhRQELERCQLDF 393
Cdd:pfam15921 606 LQEFKILKDKKDAKI-RELEARVSDLELEKVKLVnagSERLrAVKDIKQERDQLLNEVKTSRNELNSL-SEDYEVLKRNF 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 394 RDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSpvGGGGPGDPADTSSSDSLTQALQ-----LAAAN 468
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA--MGMQKQITAKRGQIDALQSKIQfleeaMTNAN 761
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 193787412 469 EPTFFLYAEQLA-RKEVEITSLRKQKHRLEVEVHQLQDRLLEE 510
Cdd:pfam15921 762 KEKHFLKEEKNKlSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-263 |
2.66e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 8 DKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLElRL 87
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA-NL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 88 EETREALAGRAYAAEQMEgfeLQTKQLTREVEELKSELQAIRDEKNQpdpRLQELQEEAARLKSHFQAqLQQEMRKTALA 167
Cdd:TIGR02168 315 ERQLEELEAQLEELESKL---DELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEE-LEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 168 EDQLRQQSQVEEQRVAALENQISEVSELLG--TYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESS 245
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250
....*....|....*...
gi 193787412 246 LDVNVLKDKMEKLKRLLQ 263
Cdd:TIGR02168 468 EELEEAEQALDAAERELA 485
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10-427 |
2.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 10 KKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLiTQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLElRLEE 89
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 90 TREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQpdprLQELQEEAARLKSHFQAQLQQEMRKTALAED 169
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 170 QLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAiQKLKERILQLDLENKTLALAASSRSPLDSH--------- 240
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 241 --GEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDL--EIMPSSEAADGEKATALYYQQELKQLKEEFERYK- 315
Cdd:COG4717 282 vlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELlaALGLPPDLSPEELLELLDRIEELQELLREAEELEe 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 316 -MRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQ-QLHRQELERCQldf 393
Cdd:COG4717 362 eLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELE--- 438
|
410 420 430
....*....|....*....|....*....|....
gi 193787412 394 rdrtlKLEEELHKQRDRALAVLTEKDLELEQLRS 427
Cdd:COG4717 439 -----EELEELEEELEELREELAELEAELEQLEE 467
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
88-216 |
3.89e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 88 EETREALAGRAYAAEQMEGFELQTKQ-LTREVEELKSELQAIRDEKNqpdpRLQELQEEAARLKSHFQAQLQQEMRKTAl 166
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQdLQDSVANLRASLSAAEAERS----RLQALLAELAGAGAAAEGRAGELAQELD- 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 193787412 167 AEDQL--RQQSQVE--EQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKER 216
Cdd:PRK09039 127 SEKQVsaRALAQVEllNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-225 |
4.32e-04 |
|
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: 43.52 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 14 QDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDhasmLRELQKLLQEERTQRQDLELRLEETREA 93
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ----RIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 94 LAGRAYAAEQMEGfelQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQ------------EM 161
Cdd:TIGR02169 870 LEELEAALRDLES---RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElseiedpkgedeEI 946
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193787412 162 RKTALAEDQLRQQSQVEEQRVAALE-------NQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENK 225
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-134 |
4.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASN----------KAEEERARLEGELKGLQEQIAETKARL--ITQQHDRAQEQSDHAsmlrelqkll 73
Cdd:COG4913 670 IAELEAELERLDASSDdlaaleeqleELEAELEELEEELDELKGEIGRLEKELeqAEEELDELQDRLEAA---------- 739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193787412 74 qeERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQ 134
Cdd:COG4913 740 --EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-510 |
5.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 331 NLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQ----EADDWKQELARLQQlHRQELERCQLDFRDRTLKLEEElhk 406
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLER-ELEERERRRARLEALLAALGLP--- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 407 qrdralAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPAdtsssdsltqalQLAAANEptfflyaeQLARKEVEI 486
Cdd:COG4913 375 ------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA------------ALRDLRR--------ELRELEAEI 428
|
170 180
....*....|....*....|....
