|
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 |
3.16e-170 |
|
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: 487.61 E-value: 3.16e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 48 EEQLPHYKLRADTIY-GYDHDDW-LHTPL-ISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKER 124
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 125 DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSV 204
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 205 QNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEI 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578805798 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 |
1.82e-80 |
|
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: 251.82 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 414 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDIGNVVLDNKTNSIILETEAADLGNDERSKKPGTPGTPGSH 493
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 494 DLETALRRLSLRRENYLSERRFFEEEQERKLQELAE----KGELRSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 569
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157
|
170
....*....|....
gi 578805798 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 |
2.04e-13 |
|
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: 73.94 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 112 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 191
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 192 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 268
Cdd:TIGR02168 777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 269 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 341
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 578805798 342 EAQEELKNLRNK 353
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-353 |
2.99e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 99 AERVGQMTKTYNDIDAVTRLL--EEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQ 176
Cdd:COG1196 212 AERYRELKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 177 FYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcVKEL 256
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----EEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 257 RDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 336
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|....*..
gi 578805798 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 |
3.81e-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: 66.62 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 79 ANIDLTTEQIEETLKyfllcaervgQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIR 158
Cdd:TIGR02168 684 EKIEELEEKIAELEK----------ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 159 EEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTET 238
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 239 ityEEKEQQLVnDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDA 318
Cdd:TIGR02168 834 ---AATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270
....*....|....*....|....*....|...
gi 578805798 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 |
3.33e-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: 57.00 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 100 ERVGQMTKTYNDID-AVTRLLEEKERDLELAARIGQslLKKnktltERNELLEEQvEHIREEVSQLRHELS--------- 169
Cdd:TIGR02169 650 EKSGAMTGGSRAPRgGILFSRSEPAELQRLRERLEG--LKR-----ELSSLQSEL-RRIENRLDELSQELSdasrkigei 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 170 MKD-ELLQFYTSAA----EESEPE-SVCSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEE 243
Cdd:TIGR02169 722 EKEiEQLEQEEEKLkerlEELEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 244 KE-QQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 322
Cdd:TIGR02169 794 PEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
250 260 270
....*....|....*....|....*....|.
gi 578805798 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 |
9.01e-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: 55.45 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 104 QMTKTYNDIDAVTRLLEEKERDLELaarigqslLKKNKTLTERNELLEEQVEHIREEVSQLRHElSMKDELLQFYTSAAE 183
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLRLE-ELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 184 ESEpesvcstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQI 263
Cdd:TIGR02168 251 AEE----------------------ELEELTAELQELEEKLEELRLEVSELEEE----IEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 264 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 343
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250
....*....|
gi 578805798 344 QEELKNLRNK 353
Cdd:TIGR02168 385 RSKVAQLELQ 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
99-366 |
1.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 99 AERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKD 172
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 173 E----LLQFYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL 248
Cdd:PRK03918 293 EeyikLSEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 249 VN--------------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHlgA 314
Cdd:PRK03918 372 EElerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--H 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 578805798 315 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHSL 366
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
119-299 |
1.93e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 119 LEEKERDLELAarigQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstplKRN 198
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---------LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 199 ESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEK----EQQLVNDCVKELRDANVQIASISEELAKKT 274
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 578805798 275 EDAARQQEEITHLLSQIVDLQKKAK 299
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-416 |
2.17e-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: 50.15 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 254 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 334 AECMEML--HEAQEELKNLRNKTMPNTTSRRYHSLGLFpMDSLAAEIEgTMRKELQLEEAESPDITHQKRVFETVRNINQ 411
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAE-ELRADLAELAALRAELEAERAELEALLAELE 184
|
....*
gi 578805798 412 VVKQR 416
Cdd:COG4942 185 EERAA 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
123-353 |
2.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 123 ERDLELAARIgQSLlKKNKTLTE--RNELLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 185
Cdd:COG4913 191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 186 EpesvcstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIAS 265
Cdd:COG4913 269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 266 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:COG4913 335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
250 260
....*....|....*....|
gi 578805798 334 AECMEMLHEAQEELKNLRNK 353
Cdd:COG4913 415 RDLRRELRELEAEIASLERR 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
210-393 |
3.76e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKKTEDAARQQEEITHLLS 289
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN----EQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 290 QIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME-----MLHEAQEELKNLRNKTMPNTTSRRYH 364
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180
....*....|....*....|....*....
