|
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 ... |
406-446 |
4.68e-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: 63.13 E-value: 4.68e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1691739872 406 SRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 446
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-432 |
5.33e-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: 65.08 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 160 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 230
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 231 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 307
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 308 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 369
Cdd:TIGR02168 836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1691739872 370 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 432
Cdd:TIGR02168 916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-426 |
5.69e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 149 EEDIADKVVFLeRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmEREKS 228
Cdd:COG1196 221 ELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 229 IEIENLQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 308
Cdd:COG1196 295 AELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 309 QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 388
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*...
gi 1691739872 389 LFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 426
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-425 |
1.47e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 159 LERRVLELEKDtAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 238
Cdd:COG1196 198 LERQLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 239 QQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQ 318
Cdd:COG1196 277 EELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 319 LEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQgAKSLFSTAFSESL 398
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEE 428
|
250 260
....*....|....*....|....*..
gi 1691739872 399 AAEISSVSRDELMEAIQKQEEINFRLQ 425
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-384 |
9.53e-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: 60.84 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 190 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 269
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 270 LDEIESLTLR---LSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHS 346
Cdd:TIGR02168 294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 1691739872 347 RAResELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 384
Cdd:TIGR02168 373 RLE--ELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-388 |
2.70e-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: 59.69 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 181 RQENLQLVHRANA---LEEQLKEQE--LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCL 255
Cdd:TIGR02168 666 AKTNSSILERRREieeLEEKIEELEekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 256 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 335
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1691739872 336 SSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 388
Cdd:TIGR02168 826 LESL-------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-378 |
9.84e-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: 57.77 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 154 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRAcEMVLEETRRQKEllckmereksiEIEN 233
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 234 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ------------ENKRRMGDRLSH----- 296
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREieqkl 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 297 ------------ERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSsmgLQEYHSRARESELEQEVRRLKQDN 364
Cdd:TIGR02169 822 nrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQL 898
|
250
....*....|....
gi 1691739872 365 RNLKEQNEELNGQI 378
Cdd:TIGR02169 899 RELERKIEELEAQI 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-375 |
1.08e-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: 57.76 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 159 LERRVLELEKDtAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 238
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 239 QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLT---LRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDL 315
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691739872 316 RKQLEHLQLLKLEAEQR-----------RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELN 375
Cdd:TIGR02168 357 EAELEELEAELEELESRleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
150-419 |
1.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 150 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREK 227
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 228 SIEIENLQTRL----QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRrmgdrlshERHQFQR 303
Cdd:COG1196 322 EEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------ELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 304 DKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 383
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 1691739872 384 QGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEE 419
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-419 |
3.21e-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: 56.22 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 153 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELRACEMVLEETRRQKEL---------LCKM 223
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELyalaneisrLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 224 EREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLS---HERHQ 300
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 301 FQRDKEATQELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 378
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLeaRLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1691739872 379 ITLSIQGAKSlfSTAFSESLAAEISSVSRDELMEAIQKQEE 419
Cdd:TIGR02168 464 EELREELEEA--EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-425 |
1.05e-07 |
|
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: 54.29 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 150 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELracEMVLEETRRQKELLCKMEREKSI 229
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 230 E-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqrd 304
Cdd:TIGR02168 785 EeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 305 kEATQELIEDLRKQLEHL----------------QLLKLEAEQRRGRSSSMGLQEYHSRARES---------ELEQEVRR 359
Cdd:TIGR02168 862 -EELEELIEELESELEALlnerasleealallrsELEELSEELRELESKRSELRRELEELREKlaqlelrleGLEVRIDN 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1691739872 360 LKQdnrNLKEQneelngQIITLSIQGAKSLFSTAFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLQ 425
