|
Name |
Accession |
Description |
Interval |
E-value |
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
419-459 |
3.20e-13 |
|
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.
Pssm-ID: 462805 [Multi-domain] Cd Length: 41 Bit Score: 63.51 E-value: 3.20e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767987898 419 SRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 459
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-445 |
3.21e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 173 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 243
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 244 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 320
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 321 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 382
Cdd:TIGR02168 836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767987898 383 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 445
Cdd:TIGR02168 916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-439 |
3.37e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 162 EEDIADKVVFLeRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmEREKS 241
Cdd:COG1196 221 ELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 242 IEIENLQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 321
Cdd:COG1196 295 AELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 322 QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 401
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*...
gi 767987898 402 LFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 439
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-397 |
7.30e-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: 61.61 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 203 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 282
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 283 LDEIESLTLR---LSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHS 359
Cdd:TIGR02168 294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 767987898 360 RAResELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 397
Cdd:TIGR02168 373 RLE--ELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-401 |
2.03e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 194 RQENLQLVHRANA---LEEQLKEQE--LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCL 268
Cdd:TIGR02168 666 AKTNSSILERRREieeLEEKIEELEekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 269 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 348
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767987898 349 SSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 401
Cdd:TIGR02168 826 LESL-------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-391 |
4.70e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 167 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRAcEMVLEETRRQKEllckmereksiEIEN 246
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 247 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ------------ENKRRMGDRLSH----- 309
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREieqkl 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 310 ------------ERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSsmgLQEYHSRARESELEQEVRRLKQDN 377
Cdd:TIGR02169 822 nrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQL 898
|
250
....*....|....
gi 767987898 378 RNLKEQNEELNGQI 391
Cdd:TIGR02169 899 RELERKIEELEAQI 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-432 |
1.02e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 163 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREK 240
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 241 SIEIENLQTRL----QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRrmgdrlshERHQFQR 316
Cdd:COG1196 322 EEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------ELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 317 DKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 396
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 767987898 397 QGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEE 432
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-432 |
2.20e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 166 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELRACEMVLEETRRQKEL---------LCKM 236
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELyalaneisrLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 237 EREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLS---HERHQ 313
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 314 FQRDKEATQELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 391
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLeaRLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767987898 392 ITLSIQGAKSlfSTAFSESLAAEISSVSRDELMEAIQKQEE 432
Cdd:TIGR02168 464 EELREELEEA--EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-438 |
6.56e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 163 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELracEMVLEETRRQKELLCKMEREKSI 242
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 243 E-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqrd 317
Cdd:TIGR02168 785 EeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 318 kEATQELIEDLRKQLEHL----------------QLLKLEAEQRRGRSSSMGLQEYHSRARES---------ELEQEVRR 372
Cdd:TIGR02168 862 -EELEELIEELESELEALlnerasleealallrsELEELSEELRELESKRSELRRELEELREKlaqlelrleGLEVRIDN 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987898 373 LKQdnrNLKEQneelngQIITLSIQGAKSLFSTAFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLQ 438
Cdd:TIGR02168 941 LQE---RLSEE------YSLTLEEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERYD 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-376 |
1.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 166 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQlkeqeLRACEMVLEETRRQKELlckmeREKSIEIE 245
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQER-----REALQRLAEYSWDEIDV-----ASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 246 NLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQR-DKEATQEL 324
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767987898 325 IEDLRKQLEHLQLLKLEAEQRRG-RSSSMGLQEYHSRAREsELEQEVRRLKQD 376
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENlEERIDALRARLNRAEE-ELERAMRAFNRE 799
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
174-394 |
2.39e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 174 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvlEETRRQKELLCKMEREKSIEIEnlqtRLQQ 253
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVE----RLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 254 LDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE 333
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987898 334 HlqllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNlKEQNEELNGQIITL 394
Cdd:pfam17380 548 M-------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
109-387 |
3.98e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 109 NRLEDLSARLSDLEMNSPTKRLSSKKVARyLHQSGA------LTMEALEDPSPELMEgpeedIADKVVFLERrvlELEKD 182
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQKLQR-LHQAFSqfvgghLAVAFAPDPEAELAA-----LRQRRSELER---ELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 183 TAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEE-------TRRQKELLCKMEREKSI------E 243
Cdd:COG3096 856 RAQEQQLRQQLDQlkEQLQLLNKllpqANLLADETLADRLEELREELDAaqeaqafIQQHGKALAQLEPLVAVlqsdpeQ 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 244 IENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDE----IESLTLRLSEEQENKRRMGDRLSHERHQFQ 315
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlNEKLRARLEQAEEARREAREQLRQAQAQYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 316 rdkEATQELI----------EDLRKQLEHLQLLKL----EAEQR-RGRSSSMGLQEYHSRAR-----------ESELEQE 369
Cdd:COG3096 1016 ---QYNQVLAslkssrdakqQTLQELEQELEELGVqadaEAEERaRIRRDELHEELSQNRSRrsqlekqltrcEAEMDSL 1092
|
330
....*....|....*...
