|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
760-1026 |
7.47e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAgEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 839
Cdd:COG1196 198 LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQ 919
Cdd:COG1196 277 EELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 920 LEHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQgAKSLFSTSFSESL 999
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEE 428
|
250 260
....*....|....*....|....*..
gi 284022108 1000 AAEISSVSRDELMEAIQKQEEINFRLQ 1026
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE 455
|
|
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
1007-1047 |
2.96e-14 |
|
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: 67.36 E-value: 2.96e-14
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 284022108 1007 SRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1047
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
762-1027 |
2.97e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 762 RRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKEllckmEREKSIEIENLQARLQQ 841
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 842 LDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLE 921
Cdd:COG1196 307 LEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 922 HLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAA 1001
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260
....*....|....*....|....*.
gi 284022108 1002 EISSVSRDELMEAIQKQEEINFRLQD 1027
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
760-1031 |
7.99e-14 |
|
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: 76.25 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQ-----EFRAQEKVLEETRKQ-KELLCKMEREKSI--- 830
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELeerleEAEEELAEAEAEIEElEAQIEQLKEELKAlre 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 EIENLQARLQQLDEENSELRSCTPCLKAN-------IERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLshERHQFQ 903
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 904 RDKEatQELIEDLRKQLEHLQLLRLEVEQRRGRSsslglqEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQ-IITL 982
Cdd:TIGR02168 882 RASL--EEALALLRSELEELSEELRELESKRSEL------RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTL 953
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 983 SIQGAKSLFSTSFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLqDYIDR 1031
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERY-DFLTA 1007
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
755-1028 |
1.87e-12 |
|
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: 71.64 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 755 DKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEkVLEETRKQKEllckmereksiEIEN 834
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 835 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEE-----------------------QENKRKM 891
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelskleeevsriearlREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 892 GDR------LSHERHQFQRDKEATQELIEDLRKQLEhlqLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDN 965
Cdd:TIGR02169 822 NRLtlekeyLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 966 RNLKEQNDELNGQIITLSIQ--------GAKSLFSTSFSESLAAEISSVS-----------RDELMEAIQKQEEINFR-L 1025
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRlselkaklEALEEELSEIEDPKGEDEEIPEeelsledvqaeLQRVEEEIRALEPVNMLaI 978
|
...
gi 284022108 1026 QDY 1028
Cdd:TIGR02169 979 QEY 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
791-985 |
2.19e-12 |
|
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: 71.63 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 791 RANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM 870
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 871 LDEIEELTQR---LSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQllrLEVEQRRGRSSSLGLQEYNS 947
Cdd:TIGR02168 294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK---EELESLEAELEELEAELEEL 370
|
170 180 190
....*....|....*....|....*....|....*...
gi 284022108 948 RARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 985
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
760-1020 |
2.70e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ--EKVLEETRKQKELLCKMEREKSIEIENLQA 837
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRelEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 838 RLQQLDEENSELRSCtpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQfQRDKEATQELIEDLR 917
Cdd:COG1196 345 ELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 918 KQLEHLQLLRLEVEQRRGRssslglqeynSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAkslfstsfsE 997
Cdd:COG1196 421 EELEELEEALAELEEEEEE----------EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA---------E 481
|
250 260
....*....|....*....|...
gi 284022108 998 SLAAEISSVSRDELMEAIQKQEE 1020
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
760-1028 |
3.77e-12 |
|
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: 70.86 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAgEQHGRLRQE--NLQL---VHRANALEEQLKEQEFRAQEKVLEETRKQKELlckmeREKSIEIEN 834
Cdd:TIGR02168 198 LERQLKSLERQAEKA-ERYKELKAElrELELallVLRLEELREELEELQEELKEAEEELEELTAEL-----QELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 835 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQ---RLSEEQENKRKMGDRLSHERHQFQRDKEATQE 911
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 912 LIEDLRKQLE-----------HLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQII 980
Cdd:TIGR02168 352 ELESLEAELEeleaeleelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 284022108 981 TLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQ-EEINFRLQDY 1028
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREElEEAEQALDAA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
761-1033 |
7.63e-12 |
|
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: 69.70 E-value: 7.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQL--KEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQAR 838
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA-------LAELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 839 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQR---LSEEQENKRKMGDRLSHE--------------RHQ 901
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALREALDELRAEltllneeaanlrerLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 902 FQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSLG----------LQEYNS--------RARESELEQEVRRLKQ 963
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleselealLNERASleealallRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284022108 964 DNRNLKEQNDELNGQI--ITLSIQGAKSLFstsfsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 1033
Cdd:TIGR02168 909 KRSELRRELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
754-963 |
7.19e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 754 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIE 833
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLDEENSELRsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELI 913
Cdd:COG1196 388 LLEALRAAAELAAQLEE-----LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 284022108 914 EDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEY---NSRARESELEQEVRRLKQ 963
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLlllEAEADYEGFLEGVKAALL 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
760-1020 |
1.81e-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: 65.46 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVleetRKQKELLCKMEREKSiEIENLQARL 839
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE----RQLEELEAQLEELES-KLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSElrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKrkmgDRLSHERHQFQRDKEATQELIEDLRKQ 919
Cdd:TIGR02168 340 AELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQL----ETLRSKVAQLELQIASLNNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 920 LEhlqllRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESL 999
Cdd:TIGR02168 409 LE-----RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250 260
....*....|....*....|.
