|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
48-353 |
9.51e-172 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 493.77 E-value: 9.51e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 48 EEQLPHYKLRADTIY-GYDHDDW-LHTPL-ISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKER 124
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 125 DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSV 204
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 205 QNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEI 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622905972 285 THLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
414-583 |
1.40e-78 |
|
Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.
Pssm-ID: 463588 Cd Length: 171 Bit Score: 248.74 E-value: 1.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 414 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDIGNVVLDNKTNSIILETEAADLGNDERSKKLGTPGTPGSH 493
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 494 DLETALRRLSLRRENYLSERRFFEEEQERKLQELAE----KGELRSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 569
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157
|
170
....*....|....
gi 1622905972 570 LPEKLQIVKPLEGS 583
Cdd:pfam12448 158 LPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-353 |
8.03e-14 |
|
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: 75.48 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 112 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 191
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 192 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 268
Cdd:TIGR02168 777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 269 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 341
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 1622905972 342 EAQEELKNLRNK 353
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-353 |
1.47e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 99 AERVGQMTKTYNDIDAVTRLL--EEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQ 176
Cdd:COG1196 212 AERYRELKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 177 FYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcVKEL 256
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----EEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 257 RDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 336
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|....*..
gi 1622905972 337 MEMLHEAQEELKNLRNK 353
Cdd:COG1196 448 AEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-351 |
1.78e-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: 67.77 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 79 ANIDLTTEQIEETLKyfllcaervgQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIR 158
Cdd:TIGR02168 684 EKIEELEEKIAELEK----------ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 159 EEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTET 238
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 239 ityEEKEQQLVnDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDA 318
Cdd:TIGR02168 834 ---AATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270
....*....|....*....|....*....|...
gi 1622905972 319 QRQLTAELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-353 |
1.11e-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: 58.54 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 100 ERVGQMTKTYNDID-AVTRLLEEKERDLELAARIGQslLKKnktltERNELLEEQvEHIREEVSQLRHELS--------- 169
Cdd:TIGR02169 650 EKSGAMTGGSRAPRgGILFSRSEPAELQRLRERLEG--LKR-----ELSSLQSEL-RRIENRLDELSQELSdasrkigei 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 170 MKD-ELLQFYTSAA----EESEPE-SVCSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEE 243
Cdd:TIGR02169 722 EKEiEQLEQEEEKLkerlEELEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 244 KE-QQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 322
Cdd:TIGR02169 794 PEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
250 260 270
....*....|....*....|....*....|.
gi 1622905972 323 TAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-353 |
4.00e-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: 56.99 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 104 QMTKTYNDIDAVTRLLEEKERDLELaarigqslLKKNKTLTERNELLEEQVEHIREEVSQLRHElSMKDELLQFYTSAAE 183
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLRLE-ELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 184 ESEpesvcstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQI 263
Cdd:TIGR02168 251 AEE----------------------ELEELTAELQELEEKLEELRLEVSELEEE----IEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 264 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 343
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250
....*....|
gi 1622905972 344 QEELKNLRNK 353
Cdd:TIGR02168 385 RSKVAQLELQ 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
99-392 |
2.30e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 99 AERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKD 172
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 173 E----LLQFYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL 248
Cdd:PRK03918 293 EeyikLSEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 249 VN--------------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHlgA 314
Cdd:PRK03918 372 EElerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--H 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 315 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTsrryhslgLFPMDSLAAEIEGTMRK--ELQLEEAE 392
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKELEEKlkKYNLEELE 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
119-299 |
7.23e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 119 LEEKERDLELAarigQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstplKRN 198
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---------LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 199 ESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEK----EQQLVNDCVKELRDANVQIASISEELAKKT 274