gi 767987898 370 VRRLKQDNRNLKEQNEEL 387
Cdd:COG3096 1093 QKRLRKAERDYKQEREQV 1110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-394 |
4.21e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 162 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqKELLCKMEREKs 241
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI----EELEEKVKELK- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 242 iEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 316
Cdd:PRK03918 287 -ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767987898 317 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITL 394
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
203-391 |
5.25e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 203 RANALEEQLkeQELRACEMVLEETRRQKELLCKMeREKSIEIENLQTRLQQLDEENSELRS-----CTPCLKANIERLEE 277
Cdd:COG4913 226 AADALVEHF--DDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 278 EKQKLLDEIESLTLRLSEEQENKRRMgdRLSHERHQFQRdkeatqelIEDLRKQLEHLQLLKLEAEQRRGR--------- 348
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARleallaalg 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767987898 349 ----SSSMGLQEYHSRARE---------SELEQEVRRLKQDNRNLKEQNEELNGQI 391
Cdd:COG4913 373 lplpASAEEFAALRAEAAAllealeeelEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-367 |
5.78e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 144 ALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQ--ELRACEM 221
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 222 VLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL---TLRLSEEQE 298
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987898 299 NKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHSRARESELE 367
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
183-401 |
8.61e-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: 47.84 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 183 TAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSE 260
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 261 LRsctpclkANIERLEEEKQKLLDEI------ESLTLRLSEEQENK--------RRMGDRLSHERHQFQRDKEATQELIE 326
Cdd:COG4942 95 LR-------AELEAQKEELAELLRALyrlgrqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767987898 327 DLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 401
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-374 |
9.82e-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: 47.45 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 162 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElracemvlEETRRQKELLCKMEREKS 241
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--------EELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 242 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkqklLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 321
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767987898 322 QELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLK 374
Cdd:COG4942 198 QKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-444 |
1.12e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 195 QENLQlvhRANALEEQLKEQelracemvLEETRRQKEllcKMER--EKSIEIENLQTRLQQLDEENselrsctpcLKANI 272
Cdd:COG1196 185 EENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE---------LEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 273 ERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSM 352
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 353 GLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLsiQGAKSLFSTAFSESLAAEISsvSRDELMEAIQKQEE 432
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELLEALRAAAE 397
|
250
....*....|..