Cdd:TIGR02168 941 LQE---RLSEE------YSLTLEEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERYD 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
153-363 |
1.74e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 153 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQlkeqeLRACEMVLEETRRQKELlckmeREKSIEIE 232
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQER-----REALQRLAEYSWDEIDV-----ASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 233 NLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQR-DKEATQEL 311
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1691739872 312 IEDLRKQLEHLQLLKLEAEQRRG-RSSSMGLQEYHSRAREsELEQEVRRLKQD 363
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENlEERIDALRARLNRAEE-ELERAMRAFNRE 799
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-381 |
2.54e-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: 49.74 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 161 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvlEETRRQKELLCKMEREKSIEIEnlqtRLQQ 240
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVE----RLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 241 LDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE 320
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691739872 321 HlqllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNlKEQNEELNGQIITL 381
Cdd:pfam17380 548 M-------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-378 |
6.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 190 RANALEEQLkeQELRACEMVLEETRRQKELLCKMeREKSIEIENLQTRLQQLDEENSELRS-----CTPCLKANIERLEE 264
Cdd:COG4913 226 AADALVEHF--DDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 265 EKQKLLDEIESLTLRLSEEQENKRRMgdRLSHERHQFQRdkeatqelIEDLRKQLEHLQLLKLEAEQRRGR--------- 335
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARleallaalg 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1691739872 336 ----SSSMGLQEYHSRARE---------SELEQEVRRLKQDNRNLKEQNEELNGQI 378
Cdd:COG4913 373 lplpASAEEFAALRAEAAAllealeeelEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-388 |
7.46e-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: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 170 TAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSE 247
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 248 LRsctpclkANIERLEEEKQKLLDEI------ESLTLRLSEEQENK--------RRMGDRLSHERHQFQRDKEATQELIE 313
Cdd:COG4942 95 LR-------AELEAQKEELAELLRALyrlgrqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1691739872 314 DLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 388
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
149-361 |
8.44e-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: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 149 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElracemvlEETRRQKELLCKMEREKS 228
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--------EELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 229 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkqklLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 308
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1691739872 309 QELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLK 361
Cdd:COG4942 198 QKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-381 |
9.19e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 149 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREkS 228
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEER-----IEELKKEIEELEEKVKE-L 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 229 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 303
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1691739872 304 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITL 381
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-354 |
9.31e-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: 48.14 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 131 ALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQ--ELRACEM 208
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 209 VLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL---TLRLSEEQE 285
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1691739872 286 NKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHSRARESELE 354
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-375 |
2.02e-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: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 154 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLvhraNALEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIEN 233
Cdd:COG4913 654 AEYSWDEIDVASAEREIAELEAELERLDASSDDL----AALEEQLEELEAE-----LEELEEELDELKGEIGRLEKELEQ 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 234 LQTRLQQLDEENSELRSctPCLKANIERLEEEKQKLLDE------IESLTLRLSEEQENKRRMGDRLSHERHQFQRD-KE 306
Cdd:COG4913 725 AEEELDELQDRLEAAED--LARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFNREwPA 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1691739872 307 ATQELIEDLRKQLEHLQLL-KLEAEqrrgrsssmGLQEYHSRARESELEQE-------VRRLKQDNRNLKEQNEELN 375
Cdd:COG4913 803 ETADLDADLESLPEYLALLdRLEED---------GLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLN 870
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
182-378 |
2.29e-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: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 182 QENLQLVHRANaleEQLKEQELRACEMVLEETRRQKELLCKMereksieienlqtRLQQLDEenselrsctpclkanIER 261
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 262 LEEEKQKLLDEIESLTLRLSEEQENK----RRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRgrsS 337
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQeklmRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAK---K 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1691739872 338 SMGLQEYHSRARESELEQEVRRLKQDNR-----NLKEQNEELNGQI 378
Cdd:pfam10168 657 KMNYQRYQIAKSQSIRKKSSLSLSEKQRktikeILKQLGSEIDELI 702
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-367 |
2.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 172 ATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSc 251
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 252 tpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQ 331
Cdd:COG4913 338 -----DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180 190
....*....|....*....|....*....|....*.
gi 1691739872 332 RRGRsssmglqeyhSRARESELEQEVRRLKQDNRNL 367
Cdd:COG4913 413 ALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-431 |
2.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 182 QENLQlvhRANALEEQLKEQelracemvLEETRRQKEllcKMER--EKSIEIENLQTRLQQLDEENselrsctpcLKANI 259
Cdd:COG1196 185 EENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE---------LEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 260 ERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSM 339
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 340 GLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLsiQGAKSLFSTAFSESLAAEISsvSRDELMEAIQKQEE 419
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELLEALRAAAE 397
|
250
....*....|..