gi 578805798 365 SLGLFPMDSLAAEIEGTMRKELQLEEAES 393
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
82-358 |
6.22e-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: 49.33 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 82 DLTTEQIEETLKYFLL---CAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIR 158
Cdd:pfam05483 475 DLKTELEKEKLKNIELtahCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 159 EEVSQLRHELSMKDEllqfytsaAEESEPESVCSTPLKRNESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAS- 232
Cdd:pfam05483 555 EEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKEKQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSa 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 233 -------------QLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKK---TEDAARQQEEI----THLLSQIV 292
Cdd:pfam05483 627 enkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMV 706
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578805798 293 DLQKKAKACAVE-NEELVQHLGAAKDAQRQ-------LTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNT 358
Cdd:pfam05483 707 ALMEKHKHQYDKiIEERDSELGLYKNKEQEqssakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-371 |
1.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLktetityeEKEQQLVNDcVKELRDANVQIASISEELAK---KTEDAARQQEEITH 286
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKL--------EKLLQLLPL-YQELEALEAELAELPERLEEleeRLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 287 LLSQIVDLQKK-AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHS 365
Cdd:COG4717 168 LEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
....*.
gi 578805798 366 LGLFPM 371
Cdd:COG4717 248 ARLLLL 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-392 |
1.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 86 EQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKER-DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQL 164
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 165 RHELSMKDELLQFYTSAAEESepeSVCSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEASQLktETITYEE 243
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLKKE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 244 KEQQLVNDCVKELRDANVQIASIS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 322
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL 572
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 323 TAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHSLGLFPMDSLAAEIEGTmRKELQLEEAE 392
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKR 641
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
141-350 |
2.22e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 141 KTLTERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESV--CSTPLKRNESSSSvqnyfHLDS 212
Cdd:PRK04863 841 QLNRRRVELeraladHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVeeIREQLDEAEEAKR-----FVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 213 LQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLL 288
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--------RDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578805798 289 SQivdLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:PRK04863 988 EK---LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-346 |
2.47e-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: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdcVKELRDANVQIASISEELAkktedaaRQQEEITHLL- 288
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIA-------ELEAELERLDa 682
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 289 --SQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 346
Cdd:COG4913 683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-351 |
4.02e-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: 46.98 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 112 IDAVTRLLEEKERDLELAArigqslLKKNKTLTERNELLEEqVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvc 191
Cdd:TIGR02169 197 RQQLERLRREREKAERYQA------LLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISELE----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 192 stplKRNESSSSVqnyfhLDSLQKKLKDL-EEENVVLRSEASQLKTETI----TYEEKEQQLvNDCVKELRDANVQIASI 266
Cdd:TIGR02169 265 ----KRLEEIEQL-----LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 267 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 346
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
....*
gi 578805798 347 LKNLR 351
Cdd:TIGR02169 415 LQRLS 419
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-349 |
4.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 132 IGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplkrnESSSSVQNyfHLD 211
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE----------IDVASAER--EIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 212 SLQKKLKDLEEENVVLRSEASQLktetityeEKEQQLVNDCVKELRDANVQIASISEELakktEDAARQQEEITHLLSQI 291
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQL--------EELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578805798 292 VDLqkkakACAVENEELVQHLGAA------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 349
Cdd:COG4913 740 EDL-----ARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-357 |
4.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 112 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREE--VSQLRHELSMKDELLQfytsAAEESEPEs 189
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELE----RLDASSDD- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 190 vcstplkrnessssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCvKELRDANVQIASIS-- 267
Cdd:COG4913 687 --------------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLArl 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 268 ------EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEEL-----------VQHLGAAKDAQRQLTAELRELE 330
Cdd:COG4913 746 elrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPEYLALLDRLE 825
|
250 260
....*....|....*....|....*..