gi 767987898 433 INFRLQDYIDRI 444
Cdd:COG1196 398 LAAQLEELEEAE 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-388 |
1.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 167 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVhranALEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIEN 246
Cdd:COG4913 654 AEYSWDEIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEELEAE-----LEELEEELDELKGEIGRLEKELEQ 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 247 LQTRLQQLDEENSELRSctPCLKANIERLEEEKQKLLDE------IESLTLRLSEEQENKRRMGDRLSHERHQFQRD-KE 319
Cdd:COG4913 725 AEEELDELQDRLEAAED--LARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFNREwPA 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987898 320 ATQELIEDLRKQLEHLQLL-KLEAEqrrgrsssmGLQEYHSRARESELEQE-------VRRLKQDNRNLKEQNEELN 388
Cdd:COG4913 803 ETADLDADLESLPEYLALLdRLEED---------GLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLN 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-432 |
1.83e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 173 ERRVLELEKDTAATGEQHSRLRQENLQLVhRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQ 252
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 253 QLDEENSELRSCTPCLKANIERLEEEKQ--------KLLDEIESLTLRLSEEQENKRRMGDRLSH---ERHQFQRDKEAT 321
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKleaEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 322 QELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 399
Cdd:TIGR02169 342 EREIEEERKRRDKLTeeYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270
....*....|....*....|....*....|....*
gi 767987898 400 KSLFSTAFSESLAAEISSV--SRDELMEAIQKQEE 432
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELeeEKEDKALEIKKQEW 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-380 |
1.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 185 ATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSc 264
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 265 tpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQ 344
Cdd:COG4913 338 -----DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180 190
....*....|....*....|....*....|....*.
gi 767987898 345 RRGRsssmglqeyhSRARESELEQEVRRLKQDNRNL 380
Cdd:COG4913 413 ALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
195-391 |
2.41e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 46.96 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 195 QENLQLVHRANaleEQLKEQELRACEMVLEETRRQKELLCKMereksieienlqtRLQQLDEenselrsctpclkanIER 274
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 275 LEEEKQKLLDEIESLTLRLSEEQENK----RRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRgrsS 350
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQeklmRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAK---K 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767987898 351 SMGLQEYHSRARESELEQEVRRLKQDNR-----NLKEQNEELNGQI 391
Cdd:pfam10168 657 KMNYQRYQIAKSQSIRKKSSLSLSEKQRktikeILKQLGSEIDELI 702
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
157-351 |
4.95e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.44 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 157 LMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLC 234
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 235 KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLS-EEQENKR--RMGDRLSHER 311
Cdd:pfam19220 111 IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlLEQENRRlqALSEEQAAEL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767987898 312 HQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSS 351
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEA 230
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
191-399 |
7.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 191 SRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSI--EIENLQTRLQQLDEENSELRSCTP 266
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPElrKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 267 CLKANIERLEEEKQKLLD--EIESLTLRLSEEQENKRRMGDRLShERHQfqrDKEATQELIEDLRKQLEH-----LQLLK 339
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYT-PNHP---DVIALRAQIAALRAQLQQeaqriLASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987898 340 LEAEQRRGRSSSMG--LQEYHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 399
Cdd:COG3206 320 AELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-387 |
7.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 163 EDIADKVVFLERRVLELEKdtaaTGEQHSRLRQeNLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREksi 242
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK----VLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 243 eIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGD-------RLSHERHQFQ 315
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylELKDAEKELE 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987898 316 RDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGL---QEYHSRARES--ELEQEVRRLKQDNRNLKEQNEEL 387
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysEEEYEELREEylELSRELAGLRAELEELEKRREEI 692
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
172-391 |
2.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 172 LERRVLELEKDTAATGEQHsRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 251
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 252 QQLDEENSELRS----CTPC---------------LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRMGDRLSHERH 312
Cdd:PRK03918 422 KELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 313 QFQRDKEATQEL----IEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESELEQEVRRLKQDNRNLKEQNEELN 388
Cdd:PRK03918 501 LAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELL 576
|
...
