|
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 ... |
451-491 |
3.30e-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: 3.30e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767987895 451 SRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 491
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-477 |
2.52e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 205 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 275
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 276 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 352
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 353 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 414
Cdd:TIGR02168 836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767987895 415 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 477
Cdd:TIGR02168 916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
194-471 |
3.49e-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: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 194 EEDIADKVVFLeRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmEREKS 273
Cdd:COG1196 221 ELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 274 IEIENLQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 353
Cdd:COG1196 295 AELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 354 QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 433
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*...
gi 767987895 434 LFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 471
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-429 |
6.06e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 235 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 314
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 315 LDEIESLTLR---LSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHS 391
Cdd:TIGR02168 294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 767987895 392 RAResELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 429
Cdd:TIGR02168 373 RLE--ELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-475 |
1.76e-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: 60.46 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 226 RQENLQLVHRANA---LEEQLKEQE--LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCL 300
Cdd:TIGR02168 666 AKTNSSILERRREieeLEEKIEELEekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 301 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 380
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 381 SSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS-------LFSTAFSESLAAEISSvSRD 453
Cdd:TIGR02168 826 LESL-------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeselealLNERASLEEALALLRS-ELE 897
|
250 260
....*....|....*....|..
gi 767987895 454 ELMEAIQKQEEINFRLQDYIDR 475
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-423 |
3.98e-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: 59.31 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 199 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRAcEMVLEETRRQKEllckmereksiEIEN 278
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 279 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ------------ENKRRMGDRLSH----- 341
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREieqkl 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 342 ------------ERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSsmgLQEYHSRARESELEQEVRRLKQDN 409
Cdd:TIGR02169 822 nrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQL 898
|
250
....*....|....
gi 767987895 410 RNLKEQNEELNGQI 423
Cdd:TIGR02169 899 RELERKIEELEAQI 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-464 |
1.03e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 195 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREK 272
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 273 SIEIENLQTRL----QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRrmgdrlshERHQFQR 348
Cdd:COG1196 322 EEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------ELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 349 DKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 428
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 767987895 429 QGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEE 464
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-464 |
1.73e-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: 57.37 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 198 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELRACEMVLEETRRQKEL---------LCKM 268
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELyalaneisrLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 269 EREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLS---HERHQ 345
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 346 FQRDKEATQELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 423
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLeaRLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767987895 424 ITLSIQGAKSlfSTAFSESLAAEISSVSRDELMEAIQKQEE 464
Cdd:TIGR02168 464 EELREELEEA--EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-470 |
4.51e-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: 55.83 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 195 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELracEMVLEETRRQKELLCKMEREKSI 274
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 275 E-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqrd 349
Cdd:TIGR02168 785 EeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 350 kEATQELIEDLRKQLEHL----------------QLLKLEAEQRRGRSSSMGLQEYHSRARES---------ELEQEVRR 404
Cdd:TIGR02168 862 -EELEELIEELESELEALlnerasleealallrsELEELSEELRELESKRSELRRELEELREKlaqlelrleGLEVRIDN 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987895 405 LKQdnrNLKEQneelngQIITLSIQGAKSLFSTAFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLQ 470
Cdd:TIGR02168 941 LQE---RLSEE------YSLTLEEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERYD 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-408 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 198 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQlkeqeLRACEMVLEETRRQKELlckmeREKSIEIE 277
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQER-----REALQRLAEYSWDEIDV-----ASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 278 NLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQR-DKEATQEL 356
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767987895 357 IEDLRKQLEHLQLLKLEAEQRRG-RSSSMGLQEYHSRAREsELEQEVRRLKQD 408
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENlEERIDALRARLNRAEE-ELERAMRAFNRE 799
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
206-426 |
1.03e-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: 51.28 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 206 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvlEETRRQKELLCKMEREKSIEIEnlqtRLQQ 285
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVE----RLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 286 LDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE 365
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987895 366 HlqllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNlKEQNEELNGQIITL 426
Cdd:pfam17380 548 M-------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
141-419 |
3.17e-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: 49.95 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 141 NRLEDLSARLSDLEMNSPTKRLSSKKVARyLHQSGA------LTMEALEDPSPELMEgpeedIADKVVFLERrvlELEKD 214
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQKLQR-LHQAFSqfvgghLAVAFAPDPEAELAA-----LRQRRSELER---ELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 215 TAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEE-------TRRQKELLCKMEREKSI------E 275
Cdd:COG3096 856 RAQEQQLRQQLDQlkEQLQLLNKllpqANLLADETLADRLEELREELDAaqeaqafIQQHGKALAQLEPLVAVlqsdpeQ 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 276 IENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDE----IESLTLRLSEEQENKRRMGDRLSHERHQFQ 347
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlNEKLRARLEQAEEARREAREQLRQAQAQYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 348 rdkEATQELI----------EDLRKQLEHLQLLKL----EAEQR-RGRSSSMGLQEYHSRAR-----------ESELEQE 401
Cdd:COG3096 1016 ---QYNQVLAslkssrdakqQTLQELEQELEELGVqadaEAEERaRIRRDELHEELSQNRSRrsqlekqltrcEAEMDSL 1092
|
330
....*....|....*...