gi 578805798 331 DkyaecmEMLHEAQEELKNLRNKTMPN 357
Cdd:COG4913 826 E------DGLPEYEERFKELLNENSIE 846
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
70-342 |
4.86e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 70 LHTPLISPDANIDLTTEQIEEtlkyfllCAERVGQMTKTYNDIDAVTRLLEEKERDLE-LAARIGQSLLKKNKTLTERNE 148
Cdd:PRK02224 204 LHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELEtLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 149 LLEEqVEHIREEVSQLRHELsmkDELLQfyTSAAEESEPESVCStplkrnessssvqnyfHLDSLQKKLKDLEEENVVLR 228
Cdd:PRK02224 277 LAEE-VRDLRERLEELEEER---DDLLA--EAGLDDADAEAVEA----------------RREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 229 SEASQLKTETITYEEKEQQLvNDCVKELRDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVE---- 304
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgna 410
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578805798 305 ---NEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 342
Cdd:PRK02224 411 edfLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-350 |
8.15e-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: 45.53 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 152 EQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEA 231
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ------LAALERR--------IAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 232 SQLKTETITYEEKEQQLVNDCVKELRDANVQ------------------------IASISEELAKKTEDAARQQEEITHL 287
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578805798 288 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
127-351 |
8.97e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 127 ELAARIGQSLLK--KNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstplkrnESSSSV 204
Cdd:COG3206 148 ELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---------EAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 205 QNyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCV-----KELRDANVQIASISEELAKKTEDAAR 279
Cdd:COG3206 219 QQ---LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578805798 280 QQEEITHLLSQIVDLQKKAKAcAVENEelvqhLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLR 351
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILA-SLEAE-----LEALQAREASLQAQLAQLEARLAE----LPELEAELRRLE 357
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
130-343 |
1.42e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 130 ARIgQSLLKKNKTLTERnelleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESVCSTPLK-RNE-SSSSVQNY 207
Cdd:PLN02939 150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 208 FHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdCVKE--LRDANVQiasiseELAKKTEDAarqQEEIt 285
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578805798 286 hllSQIVDLQKKAKACAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA 343
Cdd:PLN02939 288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEA 343
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-300 |
2.37e-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: 43.98 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 104 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkdELLQFYTSAAE 183
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 184 ESEPESVcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQI 263
Cdd:COG4942 119 QPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 578805798 264 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-348 |
2.42e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQ-------------------------IA 264
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 265 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 344
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....
gi 578805798 345 EELK 348
Cdd:COG3883 206 AAAE 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-393 |
3.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 107 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESE 186
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 187 pesvcstPLKRNESsssvqnyfhldSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASI 266
Cdd:PRK03918 242 -------ELEKELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 267 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKacavENEELVQHLGAAKDAQRQLTAELRELEdKYAECMEMLHEAQEE 346
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578805798 347 LKNLRNKtmpnttsrryhsLGLFPMDSLAAEIEGTMRKELQLEEAES 393
Cdd:PRK03918 374 LERLKKR------------LTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-353 |
3.69e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 151 EEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESvcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEenvvLRS 229
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERAEE----LRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 230 EASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENE 306
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578805798 307 ELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-353 |
3.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 86 EQIEETLKYFLLcaERVGQMTKTYndidavtRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLR 165
Cdd:PRK03918 506 KELEEKLKKYNL--EELEKKAEEY-------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 166 HELsmkdELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNyfhLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKE 245
Cdd:PRK03918 577 KEL----EELGFESVEELEERLKELEPFYNEYLELKDAEKE---LEREEKELKKLEEELDKAFEELAETEKR---LEELR 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 246 QQLvndcvkelrdanvqiasisEELAKK--TEDAARQQEEITHLLSQIVDLQKkakacavENEELVQHLGAAKDAQRQLT 323
Cdd:PRK03918 647 KEL-------------------EELEKKysEEEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKLK 700
|
250 260 270
....*....|....*....|....*....|
gi 578805798 324 AELRELEdKYAECMEMLHEAQEELKNLRNK 353
Cdd:PRK03918 701 EELEERE-KAKKELEKLEKALERVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-355 |
3.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 106 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEeQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 184
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 185 SEPE-SVCSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETIT-YEEKEQQL---------VNDCV 253
Cdd:PRK03918 537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 254 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcaVENEELVQHLGAAKDAQRQLTAELRELEDKY 333
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260
....*....|....*....|..