gi 767987898 389 GQI 391
Cdd:PRK03918 577 KEL 579
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
109-390 |
2.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 109 NRLEDLSARLSDLEMNSPTKRLSSKKVARyLHQSG--------ALTMEAleDPSPELmegpeEDIADKVVFLERRVLELE 180
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQR-LHQAFsrfigshlAVAFEA--DPEAEL-----RQLNRRRVELERALADHE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 181 kdtAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEET-------RRQKELLCKMEREKSI----- 242
Cdd:PRK04863 858 ---SQEQQQRSQLEQakEGLSALNRllprLNLLADETLADRVEEIREQLDEAeeakrfvQQHGNALAQLEPIVSVlqsdp 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 243 -EIENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHE----RHQ 313
Cdd:PRK04863 935 eQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQlrqaQAQ 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 314 FQRDKEATQELIEDLRKQLEHLQLLKLE-----------AEQR-RGRSSSMGLQEYHSRAR-----------ESELEQEV 370
Cdd:PRK04863 1015 LAQYNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsgAEERaRARRDELHARLSANRSRrnqlekqltfcEAEMDNLT 1094
|
330 340
....*....|....*....|
gi 767987898 371 RRLKQDNRNLKEQNEELNGQ 390
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNA 1114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
208-457 |
3.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 208 EEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEI-----ENLQTRLQQLDEENSELRSCTPCLKANIER--LEEEKQ 280
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 281 KLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELiEDLRKQLEhlQLLKLEAEQRRGRSSSMGLQEYHSR 360
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE-EDEKKAAE--ALKKEAEEAKKAEELKKKEAEEKKK 1717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 361 ARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQdy 440
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME-- 1795
|
250
....*....|....*..
gi 767987898 441 IDRIIVAIMETNPSILE 457
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-451 |
4.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 272 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSH----ERHQFQR-DKEATQELIEDLRKQLEHL-----QLLKLE 341
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEiDVASAEREIAELEAELERLdassdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 342 AEQRRgrsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS------IQGAKSLFSTAFSESLAAEI 415
Cdd:COG4913 692 EQLEE------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*.
gi 767987898 416 SSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMET 451
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
109-337 |
7.92e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 109 NRLEDLSARLSDLEmnsptkrlssKKVARYLHQSGALTMEALEDpspelmegpeeDIADKVVFLERRVLELEKDTAATGE 188
Cdd:COG3206 182 EQLPELRKELEEAE----------AALEEFRQKNGLVDLSEEAK-----------LLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 189 QHSRLRQenlQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE-NSELRSCTPC 267
Cdd:COG3206 241 RLAALRA---QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 268 LKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgdrlsherHQFQRDKEATQELIEDLRKQLEHLQL 337
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAEL--------RRLEREVEVARELYESLLQRLEEARL 379
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
220-346 |
8.98e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 220 EMVLEETRRqkELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQEN 299
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767987898 300 KRRMGDRlshERHQFQRDKEAT--QELIEDLRKQLEHLQ--LLKLEAEQRR 346
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELEEERerIEELKRKLER 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
191-397 |
1.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 191 SRLRQENLQLvHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI---EIENLQTRLQQLDEENSELRsctpc 267
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLE----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 268 LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRmgdrlshERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRG 347
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERL-EELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767987898 348 RSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 397
Cdd:COG4717 195 QDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
200-375 |
1.12e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 200 LVHRANALEEQLKEQELRACEmvLEETRRQKELLCK---MEREKSIEIENLQTRLQQLDEENSE-LRSCtpclkanIERL 275
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEqAAEA-------VEQR 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 276 EEEKQKLlDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglq 355
Cdd:COG3096 581 SELRQQL-EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE----------- 648
|
170 180
....*....|....*....|
gi 767987898 356 eyhSRARESELEQEVRRLKQ 375
Cdd:COG3096 649 ---LAARKQALESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-346 |
1.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 173 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqkellckmereksiEIENLQTRLQ 252
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 253 QLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK-RRMGDRLSH---ERHQFQRDKEATQELIEDL 328
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*...
gi 767987898 329 RKQLEHLQLLKLEAEQRR 346
Cdd:COG4717 226 EEELEQLENELEAAALEE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-380 |
2.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 177 LELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDE 256
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 257 ENSELRSCTPcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ 336
Cdd:COG1196 657 SAGGSLTGGS-RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767987898 337 LLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL 380
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-388 |
2.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 222 VLEETRRQKELLCK-MEREKSIE--IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL---LDEIESLTLRLSE 295
Cdd:PRK03918 170 VIKEIKRRIERLEKfIKRTENIEelIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 296 EQENKRRMGDRLSherhQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMglQEYhsRARESELEQEVRRLKQ 375
Cdd:PRK03918 250 LEGSKRKLEEKIR----ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY--EEY--LDELREIEKRLSRLEE 321
|
170
....*....|...