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 1622905972 275 EDAARQQEEITHLLSQIVDLQKKAK 299
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
208-393 |
1.18e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 208 FHLDSLQKKLKDLEEENVVLRSEASQLKTEtITYEEKEQQLVNDCVKE----LRDANVQIASISEELAKKTEDAARQQEE 283
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEE-LEQARSELEQLEEELEElneqLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 284 ITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME-----MLHEAQEELKNLRNKTMPNT 358
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNA 196
|
170 180 190
....*....|....*....|....*....|....*
gi 1622905972 359 TSRRYHSLGLFPMDSLAAEIEGTMRKELQLEEAES 393
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-416 |
1.33e-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: 51.30 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 254 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 334 AECMEML--HEAQEELKNLRNKTMPNTTSRRYHSLGLFpMDSLAAEIEgTMRKELQLEEAESPDITHQKRVFETVRNINQ 411
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAE-ELRADLAELAALRAELEAERAELEALLAELE 184
|
....*
gi 1622905972 412 VVKQR 416
Cdd:COG4942 185 EERAA 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
123-353 |
1.36e-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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 123 ERDLELAARIgQSLlKKNKTLTE--RNELLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 185
Cdd:COG4913 191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 186 EpesvcstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIAS 265
Cdd:COG4913 269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 266 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:COG4913 335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
250 260
....*....|....*....|
gi 1622905972 334 AECMEMLHEAQEELKNLRNK 353
Cdd:COG4913 415 RDLRRELRELEAEIASLERR 434
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
82-358 |
1.92e-06 |
|
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: 51.26 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 82 DLTTEQIEETLKYFLL---CAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIR 158
Cdd:pfam05483 475 DLKTELEKEKLKNIELtahCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 159 EEVSQLRHELSMKDEllqfytsaAEESEPESVCSTPLKRNESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAS- 232
Cdd:pfam05483 555 EEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKEKQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSa 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 233 -------------QLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKK---TEDAARQQEEI----THLLSQIV 292
Cdd:pfam05483 627 enkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMV 706
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622905972 293 DLQKKAKACAVE-NEELVQHLGAAKDAQRQ-------LTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNT 358
Cdd:pfam05483 707 ALMEKHKHQYDKiIEERDSELGLYKNKEQEqssakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-392 |
4.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 86 EQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKER-DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQL 164
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 165 RHELSMKDELLQFYTSAAEESepeSVCSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEASQLktETITYEE 243
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLKKE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 244 KEQQLVNDCVKELRDANVQIASIS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 322
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL 572
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 323 TAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHSLGLFPMDSLAAEIEGTmRKELQLEEAE 392
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKR 641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-371 |
5.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLktetityeEKEQQLVNDcVKELRDANVQIASISEELAK---KTEDAARQQEEITH 286
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKL--------EKLLQLLPL-YQELEALEAELAELPERLEEleeRLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 287 LLSQIVDLQKK-AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHS 365
Cdd:COG4717 168 LEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
....*.
gi 1622905972 366 LGLFPM 371
Cdd:COG4717 248 ARLLLL 253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
141-350 |
1.59e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 141 KTLTERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESV--CSTPLKRNESSSSvqnyfHLDS 212
Cdd:PRK04863 841 QLNRRRVELeraladHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVeeIREQLDEAEEAKR-----FVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 213 LQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLL 288
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--------RDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622905972 289 SQivdLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:PRK04863 988 EK---LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-353 |
1.75e-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: 48.14 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 112 IDAVTRLLEEKERDLELAArigqslLKKNKTLTERNELLEEqVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvc 191
Cdd:TIGR02169 197 RQQLERLRREREKAERYQA------LLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISELE----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 192 stplKRNESSSSVqnyfhLDSLQKKLKDL-EEENVVLRSEASQLKTETI----TYEEKEQQLvNDCVKELRDANVQIASI 266
Cdd:TIGR02169 265 ----KRLEEIEQL-----LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 267 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQ-------LTAELRELEDKYAECMEM 339
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreklekLKREINELKRELDRLQEE 414
|
250
....*....|....