gi 1691739872 420 INFRLQDYIDRI 431
Cdd:COG1196 398 LAAQLEELEEAE 409
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
178-386 |
3.03e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 178 SRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSI--EIENLQTRLQQLDEENSELRSCTP 253
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPElrKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 254 CLKANIERLEEEKQKLLD--EIESLTLRLSEEQENKRRMGDRLShERHQfqrDKEATQELIEDLRKQLEH-----LQLLK 326
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYT-PNHP---DVIALRAQIAALRAQLQQeaqriLASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1691739872 327 LEAEQRRGRSSSMG--LQEYHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 386
Cdd:COG3206 320 AELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-419 |
3.51e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 160 ERRVLELEKDTAATGEQHSRLRQENLQLVhRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQ 239
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 240 QLDEENSELRSCTPCLKANIERLEEEKQ--------KLLDEIESLTLRLSEEQENKRRMGDRLSH---ERHQFQRDKEAT 308
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKleaEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 309 QELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 386
Cdd:TIGR02169 342 EREIEEERKRRDKLTeeYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270
....*....|....*....|....*....|....*
gi 1691739872 387 KSLFSTAFSESLAAEISSV--SRDELMEAIQKQEE 419
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELeeEKEDKALEIKKQEW 455
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
144-338 |
5.35e-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: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 144 LMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLC 221
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 222 KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLS-EEQENKR--RMGDRLSHER 298
Cdd:pfam19220 111 IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlLEQENRRlqALSEEQAAEL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1691739872 299 HQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSS 338
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEA 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-437 |
6.31e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 150 EDIADKVVfleRRVLELEK-----DTAATGEQHSRLRQENLQ-LVHRANALEEQLKEQELRacemvLEETRRQKELLCKM 223
Cdd:PRK03918 144 DESREKVV---RQILGLDDyenayKNLGEVIKEIKRRIERLEkFIKRTENIEELIKEKEKE-----LEEVLREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 224 EREKSIEIENLQTRLQQLD---EENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGD-------- 292
Cdd:PRK03918 216 LPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeey 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 293 -RLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQN 371
Cdd:PRK03918 296 iKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELYEEAK 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1691739872 372 EELNgqiitlSIQGAKSLFSTAFSESLAAEISSVSR--DELMEAIQKQEEINFRLQDYIDRIIVAIME 437
Cdd:PRK03918 369 AKKE------ELERLKKRLTGLTPEKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
138-374 |
7.71e-05 |
|
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: 45.33 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 138 EDPSPELMEgpeedIADKVVFLERrvlELEKDTAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLE 211
Cdd:COG3096 832 PDPEAELAA-----LRQRRSELER---ELAQHRAQEQQLRQQLDQlkEQLQLLNKllpqANLLADETLADRLEELREELD 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 212 E-------TRRQKELLCKMEREKSI------EIENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDE-- 272
Cdd:COG3096 904 AaqeaqafIQQHGKALAQLEPLVAVlqsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEns 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 273 --IESLTLRLSEEQENKRRMGDRLSHERHQFQrdkEATQELI----------EDLRKQLEHLQLLKL----EAEQR-RGR 335
Cdd:COG3096 984 dlNEKLRARLEQAEEARREAREQLRQAQAQYS---QYNQVLAslkssrdakqQTLQELEQELEELGVqadaEAEERaRIR 1060
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1691739872 336 SSSMGLQEYHSRAR-----------ESELEQEVRRLKQDNRNLKEQNEEL 374
Cdd:COG3096 1061 RDELHEELSQNRSRrsqlekqltrcEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-374 |
1.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 150 EDIADKVVFLERRVLELEKdtaaTGEQHSRLRQeNLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREksi 229
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK----VLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 230 eIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGD-------RLSHERHQFQ 302
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylELKDAEKELE 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1691739872 303 RDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGL---QEYHSRARES--ELEQEVRRLKQDNRNLKEQNEEL 374
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysEEEYEELREEylELSRELAGLRAELEELEKRREEI 692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-323 |
2.76e-04 |
|
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: 43.51 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 150 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELlckmeREKSI 229
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 230 EIENLQTRLQQLDEENSELRS--CTPCLKANIERLEEEKQKLLDEIESLTlRLSEEQENKRRMGDRLSHERHQFQRDKEA 307
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQ 486
|
170
....*....|....*.
