|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
144-449 |
1.16e-180 |
|
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: 527.67 E-value: 1.16e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 144 EEQLPHYKLRADTIY-GYDHDDW-LHTPL-ISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKER 220
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 221 DLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESICSTPLKRNESSSSV 300
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 301 QNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANIQIANISEELAKKTEDAARQQEEI 380
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024374521 381 THLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
510-678 |
1.06e-79 |
|
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: 257.21 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 510 KQRSMTPSPMNIPGSNQSSAMNSLISSCISTPRSSFYGGDISNIVIDNKTNSIILETD-SENGNEDRMKKPGTPGTPGSS 588
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSsSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 589 DLETALRRLSLRRENYLSERKFFEEEQERKLRELAE----KGELRSGSITPTESIMSLGTHSRfSEFTGYSGMsiSSRSY 664
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSGF--SSRSY 157
|
170
....*....|....
gi 2024374521 665 LPEKLQIVKPLEGS 678
Cdd:pfam12448 158 LPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-449 |
1.07e-15 |
|
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: 82.41 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 208 IDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsic 287
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 288 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANIQIANISE 364
Cdd:TIGR02168 777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 365 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 437
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 2024374521 438 EAQEELKNLRNK 449
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-449 |
5.12e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 195 AERVGQMTKTYNDIDAVTRLL--EEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQ 272
Cdd:COG1196 212 AERYRELKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 273 FYTSAAEESEPESICSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQLvNDCVKEL 352
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE---LEELEEELEEAEEELEEAEAEL-AEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 353 RDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 432
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|....*..
gi 2024374521 433 MEMLHEAQEELKNLRNK 449
Cdd:COG1196 448 AEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-449 |
5.59e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 182 EQIEETLKyfllcaervgQMTKTYNDIDAVTRLLEEKERDLELaarigqslLKKNKSLTERNEFLEEQVEHIREEVSQLR 261
Cdd:TIGR02168 172 ERRKETER----------KLERTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 262 HElSMKDELLQFYTSAAEESEPESICSTPLKRNESSSSVQNYFHLdSLQKKLKDLEEENVVLRSEACQLKTETITYEEKE 341
Cdd:TIGR02168 234 LE-ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 342 QQLVNdcvkELRDANIQIANISEELAKKTEDAARQQEEIThllsqivDLQKKAKACAVENEELVQHLGAAKDAQRQLTAE 421
Cdd:TIGR02168 312 ANLER----QLEELEAQLEELESKLDELAEELAELEEKLE-------ELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260
....*....|....*....|....*...
gi 2024374521 422 LRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-449 |
7.01e-10 |
|
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: 63.55 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 196 ERVGQMTKTYNDID-AVTRLLEEKERDLELAARIGQslLKKNKslternEFLEEQVEHIREEVSQLRHELS--------- 265
Cdd:TIGR02169 650 EKSGAMTGGSRAPRgGILFSRSEPAELQRLRERLEG--LKREL------SSLQSELRRIENRLDELSQELSdasrkigei 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 266 MKD-ELLQFYTSAA----EESEPE-SICSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEE 339
Cdd:TIGR02169 722 EKEiEQLEQEEEKLkerlEELEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 340 KE-QQLVNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 418
Cdd:TIGR02169 794 PEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
250 260 270
....*....|....*....|....*....|.
gi 2024374521 419 TAELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERK 904
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
306-456 |
6.29e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVndcvKELRDANIQIANISEELAKKTEDAARQQEEITHLLS 385
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN----EQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024374521 386 QIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME-----MLHEAQEELKNLRNKTMPNAVS 456
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEK 198
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
178-453 |
4.13e-08 |
|
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: 57.42 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 178 DLTTEQIEETLKYFLL---CAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIR 254
Cdd:pfam05483 475 DLKTELEKEKLKNIELtahCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 255 EEVSQLRHELSMKDEllqfytsaAEESEPESICSTPLKRNESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAC- 328
Cdd:pfam05483 555 EEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKEKQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSa 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 329 -------------QLKTETITYEEKEQQLVNDCVKELRDANIQIANISEELAKK---TEDAARQQEEI----THLLSQIV 388
Cdd:pfam05483 627 enkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMV 706
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024374521 389 DLQKKAKACAVE-NEELVQHLGAAKDAQRQ-------LTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPN 453
Cdd:pfam05483 707 ALMEKHKHQYDKiIEERDSELGLYKNKEQEqssakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
195-503 |
5.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 195 AERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKSLTERNEFLEEQVEHIREEVSQLRH------ELSMKD 268
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 269 E----LLQFYTSAAEESEPESICSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL 344
Cdd:PRK03918 293 EeyikLSEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 345 vndcvKELRDANIQIANIS-EELAKKTEDAARQQEEITHLLSQIVDLQ-----------------KKAKA-CAVENEELV 405
Cdd:PRK03918 372 -----EELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIgelkkeikelkkaieelKKAKGkCPVCGRELT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 406 QHlgAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTmpNAVSRryhslgLFPMDSLAAEIEgSMRKElhLD 485
Cdd:PRK03918 447 EE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL--KKESE------LIKLKELAEQLK-ELEEK--LK 513
|
330
....*....|....*...
gi 2024374521 486 EPDSPDLAHQKRVFETVR 503
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLK 531
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
306-467 |
6.01e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLktetityeEKEQQLVNDcVKELRDANIQIANISEELAK---KTEDAARQQEEITH 382
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKL--------EKLLQLLPL-YQELEALEAELAELPERLEEleeRLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 383 LLSQIVDLQKK-AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNAVSRRYHS 461
Cdd:COG4717 168 LEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
....*.
gi 2024374521 462 LGLFPM 467
Cdd:COG4717 248 ARLLLL 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
215-395 |
1.05e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 215 LEEKERDLELAarigQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesicstplKRN 294
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---------LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 295 ESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEK----EQQLVNDCVKELRDANIQIANISEELAKKT 370
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 2024374521 371 EDAARQQEEITHLLSQIVDLQKKAK 395
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
181-431 |
1.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 181 TEQIEETLKYFLLCAERVGQMTKtynDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQL 260
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQ---DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 261 RHELSMKDELLQfytSAAEESEPEsicstplkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEAcQLKTETITYEEK 340
Cdd:COG1196 357 EAELAEAEEALL---EAEAELAEA----------EEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 341 EQQLvndcVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKdAQRQLTA 420
Cdd:COG1196 423 LEEL----EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA-ARLLLLL 497
|
250
....*....|.