gi 1622905972 340 LHEAQEELKNLRNK 353
Cdd:TIGR02169 415 LQRLSEELADLNAA 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-346 |
1.81e-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: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdcVKELRDANVQIASISEELAkktedaaRQQEEITHLL- 288
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIA-------ELEAELERLDa 682
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 289 --SQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 346
Cdd:COG4913 683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-349 |
2.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 132 IGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplkrnESSSSVQNyfHLD 211
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE----------IDVASAER--EIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 212 SLQKKLKDLEEENVVLRSEASQLktetityeEKEQQLVNDCVKELRDANVQIASISEELakktEDAARQQEEITHLLSQI 291
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQL--------EELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622905972 292 VDLqkkakACAVENEELVQHLGAA------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 349
Cdd:COG4913 740 EDL-----ARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
70-342 |
3.00e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 70 LHTPLISPDANIDLTTEQIEEtlkyfllCAERVGQMTKTYNDIDAVTRLLEEKERDLE-LAARIGQSLLKKNKTLTERNE 148
Cdd:PRK02224 204 LHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELEtLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 149 LLEEqVEHIREEVSQLRHELsmkDELLQfyTSAAEESEPESVCStplkrnessssvqnyfHLDSLQKKLKDLEEENVVLR 228
Cdd:PRK02224 277 LAEE-VRDLRERLEELEEER---DDLLA--EAGLDDADAEAVEA----------------RREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 229 SEASQLKTETITYEEKEQQLvNDCVKELRDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVE---- 304
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgna 410
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622905972 305 ---NEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 342
Cdd:PRK02224 411 edfLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-357 |
3.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 112 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREE--VSQLRHELSMKDELLQfytsAAEESEPEs 189
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELE----RLDASSDD- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 190 vcstplkrnessssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCvKELRDANVQIASIS-- 267
Cdd:COG4913 687 --------------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLArl 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 268 ------EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEEL-----------VQHLGAAKDAQRQLTAELRELE 330
Cdd:COG4913 746 elrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPEYLALLDRLE 825
|
250 260
....*....|....*....|....*..
gi 1622905972 331 DkyaecmEMLHEAQEELKNLRNKTMPN 357
Cdd:COG4913 826 E------DGLPEYEERFKELLNENSIE 846
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
127-351 |
3.87e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 127 ELAARIGQSLLK--KNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstplkrnESSSSV 204
Cdd:COG3206 148 ELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---------EAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 205 QNyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCV-----KELRDANVQIASISEELAKKTEDAAR 279
Cdd:COG3206 219 QQ---LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622905972 280 QQEEITHLLSQIVDLQKKAKAcAVENEelvqhLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLR 351
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILA-SLEAE-----LEALQAREASLQAQLAQLEARLAE----LPELEAELRRLE 357
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-350 |
4.36e-05 |
|
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: 46.30 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 152 EQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEA 231
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ------LAALERR--------IAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 232 SQLKTETITYEEKEQQLVNDCVKELRDANVQ------------------------IASISEELAKKTEDAARQQEEITHL 287
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622905972 288 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-353 |
7.16e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 86 EQIEETLKYFLLcaERVGQMTKTYndidavtRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLR 165
Cdd:PRK03918 506 KELEEKLKKYNL--EELEKKAEEY-------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 166 HELsmkdELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNyfhLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKE 245
Cdd:PRK03918 577 KEL----EELGFESVEELEERLKELEPFYNEYLELKDAEKE---LEREEKELKKLEEELDKAFEELAETEKR---LEELR 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 246 QQLvndcvkelrdanvqiasisEELAKK--TEDAARQQEEITHLLSQIVDLQKkakacavENEELVQHLGAAKDAQRQLT 323
Cdd:PRK03918 647 KEL-------------------EELEKKysEEEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKLK 700
|
250 260 270
....*....|....*....|....*....|
gi 1622905972 324 AELRELEdKYAECMEMLHEAQEELKNLRNK 353
Cdd:PRK03918 701 EELEERE-KAKKELEKLEKALERVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-393 |
8.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 107 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESE 186
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 187 pesvcstPLKRNESsssvqnyfhldSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASI 266
Cdd:PRK03918 242 -------ELEKELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 267 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKacavENEELVQHLGAAKDAQRQLTAELRELEdKYAECMEMLHEAQEE 346
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622905972 347 LKNLRNKtmpnttsrryhsLGLFPMDSLAAEIEGTMRKELQLEEAES 393
Cdd:PRK03918 374 LERLKKR------------LTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-393 |
9.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 117 RLLEEKERdLELAARIGQSLLKKNKTLTErnelLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstPLK 196