gi 767987895 402 VRRLKQDNRNLKEQNEEL 419
Cdd:COG3096 1093 QKRLRKAERDYKQEREQV 1110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-426 |
3.22e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 194 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREkS 273
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEER-----IEELKKEIEELEEKVKE-L 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 274 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 348
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767987895 349 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITL 426
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-433 |
3.72e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 215 TAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSE 292
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 293 LRsctpclkANIERLEEEKQKLLDEI------ESLTLRLSEEQENK--------RRMGDRLSHERHQFQRDKEATQELIE 358
Cdd:COG4942 95 LR-------AELEAQKEELAELLRALyrlgrqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767987895 359 DLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 433
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
235-423 |
4.91e-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: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 235 RANALEEQLkeQELRACEMVLEETRRQKELLCKMeREKSIEIENLQTRLQQLDEENSELRS-----CTPCLKANIERLEE 309
Cdd:COG4913 226 AADALVEHF--DDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 310 EKQKLLDEIESLTLRLSEEQENKRRMgdRLSHERHQFQRdkeatqelIEDLRKQLEHLQLLKLEAEQRRGR--------- 380
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARleallaalg 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767987895 381 ----SSSMGLQEYHSRARE---------SELEQEVRRLKQDNRNLKEQNEELNGQI 423
Cdd:COG4913 373 lplpASAEEFAALRAEAAAllealeeelEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-406 |
5.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 194 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElracemvlEETRRQKELLCKMEREKS 273
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--------EELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 274 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkqklLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 353
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767987895 354 QELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLK 406
Cdd:COG4942 198 QKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-399 |
5.59e-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: 49.30 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 176 ALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQ--ELRACEM 253
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 254 VLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL---TLRLSEEQE 330
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987895 331 NKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHSRARESELE 399
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-476 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 227 QENLQlvhRANALEEQLKEQelracemvLEETRRQKEllcKMER--EKSIEIENLQTRLQQLDEENselrsctpcLKANI 304
Cdd:COG1196 185 EENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE---------LEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 305 ERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSM 384
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 385 GLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLsiQGAKSLFSTAFSESLAAEISsvSRDELMEAIQKQEE 464
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELLEALRAAAE 397
|
250
....*....|..