gi 2024374521 421 ELRELEDKYAE 431
Cdd:COG1196 498 EAEADYEGFLE 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-462 |
1.50e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 219 ERDLELAARIgQSLlKKNKSLTE--RNEFLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 281
Cdd:COG4913 191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 282 EpesicstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANIQIAN 361
Cdd:COG4913 269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 362 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 429
Cdd:COG4913 335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270
....*....|....*....|....*....|...
gi 2024374521 430 AECMEMLHEAQEELKNLRNKtmPNAVSRRYHSL 462
Cdd:COG4913 415 RDLRRELRELEAEIASLERR--KSNIPARLLAL 445
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-447 |
6.35e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 223 ELAARIGQSLLK---------KNKSLTERNEFLEEQVEHIREEVSQLRHELSMkdellqfYTSAAEESEPESicstplkr 293
Cdd:COG3206 148 ELAAAVANALAEayleqnlelRREEARKALEFLEEQLPELRKELEEAEAALEE-------FRQKNGLVDLSE-------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 294 nESSSSVQNyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCV-----KELRDANIQIANISEELAK 368
Cdd:COG3206 213 -EAKLLLQQ---LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTP 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024374521 369 KTEDAARQQEEITHLLSQIVDLQKKAKAcAVENEelvqhLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLR 447
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRILA-SLEAE-----LEALQAREASLQAQLAQLEARLAE----LPELEAELRRLE 357
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
304-449 |
9.03e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 304 FHLDSLQKKLKDLEEENVVLRSEACQLKTEtITYEEKEQQLVNdcvKELRDANIQIANISEELAKKTEDAARQQEEITHL 383
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEE-LEQARSELEQLE---EELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024374521 384 LSQIVDLQKkakacavENEELVQhlgaakdAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:COG4372 114 QEELEELQK-------ERQDLEQ-------QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
135-446 |
1.06e-06 |
|
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: 53.05 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 135 PEVEIISLLEEQLPHYKLRAdtiyGYDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVgqmtktyndidaVTRL 214
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLA----CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL------------QLTL 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 215 LEEKERDLELAARIGQsllkknKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEP--ESICstplk 292
Cdd:TIGR00618 656 TQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRefNEIE----- 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 293 rNESSSSVQNY-FHLDSLQKKLKDLEEEnvvlRSEACQLKTETitYEEKEQQLVndcvkelrdANIQIANISEELAKKTE 371
Cdd:TIGR00618 725 -NASSSLGSDLaAREDALNQSLKELMHQ----ARTVLKARTEA--HFNNNEEVT---------AALQTGAELSHLAAEIQ 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 372 DAARQQEEITHLLSQI-VDLQKKAK----ACAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAECMEMLHEAQEEL 443
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLeAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQLTQEQ 868
|
...
gi 2024374521 444 KNL 446
Cdd:TIGR00618 869 AKI 871
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-446 |
1.48e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 133 NLPEVEIISLlEEQLPHYKLRADTIYgyDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIdavt 212
Cdd:TIGR04523 120 NKLEVELNKL-EKQKKENKKNIDKFL--TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI---- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 213 rllEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEE--SEPESIcSTP 290
Cdd:TIGR04523 193 ---KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkDEQNKI-KKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 291 LKRNEsSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQ-----LKTETITYEEKEQQLVNDCV---KELRDANIQIANI 362
Cdd:TIGR04523 269 LSEKQ-KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 363 SEELAKKTEDAARQQEEITHLLSQIVDLQKkakacavENEELvqhlgaaKDAQRQLTAELRELEDKYAECMEMLHEAQEE 442
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKK-------ENQSY-------KQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
....
gi 2024374521 443 LKNL 446
Cdd:TIGR04523 414 IKKL 417
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-457 |
1.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 180 TTEQIEETLKYFLLCAERVgqmtKTYNDIDAvtrLLEEKER-DLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVS 258
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH----ELYEEAKA---KKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 259 QLRHELSMKDELLQFYTSAAEESepeSICSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEACQLktETITY 337
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 338 EEKEQQLVNDCVKELRDANIQIANIS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQR 416
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024374521 417 QLTAELRELEDKYAECMEMLHEAQEELKNLRNK--TMPNAVSR 457
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKE 613
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
213-480 |
2.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 213 RLLEEKERdlelaARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEesepesicstpLK 292
Cdd:PRK03918 443 RELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----------LK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 293 RNESSSSVqnyFHLDSLQKKLKDLEEenvvLRSEACQLKTETITYEEKEQQLvNDCVKELRDANIQIANISEELAK---- 368
Cdd:PRK03918 507 ELEEKLKK---YNLEELEKKAEEYEK----LKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAEllke 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 369 --------KTEDAARQQE---------EITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 431
Cdd:PRK03918 579 leelgfesVEELEERLKElepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024374521 432 cmemlheaqEELKNLRNKTMpnAVSRRYHSL--GLFPMDSLAAEIEGSMRK 480
Cdd:PRK03918 659 ---------EEYEELREEYL--ELSRELAGLraELEELEKRREEIKKTLEK 698
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
176-448 |