gi 578805798 334 AECMEMLHEAQEELKNLRNKTM 355
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKK 711
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-393 |
4.13e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 117 RLLEEKERdLELAARIGQSLLKKNKTLTErnelLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstPLK 196
Cdd:PRK03918 443 RELTEEHR-KELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE----KLK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 197 RNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQ---LKTETITYEEKEQQL---VNDCVKELRDANVQIASISEEL 270
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEER 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 271 AKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemlheaqEELKNL 350
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EEYEEL 664
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 578805798 351 RNKTMpnTTSRRYHSL--GLFPMDSLAAEIEGTMRK-ELQLEEAES 393
Cdd:PRK03918 665 REEYL--ELSRELAGLraELEELEKRREEIKKTLEKlKEELEEREK 708
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
210-353 |
4.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTEtITYEEKEQQLVNdcvKELRDANVQIASISEEL--AKKTEDAARQQEEITHL 287
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLE---LEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578805798 288 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-350 |
4.97e-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: 43.09 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 69 WLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIdavtrllEEKERDLELAARIGQSLLKKNKTLTERNE 148
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKKKIQKNKSLESQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 149 LLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLR 228
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 229 SEASQ-----LKTETITYEEKEQQLVNDCV---KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKkaka 300
Cdd:TIGR04523 302 NQKEQdwnkeLKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK---- 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578805798 301 cavENEELvqhlgaaKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:TIGR04523 378 ---ENQSY-------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-300 |
5.84e-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: 43.09 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 80 NIDLTTEQIEETLKYFLlcaervGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIRE 159
Cdd:TIGR04523 458 NLDNTRESLETQLKVLS------RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 160 EVSQLRHELS-MKDELLQFytsaaeesepesvcSTPLKRNESSSSVqnyfhlDSLQKKLKDLEEENVVLRSEASQLKTET 238
Cdd:TIGR04523 532 EKKEKESKISdLEDELNKD--------------DFELKKENLEKEI------DEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578805798 239 ITYEEKeqqlVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:TIGR04523 592 DQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-353 |
5.94e-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: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHlls 289
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---LEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578805798 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 |
6.02e-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: 42.44 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 110 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS--------MKDELLQF---- 177
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 178 YTSAAEESEPESVCSTPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL--- 248
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeal 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578805798 249 VNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 300
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-351 |
7.55e-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: 42.44 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELAKKTEDAARQ------ 280
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578805798 281 ---QEEITHLLSQ--IVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:COG4942 116 lgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
116-350 |
8.41e-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: 42.65 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 116 TRLLEEKERDLELAARIGQsllkknKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcsTPL 195
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF---NEI 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 196 KRNESSSSVQNYFHLDSLQKKLKDLEEEnvvlrsEASQLKTETITYEEKEQQLVndcVKELRDANVQiasiseELAKKTE 275
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVT---AALQTGAELS------HLAAEIQ 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 276 DAARQQEEITHLLSQI-VDLQKKAK----ACAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAECMEMLHEAQEEL 347
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLeAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQLTQEQ 868
|
...