gi 767987895 465 INFRLQDYIDRI 476
Cdd:COG1196 398 LAAQLEELEEAE 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-420 |
1.50e-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: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 199 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLvhraNALEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIEN 278
Cdd:COG4913 654 AEYSWDEIDVASAEREIAELEAELERLDASSDDL----AALEEQLEELEAE-----LEELEEELDELKGEIGRLEKELEQ 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 279 LQTRLQQLDEENSELRSctPCLKANIERLEEEKQKLLDE------IESLTLRLSEEQENKRRMGDRLSHERHQFQRD-KE 351
Cdd:COG4913 725 AEEELDELQDRLEAAED--LARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFNREwPA 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987895 352 ATQELIEDLRKQLEHLQLL-KLEAEqrrgrsssmGLQEYHSRARESELEQE-------VRRLKQDNRNLKEQNEELN 420
Cdd:COG4913 803 ETADLDADLESLPEYLALLdRLEED---------GLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLN 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-464 |
1.71e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 205 ERRVLELEKDTAATGEQHSRLRQENLQLVhRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQ 284
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 285 QLDEENSELRSCTPCLKANIERLEEEKQ--------KLLDEIESLTLRLSEEQENKRRMGDRLSH---ERHQFQRDKEAT 353
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKleaEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 354 QELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 431
Cdd:TIGR02169 342 EREIEEERKRRDKLTeeYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270
....*....|....*....|....*....|....*
gi 767987895 432 KSLFSTAFSESLAAEISSV--SRDELMEAIQKQEE 464
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELeeEKEDKALEIKKQEW 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
217-412 |
2.05e-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: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 217 ATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSc 296
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 297 tpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQ 376
Cdd:COG4913 338 -----DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180 190
....*....|....*....|....*....|....*.
gi 767987895 377 RRGRsssmglqeyhSRARESELEQEVRRLKQDNRNL 412
Cdd:COG4913 413 ALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-431 |
2.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 223 SRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSI--EIENLQTRLQQLDEENSELRSCTP 298
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPElrKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 299 CLKANIERLEEEKQKLLD--EIESLTLRLSEEQENKRRMGDRLShERHQfqrDKEATQELIEDLRKQLEH-----LQLLK 371
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYT-PNHP---DVIALRAQIAALRAQLQQeaqriLASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987895 372 LEAEQRRGRSSSMG--LQEYHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 431
Cdd:COG3206 320 AELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
227-423 |
2.39e-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: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 227 QENLQLVHRANaleEQLKEQELRACEMVLEETRRQKELLCKMereksieienlqtRLQQLDEenselrsctpclkanIER 306
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 307 LEEEKQKLLDEIESLTLRLSEEQENK----RRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRgrsS 382
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQeklmRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAK---K 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767987895 383 SMGLQEYHSRARESELEQEVRRLKQDNR-----NLKEQNEELNGQI 423
Cdd:pfam10168 657 KMNYQRYQIAKSQSIRKKSSLSLSEKQRktikeILKQLGSEIDELI 702
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
189-383 |
3.76e-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: 45.83 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 189 LMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLC 266
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 267 KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLS-EEQENKR--RMGDRLSHER 343
Cdd:pfam19220 111 IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlLEQENRRlqALSEEQAAEL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767987895 344 HQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSS 383
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEA 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
195-419 |
5.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 195 EDIADKVVFLERRVLELEKdtaaTGEQHSRLRQeNLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREksi 274
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK----VLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 275 eIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGD-------RLSHERHQFQ 347
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylELKDAEKELE 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987895 348 RDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGL---QEYHSRARES--ELEQEVRRLKQDNRNLKEQNEEL 419
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysEEEYEELREEylELSRELAGLRAELEELEKRREEI 692
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
141-422 |
1.59e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 141 NRLEDLSARLSDLEMNSPTKRLSSKKVARyLHQSG--------ALTMEAleDPSPELmegpeEDIADKVVFLERRVLELE 212
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQR-LHQAFsrfigshlAVAFEA--DPEAEL-----RQLNRRRVELERALADHE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 213 kdtAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEET-------RRQKELLCKMEREKSI----- 274
Cdd:PRK04863 858 ---SQEQQQRSQLEQakEGLSALNRllprLNLLADETLADRVEEIREQLDEAeeakrfvQQHGNALAQLEPIVSVlqsdp 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 275 -EIENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHE----RHQ 345
Cdd:PRK04863 935 eQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQlrqaQAQ 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 346 FQRDKEATQELIEDLRKQLEHLQLLKLE-----------AEQR-RGRSSSMGLQEYHSRAR-----------ESELEQEV 402
Cdd:PRK04863 1015 LAQYNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsgAEERaRARRDELHARLSANRSRrnqlekqltfcEAEMDNLT 1094
|
330 340
....*....|....*....|
gi 767987895 403 RRLKQDNRNLKEQNEELNGQ 422
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNA 1114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-423 |
1.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 204 LERRVLELEKDTAATGEQHsRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 283
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 284 QQLDEENSELRS----CTPC---------------LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRMGDRLSHERH 344
Cdd:PRK03918 422 KELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 345 QFQRDKEATQEL----IEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESELEQEVRRLKQDNRNLKEQNEELN 420
Cdd:PRK03918 501 LAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELL 576
|
...