2.38e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 176 NIDLTTEQIEETLKYFLlcaervGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIRE 255
Cdd:TIGR04523 458 NLDNTRESLETQLKVLS------RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 256 EVSQLRHELS-MKDELLQFYTSAAEESEPESICStplKRNESSSSVQNYFHLDS----LQKKLKDLEEENVVLRSEacqL 330
Cdd:TIGR04523 532 EKKEKESKISdLEDELNKDDFELKKENLEKEIDE---KNKEIEELKQTQKSLKKkqeeKQELIDQKEKEKKDLIKE---I 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 331 KTETITYEEKEQQLvNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVE---------- 400
Cdd:TIGR04523 606 EEKEKKISSLEKEL-EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKiddiielmkd 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2024374521 401 -NEELVQHLgaAKDAQRQL-TAELRELEDKYAECMEMLHEAQEELKNLRN 448
Cdd:TIGR04523 685 wLKELSLHY--KKYITRMIrIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
200-451 |
3.14e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 200 QMTKTYNDIDAVTRLLEEKERDL--------ELAARIgQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHElsmKDELL 271
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRdelneelkELAEKR-DELNAQVKELREEAQELREKRDELNEKVKELKEE---RDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 272 QFYTSAAEESEPesicstplKRNESSSSVQNYFHLDSLQKKLKDLEEEnvvlrseacqLKTETITyEEKEQQLVNdcvke 351
Cdd:COG1340 85 EKLNELREELDE--------LRKELAELNKAGGSIDKLRKEIERLEWR----------QQTEVLS-PEEEKELVE----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 352 lrdaniQIANISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKD------------------ 413
Cdd:COG1340 141 ------KIKELEKEL-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEemielykeadelrkeade 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2024374521 414 AQRQLT---AELRELEDKYAECMEMLHEAQEELKNLRNKTM 451
Cdd:COG1340 214 LHKEIVeaqEKADELHEEIIELQKELRELRKELKKLRKKQR 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-474 |
3.67e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 182 EQIEETLKYFLLcaERVGQMTKTYndidavtRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLR 261
Cdd:PRK03918 506 KELEEKLKKYNL--EELEKKAEEY-------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 262 HELsmkdELLQFYTSAAEESEPESICSTPLKRNESSSSVQNyfhLDSLQKKLKDLEEEnvvlrseacqlktetITYEEKE 341
Cdd:PRK03918 577 KEL----EELGFESVEELEERLKELEPFYNEYLELKDAEKE---LEREEKELKKLEEE---------------LDKAFEE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 342 QQLVNDCVKELRDaniQIanisEELAKK--TEDAARQQEEITHLLSQIVDLQKkakacavENEELVQHLGAAKDAQRQLT 419
Cdd:PRK03918 635 LAETEKRLEELRK---EL----EELEKKysEEEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKLK 700
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024374521 420 AELRELEdKYAECMEMLHEAQEELKNLRNKTmpnavsRRYHSL----GLFPMDSLAAEI 474
Cdd:PRK03918 701 EELEERE-KAKKELEKLEKALERVEELREKV------KKYKALlkerALSKVGEIASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
166-449 |
5.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 166 LHTPLISPDANIDLTTEQIEEtlkyfllCAERVGQMTKTYNDIDAVTRLLEEKERDLE-LAARIGQSLLKKNKSLTERNE 244
Cdd:PRK02224 204 LHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELEtLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 245 F------LEEQVEHIREEVSQLRHELSMKD------ELLQFYTSAAEESEPESI--CSTPLKRNESSSsvqnyfhlDSLQ 310
Cdd:PRK02224 277 LaeevrdLRERLEELEEERDDLLAEAGLDDadaeavEARREELEDRDEELRDRLeeCRVAAQAHNEEA--------ESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 311 KKLKDLEEENVVLRSEACQLKTE------TITYEEKEQQLVNDCVKELR----DANIQIANISEELAKKTEDAARQQEEI 380
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESEleeareAVEDRREEIEELEEEIEELRerfgDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 381 THL---LSQIVDLQKKAKA---------CA--VENEELVQHLGAAKDAQRQLTAELRELEDKYA------ECMEMLHEAQ 440
Cdd:PRK02224 429 AELeatLRTARERVEEAEAlleagkcpeCGqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEeveerlERAEDLVEAE 508
|
....*....
gi 2024374521 441 EELKNLRNK 449
Cdd:PRK02224 509 DRIERLEER 517
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
239-426 |
6.13e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 239 LTERNEFLEEQVEHIREEVSQLRHELSMKDELLQfytsaAEESEPESicstplKRNESSSSVQNyfhLDSLQKKLKDLEE 318
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELE-----QLEEELEQ------ARSELEQLEEE---LEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 319 ENVVLRSEACQLKTETITYEEKEQQLvndcVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACA 398
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180
....*....|....*....|....*...
gi 2024374521 399 VENEELVQHlgaakDAQRQLTAELRELE 426
Cdd:COG4372 171 QELQALSEA-----EAEQALDELLKEAN 193
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
215-449 |
7.00e-06 |
|
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: 49.18 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 215 LEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELS----MKDELlqfytsaaeesepESICSTp 290
Cdd:pfam09728 13 LDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailAKSKL-------------EKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 291 lkrnessssvqnyfhldsLQKKLKDLEEENVVLRSEACQLKTETItyeEKEQQLVND---CVKELRDANIQIANISEELA 367
Cdd:pfam09728 79 ------------------LQKQNKKLKEESKKLAKEEEEKRKELS---EKFQSTLKDiqdKMEEKSEKNNKLREENEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 368 KKTEDAARQQEeithLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEM---LHEAQEELK 444
Cdd:pfam09728 138 EKLKSLIEQYE----LRELHFEKLLKTK-------ELEVQLAEAKLQQATEEEEKKAQEKEVAKARELkaqVQTLSETEK 206
|
....*
gi 2024374521 445 NLRNK 449
Cdd:pfam09728 207 ELREQ 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-449 |
7.67e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 216 EEKERDLELAARIG---QSLLKKNKslternEFLEEQVEHIREEVSQLRHELSMKDELLQfytsaAEESEPESICSTplk 292
Cdd:TIGR02169 208 EKAERYQALLKEKReyeGYELLKEK------EALERQKEAIERQLASLEEELEKLTEEIS-----ELEKRLEEIEQL--- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 293 rnessssvqnyfhLDSLQKKLKDL-EEENVVLRSEACQLKTETI----TYEEKEQQLvNDCVKELRDANIQIANISEELA 367
Cdd:TIGR02169 274 -------------LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 368 KKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQ-------LTAELRELEDKYAECMEMLHEAQ 440
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreklekLKREINELKRELDRLQEELQRLS 419
|
....*....