gi 578805798 348 KNL 350
Cdd:TIGR00618 869 AKI 871
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-452 |
1.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE---DAARQQ----- 281
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEE---YNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREelgERARALyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 282 -----------EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 350
Cdd:COG3883 101 svsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 351 RNKtmpnttsrryhslglfpMDSLAAEIEGTMRKELQLE-EAESPDITHQKRVFETVRNINQVVKQRSLTPSPMNIPGSN 429
Cdd:COG3883 181 EAL-----------------LAQLSAEEAAAEAQLAELEaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 578805798 430 QSSAMNSLLSSCVSTPRSSFYGS 452
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
114-350 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 114 AVTRLLEEKERDLE-LAARIGQsllKKNKTLTER-NEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 185
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 186 EP---------ESVCSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEASqlktetitYEEKEQQLVNDCVKEL 256
Cdd:PRK02224 254 ETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 257 RDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 336
Cdd:PRK02224 320 ED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250
....*....|....
gi 578805798 337 MEMLHEAQEELKNL 350
Cdd:PRK02224 397 RERFGDAPVDLGNA 410
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
83-353 |
1.69e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 83 LTTEQIEETLKYFLLCAERVGQMTKTYNdidaVTRLLEEKERDL---ELAARIGQSLLKKNKTLTERNELLEEQ----VE 155
Cdd:COG5022 803 LSLLGSRKEYRSYLACIIKLQKTIKREK----KLRETEEVEFSLkaeVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 156 HIREEVSQLRHELSMKDEL-LQFYTSAAEESEpesvcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEEN--VVLRSEAS 232
Cdd:COG5022 879 LAERQLQELKIDVKSISSLkLVNLELESEIIE--------LKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 233 QLKTETITYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEElVQHL 312
Cdd:COG5022 951 VKLPELNKLHEVESKL-KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE-VAEL 1028
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578805798 313 GAAKDAQRQLTAELR---ELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG5022 1029 QSASKIISSESTELSilkPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
105-353 |
1.97e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 105 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMK-------DELLQF 177
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELlrdeqeeIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 178 YTSAAEESEPESvcstpLKRNESSSSVQNYfhLDSLQKKLKDLEEEnvvLRSEASQLKTETITYEEKEQQLVNDCVKELR 257
Cdd:pfam02463 259 EIEKEEEKLAQV-----LKENKEEEKEKKL--QEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 258 DANVQIASISEELAKKTEDAARQQEEIThllsQIVDLQKKAKAcavENEELVQHLGAAKDAQRQLTAELRELEDKYAECM 337
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEE----EEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250
....*....|....*.
gi 578805798 338 EMLHEAQEELKNLRNK 353
Cdd:pfam02463 402 EEEKEAQLLLELARQL 417
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
116-336 |
2.15e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 116 TRLLEEKERDLELAARIGQSLLKKNKTL-TERNELLEE--QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcs 192
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALeSENAELQAElrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 193 tplkRNESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEASQLK-----TETITYEEKEQQLVNDcvKELRDANVQIASIS 267
Cdd:pfam01576 431 ----LAEKLSKLQS--ELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLS--TRLRQLEDERNSLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578805798 268 EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQhlgAAKDAQRQLTAELRELEDKYAEC 336
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE---GKKRLQRELEALTQQLEEKAAAY 568
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
119-353 |
2.91e-03 |
|
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: 40.32 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 119 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS----MKDELlqfytsaaeesepESVCSTp 194
Cdd:pfam09728 13 LDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailAKSKL-------------EKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 195 lkrnessssvqnyfhldsLQKKLKDLEEENVVLRSEASQLKTETItyeEKEQQLVND---CVKELRDANVQIASISEELA 271
Cdd:pfam09728 79 ------------------LQKQNKKLKEESKKLAKEEEEKRKELS---EKFQSTLKDiqdKMEEKSEKNNKLREENEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 272 KKTEDAARQQEeithLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEM---LHEAQEELK 348
Cdd:pfam09728 138 EKLKSLIEQYE----LRELHFEKLLKTK-------ELEVQLAEAKLQQATEEEEKKAQEKEVAKARELkaqVQTLSETEK 206
|
....*
gi 578805798 349 NLRNK 353
Cdd:pfam09728 207 ELREQ 211
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-353 |
3.25e-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: 40.80 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 148 ELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVL 227
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 228 RSEASQL---KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEeithLLSQIVDLQKKAKACAVE 304
Cdd:TIGR00606 715 ESELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTD 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578805798 305 NEELVQHLGAAKDAQR---QLTAELR--ELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:TIGR00606 791 VTIMERFQMELKDVERkiaQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
207-355 |
4.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 207 YFHLDSLQKKLKDLEEENVVL----RSEASQLKTETIT-YEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQ 281
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578805798 282 EEITHllsqivdlqkkakacavENEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTM 355
Cdd:PRK12704 103 ELLEK-----------------REEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-351 |
4.47e-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: 40.34 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 86 EQIEETLKYFLLCAERVGQMT-KTYNDIDAVTRLLEEKERDLELAArigqSLLKKNKTLTERNELLEEQVEHIREEVSQL 164
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 165 RHELSMKDELLQFYtSAAEESEPESVCSTPLKRNESSSSvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEK 244
Cdd:TIGR00618 548 YHQLTSERKQRASL-KEQMQEIQQSFSILTQCDNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 245 EQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLgaakdaQRQLTA 324
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE------KEQLTY 694
|
250 260
....*....|....*....|....*..