gi 767987895 421 GQI 423
Cdd:PRK03918 577 KEL 579
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
141-369 |
2.83e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 141 NRLEDLSARLSDLEmnsptkrlssKKVARYLHQSGALTMEALEDpspelmegpeeDIADKVVFLERRVLELEKDTAATGE 220
Cdd:COG3206 182 EQLPELRKELEEAE----------AALEEFRQKNGLVDLSEEAK-----------LLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 221 QHSRLRQenlQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE-NSELRSCTPC 299
Cdd:COG3206 241 RLAALRA---QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 300 LKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgdrlsherHQFQRDKEATQELIEDLRKQLEHLQL 369
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAEL--------RRLEREVEVARELYESLLQRLEEARL 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-489 |
3.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 240 EEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSelRSCTPCLKANIERLEEEKQKLLDEIE 319
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK--MKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 320 SLTLRLSEEQENKRRMGDRLSHE-------RHQFQRDKEATQELIEDLRKQLEHL-----QLLKLEAEQRRGRSSSMGLQ 387
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAeeenkikAAEEAKKAEEDKKKAEEAKKAEEDEkkaaeALKKEAEEAKKAEELKKKEA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 388 EYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINF 467
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
250 260
....*....|....*....|..
gi 767987895 468 RLQdyIDRIIVAIMETNPSILE 489
Cdd:PTZ00121 1793 RME--VDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-483 |
4.83e-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: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 304 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSH----ERHQFQR-DKEATQELIEDLRKQLEHL-----QLLKLE 373
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEiDVASAEREIAELEAELERLdassdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 374 AEQRRgrsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS------IQGAKSLFSTAFSESLAAEI 447
Cdd:COG4913 692 EQLEE------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*.
gi 767987895 448 SSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMET 483
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-429 |
7.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 223 SRLRQENLQLvHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI---EIENLQTRLQQLDEENSELRsctpc 299
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLE----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 300 LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRmgdrlshERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRG 379
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERL-EELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767987895 380 RSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 429
Cdd:COG4717 195 QDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
252-378 |
7.79e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 252 EMVLEETRRqkELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQEN 331
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767987895 332 KRRMGDRlshERHQFQRDKEAT--QELIEDLRKQLEHLQ--LLKLEAEQRR 378
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELEEERerIEELKRKLER 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
205-378 |
9.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 205 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqkellckmereksiEIENLQTRLQ 284
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 285 QLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK-RRMGDRLSH---ERHQFQRDKEATQELIEDL 360
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*...