gi 767987898 376 DNRNLKEQNEELN 388
Cdd:PRK03918 322 EINGIEERIKELE 334
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
173-385 |
2.94e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 173 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElRACEMVLEETRRQK---ELLCKMEREKSieienlqT 249
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE-EALREQAELNRLKKkylEALNKKLNEKE-------S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 250 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQElIEDLR 329
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR-IKELE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767987898 330 KQLEHLQLLKLEAEQRRGRsssmglqeyhsRARESELEQEVRRLKQDNRNLKEQNE 385
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSE-----------LARIPELEKELERLREHNKHLNENIE 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-385 |
3.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 172 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSIEIEnLQT 249
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQ-LLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 250 RLQQLDEENSELRSCTPCLKANIERLEEEKQkLLDEIESLTLRLSEEQEnkrrmgdrlsHERHQFQRDKEATQELIEDLR 329
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQE----------ELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767987898 330 KQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNE 385
Cdd:COG4717 199 EELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALEER 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
170-387 |
3.90e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 170 VFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRA-----------CEMVLEETRRQKELLCKMER 238
Cdd:pfam01576 127 VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkheAMISDLEERLKKEEKGRQEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 239 EKSieIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDK 318
Cdd:pfam01576 207 EKA--KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987898 319 EATQELIEDLRKQLEHLQLLKLEAEQRRGrsSSMGLQEYHSRaRESELEQEVRRLKQDNRNLKEQNEEL 387
Cdd:pfam01576 285 AARNKAEKQRRDLGEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
188-339 |
4.03e-03 |
|
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: 39.23 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 188 EQHSRLRQENLQLVHRANALEEQLkeQELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctp 266
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIK--PKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK--- 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987898 267 clkaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 339
Cdd:smart00787 226 ----KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
163-386 |
4.07e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 163 EDIADKVVFLERRVLELEKDTAATGEQHSRLrqenlqlvhranaleEQLKEQELRacemvLEETRRQKELLCKMEREKSI 242
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERA---------------EDLVEAEDR-----IERLEERREDLEELIAERRE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 243 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeQENKRRMgDRLSHERHQFQRDKEATQ 322
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL---AELKERI-ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987898 323 ElIEDLRKQLEHLQLLKleaEQRRGRsssmgLQEYHSRARESELEQEVRRLkQDNRNLKEQNEE 386
Cdd:PRK02224 607 E-IERLREKREALAELN---DERRER-----LAEKRERKRELEAEFDEARI-EEAREDKERAEE 660
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
207-391 |
4.14e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 39.45 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 207 LEEQLK--EQELRACEMVLEETRRQKELLCKMEReksieieNLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLD 284
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 285 EIESLTLRLSEEQENKRRMGDRLSHERhQFQRDKEATQEliedlrkqlehlQLLKLEAEQRRGRSSSMglqeyhsRARES 364
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 767987898 365 ELEQEVRRLKQDNRNLKEQNEELNGQI 391
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
275-427 |
4.15e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 275 LEEEKQKLLDEIESLTLRLSEEQENKRR-MGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLlKLEAEQRRGRSS 350
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTeEEEEIRRLEEQVERLEAEVEELeaeLEEKDERIERLER-ELSEARSEERRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 351 smglqeyHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLsiqgaKSLFSTAFSESLAA--EISSVSRDELMEAI 427
Cdd:COG2433 461 -------IRKDREiSRLDREIERLERELEEERERIEELKRKLERL-----KELWKLEHSGELVPvkVVEKFTKEAIRRLE 528
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
203-397 |
4.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 203 RANALEEQLKEQELRAcEMVLEETRRQKEllcKMEREKSIEIEnlqtrlqqldEENSELRSctpclkanieRLEEEKQKL 282
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAE---AIKKEALLEAK----------EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 283 LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrAR 362
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767987898 363 E---SELEQEVR-----RLKQDNRNLKEQNEELNGQIITLSIQ 397
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
163-386 |
4.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 163 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvleETRRQKELLCKMEREKSI 242
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 243 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 322