gi 2024374521 441 EELKNLRNK 449
Cdd:TIGR02169 420 EELADLNAA 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
350-512 |
9.22e-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: 49.38 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 350 KELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 429
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 430 AECMEML--HEAQEELKNLRNKTMPNAVSRRYHSLGLFpMDSLAAEIEGsMRKELHLDEPDSPDLAHQKRVFETVRNVNQ 507
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEE-LRADLAELAALRAELEAERAELEALLAELE 184
|
....*
gi 2024374521 508 VVKQR 512
Cdd:COG4942 185 EERAA 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
182-481 |
1.15e-05 |
|
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: 49.58 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 182 EQIEETLKYFLLCAERVGQMT-KTYNDIDAVTRLLEEKERDLELAArigqSLLKKNKSLTERNEFLEEQVEHIREEVSQL 260
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 261 RHELSMKDELLQFYtSAAEESEPESICSTPLKRNESSSSvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEK 340
Cdd:TIGR00618 548 YHQLTSERKQRASL-KEQMQEIQQSFSILTQCDNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 341 EQQLVNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLgaakdaQRQLTA 420
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE------KEQLTY 694
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024374521 421 ELRELEdkyaECMEMLHEAQEELKNLRNKTmpNAVSRRYHSLG--LFPMDSLAAEIEGSMRKE 481
Cdd:TIGR00618 695 WKEMLA----QCQTLLRELETHIEEYDREF--NEIENASSSLGsdLAAREDALNQSLKELMHQ 751
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
323-443 |
1.48e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 45.71 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 323 LRSEACQLKTETITYEEKEQQLVNDCVKELRDANIQIANISEELAKKTEDAARQQ---EEITHLLSQIVDLQKKAKACAV 399
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQalrEELNELKAEIAELKAEAESAKA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2024374521 400 ENEELVQHLGAAKDaqrQLTAELRELEDKYAECME---MLHEAQEEL 443
Cdd:pfam07926 86 ELEESEESWEEQKK---ELEKELSELEKRIEDLNEqnkLLHDQLESL 129
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
201-449 |
1.54e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 201 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQ--FYTSAA 278
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQeeIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 279 EESEPESICSTPLKRNESSSSVQNYfhLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQLVNDCVKELRDANIQ 358
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEEEKEKKL--QEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 359 IANISEELAKKTEDAARQQEEIThllsQIVDLQKKAKAcavENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 438
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEE----EEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250
....*....|.
gi 2024374521 439 AQEELKNLRNK 449
Cdd:pfam02463 407 AQLLLELARQL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
208-456 |
2.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 208 IDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREE--VSQLRHELSMKDELLQfytsAAEESEPEs 285
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELE----RLDASSDD- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 286 icstplkrnessssvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCvKELRDANIQIANIS-- 363
Cdd:COG4913 687 --------------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLArl 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 364 ------EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEEL-----------VQHLGAAKDAQRQLTAELRELE 426
Cdd:COG4913 746 elrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPEYLALLDRLE 825
|
250 260 270
....*....|....*....|....*....|
gi 2024374521 427 DkyaecmEMLHEAQEELKNLRNKTMPNAVS 456
Cdd:COG4913 826 E------DGLPEYEERFKELLNENSIEFVA 849
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
254-451 |
2.27e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.70 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 254 REEVSQLRHELsMKDE--LLQFYTSAAEEsepesicsTPLKRNESSSSVQNYFHLDS----------LQKKLKDLEEENV 321
Cdd:smart00787 83 RDLFKEIEEET-LINNppLFKEYFSASPD--------VKLLMDKQFQLVKTFARLEAkkmwyewrmkLLEGLKEGLDENL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 322 -VLRSEACQLKtetityeeKEQQLVNDCVKELRDANI-------QIANISEELAK-KTEDAARQQEEITHLLSQIVDLQK 392
Cdd:smart00787 154 eGLKEDYKLLM--------KELELLNSIKPKLRDRKDaleeelrQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIKVK 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024374521 393 KAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEM-LHEA---QEELKNLRNKTM 451
Cdd:smart00787 226 KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIeklKEQLKLLQSLTG 288
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
306-462 |
2.33e-05 |
|
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: 46.84 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLKTEtITYEEKEQQLVNdcvKELRDANIQIANISEEL--AKKTEDAARQQEEITHL 383
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLE---LEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 384 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRN---KTMPNAVSRRYH 460
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREelaAKIPPELLALYE 181
|
..
gi 2024374521 461 SL 462
Cdd:COG1579 182 RI 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
210-446 |
2.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 210 AVTRLLEEKERDLE-LAARIGQsllKKNKSL--------TERNEfLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEE 280
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLherlngleSELAE-LDEEIERYEEQREQARETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 281 SEP---------ESICSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEAcqlktetiTYEEKEQQLVNDCVKE 351
Cdd:PRK02224 253 LETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEA--------GLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 352 LRDaniQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 431
Cdd:PRK02224 319 LED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250
....*....|....*
gi 2024374521 432 CMEMLHEAQEELKNL 446
Cdd:PRK02224 396 LRERFGDAPVDLGNA 410
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
214-429 |
3.08e-05 |
|
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: 47.38 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 214 LLEEKERDLELAARI-----GQSLLKKNKSLterNEFL-EEQVEHIREEVSQLRHEL-----SMKDELLQFYTSAAEEse 282
Cdd:pfam04108 75 ALERLEETLDKLRNTpvepaLPPGEEKQKTL---LDFIdEDSVEILRDALKELIDELqaaqeSLDSDLKRFDDDLRDL-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 283 pESICSTPLKRNESSSSVQNYFH-LDSLQKKLKDLeeenvvLRS-----EACQL--------KTETITYEEKEQQLVNDC 348
Cdd:pfam04108 150 -QKELESLSSPSESISLIPTLLKeLESLEEEMASL------LESltnhyDQCVTavklteggRAEMLEVLENDARELDDV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 349 VKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDK 428
Cdd:pfam04108 223 VPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREF 302
|
.
gi 2024374521 429 Y 429
Cdd:pfam04108 303 Y 303
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
293-449 |
4.45e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 293 RNESS-SSVQNYFH---LDSLQKKLKDLEEENVVLRSEACQlktetiTYEEKEQQLvndcvKELRDANIQIANISEELAK 368
Cdd:COG4717 31 PNEAGkSTLLAFIRamlLERLEKEADELFKPQGRKPELNLK------ELKELEEEL-----KEAEEKEEEYAELQEELEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 369 KTEDAARQQEEITHLLSQIVDLQKkakacAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLRN 448
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEA 170
|
.
gi 2024374521 449 K 449
Cdd:COG4717 171 E 171
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
247-449 |
4.82e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 247 EEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESicstpLKRNESSSSVQNYFHLDSLQKKLKDLEEenvvLRS 325
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERAEE----LRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 326 EACQLKTETITYEEKEQQL---VNDCVKELRDANIQIANISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENE 402
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024374521 403 ELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
202-451 |
6.49e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 202 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTeRNEFLEEQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 280
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI-KLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 281 SEPE-SICSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETIT-YEEKEQQL---------VNDCV 349
Cdd:PRK03918 537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 350 KELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcaVENEELVQHLGAAKDAQRQLTAELRELEDKY 429
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260
....*....|....*....|..