gi 1691739872 308 TQELIEDLRKQLEHLQ 323
Cdd:TIGR02168 487 LQARLDSLERLQENLE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-378 |
4.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 159 LERRVLELEKDTAATGEQHsRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 238
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 239 QQLDEENSELRS----CTPC---------------LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRMGDRLSHERH 299
Cdd:PRK03918 422 KELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 300 QFQRDKEATQEL----IEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESELEQEVRRLKQDNRNLKEQNEELN 375
Cdd:PRK03918 501 LAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELL 576
|
...
gi 1691739872 376 GQI 378
Cdd:PRK03918 577 KEL 579
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-444 |
4.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 195 EEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSelRSCTPCLKANIERLEEEKQKLLDEIE 274
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK--MKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 275 SLTLRLSEEQENKRRMGDRLSHE-------RHQFQRDKEATQELIEDLRKQLEHL-----QLLKLEAEQRRGRSSSMGLQ 342
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAeeenkikAAEEAKKAEEDKKKAEEAKKAEEDEkkaaeALKKEAEEAKKAEELKKKEA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 343 EYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINF 422
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
250 260
....*....|....*....|..
gi 1691739872 423 RLQdyIDRIIVAIMETNPSILE 444
Cdd:PTZ00121 1793 RME--VDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-438 |
5.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 259 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSH----ERHQFQR-DKEATQELIEDLRKQLEHL-----QLLKLE 328
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEiDVASAEREIAELEAELERLdassdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 329 AEQRRgrsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS------IQGAKSLFSTAFSESLAAEI 402
Cdd:COG4913 692 EQLEE------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*.
gi 1691739872 403 SSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMET 438
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
207-333 |
1.20e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 207 EMVLEETRRqkELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQEN 286
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1691739872 287 KRRMGDRlshERHQFQRDKEAT--QELIEDLRKQLEHLQ--LLKLEAEQRR 333
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELEEERerIEELKRKLER 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
159-324 |
1.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 159 LERRVLELEKDTAATGEQHSRLRQenlQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 238
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRA---QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 239 QQLDEE-NSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgdrlsherHQFQRDKEATQELIEDLRK 317
Cdd:COG3206 301 AALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL--------RRLEREVEVARELYESLLQ 372
|
....*..
gi 1691739872 318 QLEHLQL 324
Cdd:COG3206 373 RLEEARL 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
178-384 |
1.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 178 SRLRQENLQLvHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI---EIENLQTRLQQLDEENSELRsctpc 254
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLE----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 255 LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRmgdrlshERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRG 334
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERL-EELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1691739872 335 RSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 384
Cdd:COG4717 195 QDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
187-362 |
1.43e-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: 41.09 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 187 LVHRANALEEQLKEQELRACEmvLEETRRQKELLCK---MEREKSIEIENLQTRLQQLDEENSE-LRSCtpclkanIERL 262
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEqAAEA-------VEQR 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 263 EEEKQKLlDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglq 342
Cdd:COG3096 581 SELRQQL-EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE----------- 648
|
170 180
....*....|....*....|
gi 1691739872 343 eyhSRARESELEQEVRRLKQ 362
Cdd:COG3096 649 ---LAARKQALESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-333 |
1.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 160 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqkellckmereksiEIENLQTRLQ 239
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 240 QLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK-RRMGDRLSH---ERHQFQRDKEATQELIEDL 315
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*...