Cdd:PRK03918 443 RELTEEHR-KELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE----KLK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 197 RNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQ---LKTETITYEEKEQQL---VNDCVKELRDANVQIASISEEL 270
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEER 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 271 AKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemlheaqEELKNL 350
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EEYEEL 664
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622905972 351 RNKTMpnTTSRRYHSL--GLFPMDSLAAEIEGTMRK-ELQLEEAES 393
Cdd:PRK03918 665 REEYL--ELSRELAGLraELEELEKRREEIKKTLEKlKEELEEREK 708
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-350 |
9.27e-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: 45.78 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 69 WLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIdavtrllEEKERDLELAARIGQSLLKKNKTLTERNE 148
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKKKIQKNKSLESQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 149 LLEEQVEHIREEVSQLRHELSMKDELLQfytSAAEESEPESVCSTPLKR---NESSSSVQNYFHLDSLQKKLKDLEEENV 225
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEIS---NTQTQLNQLKDEQNKIKKqlsEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 226 VLRSEASQ-----LKTETITYEEKEQQLVNDCV---KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKk 297
Cdd:TIGR04523 299 DLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK- 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622905972 298 akacavENEELvqhlgaaKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:TIGR04523 378 ------ENQSY-------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
130-343 |
1.07e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 130 ARIgQSLLKKNKTLTERnelleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESVCSTPLK-RNE-SSSSVQNY 207
Cdd:PLN02939 150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 208 FHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdCVKE--LRDANVQiasiseELAKKTEDAarqQEEIt 285
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622905972 286 hllSQIVDLQKKAKACAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA 343
Cdd:PLN02939 288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEA 343
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-355 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 106 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEeQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 184
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 185 SEPE-SVCSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETIT-YEEKEQQL---------VNDCV 253
Cdd:PRK03918 537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 254 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcaVENEELVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260
....*....|....*....|..
gi 1622905972 334 AECMEMLHEAQEELKNLRNKTM 355
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKK 711
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-300 |
1.24e-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: 45.40 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 80 NIDLTTEQIEETLKYFLlcaervGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIRE 159
Cdd:TIGR04523 458 NLDNTRESLETQLKVLS------RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 160 EVSQLRHELS-MKDELLQFytsaaeesepesvcSTPLKRNESSSSVqnyfhlDSLQKKLKDLEEENVVLRSEASQLKTET 238
Cdd:TIGR04523 532 EKKEKESKISdLEDELNKD--------------DFELKKENLEKEI------DEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622905972 239 ITYEEKeqqlVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:TIGR04523 592 DQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-300 |
1.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 104 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkdELLQFYTSAAE 183
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 184 ESEPESVcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQI 263
Cdd:COG4942 119 QPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622905972 264 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-348 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQ-------------------------IA 264
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 265 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 344
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....
gi 1622905972 345 EELK 348
Cdd:COG3883 206 AAAE 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
210-353 |
2.25e-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: 43.37 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLKTEtITYEEKEQQLVNdcvKELRDANVQIASISEEL--AKKTEDAARQQEEITHL 287
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLE---LEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622905972 288 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-353 |
2.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 151 EEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESvcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEenvvLRS 229
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERAEE----LRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 230 EASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENE 306
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622905972 307 ELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
116-350 |
3.10e-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: 44.19 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 116 TRLLEEKERDLELAARIGQsllkknKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpl 195
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE------- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 196 kRNE----SSSSVQNY-FHLDSLQKKLKDLEEEnvvlrsEASQLKTETITYEEKEQQLVndcVKELRDANVQiasiseEL 270
Cdd:TIGR00618 720 -FNEienaSSSLGSDLaAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVT---AALQTGAELS------HL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 271 AKKTEDAARQQEEITHLLSQI-VDLQKKAK----ACAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAECMEMLHE 342
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLeAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQ 863
|
....*...