gi 578805798 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 |
4.77e-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: 39.14 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 117 RLLEEKERDLELA--ARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstp 194
Cdd:COG1579 8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 195 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKT 274
Cdd:COG1579 80 ----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|.
gi 578805798 275 EDAARQQEEIT 285
Cdd:COG1579 152 AELEAELEELE 162
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
113-347 |
4.83e-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: 40.21 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 113 DAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAEesepesvc 191
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELeALEDQHGAFLDADIE-------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 192 stplkrnessSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLVNDCVKElrdanvqIASISEELA 271
Cdd:pfam12128 341 ----------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK---YNRRRSKIKEQNNRD-------IAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 272 KKTEDAARQQEEITHLL----SQIVDLQKKAKACAVENEE-LVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEE 346
Cdd:pfam12128 401 KIREARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYrLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREE 479
|
.
gi 578805798 347 L 347
Cdd:pfam12128 480 Q 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-353 |
5.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 210 LDSLQKKLKDLeeenvvLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASISEELAKKTEDAARQQEEITHLLS 289
Cdd:COG4717 48 LERLEKEADEL------FKPQGRKPELNLKELKELEEEL-----KEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578805798 290 QIVDLQKkakacAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLRNK 353
Cdd:COG4717 117 ELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAE 171
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
144-350 |
5.36e-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: 39.94 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 144 TERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTplkRNESSSSVQNYFHLDSLQKKL 217
Cdd:COG3096 843 QRRSELerelaqHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEEL---REELDAAQEAQAFIQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 218 KDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLlsqivd 293
Cdd:COG3096 920 AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--------RRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDL------ 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578805798 294 lqkkakacaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECM--------------EMLHEAQEELKNL 350
Cdd:COG3096 986 -----------NEKLRARLEQAEEARREAREQLRQAQAQYSQYNqvlaslkssrdakqQTLQELEQELEEL 1045
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-351 |
5.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 214 QKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLV------NDCVKELRDANVQIASISEELAKKTEDAARQQEEITHL 287
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578805798 288 LSQIVDLQKKAKACAVENEELVQHLG-------AAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
214-335 |
5.92e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 214 QKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQI---ASISEELAKKTEDAARQQEEithllsq 290
Cdd:PRK09510 100 QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAeaeAKRAAAAAKKAAAEAKKKAE------- 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578805798 291 iVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 335
Cdd:PRK09510 173 -AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
118-353 |
5.98e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 118 LLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEEsepesvcstplkR 197
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 198 NESSSSVQNYF-HLDSLQKKLKDLEEENV---VLRSEASQL----KTETITyEEKEQQLVNdcvkelrdanvQIASISEE 269
Cdd:COG1340 81 DELNEKLNELReELDELRKELAELNKAGGsidKLRKEIERLewrqQTEVLS-PEEEKELVE-----------KIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 270 LaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 349
Cdd:COG1340 149 L-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
....