gi 193787412 487 TSLRKQKHRLEVEVHQLQDRLLEE 510
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
13-209 |
6.54e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 13 KQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLELRLEETRE 92
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 93 ALAGRAY------------AAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHfQAQLQQE 160
Cdd:COG3883 98 SGGSVSYldvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA-KAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 193787412 161 MRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLA 209
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
68-420 |
7.17e-04 |
|
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: 42.65 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 68 ELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEaa 147
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 148 rlkshFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERI--LQLDLENK 225
Cdd:pfam02463 252 -----EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLkeSEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 226 TLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYY--QQE 303
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 304 LKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHR 383
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350
....*....|....*....|....*....|....*..
gi 193787412 384 QELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDL 420
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
7-540 |
8.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 7 ADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSdHASMLRELQKLLQEERTQRQDLELR 86
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 87 LEETREALAGRAYAAEQMEGFELQTK--QLTREVEELKSELQAIR-----DEKNQPDPRLQELQEEAARLKSHFQAQLQ- 158
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKkadeaKKKAEEKKKADEAKKKAEEAKKADEAKKKa 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 159 QEMRKTALAEDQLRQQSQVEEQRVAALENQISEvsELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLD 238
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 239 SHGEESSLDVNVLKDKMEKLKRLLQVaaRKSQVTLDVEKlcdleimpsSEAADGEKATALYYQQELKQLKEEFERYKMRA 318
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEEL--KKAEEKKKAEE---------AKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 319 QVVLKSKNTKDGNLGKELEAAQEQL---AELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQldfRD 395
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KA 1677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 396 RTLKLEEELHKQRDRALAVLTEKDLELEQLRSvalasglpGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTffly 475
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKK--------KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK---- 1745
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787412 476 AEQLARKEVE---ITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQshIEKNIRDQSREGANLE 540
Cdd:PTZ00121 1746 AEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANII 1811
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-195 |
8.49e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 2 EASYLADKKKMKQDL-EDASNKAEEERARLEGELKGLQEQIAETKarlitQQHDRAQEQSDHASMLRELQKLLQEERTQR 80
Cdd:PRK02224 510 RIERLEERREDLEELiAERRETIEEKRERAEELRERAAELEAEAE-----EKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 81 QDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQ-----PDPRLQELQEEAARLKShFQA 155
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKREleaefDEARIEEAREDKERAEE-YLE 663
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 193787412 156 QLQQEMRKTALAEDQLrqqsqveEQRVAALENQISEVSEL 195
Cdd:PRK02224 664 QVEEKLDELREERDDL-------QAEIGAVENELEELEEL 696
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
112-196 |
8.75e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 112 KQLTREVEELKSELQAIRDEKNQPD-PRLQELQEEAARLKSHFQAQLQQ-EMRKTALAEDQ-LRQQSQVEEQRVAALENQ 188
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASfERLAELRDELAELEEELEALKARwEAEKELIEEIQeLKEELEQRYGKIPELEKE 493
|
....*...
gi 193787412 189 ISEVSELL 196
Cdd:COG0542 494 LAELEEEL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-274 |
9.07e-04 |
|
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: 42.36 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 28 ARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLElRLEETREALAgrayaaEQMEGF 107
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLK------ERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 108 ELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEE----AARLKSHFQAQLQQEMRK-------------------- 163
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRIPEIQAELSKleeevsriearlreieqkln 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 164 -TALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLalaASSRSPLDSHGE 242
Cdd:TIGR02169 823 rLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL---KKERDELEAQLR 899
|
250 260 270
....*....|....*....|....*....|..
gi 193787412 243 ESSLDVNVLKDKMEKLKRLLQVAARKSQVTLD 274
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-186 |
1.63e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 6 LADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLEL 85
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 86 RLEETREALAGRAYAAEQMEGFELQTKQLTREVEELK-------SELQAIRDEKNQPDPRLQELQEEAARLKSHFQAqLQ 158
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlskyeQELYDLKEEYDRVEKELSKLQRELAEAEAQARA-SE 503
|
170 180 190
....*....|....*....|....*....|....*....