gi 767987895 361 RKQLEHLQLLKLEAEQRR 378
Cdd:COG4717 226 EEELEQLENELEAAALEE 243
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-407 |
1.01e-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: 41.86 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 232 LVHRANALEEQLKEQELRACEmvLEETRRQKELLCK---MEREKSIEIENLQTRLQQLDEENSE-LRSCtpclkanIERL 307
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEqAAEA-------VEQR 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 308 EEEKQKLlDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglq 387
Cdd:COG3096 581 SELRQQL-EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE----------- 648
|
170 180
....*....|....*....|
gi 767987895 388 eyhSRARESELEQEVRRLKQ 407
Cdd:COG3096 649 ---LAARKQALESQIERLSQ 665
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
205-417 |
1.68e-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: 40.88 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 205 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElRACEMVLEETRRQK---ELLCKMEREKSieienlqT 281
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE-EALREQAELNRLKKkylEALNKKLNEKE-------S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 282 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQElIEDLR 361
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR-IKELE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767987895 362 KQLEHLQLLKLEAEQRRGRsssmglqeyhsRARESELEQEVRRLKQDNRNLKEQNE 417
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSE-----------LARIPELEKELERLREHNKHLNENIE 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-420 |
1.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 254 VLEETRRQKELLCK-MEREKSIE--IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL---LDEIESLTLRLSE 327
Cdd:PRK03918 170 VIKEIKRRIERLEKfIKRTENIEelIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 328 EQENKRRMGDRLSherhQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMglQEYhsRARESELEQEVRRLKQ 407
Cdd:PRK03918 250 LEGSKRKLEEKIR----ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY--EEY--LDELREIEKRLSRLEE 321
|
170
....*....|...
gi 767987895 408 DNRNLKEQNEELN 420
Cdd:PRK03918 322 EINGIEERIKELE 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
204-417 |
2.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 204 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSIEIEnLQT 281
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQ-LLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 282 RLQQLDEENSELRSCTPCLKANIERLEEEKQkLLDEIESLTLRLSEEQEnkrrmgdrlsHERHQFQRDKEATQELIEDLR 361
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQE----------ELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767987895 362 KQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNE 417
Cdd:COG4717 199 EELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALEER 244
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
239-423 |
2.33e-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: 40.61 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 239 LEEQLK--EQELRACEMVLEETRRQKELLCKMEReksieieNLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLD 316
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 317 EIESLTLRLSEEQENKRRMGDRLSHERhQFQRDKEATQEliedlrkqlehlQLLKLEAEQRRGRSSSMglqeyhsRARES 396
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 767987895 397 ELEQEVRRLKQDNRNLKEQNEELNGQI 423
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-412 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 209 LELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDE 288
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 289 ENSELRSCTPcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ 368
Cdd:COG1196 657 SAGGSLTGGS-RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767987895 369 LLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL 412
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
220-371 |
3.10e-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: 39.62 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 220 EQHSRLRQENLQLVHRANALEEQLkeQELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctp 298
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIK--PKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK--- 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987895 299 clkaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 371
Cdd:smart00787 226 ----KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-419 |
3.16e-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: 40.16 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 202 VFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRA-----------CEMVLEETRRQKELLCKMER 270
Cdd:pfam01576 127 VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkheAMISDLEERLKKEEKGRQEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 271 EKSieIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDK 350
Cdd:pfam01576 207 EKA--KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987895 351 EATQELIEDLRKQLEHLQLLKLEAEQRRGrsSSMGLQEYHSRaRESELEQEVRRLKQDNRNLKEQNEEL 419
Cdd:pfam01576 285 AARNKAEKQRRDLGEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
307-459 |
3.32e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 307 LEEEKQKLLDEIESLTLRLSEEQENKRR-MGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLlKLEAEQRRGRSS 382
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTeEEEEIRRLEEQVERLEAEVEELeaeLEEKDERIERLER-ELSEARSEERRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 383 smglqeyHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLsiqgaKSLFSTAFSESLAA--EISSVSRDELMEAI 459
Cdd:COG2433 461 -------IRKDREiSRLDREIERLERELEEERERIEELKRKLERL-----KELWKLEHSGELVPvkVVEKFTKEAIRRLE 528
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
224-417 |
3.50e-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: 40.11 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 224 RLRQENLQLVHRANALEEQLKEQELRACEMV---LEETRRQKELlckmEREKSIEIENLQTRLQQLDEENSELRsctpcl 300
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVrqeLEAARKVKIL----EEERQRKIQQQKVEMEQIRAEQEEAR------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 301 KANIERLEEEKQKLLDEIESLTL-------RLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlrKQLEHLQLLKLE 373
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE---KELEERKQAMIE 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767987895 374 AEQRRgrssSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNE 417
Cdd:pfam17380 511 EERKR----KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-491 |
3.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 235 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 314
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 315 LDEIEsltlRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQllkleAEQRRGRSSSMGLQEYHSRAR 394
Cdd:COG4372 114 QEELE----ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ-----EELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 395 ESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYID 474
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250
....*....|....*..