gi 2024374521 430 AECMEMLHEAQEELKNLRNKTM 451
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKK 711
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
331-449 |
7.05e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 331 KTETITYEEKEQQLVNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGA 410
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024374521 411 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
350-512 |
1.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 350 KELRDANIQIanisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQR--QLTAELRELED 427
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 428 KYAEcmemLHEAQEELKNLRNKtmpnavsrryhslglfpMDSLAAEIEgsmRKELHLDE-PDSPDLAHQKRVFETVRNVN 506
Cdd:COG4717 147 RLEE----LEERLEELRELEEE-----------------LEELEAELA---ELQEELEElLEQLSLATEEELQDLAEELE 202
|
....*.
gi 2024374521 507 QVVKQR 512
Cdd:COG4717 203 ELQQRL 208
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
226-487 |
1.05e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 226 ARIgQSLLKKNKSLTERnefleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESICSTPLK-RNE-SSSSVQNY 303
Cdd:PLN02939 150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 304 FHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNdCVKE--LRDANIQianiseELAKKTEDAarqQEEIt 381
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 382 hllSQIVDLQKKAKACAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA-------------QEELKN 445
Cdd:PLN02939 288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEAnvskfssykvellQQKLKL 362
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024374521 446 LR------NKTMPNAVSRRYHSLGLFpMDSLAAEIEGSMRKElhLDEP 487
Cdd:PLN02939 363 LEerlqasDHEIHSYIQLYQESIKEF-QDTLSKLKEESKKRS--LEHP 407
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
291-425 |
1.36e-04 |
|
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: 43.05 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 291 LKRNES-SSSVQNyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVndcvKELRDANIQIANISEELAKK 369
Cdd:pfam10473 12 LKESERkADSLKD--KVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSEKENL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024374521 370 TEDAARQQEEITHLLSQIVDLQKKAKacaVENEELVQHLGAAKDAQRQLTAELREL 425
Cdd:pfam10473 86 TKELQKKQERVSELESLNSSLENLLE---EKEQEKVQMKEESKTAVEMLQTQLKEL 138
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-446 |
1.42e-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: 45.53 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 248 EQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsicstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEA 327
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ------LAALERR--------IAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 328 CQLKTETITYEEKEQQLVNDCVKELR------------------DAN------IQIANISEELAKKTEDAARQQEEITHL 383
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRalyrlgrqpplalllspeDFLdavrrlQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024374521 384 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 446
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
196-449 |
1.59e-04 |
|
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: 45.62 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 196 ERVGQMTKTYNDIdaVTRLLEEKERDL----ELAARIgqSLLKKNKSLTERNEFL---EEQVEHIREEVSQLR--HELSM 266
Cdd:pfam06160 45 EKFEEWRKKWDDI--VTKSLPDIEELLfeaeELNDKY--RFKKAKKALDEIEELLddiEEDIKQILEELDELLesEEKNR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 267 K--DELLQFYtsaaeesepESICSTPLKRNESSSSVqnyfhLDSLQKKLKDLEEE-----------------NVVLrsea 327
Cdd:pfam06160 121 EevEELKDKY---------RELRKTLLANRFSYGPA-----IDELEKQLAEIEEEfsqfeeltesgdylearEVLE---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 328 cQLKTETITYEEK-EQ--QLVNDCVKELRDA---------------------NI--QIANISEELAK--------KTEDA 373
Cdd:pfam06160 183 -KLEEETDALEELmEDipPLYEELKTELPDQleelkegyremeeegyalehlNVdkEIQQLEEQLEEnlallenlELDEA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 374 ARQQEEITHLLSQIVDL---QKKAKACAVEN-EELVQHLGAAKDAQRQLTAELRELEDKY---AECMEMLHEAQEELKNL 446
Cdd:pfam06160 262 EEALEEIEERIDQLYDLlekEVDAKKYVEKNlPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEEL 341
|
...
gi 2024374521 447 RNK 449
Cdd:pfam06160 342 EKR 344
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
213-410 |
1.88e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 213 RLLEEKERDLELA--ARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesicstp 290
Cdd:COG1579 8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 291 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLrseacqlktetityEEKEQQLvndcVKELRDANIQIANISEELAKKT 370
Cdd:COG1579 80 ----EQLGNVRNNKEYEALQKEIESLKRRISDL--------------EDEILEL----MERIEELEEELAELEAELAELE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024374521 371 EDAARQQEEithLLSQIVDLQKKAKACAVENEELVQHLGA 410
Cdd:COG1579 138 AELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
200-449 |
1.96e-04 |
|
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: 45.81 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 200 QMTKTYNDIDAVTRLLEEKERDLEL----AARIGQSLLKKNKSLTER-------------NEFLEEQVEHIREEVSQLRH 262
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKelasLEQNKNHINNELESKEEQlssyedklfdvcgSQDEESDLERLKEEIEKSSK 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 263 ELSMKDELLQFYTSAAEESEPESICSTPL---------KRNESSSSVQNYF-----HLDSLQKKLKDLEEEnvvlrseac 328
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVcqrvfqteaELQEFISDLQSKLrlapdKLKSTESELKKKEKR--------- 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 329 qlKTETITYEEKEQQLVNDCVKELRDANIQIANISEELAKKTEDAARQQEeithLLSQIVDLQKKAKACAVENEELVQHL 408
Cdd:TIGR00606 725 --RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTDVTIMERFQ 798
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2024374521 409 GAAKDAQR---QLTAELR--ELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:TIGR00606 799 MELKDVERkiaQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
306-444 |
2.32e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANIQ-------------------------IA 360
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 361 NISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 440
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....