gi 1622905972 343 AQEELKNL 350
Cdd:TIGR00618 864 LTQEQAKI 871
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-353 |
3.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHlls 289
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---LEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622905972 290 QIVDLQKKAKACAVEN--------EELVQHLGAAK---DAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-300 |
3.54e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 110 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS--------MKDELLQF---- 177
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 178 YTSAAEESEPESVCSTPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL--- 248
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeal 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622905972 249 VNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
105-353 |
3.55e-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: 44.19 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 105 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMK-------DELLQF 177
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELlrdeqeeIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 178 YTSAAEESEPESvcstpLKRNESSSSVQNYfhLDSLQKKLKDLEEEnvvLRSEASQLKTETITYEEKEQQLVNDCVKELR 257
Cdd:pfam02463 259 EIEKEEEKLAQV-----LKENKEEEKEKKL--QEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 258 DANVQIASISEELAKKTEDAARQQEEIThllsQIVDLQKKAKAcavENEELVQHLGAAKDAQRQLTAELRELEDKYAECM 337
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEE----EEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250
....*....|....*.
gi 1622905972 338 EMLHEAQEELKNLRNK 353
Cdd:pfam02463 402 EEEKEAQLLLELARQL 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-351 |
4.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELAKKTEDAARQ------ 280
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622905972 281 ---QEEITHLLSQ--IVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:COG4942 116 lgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-452 |
5.35e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 210 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE---DAARQQ----- 281
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEE---YNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREelgERARALyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 282 -----------EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:COG3883 101 svsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 351 RNKtmpnttsrryhslglfpMDSLAAEIEGTMRKELQLE-EAESPDITHQKRVFETVRNINQVVKQRSLTPSPMNIPGSN 429
Cdd:COG3883 181 EAL-----------------LAQLSAEEAAAEAQLAELEaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 1622905972 430 QSSAMNSLLSSCVSTPRSSFYGS 452
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
119-353 |
6.63e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 42.25 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 119 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS----MKDELlqfytsaaeesepESVCSTp 194
Cdd:pfam09728 13 LDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailAKSKL-------------EKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 195 lkrnessssvqnyfhldsLQKKLKDLEEENVVLRSEASQLKTETItyeEKEQQLVND---CVKELRDANVQIASISEELA 271
Cdd:pfam09728 79 ------------------LQKQNKKLKEESKKLAKEEEEKRKELS---EKFQSTLKDiqdKMEEKSEKNNKLREENEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 272 KKTEDAARQQEeithLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEM---LHEAQEELK 348
Cdd:pfam09728 138 EKLKSLIEQYE----LRELHFEKLLKTK-------ELEVQLAEAKLQQATEEEEKKAQEKEVAKARELkaqVQTLSETEK 206
|
....*
gi 1622905972 349 NLRNK 353
Cdd:pfam09728 207 ELREQ 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
114-350 |
7.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 114 AVTRLLEEKERDLE-LAARIGQsllKKNKTLTER-NEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 185
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 186 EP---------ESVCSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEASqlktetitYEEKEQQLVNDCVKEL 256
Cdd:PRK02224 254 ETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 257 RDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 336
Cdd:PRK02224 320 ED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250
....*....|....