gi 767987895 475 RIIVAIMETNPSILEVK 491
Cdd:COG4372 265 LAILVEKDTEEEELEIA 281
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
235-429 |
4.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 235 RANALEEQLKEQELRAcEMVLEETRRQKEllcKMEREKSIEIEnlqtrlqqldEENSELRSctpclkanieRLEEEKQKL 314
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAE---AIKKEALLEAK----------EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 315 LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrAR 394
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767987895 395 E---SELEQEVR-----RLKQDNRNLKEQNEELNGQIITLSIQ 429
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
220-366 |
4.45e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 220 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmerEKSIEIENLQTRLQQLDEENselrsctpc 299
Cdd:PRK12705 34 EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLVQKEEQLDARA--------- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987895 300 lkaniERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLshERHQFQRDKEATQELIEDLRKQLEH 366
Cdd:PRK12705 98 -----EKLDNLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLLDAELEE 157
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
210-474 |
4.58e-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: 39.57 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 210 ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE 289
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 290 NSELRSCTpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsHERHQFQRDKEATQELIEDLRKQLEHLQL 369
Cdd:pfam02463 261 EKEEEKLA--QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL------KLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 370 LKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQ-DNRNLKEQNEELNGQIITLSIQG-AKSLFSTAFSE-SLAAE 446
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLE 412
|
250 260
....*....|....*....|....*...
gi 767987895 447 ISSVSRDELMEAIQKQEEINFRLQDYID 474
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIE 440
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-418 |
4.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 195 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvleETRRQKELLCKMEREKSI 274
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 275 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 354
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV-MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987895 355 ELIEDLRKQLEhlqlLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEE 418
Cdd:PTZ00121 1641 KEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-421 |
4.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 141 NRLEDLSARLSDLEmnsptKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGE 220
Cdd:PRK03918 338 ERLEELKKKLKELE-----KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 221 QHSRLRQENLQLVHRANALEEqlKEQELRACEMVLEETRRqKELLckmeREKSIEIENLQTRLQQLDEENSELRSCTPCL 300
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHR-KELL----EEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 301 KANIERLEE--EKQKLLDEIESLTLRLS-----------EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHL 367
Cdd:PRK03918 486 EKVLKKESEliKLKELAEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987895 368 QLLKLEAEQRRGRSSSMG-------------LQEYHSR-----ARESELEQEVRRLKQDNRNLKEQNEELNG 421
Cdd:PRK03918 566 DELEEELAELLKELEELGfesveeleerlkeLEPFYNEylelkDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
161-377 |
5.71e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.16 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 161 RLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVF----LERRVLELEKDTAATGEQHsRLRQENLQlvhRA 236
Cdd:pfam15709 296 RSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLraerAEMRRLEVERKRREQEEQR-RLQQEQLE---RA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 237 NALEEQLK-EQELRACEMVL------------EETRRQKELLCKMEREKS-IEIENLQTRLQQLDEENSElrsctpclkA 302
Cdd:pfam15709 372 EKMREELElEQQRRFEEIRLrkqrleeerqrqEEEERKQRLQLQAAQERArQQQEEFRRKLQELQRKKQQ---------E 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987895 303 NIERLEEEKQKLldeiESLTLRLSEEQENKRRMG--DRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQR 377
Cdd:pfam15709 443 EAERAEAEKQRQ----KELEMQLAEEQKRLMEMAeeERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-328 |
6.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 188 ELMEGPEE--DIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQ 261
Cdd:COG1579 25 RLKELPAElaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987895 262 KELLCKMEREKSIEIENLQTRLQ----QLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE 328
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAeleaELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-423 |
7.29e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.85 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 227 QENLQLVHRANALEEQLKEQElracemvleetrrqkellcKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIER 306
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 307 LEEEKQKLLDEIESLTlRLSEEQENKRrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLqllkleaeqrrgrsssmgl 386
Cdd:TIGR04523 445 LTNQDSVKELIIKNLD-NTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEKELKKL------------------- 501
|
170 180 190
....*....|....*....|....*....|....*..