gi 2024374521 441 EELK 444
Cdd:COG3883 206 AAAE 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
211-449 |
2.80e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 211 VTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLE---EQVEHIREEVSQLRHELsmkdELLQFYTSAAEESepesic 287
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKEL----ESLEGSKRKLEEK------ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 288 stpLKRNESSssvqnyfhLDSLQKKLKDLEEenVVLRSEacQLKTETITYEEKEqQLVNDCVKELRDANIQIANISEELA 367
Cdd:PRK03918 261 ---IRELEER--------IEELKKEIEELEE--KVKELK--ELKEKAEEYIKLS-EFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 368 ---KKTEDAARQQEEITHLLSQIVDLQKKaKACAVENEELVQHLGAAKDAQRQLTAELR-----ELEDKYAECMEMLHEA 439
Cdd:PRK03918 325 gieERIKELEEKEERLEELKKKLKELEKR-LEELEERHELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEI 403
|
250
....*....|
gi 2024374521 440 QEELKNLRNK 449
Cdd:PRK03918 404 EEEISKITAR 413
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
212-446 |
3.10e-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: 44.78 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 212 TRLLEEKERDLELAARIGQSLLKKNKSL-TERNEFLEE--QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsics 288
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALeSENAELQAElrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 289 tplkRNESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEACQLK-----TETITYEEKEQQL-VNDCVKELRDaniQIANI 362
Cdd:pfam01576 431 ----LAEKLSKLQS--ELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLnLSTRLRQLED---ERNSL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 363 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAK--ACAVENEElvqhlGAAKDAQRQLTAELRELEDKyAECMEMLHEA- 439
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEedAGTLEALE-----EGKKRLQRELEALTQQLEEK-AAAYDKLEKTk 575
|
250
....*....|
gi 2024374521 440 ---QEELKNL 446
Cdd:pfam01576 576 nrlQQELDDL 585
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
350-449 |
3.18e-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: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 350 KELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQH-------LGAAKDAqRQLTA-- 420
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqLGNVRNN-KEYEAlq 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 2024374521 421 --------ELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:COG1579 96 keieslkrRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
209-443 |
3.21e-04 |
|
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: 44.83 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 209 DAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESICS 288
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 289 TPLKRNESSSSVQNyfhLDSLQKKLKDLEEEnvvlrseacqlktetitYEEKEQQLVNDCVKElrdaniqIANISEELAK 368
Cdd:pfam12128 349 LPSWQSELENLEER---LKALTGKHQDVTAK-----------------YNRRRSKIKEQNNRD-------IAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 369 KTEDAARQQEEITHLL----SQIVDLQKKAKACAVENEE-LVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEEL 443
Cdd:pfam12128 402 IREARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYrLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQ 480
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
306-448 |
4.19e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 42.58 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRseACQLKTETI--TYEEKE---QQLVNDCVKELRDANIQIANiSEELAKKTEDAARQQE-E 379
Cdd:pfam15619 20 LAELQSKLEELRKENRLLK--RLQKRQEKAlgKYEGTEselPQLIARHNEEVRVLRERLRR-LQEKERDLERKLKEKEaE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 380 ITHLLSQIVDLQK--KAKACAvENEELVQHLGAA-----------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 446
Cdd:pfam15619 97 LLRLRDQLKRLEKlsEDKNLA-EREELQKKLEQLeakledkdekiQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKIL 175
|
..
gi 2024374521 447 RN 448
Cdd:pfam15619 176 QE 177
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
215-447 |
5.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 215 LEEKERDlELAARIGqslLKKNKSLTERNEFLE--EQVEHIREEVSQLRHELSMK---DELLQFYTSAAEESEPESIcst 289
Cdd:COG4717 316 LEEEELE-ELLAALG---LPPDLSPEELLELLDriEELQELLREAEELEEELQLEeleQEIAALLAEAGVEDEEELR--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 290 plkrnessSSVQNYFHLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQlvndcvKELRDANIQIANISEELAKK 369
Cdd:COG4717 389 --------AALEQAEEYQELKEELEELEEQ---LEELLGELEELLEALDEEELE------EELEELEEELEELEEELEEL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 370 TEDAARQQEEITHLlsqivdlqkkakacavENEELVQHLgaaKDAQRQLTAELRELEDKYAECM---EMLHEAQEELKNL 446
Cdd:COG4717 452 REELAELEAELEQL----------------EEDGELAEL---LQELEELKAELRELAEEWAALKlalELLEEAREEYREE 512
|
.
gi 2024374521 447 R 447
Cdd:COG4717 513 R 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-475 |
5.71e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 182 EQIEETLKYFLLCAERVGQMTKTY----NDIDAVTRLLEEKERDLELAARIG--------QSLLKKNKSLTERNEFLEEQ 249
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELreleEELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 250 VEHIREEVSQLRHEL-SMKDELLQFY------------------------------------------------------ 274
Cdd:COG4717 215 LEEAQEELEELEEELeQLENELEAAAleerlkearlllliaaallallglggsllsliltiagvlflvlgllallfllla 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 275 -TSAAEESEPESICSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETItyEEKEQQLVNDCVKELR 353
Cdd:COG4717 295 rEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 354 DANIQIANIS--EELAKKTEdAARQQEEITHLLSQIvDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 431
Cdd:COG4717 373 AALLAEAGVEdeEELRAALE-QAEEYQELKEELEEL-EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2024374521 432 CMEMLHEAQEELKNLRNKtmpNAVSRRYHSLglfpmDSLAAEIE 475
Cdd:COG4717 451 LREELAELEAELEQLEED---GELAELLQEL-----EELKAELR 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
306-449 |
6.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEE-NVVLRseACQLKTEtitYEEKEQQLVndcVKELRDANIQIANISEELAKKTEDAARQQEEITHLL 384
Cdd:COG1196 195 LGELERQLEPLERQaEKAER--YRELKEE---LKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024374521 385 SQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
173-450 |
6.46e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 173 PDANIDLTTEQIEETLKyflLCAERVGQMtktynDIDAVtrllEEKERDLElaARIGQ--SLLKK----NKSLTERNEFL 246
Cdd:PRK04778 250 DHLDIEKEIQDLKEQID---ENLALLEEL-----DLDEA----EEKNEEIQ--ERIDQlyDILERevkaRKYVEKNSDTL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 247 EEQVEHIREEVSQLRHELsmkDELLQFYTSAAEESEpesicstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSE 326
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEI---DRVKQSYTLNESELE----------------------SVRQLEKQLESLEKQYDEITER 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 327 acqLKTETITYEEKEQQLvNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKakacaVEN----- 401
Cdd:PRK04778 371 ---IAEQEIAYSELQEEL-EEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRY-----LEKsnlpg 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024374521 402 --EELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKT 450
Cdd:PRK04778 442 lpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEET 492
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
306-449 |
8.39e-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: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANIQIANISEELAKKTE---DAARQQ----- 377
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEE---YNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREelgERARALyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 378 -----------EEITHLLSQIVDLQKKAKAcaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 446
Cdd:COG3883 101 svsyldvllgsESFSDFLDRLSALSKIADA----DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
...