gi 578805798 350 LRNK 353
Cdd:COG1340 228 LHEE 231
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
264-356 |
7.14e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 37.36 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 264 ASISEELAKKTEDAArqqeEITHLLSQIVDLQKKAKACAveNEELVQHLGAAKD-AQRQLTAELRELEDKYAECMEMLHE 342
Cdd:PRK08476 41 ASIKNDLEKVKTNSS----DVSEIEHEIETILKNAREEA--NKIRQKAIAKAKEeAEKKIEAKKAELESKYEAFAKQLAN 114
|
90
....*....|....
gi 578805798 343 AQEELKNLRNKTMP 356
Cdd:PRK08476 115 QKQELKEQLLSQMP 128
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
141-353 |
7.37e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 141 KTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSV----QNYFHLDSLQKK 216
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVeeakTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 217 LKDLEEENVVLRSEASQLKTETITYEEKEQQLVND------------CVKELRDANVQIASISE---ELAKKTEDAARQQ 281
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptCTQQISEGPDRITKIKDklkELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578805798 282 EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
135-355 |
7.93e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 135 SLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEEsepesvcstplKRNESSSSVQNYFHLDSLQ 214
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE-----------LRKELAELNKAGGSIDKLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 215 KKLKDLEEEnvvlrseasqLKTETITyEEKEQQLVNdcvkelrdanvQIASISEELaKKTEDAARQQEEITHLLSQIVDL 294
Cdd:COG1340 116 KEIERLEWR----------QQTEVLS-PEEEKELVE-----------KIKELEKEL-EKAKKALEKNEKLKELRAELKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 295 QKKAKACAVENEELVQHLGAAKDAQRQLT---------------------AELRELEDKYAECMEMLHEAQEELKNLRNK 353
Cdd:COG1340 173 RKEAEEIHKKIKELAEEAQELHEEMIELYkeadelrkeadelhkeiveaqEKADELHEEIIELQKELRELRKELKKLRKK 252
|
..
gi 578805798 354 TM 355
Cdd:COG1340 253 QR 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-351 |
8.73e-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: 39.27 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 78 DANIDLTTEQIEETLKYFLLCAERVGQMTKTYN----DIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQ 153
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 154 VEHIREEVSQLRHEL-SMKDELLQFYTSAAE-ESEPESVcstplkRNESSSSVQnyfHLDSLQKKLKDLEEENVVLRSEA 231
Cdd:TIGR02168 840 LEDLEEQIEELSEDIeSLAAEIEELEELIEElESELEAL------LNERASLEE---ALALLRSELEELSEELRELESKR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 232 SQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAkktEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQH 311
Cdd:TIGR02168 911 SELRRE---LEELREKL-AQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578805798 312 LGAAkdaqrQLTA--ELRELEDKYAECMEMLHEAQEELKNLR 351
Cdd:TIGR02168 984 LGPV-----NLAAieEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-349 |
9.52e-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: 39.23 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 116 TRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDellqfytsaaeesepesvcstpl 195
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----------------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 196 krnessssvQNYfhlDSLQKKLKDLEEENVVLRSEASQLkTETITYEEKE----QQLVNDCVKELRDANVQIASISEELA 271
Cdd:TIGR04523 419 ---------QEK---ELLEKEIERLKETIIKNNSEIKDL-TNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLE 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578805798 272 KKTEDAARQQEEITHLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 349
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVK-------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
254-416 |
9.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 254 KELRDANVQIasisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQR--QLTAELRELED 331
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805798 332 KYAEcmemLHEAQEELKNLRNKtmpnttsrryhslglfpMDSLAAEIEgtmRKELQLEEA-ESPDITHQKRVFETVRNIN 410
Cdd:COG4717 147 RLEE----LEERLEELRELEEE-----------------LEELEAELA---ELQEELEELlEQLSLATEEELQDLAEELE 202
|
....*.
gi 578805798 411 QVVKQR 416
Cdd:COG4717 203 ELQQRL 208
|
|
| |