gi 193787412 159 QEMRKTALAED-----------QLRQQSQVEEQRVAALE 186
Cdd:TIGR02169 504 ERVRGGRAVEEvlkasiqgvhgTVAQLGSVGERYATAIE 542
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
3-230 |
1.96e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 3 ASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLI-TQQHDRAQEqsDHASMLRELQKLLQEERTQRQ 81
Cdd:PRK10929 19 AATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLErAKQYQQVID--NFPKLSAELRQQLNNERDEPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 82 DLELRLeeTREALagrayaAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQpdprLQELQEEAARLKSHFQAQLQ-QE 160
Cdd:PRK10929 97 SVPPNM--STDAL------EQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQ----LPQQQTEARRQLNEIERRLQtLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 161 MRKTALAEDQL--------RQQSQVEEQRVAALE-NQISEVSEL-LGTYEKAKQKDQLAIQKLKERILQLDLENKTLALA 230
Cdd:PRK10929 165 TPNTPLAQAQLtalqaesaALKALVDELELAQLSaNNRQELARLrSELAKKRSQQLDAYLQALRNQLNSQRQREAERALE 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
155-368 |
2.02e-03 |
|
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: 40.90 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 155 AQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERI--LQLDLENKTLALAAS 232
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaeLRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 233 SRSpLDSHGEESSLDVNVLKDKMEKLKRLLQ-----VAARKSQVTLDVEKLCDLEimpsseaadGEKATALYYQQELKQL 307
Cdd:COG4942 110 LRA-LYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELA---------ALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193787412 308 KEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEA 368
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
3-349 |
2.77e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 3 ASYLADKKKMKQDLEDASNKAEEERArLEGELKGLQEQIAETKARLITQQHDRAQEqsdhasmLRELQKLLQEERTQRQD 82
Cdd:PLN02939 100 ASMQRDEAIAAIDNEQQTNSKDGEQL-SDFQLEDLVGMIQNAEKNILLLNQARLQA-------LEDLEKILTEKEALQGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 83 ---LELRLEETREALagrAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAqLQQ 159
Cdd:PLN02939 172 iniLEMRLSETDARI---KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQF-LKA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 160 EMRKTALAEDQLrqqSQVEEQRvAALENQISEV-SELLGTYEKAKQKDQLAIQKLKERILQL-DLENKTLALAASSRSPL 237
Cdd:PLN02939 248 ELIEVAETEERV---FKLEKER-SLLDASLRELeSKFIVAQEDVSKLSPLQYDCWWEKVENLqDLLDRATNQVEKAALVL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 238 DSHGEessldvnvLKDKMEKLKRLLQVAarksqvtlDVEKLCD--LEIMpsseaadgekatalyyQQELKQLKEEFER-- 313
Cdd:PLN02939 324 DQNQD--------LRDKVDKLEASLKEA--------NVSKFSSykVELL----------------QQKLKLLEERLQAsd 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 193787412 314 YKMRAQVVLKSKNTKDgnlgkeleaAQEQLAELKEK 349
Cdd:PLN02939 372 HEIHSYIQLYQESIKE---------FQDTLSKLKEE 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
22-517 |
3.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 22 KAEEERARLEGELKGLQEQIAETKARLITQQHDRAQ--EQSDHASMLRELQKLLQEERTQRQDLELRLEETREALAGRAY 99
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKkaEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 100 AAEQmegfelQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTAlaeDQLRQQSQVEE 179
Cdd:PTZ00121 1221 EDAK------KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKK 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 180 QRVAALENQISEVSELLGTYEKAKQKDQL------------AIQKLKERILQLDLENKTLALAASSRSPL--------DS 239
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeakkkadAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeekaeaaEK 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 240 HGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEE---FERYKM 316
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkADEAKK 1451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 317 RAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEhQHQQEADDWKQELARLQQLHRQELERCQLDFRD- 395