gi 2024374521 447 RNK 449
Cdd:COG3883 177 QAE 179
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
303-454 |
8.95e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 303 YFHLDSLQKKLKDLEEENVVLRSEAcQLKTETITYE------EKEQQLVNDCVKELRDANIQIANISEELAKKTEDAARQ 376
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEA-KKEAEAIKKEalleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024374521 377 QEeithllsqivDLQKKakacaveNEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNA 454
Cdd:PRK12704 102 LE----------LLEKR-------EEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEA 155
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
206-398 |
1.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 206 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELS--------MKDEL---LQFY 274
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELaelLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 275 TSAAEESEPESICS-TPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvnd 347
Cdd:COG4942 114 YRLGRQPPLALLLSpEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024374521 348 cVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACA 398
Cdd:COG4942 191 -EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
306-449 |
1.34e-03 |
|
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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHlls 385
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---LEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024374521 386 QIVDLQKKAKACAVEN--------EELVQHLGAAK---DAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 449
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
207-451 |
1.40e-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: 42.70 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 207 DIDAVTRLLEEKERDLELAArigQSLLKKNKSLTERNEFLEEQVEHIREEVSQLrhELSMKDelLQFYTSAAE------E 280
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEK---ELLEKEIERLKETIIKNNSEIKDLTNQDSVK--ELIIKN--LDNTRESLEtqlkvlS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 281 SEPESICST------PLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKtetityeEKEQQLVNdcvkELRD 354
Cdd:TIGR04523 475 RSINKIKQNleqkqkELKSKEK--------ELKKLNEEKKELEEKVKDLTKKISSLK-------EKIEKLES----EKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 355 ANIQIANISEELAKKTEDAARQQ--EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 432
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
250
....*....|....*....
gi 2024374521 433 MEMLHEAQEELKNLRNKTM 451
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIK 634
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
351-449 |
1.59e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 351 ELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcAVE--NEELvqhlgaAKDA---QRQLTAELREL 425
Cdd:COG1842 31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEkgREDL------AREAlerKAELEAQAEAL 103
|
90 100
....*....|....*....|....
gi 2024374521 426 EDKYAECMEMLHEAQEELKNLRNK 449
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESK 127
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
223-446 |
1.84e-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: 42.47 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 223 ELAARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSmkDELLQFytsaaeesepesicstplKRNESSssvqn 302
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT--EQLEQA------------------KRNKAN----- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 303 yfhldsLQKKLKDLEEENVVLRSEA---CQLKTETITYEEKEQQLVNDCVKELRDANIQianiSEELAKKTEDAARQQEE 379
Cdd:pfam01576 375 ------LEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQ----RAELAEKLSKLQSELES 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024374521 380 ITHLLSQI-VDLQKKAKACAVENEEL--VQHLGAAKDAQR-QLTAELRELEDKYAECMEMLHEAQEELKNL 446
Cdd:pfam01576 445 VSSLLNEAeGKNIKLSKDVSSLESQLqdTQELLQEETRQKlNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
301-446 |
1.99e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 301 QNYF------HLDsLQKKLKDleeenvvlrsEACQLKTEtityEEKEQQLVNDCVKE-------LRDANIQIanisEELA 367
Cdd:pfam13851 14 KNYYnditrnNLE-LIKSLKE----------EIAELKKK----EERNEKLMSEIQQEnkrltepLQKAQEEV----EELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 368 KKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLgaakdaqRQLTAELRELEDKYAecmEMLHEAQE--ELKN 445
Cdd:pfam13851 75 KQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRF-------EKVERERDELYDKFE---AAIQDVQQktGLKN 144
|
.
gi 2024374521 446 L 446
Cdd:pfam13851 145 L 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
306-449 |
2.02e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 306 LDSLQKKLKDLEEENVVLRSEACQLKTEtityeEKEQQlvndcvKELRDANIQIANISEELAKKTEDAARQQEEITHLLS 385
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE-----EKALL------KQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 386 QIVDLQKKAKAcavENEELVQHLGAA------------------KDAQRQLTAeLRELEDKYAECMEMLHEAQEELKNLR 447
Cdd:COG4942 91 EIAELRAELEA---QKEELAELLRALyrlgrqpplalllspedfLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR 166
|
..
gi 2024374521 448 NK 449
Cdd:COG4942 167 AE 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-434 |
3.11e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 182 EQIEETLKYFLLCAERV-GQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNEFLEEQVEHI------- 253
Cdd:TIGR02169 304 ASLERSIAEKERELEDAeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaet 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 254 REEVSQLRHELSM-KDELlqfytsaaeesepesicsTPLKRNES---SSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQ 329
Cdd:TIGR02169 384 RDELKDYREKLEKlKREI------------------NELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 330 LKTETITYEEKEQQLVNDCVKElrdaniqianiSEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVE------NEE 403
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKY-----------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggraVEE 514
|
250 260 270
....*....|....*....|....*....|.
gi 2024374521 404 LvqhLGAAKDAQRQLTAELRELEDKYAECME 434
Cdd:TIGR02169 515 V---LKASIQGVHGTVAQLGSVGERYATAIE 542
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
208-332 |
4.10e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 208 IDAVTRLLEEKERDLEL--AARIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYT---SAAEESE 282
Cdd:COG2433 378 IEEALEELIEKELPEEEpeAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLErelSEARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2024374521 283 PESIcstpLKRNESSSsvqnyfhLD----SLQKKLKDLEEENVVLRSEACQLKT 332
Cdd:COG2433 458 RREI----RKDREISR-------LDreieRLERELEEERERIEELKRKLERLKE 500
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
184-450 |
4.34e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 184 IEETLKYFLLCAERVGQMtKTYNDidAVTRLLEEKErDLELAARIGQSLLKKNKSltERNEFLEEQVEHIREEVSQLRHE 263
Cdd:COG5185 231 IEEALKGFQDPESELEDL-AQTSD--KLEKLVEQNT-DLRLEKLGENAESSKRLN--ENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 264 LSMKDELLQFYTSAAEESEPESICStplKRNESSSSVQNYFHldSLQKKLKDLEEENVVLRSEACQLKTETItYEEKEQQ 343
Cdd:COG5185 305 IDIKKATESLEEQLAAAEAEQELEE---SKRETETGIQNLTA--EIEQGQESLTENLEAIKEEIENIVGEVE-LSKSSEE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 344 LvNDCVKELRDANIQIANISEELAKKTEDAARQ-QEEITHLLSQIVDLQKKAKACAVENEElvqhlgaakdAQRQLTAEL 422
Cdd:COG5185 379 L-DSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEE----------VSKLLNELI 447
|
250 260
....*....|....*....|....*...