gi 1622905972 337 MEMLHEAQEELKNL 350
Cdd:PRK02224 397 RERFGDAPVDLGNA 410
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
116-336 |
9.80e-04 |
|
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: 42.47 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 116 TRLLEEKERDLELAARIGQSLLKKNKTL-TERNELLEE--QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcs 192
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALeSENAELQAElrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 193 tplkRNESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEASQLK-----TETITYEEKEQQLVNDcvKELRDANVQIASIS 267
Cdd:pfam01576 431 ----LAEKLSKLQS--ELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLS--TRLRQLEDERNSLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622905972 268 EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQhlgAAKDAQRQLTAELRELEDKYAEC 336
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE---GKKRLQRELEALTQQLEEKAAAY 568
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
83-353 |
1.06e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 83 LTTEQIEETLKYFLLCAERVGQMTKTYNdidaVTRLLEEKERDL---ELAARIGQSLLKKNKTLTERNELLEEQ----VE 155
Cdd:COG5022 803 LSLLGSRKEYRSYLACIIKLQKTIKREK----KLRETEEVEFSLkaeVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 156 HIREEVSQLRHELSMKDEL-LQFYTSAAEESEpesvcstpLKRNESSSSVQNYFHLDSLQKKLKDL--EEENVVLRSEAS 232
Cdd:COG5022 879 LAERQLQELKIDVKSISSLkLVNLELESEIIE--------LKKSLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 233 QLKTETITYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEElVQHL 312
Cdd:COG5022 951 VKLPELNKLHEVESKL-KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE-VAEL 1028
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622905972 313 GAAKDAQRQLTAELR---ELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG5022 1029 QSASKIISSESTELSilkPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
118-353 |
1.23e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 118 LLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEEsepesvcstplkR 197
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 198 NESSSSVQNYF-HLDSLQKKLKDLEEENV---VLRSEASQL----KTETITyEEKEQQLVNdcvkelrdanvQIASISEE 269
Cdd:COG1340 81 DELNEKLNELReELDELRKELAELNKAGGsidKLRKEIERLewrqQTEVLS-PEEEKELVE-----------KIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 270 LaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 349
Cdd:COG1340 149 L-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
....
gi 1622905972 350 LRNK 353
Cdd:COG1340 228 LHEE 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-353 |
1.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 197 RNESS-SSVQNYFH---LDSLQKKLKDLeeenvvLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASISEELAK 272
Cdd:COG4717 31 PNEAGkSTLLAFIRamlLERLEKEADEL------FKPQGRKPELNLKELKELEEEL-----KEAEEKEEEYAELQEELEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 273 KTEDAARQQEEITHLLSQIVDLQKkakacAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLRN 352
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEA 170
|
.
gi 1622905972 353 K 353
Cdd:COG4717 171 E 171
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-351 |
2.07e-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: 41.49 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 86 EQIEETLKYFLLCAERVGQMT-KTYNDIDAVTRLLEEKERDLELAArigqSLLKKNKTLTERNELLEEQVEHIREEVSQL 164
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 165 RHELSMKDELLQFYtSAAEESEPESVCSTPLKRNESSSSvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEK 244
Cdd:TIGR00618 548 YHQLTSERKQRASL-KEQMQEIQQSFSILTQCDNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 245 EQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLgaakdaQRQLTA 324
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE------KEQLTY 694
|
250 260
....*....|....*....|....*..
gi 1622905972 325 ELRELEdkyaECMEMLHEAQEELKNLR 351
Cdd:TIGR00618 695 WKEMLA----QCQTLLRELETHIEEYD 717
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-285 |
2.21e-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: 40.29 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 117 RLLEEKERDLELA--ARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstp 194
Cdd:COG1579 8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 195 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKT 274
Cdd:COG1579 80 ----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|.