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK-KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKa 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 396 RTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASglPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLY 475
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE--EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 193787412 476 AEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREE 517
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
11-212 |
4.08e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 11 KMKQDLEDASNKAEEERARLEGEL--KGLQEQIAET------KARLITQQHDRAQEQSDHASMLRELQkllQEERTQRQD 82
Cdd:PRK10929 79 KLSAELRQQLNNERDEPRSVPPNMstDALEQEILQVssqlleKSRQAQQEQDRAREISDSLSQLPQQQ---TEARRQLNE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 83 LELRLeetrEALAGRAYAAEQMEGFELQTKQLTRE--VEEL---------KSELQAIRDEKNQpdPRLQELQEEAARLKS 151
Cdd:PRK10929 156 IERRL----QTLGTPNTPLAQAQLTALQAESAALKalVDELelaqlsannRQELARLRSELAK--KRSQQLDAYLQALRN 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787412 152 HFQAQLQQEmrktalAEDQLRQQSQVEEQrVAALENQIS-------EVSELLGtyEKAKQKDQLAIQK 212
Cdd:PRK10929 230 QLNSQRQRE------AERALESTELLAEQ-SGDLPKSIVaqfkinrELSQALN--QQAQRMDLIASQQ 288
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
9-144 |
4.20e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 9 KKKMKQDLEDASNkAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHasmlRELQKLLQEERTQRQDLELRLE 88
Cdd:PRK04863 543 CKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI----QRLAARAPAWLAAQDALARLRE 617
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193787412 89 ETREALAGRAYAAEQMEGFELQTKQLTREVEEL---KSELQAIRDEKNQP----DPRLQELQE 144
Cdd:PRK04863 618 QSGEEFEDSQDVTEYMQQLLERERELTVERDELaarKQALDEEIERLSQPggseDPRLNALAE 680
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-426 |
4.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 10 KKMKQDLEDASNKAEEERARLEGELKGLQEQIaetkarlitqqhdraQEQSDHASMLRELQKLLQEERTQRQDLELRLEE 89
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERI---------------KELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 90 TREALAgrayAAEQMEgfELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHF-QAQLQQEMRKTALAE 168
Cdd:PRK03918 364 YEEAKA----KKEELE--RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIkELKKAIEELKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 169 DQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDV 248
Cdd:PRK03918 438 CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 249 NVLKDKMEKLKRLLqvaarksqvtldvEKLCDLEIMPSSEAADGEKAtalyyqQELKQLKEEFERYKMRAQVVLKSKNTK 328
Cdd:PRK03918 518 EELEKKAEEYEKLK-------------EKLIKLKGEIKSLKKELEKL------EELKKKLAELEKKLDELEEELAELLKE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 329 DGNLG----KELEAAQEQLAELKEKYISLRLSCEELEHQH------QQEADDWKQELARLQ---QLHRQELERCQLDFRD 395
Cdd:PRK03918 579 LEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEkelkklEEELDKAFEELAETEkrlEELRKELEELEKKYSE 658
|
410 420 430
....*....|....*....|....*....|.
gi 193787412 396 RTLKLEEELHKQRDRALAVLTEKDLELEQLR 426
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
79-356 |
5.93e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 79 QRQDLELRLEETREALagrayaaeqmEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARlkshfqAQLQ 158
Cdd:COG3206 162 LEQNLELRREEARKAL----------EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL------SELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 159 QEMRktalaedQLRQQSQVEEQRVAALENQISEVSELLgtyekAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPld 238
Cdd:COG3206 226 SQLA-------EARAELAEAEARLAALRAQLGSGPDAL-----PELLQSPVIQQLRAQLAELEAELAELSARYTPNHP-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 239 shgeesslDVNVLKDKMEKLKRLLQVAARKSQVTLDVEklcdleimpsseaADGEKATALYYQQELKQLKEEFERYKMRA 318
Cdd:COG3206 292 --------DVIALRAQIAALRAQLQQEAQRILASLEAE-------------LEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260 270
....*....|....*....|....*....|....*...