gi 2024374521 423 RELEDKYAECMEMLHEAQEELKNLRNKT 450
Cdd:COG5185 448 SELNKVMREADEESQSRLEEAYDEINRS 475
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
360-452 |
4.45e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 38.52 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 360 ANISEELAKKTEDAArqqeEITHLLSQIVDLQKKAKACAveNEELVQHLGAAKD-AQRQLTAELRELEDKYAECMEMLHE 438
Cdd:PRK08476 41 ASIKNDLEKVKTNSS----DVSEIEHEIETILKNAREEA--NKIRQKAIAKAKEeAEKKIEAKKAELESKYEAFAKQLAN 114
|
90
....*....|....
gi 2024374521 439 AQEELKNLRNKTMP 452
Cdd:PRK08476 115 QKQELKEQLLSQMP 128
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
214-511 |
4.48e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 214 LLEEKERDLELaarigqsLLKKNKSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLqfytSAAEE--SEPESICSTpL 291
Cdd:pfam10174 388 MLDVKERKINV-------LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----TTLEEalSEKERIIER-L 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 292 KRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKE---LRDANIQIANISEEL-- 366
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdskLKSLEIAVEQKKEECsk 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 367 -------AKKTEDAARQQEEITHLLSQI-VDLQKKAKACAVENEELVQHLGAAKDAQRQltaelRELEDKYAECMEMLHE 438
Cdd:pfam10174 536 lenqlkkAHNAEEAVRTNPEINDRIRLLeQEVARYKEESGKAQAEVERLLGILREVENE-----KNDKDKKIAELESLTL 610
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024374521 439 AQ--EELKNLRNKTMPNAVSRRyhslglfpmdslaaeiEGSMRKELHLDEPDSPDLAHQKRVFETVRNVNQVVKQ 511
Cdd:pfam10174 611 RQmkEQNKKVANIKHGQQEMKK----------------KGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ 669
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
237-443 |
4.67e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 237 KSLTERNEFLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAeesepESICST--PLKRNESSSSVQ-------NYFHLD 307
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAY-----QLVRKIagEVSRSEAWDVARellrrlrEQRHLA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 308 ----SLQKKLKDLE-----EENVV-LRSEACQLKTETITYEEKEQQLvndcvkeLRDANIQIANISEELAKKTEDAARQQ 377
Cdd:PRK04863 513 eqlqQLRMRLSELEqrlrqQQRAErLLAEFCKRLGKNLDDEDELEQL-------QEELEARLESLSESVSEARERRMALR 585
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024374521 378 EEITHLLSQIVDLQKKAKACAVENEELVQ---HLGAAKDAQRQLTA----------ELRELEDKYAECMEMLHEAQEEL 443
Cdd:PRK04863 586 QQLEQLQARIQRLAARAPAWLAAQDALARlreQSGEEFEDSQDVTEymqqllererELTVERDELAARKQALDEEIERL 664
|
|
| FCH_F-BAR |
cd07610 |
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ... |
227-434 |
5.14e-03 |
|
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.
Pssm-ID: 153294 [Multi-domain] Cd Length: 191 Bit Score: 39.25 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 227 RIGQSLLKKNKSLTERNEFLEEQVEhIREEVSQLRHELSMKdellqfyTSAAEESEPESICSTPLKRNESSSSVQNYfHL 306
Cdd:cd07610 4 LLEKRTELGLDLLKDLREFLKKRAA-IEEEYAKNLQKLAKK-------FSKKPESGKTSLGTSWNSLREETESAATV-HE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 307 DSLQKKLKDLEEenvvlrseacqlKTETITyEEKEQQLVNdCVKELRDANIQIANISEELAKKTEDAARQQEEIThLLSQ 386
Cdd:cd07610 75 ELSEKLSQLIRE------------PLEKVK-EDKEQARKK-ELAEGEKLKKKLQELWAKLAKKADEEYREQVEKL-NPAQ 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024374521 387 IVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME 434
Cdd:cd07610 140 SEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELE 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
214-447 |
6.55e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 214 LLEEKERDLELAARIGQsLLKKNKSLTERNEFLEEQVEHIRE---EVSQLRHELSMK----DELLQFYTSAAEESEPesi 286
Cdd:pfam01576 14 LQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARkqelEEILHELESRLEEEEE--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 287 CSTPLKrNESSSSVQNYF----HLD--------------SLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDC 348
Cdd:pfam01576 90 RSQQLQ-NEKKKMQQHIQdleeQLDeeeaarqklqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 349 VKELRDA-------NIQIANIS--EELAKKTEDAARQQE--------EITHLLSQIVDLQKKAKACAVENEELVQHLGAA 411
Cdd:pfam01576 169 AEEEEKAkslsklkNKHEAMISdlEERLKKEEKGRQELEkakrklegESTDLQEQIAELQAQIAELRAQLAKKEEELQAA 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 2024374521 412 KDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 447
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESER 284
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
214-426 |
6.66e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 214 LLEEKERDLELaarIGQSLLKKNKSLTERNEFLEEQVEHIREEVSQLR--HELSMKDELLQFYTSAAEESEPESICSTPL 291
Cdd:pfam17045 50 TLERKHKEIGL---LRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKrsYEKLQRKQLKEAREEAKSREEDRSELSRLN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 292 KRNESsssvqnyFHLDSL---------QKKLKDLEEENVVLrSEACQLktetITYEEKEQQLVN-DCVKELRDANIQiaN 361
Cdd:pfam17045 127 GKLEE-------FRQKSLeweqqrlqyQQQVASLEAQRKAL-AEQSSL----IQSAAYQVQLEGrKQCLEASQSEIQ--R 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024374521 362 ISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELE 426
Cdd:pfam17045 193 LRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQVLQNELMELK 257
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
339-416 |
9.07e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.39 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024374521 339 EKEQQLVNDCVKELRDANIQIANISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHL--GAAKDAQR 416
Cdd:cd22887 7 QELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWmaKKQQEADK 86
|
|
| |