gi 767987895 387 qeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQI 423
Cdd:TIGR04523 502 -----NEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
199-407 |
8.03e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.80 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 199 DKVVFLERRVLELEKDTAATGEQHSRLRQE----NLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMER---- 270
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQKreaqEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaah 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 271 -----EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL--LDEIESLTLRLSEEQENKRRMGDR---LS 340
Cdd:TIGR00618 299 ikavtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQqhtLT 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987895 341 HERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQ 407
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCA 444
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
220-408 |
8.05e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.87 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 220 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLC--KMEREKSIEIENLQTRLQQLDEENSELRSCT 297
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESsrEIVKSYENELDPLKNRLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 298 PCLKAnIERLEEEKQKLLDEIESLTLR--------LSEEQENKRRMGDRLSHERHQFQRDkeatqelIEDLRKQLEHLQL 369
Cdd:TIGR00606 269 NEIKA-LKSRKKQMEKDNSELELKMEKvfqgtdeqLNDLYHNHQRTVREKERELVDCQRE-------LEKLNKERRLLNQ 340
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767987895 370 LKLEAEQRRGRSS-SMGLQEYHSRARESELEQEVRRLKQD 408
Cdd:TIGR00606 341 EKTELLVEQGRLQlQADRHQEHIRARDSLIQSLATRLELD 380
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
267-373 |
8.43e-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: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 267 KMERE-KSIEIENLQTRLQQLDEENSEL-RSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH 344
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 767987895 345 QFQRDKEATQELIEDLRKQLEHLQLLKLE 373
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
195-418 |
8.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 195 EDIADKVVFLERRVLELEKDTAATGEQHSRLrqenlqlvhranaleEQLKEQELRacemvLEETRRQKELLCKMEREKSI 274
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERA---------------EDLVEAEDR-----IERLEERREDLEELIAERRE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 275 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeQENKRRMgDRLSHERHQFQRDKEATQ 354
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL---AELKERI-ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987895 355 ElIEDLRKQLEHLQLLKleaEQRRGRsssmgLQEYHSRARESELEQEVRRLkQDNRNLKEQNEE 418
Cdd:PRK02224 607 E-IERLREKREALAELN---DERRER-----LAEKRERKRELEAEFDEARI-EEAREDKERAEE 660
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-426 |
8.75e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.95 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 179 MEALEDPSPELMEGPEEDIADKVvflERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQE-LRACEMV-LE 256
Cdd:pfam15921 247 LEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsMYMRQLSdLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 257 ETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRM 335
Cdd:pfam15921 324 STVSQlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 336 GDRlsherhqfqrdKEATQELIEDLRKQLE--HLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVR------RLKQ 407
Cdd:pfam15921 404 WDR-----------DTGNSITIDHLRRELDdrNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssltaQLES 472
|
250
....*....|....*....
gi 767987895 408 DNRNLKEQNEELNGQIITL 426
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTL 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
204-464 |
9.45e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.80 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 204 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQ---KELLCKMEREKSIEIENlq 280
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQlqtKEQIHLQETRKKAVVLA-- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 281 tRLQQLDEENSELrsCTPCLKANIER----LEEEKQKLLDEIESLTLRLSEEQENKRRMGDRlshERHQFQRDKEATQEL 356
Cdd:TIGR00618 495 -RLLELQEEPCPL--CGSCIHPNPARqdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS---ERKQRASLKEQMQEI 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987895 357 IEDLRKQLEHLQLLKLEAEQRRGRSSSmgLQEYhsraRESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQgakslfs 436
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNITVR--LQDL----TEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ------- 635
|
250 260
....*....|....*....|....*...
gi 767987895 437 tAFSESLAAEISSVSRDELMEAIQKQEE 464
Cdd:TIGR00618 636 -QCSQELALKLTALHALQLTLTQERVRE 662
|
|
| |