gi 193787412 319 QVVLkskntkdgNLGKELEAAQEQLAELKEKYISLRLS 356
Cdd:COG3206 351 AELR--------RLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-427 |
6.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 10 KKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKarlitqqhdraqEQSDHASMLRELQKLLQEERTQRQDLELRLEE 89
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK------------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 90 TREALAGrayaaeqmegfelqtkqltreVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQaqlqqemrktaLAED 169
Cdd:PRK03918 319 LEEEING---------------------IEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-----------LYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 170 QLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASS-----------RSPLD 238
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcGRELT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 239 SHG-----EESSLDVNVLKDKMEKLKRLLQvAARKSQVTLDVEKLCDLEIMPSSEAADG----EKATALYYQQELKQLKE 309
Cdd:PRK03918 447 EEHrkellEEYTAELKRIEKELKEIEEKER-KLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNLEELEKKAE 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 310 EFERYKMRA------QVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRlscEELEHQHQQEADDWKQELARLQQLHR 383
Cdd:PRK03918 526 EYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL---KELEELGFESVEELEERLKELEPFYN 602
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 193787412 384 QELErcQLDFRDRTLKLEEELHKQR---DRALAVLTEKDLELEQLRS 427
Cdd:PRK03918 603 EYLE--LKDAEKELEREEKELKKLEeelDKAFEELAETEKRLEELRK 647
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
12-152 |
7.19e-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: 38.97 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 12 MKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLELRLEETR 91
Cdd:pfam09787 73 LRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLR 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193787412 92 EALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSH 152
Cdd:pfam09787 153 NQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
54-227 |
7.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 54 DRAQEQSDHASMLRELQKLLQEERTQRQDLE------LRLEETREALAGRAYAAEQMEGFELQTKQ--LTREVEELKSEL 125
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLelLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 126 QAIRDEKNQPDPRLQELQEEAARLKSHFQ-------AQLQQEMRKTALAEDQLRQQSQVEEQRVAALE-----------N 187
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRgnggdrlEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaA 384
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 193787412 188 QISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTL 227
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
33-425 |
7.51e-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: 39.55 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 33 ELKGLQEQIAETKARLITQQHDRAQEQSDHASMLRELQKLLQEERTQRQDLEL---RLEETREALAgrayAAEQMEGFEL 109
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAasdHLNLVQTALR----QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 110 QTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFqAQLQQemrktALAEDQLRQ-QSQveeQRVAALEN- 187
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-ADYQQ-----ALDVQQTRAiQYQ---QAVQALEKa 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 188 -QISEVSELL-----GTYEKAKQKDQLAIQKLkerilqLDLENKtLALAASSRSPLD---------SHGEESSLDVNVLK 252
Cdd:COG3096 426 rALCGLPDLTpenaeDYLAAFRAKEQQATEEV------LELEQK-LSVADAARRQFEkayelvckiAGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 253 DKMEKLKRLLQVAARKSQVTLdveKLCDLEIMPSSEAADGEKATALYYQQELK-QLKEEFERYKMRAQVvlkskntkdgn 331
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRA---QLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEA----------- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 332 lgkELEAAQEQLAELKEKYISLRLSCEELEHQHQQ---EADDWKQELARLQQLHRQ---ELERCQ--LDFRDRTLKLEEE 403
Cdd:COG3096 565 ---QLEELEEQAAEAVEQRSELRQQLEQLRARIKElaaRAPAWLAAQDALERLREQsgeALADSQevTAAMQQLLERERE 641
|
410 420
....*....|....*....|..
gi 193787412 404 LHKQRDRALAVLTEKDLELEQL 425
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
8-234 |
8.27e-03 |
|
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: 39.34 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 8 DKKKMKQDLEDASNKAEEERARLEGElKGLQEQIaETKARLITQQHDRAQEQSdhasmlRELQKLLQEERtQRQDLELRL 87
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAE-KARQAEM-DRQAAIYAEQERMAMERE------RELERIRQEER-KRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787412 88 EETrealagrAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQE---EAARLKSHFQAQLQQEMRK- 163
Cdd:pfam17380 368 EEI-------AMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEARQREVRRl 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193787412 164 ---TALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAiQKLKERILQLDLENKTLALAASSR 234
Cdd:pfam17380 441 eeeRAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA-EEQRRKILEKELEERKQAMIEEER 513
|
|
| |