gi 1622905972 275 EDAARQQEEIT 285
Cdd:COG1579 152 AELEAELEELE 162
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-349 |
2.29e-03 |
|
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: 41.16 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 116 TRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKdellqfytsaaeESEpesvcstpl 195
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL------------QQE--------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 196 krnessssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLkTETITYEEKE----QQLVNDCVKELRDANVQIASISEELA 271
Cdd:TIGR04523 421 --------------KELLEKEIERLKETIIKNNSEIKDL-TNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLE 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622905972 272 KKTEDAARQQEEITHLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 349
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVK-------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-353 |
2.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 148 ELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVL 227
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 228 RSEASQL---KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEeithLLSQIVDLQKKAKACAVE 304
Cdd:TIGR00606 715 ESELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTD 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622905972 305 NEELVQHLGAAKDAQR---QLTAELR--ELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:TIGR00606 791 VTIMERFQMELKDVERkiaQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
207-355 |
2.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 207 YFHLDSLQKKLKDLEEENVVL----RSEASQLKTETIT-YEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQ 281
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622905972 282 EEITHllsqivdlqkkakacavENEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTM 355
Cdd:PRK12704 103 ELLEK-----------------REEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
264-356 |
3.12e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 38.52 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 264 ASISEELAKKTEDAArqqeEITHLLSQIVDLQKKAKACAveNEELVQHLGAAKD-AQRQLTAELRELEDKYAECMEMLHE 342
Cdd:PRK08476 41 ASIKNDLEKVKTNSS----DVSEIEHEIETILKNAREEA--NKIRQKAIAKAKEeAEKKIEAKKAELESKYEAFAKQLAN 114
|
90
....*....|....
gi 1622905972 343 AQEELKNLRNKTMP 356
Cdd:PRK08476 115 QKQELKEQLLSQMP 128
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
113-347 |
3.25e-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: 40.98 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 113 DAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAEesepesvc 191
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELeALEDQHGAFLDADIE-------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 192 stplkrnessSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLVNDCVKElrdanvqIASISEELA 271
Cdd:pfam12128 341 ----------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK---YNRRRSKIKEQNNRD-------IAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 272 KKTEDAARQQEEITHLL----SQIVDLQKKAKACAVENEE-LVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEE 346
Cdd:pfam12128 401 KIREARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYrLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREE 479
|
.
gi 1622905972 347 L 347
Cdd:pfam12128 480 Q 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
254-416 |
3.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 254 KELRDANVQIasisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQR--QLTAELRELED 331
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 332 KYAEcmemLHEAQEELKNLRNKtmpnttsrryhslglfpMDSLAAEIEgtmRKELQLEEA-ESPDITHQKRVFETVRNIN 410
Cdd:COG4717 147 RLEE----LEERLEELRELEEE-----------------LEELEAELA---ELQEELEELlEQLSLATEEELQDLAEELE 202
|
....*.
gi 1622905972 411 QVVKQR 416
Cdd:COG4717 203 ELQQRL 208
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-351 |
3.61e-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: 40.81 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 78 DANIDLTTEQIEETLKYFLLCAERVGQMTKTYN----DIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQ 153
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 154 VEHIREEVSQLRHEL-SMKDELLQFYTSAAE-ESEPESVcstplkRNESSSSVQnyfHLDSLQKKLKDLEEENVVLRSEA 231
Cdd:TIGR02168 840 LEDLEEQIEELSEDIeSLAAEIEELEELIEElESELEAL------LNERASLEE---ALALLRSELEELSEELRELESKR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 232 SQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAkktEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQH 311
Cdd:TIGR02168 911 SELRRE---LEELREKL-AQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622905972 312 LGAAkdaqrQLTA--ELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:TIGR02168 984 LGPV-----NLAAieEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
144-350 |
3.99e-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: 40.71 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 144 TERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTplkRNESSSSVQNYFHLDSLQKKL 217
Cdd:COG3096 843 QRRSELerelaqHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEEL---REELDAAQEAQAFIQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 218 KDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLlsqivd 293