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV-MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987898 323 ELIEDLRKQLEhlqlLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEE 386
Cdd:PTZ00121 1641 KEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
188-334 |
4.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 188 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmerEKSIEIENLQTRLQQLDEENselrsctpc 267
Cdd:PRK12705 34 EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLVQKEEQLDARA--------- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987898 268 lkaniERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLshERHQFQRDKEATQELIEDLRKQLEH 334
Cdd:PRK12705 98 -----EKLDNLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLLDAELEE 157
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-389 |
7.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 106 KQINRLEDLSARLSDL--EMNSPTKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDT 183
Cdd:PRK03918 328 ERIKELEEKEERLEELkkKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 184 AATGEQHSRLRQENLQLVHRANALEEqlKEQELRACEMVLEETRRqKELLckmeREKSIEIENLQTRLQQLDEENSELRS 263
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHR-KELL----EEYTAELKRIEKELKEIEEKERKLRK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 264 CTPCLKANIERLEE--EKQKLLDEIESLTLRLS-----------EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRK 330
Cdd:PRK03918 481 ELRELEKVLKKESEliKLKELAEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987898 331 QLEHLQLLKLEAEQRRGRSSSMG-------------LQEYHSR-----ARESELEQEVRRLKQDNRNLKEQNEELNG 389
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfesveeleerlkeLEPFYNEylelkDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
156-296 |
7.33e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 156 ELMEGPEE--DIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQ 229
Cdd:COG1579 25 RLKELPAElaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987898 230 KELLCKMEREKSIEIENLQTRLQ----QLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE 296
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAeleaELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
178-442 |
7.39e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 178 ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE 257
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 258 NSELRSCTpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsHERHQFQRDKEATQELIEDLRKQLEHLQL 337
Cdd:pfam02463 261 EKEEEKLA--QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL------KLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 338 LKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQ-DNRNLKEQNEELNGQIITLSIQG-AKSLFSTAFSE-SLAAE 414
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLE 412
|
250 260
....*....|....*....|....*...
gi 767987898 415 ISSVSRDELMEAIQKQEEINFRLQDYID 442
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIE 440
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
235-341 |
7.72e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 235 KMERE-KSIEIENLQTRLQQLDEENSEL-RSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH 312
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 767987898 313 QFQRDKEATQELIEDLRKQLEHLQLLKLE 341
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
192-385 |
8.87e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.57 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 192 RLRQENLQLVHRANALEEQLKEQELRACEMV---LEETRRQKELlckmEREKSIEIENLQTRLQQLDEENSELRsctpcl 268
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVrqeLEAARKVKIL----EEERQRKIQQQKVEMEQIRAEQEEAR------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 269 KANIERLEEEKQKLLDEIESLTL-------RLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlrKQLEHLQLLKLE 341
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE---KELEERKQAMIE 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767987898 342 AEQRRgrssSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNE 385
Cdd:pfam17380 511 EERKR----KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
203-459 |
8.97e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 203 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 282
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 283 LDEIEsltlRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQllkleAEQRRGRSSSMGLQEYHSRAR 362
Cdd:COG4372 114 QEELE----ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ-----EELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 363 ESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYID 442
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250
....*....|....*..
gi 767987898 443 RIIVAIMETNPSILEVK 459
Cdd:COG4372 265 LAILVEKDTEEEELEIA 281
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
194-395 |
9.45e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 194 RQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKEllckmerEKSIEIENLQTRLQQLDEENSELRSctpcLKAN 271
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAEldEEIERYEEQREQARETRD-------EADEVLEEHEERREELETLEAEIED----LRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987898 272 IERLEEEKQKLLDEIESLTLRLSE-EQENKRRMGD---------RLSHERHQFQRDKEATQELIEDLRKQLehlQLLKLE 341
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEElEEERDDLLAEaglddadaeAVEARREELEDRDEELRDRLEECRVAA---QAHNEE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767987898 342 AEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 395
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| |