gi 1691739872 316 RKQLEHLQLLKLEAEQRR 333
Cdd:COG4717 226 EEELEQLENELEAAALEE 243
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
194-378 |
2.26e-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: 40.22 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 194 LEEQLK--EQELRACEMVLEETRRQKELLCKMEReksieieNLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLD 271
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 272 EIESLTLRLSEEQENKRRMGDRLSHERhQFQRDKEATQEliedlrkqlehlQLLKLEAEQRRGRSSSMglqeyhsRARES 351
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 1691739872 352 ELEQEVRRLKQDNRNLKEQNEELNGQI 378
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
160-372 |
2.72e-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: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 160 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElRACEMVLEETRRQK---ELLCKMEREKSieienlqT 236
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE-EALREQAELNRLKKkylEALNKKLNEKE-------S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 237 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQElIEDLR 316
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR-IKELE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1691739872 317 KQLEHLQLLKLEAEQRRGRsssmglqeyhsRARESELEQEVRRLKQDNRNLKEQNE 372
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSE-----------LARIPELEKELERLREHNKHLNENIE 221
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-367 |
2.82e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 164 LELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDE 243
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 244 ENSELRSCTPcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ 323
Cdd:COG1196 657 SAGGSLTGGS-RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1691739872 324 LLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL 367
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
175-326 |
3.33e-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: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 175 EQHSRLRQENLQLVHRANALEEQLkeQELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctp 253
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIK--PKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK--- 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1691739872 254 clkaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 326
Cdd:smart00787 226 ----KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
159-372 |
3.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 159 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSIEIEnLQT 236
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQ-LLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 237 RLQQLDEENSELRSCTPCLKANIERLEEEKQkLLDEIESLTLRLSEEQEnkrrmgdrlsHERHQFQRDKEATQELIEDLR 316
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQE----------ELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1691739872 317 KQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNE 372
Cdd:COG4717 199 EELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
175-321 |
4.99e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 175 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmerEKSIEIENLQTRLQQLDEENselrsctpc 254
Cdd:PRK12705 34 EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLVQKEEQLDARA--------- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1691739872 255 lkaniERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLshERHQFQRDKEATQELIEDLRKQLEH 321
Cdd:PRK12705 98 -----EKLDNLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLLDAELEE 157
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-373 |
5.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 150 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvleETRRQKELLCKMEREKSI 229
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 230 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 309
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV-MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1691739872 310 ELIEDLRKQLEhlqlLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEE 373
Cdd:PTZ00121 1641 KEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
190-384 |
5.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 190 RANALEEQLKEQELRAcEMVLEETRRQKEllcKMEREKSIEIEnlqtrlqqldEENSELRSctpclkanieRLEEEKQKL 269
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAE---AIKKEALLEAK----------EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 270 LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrAR 349
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1691739872 350 E---SELEQEVR-----RLKQDNRNLKEQNEELNGQIITLSIQ 384
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
262-414 |
5.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 262 LEEEKQKLLDEIESLTLRLSEEQENKRR-MGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLlKLEAEQRRGRSS 337
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTeEEEEIRRLEEQVERLEAEVEELeaeLEEKDERIERLER-ELSEARSEERRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 338 smglqeyHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLsiqgaKSLFSTAFSESLAA--EISSVSRDELMEAI 414
Cdd:COG2433 461 -------IRKDREiSRLDREIERLERELEEERERIEELKRKLERL-----KELWKLEHSGELVPvkVVEKFTKEAIRRLE 528
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-374 |
6.65e-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: 39.00 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 157 VFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRA-----------CEMVLEETRRQKELLCKMER 225
Cdd:pfam01576 127 VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkheAMISDLEERLKKEEKGRQEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 226 EKSieIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDK 305
Cdd:pfam01576 207 EKA--KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1691739872 306 EATQELIEDLRKQLEHLQLLKLEAEQRRGrsSSMGLQEYHSRaRESELEQEVRRLKQDNRNLKEQNEEL 374
Cdd:pfam01576 285 AARNKAEKQRRDLGEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
165-429 |
9.33e-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: 38.41 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 165 ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE 244
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 245 NSELRSCTpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsHERHQFQRDKEATQELIEDLRKQLEHLQL 324
Cdd:pfam02463 261 EKEEEKLA--QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL------KLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 325 LKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQ-DNRNLKEQNEELNGQIITLSIQG-AKSLFSTAFSE-SLAAE 401
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLE 412
|
250 260
....*....|....*....|....*...
gi 1691739872 402 ISSVSRDELMEAIQKQEEINFRLQDYID 429
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIE 440
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
222-328 |
9.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.52 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 222 KMERE-KSIEIENLQTRLQQLDEENSEL-RSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH 299
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 1691739872 300 QFQRDKEATQELIEDLRKQLEHLQLLKLE 328
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
179-372 |
9.52e-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: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 179 RLRQENLQLVHRANALEEQLKEQELRACEMV---LEETRRQKELlckmEREKSIEIENLQTRLQQLDEENSELRsctpcl 255
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVrqeLEAARKVKIL----EEERQRKIQQQKVEMEQIRAEQEEAR------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691739872 256 KANIERLEEEKQKLLDEIESLTL-------RLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlrKQLEHLQLLKLE 328
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE---KELEERKQAMIE 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1691739872 329 AEQRRgrssSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNE 372
Cdd:pfam17380 511 EERKR----KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| |