Cdd:COG3096 920 AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--------RRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDL------ 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622905972 294 lqkkakacaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECM--------------EMLHEAQEELKNL 350
Cdd:COG3096 986 -----------NEKLRARLEQAEEARREAREQLRQAQAQYSQYNqvlaslkssrdakqQTLQELEQELEEL 1045
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-353 |
4.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 227 LRSEASQ------LKTEtitYEEKEQQLVndcVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:COG1196 205 LERQAEKaeryreLKEE---LKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622905972 301 CAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-351 |
4.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 214 QKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLV------NDCVKELRDANVQIASISEELAKKTEDAARQQEEITHL 287
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622905972 288 LSQIVDLQKKAKACAVENEELVQHLG-------AAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-353 |
4.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 235 KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGA 314
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622905972 315 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
141-353 |
5.46e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 141 KTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSV----QNYFHLDSLQKK 216
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVeeakTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 217 LKDLEEENVVLRSEASQLKTETITYEEKEQQLVND------------CVKELRDANVQIASISE---ELAKKTEDAARQQ 281
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptCTQQISEGPDRITKIKDklkELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622905972 282 EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
151-333 |
6.14e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 39.68 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 151 EEQVEHIREEVSQLRHEL-----SMKDELLQFYTSAAEEsepESVCSTPLKRNESSSSVQNYFH-LDSLQKKLKDLEE-- 222
Cdd:pfam04108 111 EDSVEILRDALKELIDELqaaqeSLDSDLKRFDDDLRDL---QKELESLSSPSESISLIPTLLKeLESLEEEMASLLEsl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 223 ----ENVVLRSEASQ-LKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKK 297
Cdd:pfam04108 188 tnhyDQCVTAVKLTEgGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSR 267
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622905972 298 AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:pfam04108 268 LPEYLAALKEFEERWEEEKETIEDYLSELEDLREFY 303
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
254-353 |
6.76e-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: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 254 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQH-------LGAAKDAqRQLTA-- 324
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqLGNVRNN-KEYEAlq 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622905972 325 --------ELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG1579 96 keieslkrRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
195-329 |
7.32e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 37.28 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 195 LKRNES-SSSVQNyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKK 273
Cdd:pfam10473 12 LKESERkADSLKD--KVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSEKENL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622905972 274 TEDAARQQEEITHLLSQIVDLQKKAKacaVENEELVQHLGAAKDAQRQLTAELREL 329
Cdd:pfam10473 86 TKELQKKQERVSELESLNSSLENLLE---EKEQEKVQMKEESKTAVEMLQTQLKEL 138
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
100-353 |
8.79e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 100 ERVGQMTKTYNDIdaVTRLLEEKERDL----ELAARIgqSLLKKNKTLTERNELL---EEQVEHIREEVSQLR--HELSM 170
Cdd:pfam06160 45 EKFEEWRKKWDDI--VTKSLPDIEELLfeaeELNDKY--RFKKAKKALDEIEELLddiEEDIKQILEELDELLesEEKNR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 171 K--DELLQFYtsaaeesepESVCSTPLKRNESSSSVqnyfhLDSLQKKLKDLEEENVVL------------RSEASQLKT 236
Cdd:pfam06160 121 EevEELKDKY---------RELRKTLLANRFSYGPA-----IDELEKQLAEIEEEFSQFeeltesgdyleaREVLEKLEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 237 ETITYEEK-EQ--QLVNDCVKELRDA---------------------NV--QIASISEELAK--------KTEDAARQQE 282
Cdd:pfam06160 187 ETDALEELmEDipPLYEELKTELPDQleelkegyremeeegyalehlNVdkEIQQLEEQLEEnlallenlELDEAEEALE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622905972 283 EITHLLSQIVDL---QKKAKACAVEN-EELVQHLGAAKDAQRQLTAELRELEDKY---AECMEMLHEAQEELKNLRNK 353
Cdd:pfam06160 267 EIEERIDQLYDLlekEVDAKKYVEKNlPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKR 344
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
141-354 |
9.78e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.05 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 141 KTLTERNELLEEQVEHIREEVSQLRHELsmkDELLQFYTSAAEESEpesvcstplkrnessssvqnyfHLDSLQKKLKDL 220
Cdd:PRK04778 306 KYVEKNSDTLPDFLEHAKEQNKELKEEI---DRVKQSYTLNESELE----------------------SVRQLEKQLESL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622905972 221 EEENVVLRSEasqLKTETITYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:PRK04778 361 EKQYDEITER---IAEQEIAYSELQEEL-EEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEK 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622905972 301 CaveN-----EELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKT 354
Cdd:PRK04778 437 S---NlpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEET 492
|
|
| |