gi 284022108 1000 AAEISsvSRDELMEAIQKQEE 1020
Cdd:TIGR02168 484 LAQLQ--ARLDSLERLQENLE 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
752-987 |
1.97e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.04 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVI--FLERRVSELEKDSAAAGEQhgrLRQENLQLVHRANALEEQLkeQEFRAQEKVLEETRKQKELLCKME---- 825
Cdd:COG3206 152 AVANALAeaYLEQNLELRREEARKALEF---LEEQLPELRKELEEAEAAL--EEFRQKNGLVDLSEEAKLLLQQLSeles 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 826 --REKSIEIENLQARLQQLDEENSELRSCTPCLKAN--IERLEEEKQKMLDEIEELTQRLSEEqenkrkmgdrlsHERHQ 901
Cdd:COG3206 227 qlAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPN------------HPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 902 fqrdkeATQELIEDLRKQLEH-----LQLLRLEVEQRRGRSSSLG--LQEYNSRARE-SELEQEVRRLKQDNRNLKEQND 973
Cdd:COG3206 295 ------ALRAQIAALRAQLQQeaqriLASLEAELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYE 368
|
250
....*....|....
gi 284022108 974 ELNGQIITLSIQGA 987
Cdd:COG3206 369 SLLQRLEEARLAEA 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
754-982 |
3.21e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 754 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQlkeQEFRAQEKVLEETRKqkellckmereksiEIE 833
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL---AEYSWDEIDVASAER--------------EIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdrlsherhqfqrdkeatqelI 913
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKE-------------------------L 722
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 914 EDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRR-LKQDNRNLKEQNDELNGQIITL 982
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1036 |
4.19e-10 |
|
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: 62.86 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 791 RANALEEQLKE--QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRsctpclkANIERLEEEKQ 868
Cdd:COG4942 21 AAAEAEAELEQlqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 869 KMLDEIEELTQRLSEEQENKRKMGDR-------LSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRgrssslg 941
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 942 lqeynsrareSELEQEVRRLKQDNRNLKEQNDELNGQIITlsiqgakslfstsfSESLAAEISSvSRDELMEAIQKQEEI 1021
Cdd:COG4942 167 ----------AELEAERAELEALLAELEEERAALEALKAE--------------RQKLLARLEK-ELAELAAELAELQQE 221
|
250
....*....|....*
gi 284022108 1022 NFRLQDYIDRIIVAI 1036
Cdd:COG4942 222 AEELEALIARLEAEA 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
791-1047 |
5.28e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 791 RANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM 870
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 871 LDEIEELTQrlseEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQllrLEVEQRRGRSSSLGLQEYNSRAr 950
Cdd:COG4372 114 QEELEELQK----ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ---EELAALEQELQALSEAEAEQAL- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 951 eSELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYID 1030
Cdd:COG4372 186 -DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250
....*....|....*..
gi 284022108 1031 RIIVAILETNPSILEVK 1047
Cdd:COG4372 265 LAILVEKDTEEEELEIA 281
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
761-973 |
1.28e-09 |
|
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: 62.07 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQE--FRAQEKVLEETRKQKELLCKMEREKSieienlqAR 838
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEeaLREQAELNRLKKKYLEALNKKLNEKE-------SQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 839 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEdlrk 918
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE---- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 919 qlehlqllrLEVEQRRGRSSSLGLQEYNSR-ARESELEQEVRRLKQDNRNLKEQND 973
Cdd:pfam05557 175 ---------LEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIE 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
764-985 |
1.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 764 VSELEKDSAAAGEQHGRLRQENLQlvhRANALEEQLKEQEfrAQEKVLEETRKQKEllckmerEKSIEIENLQARLQQLD 843
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAE--EKEEEYAELQEELE-------ELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 844 EENSELrsctpclkanieRLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLsHERHQFQRDKEATQELIEDLRKQLEHL 923
Cdd:COG4717 116 EELEKL------------EKLLQLLPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284022108 924 QLLRLEVEQRRGRSSSLGLQEynSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 985
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
761-1047 |
1.38e-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: 62.39 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGRLRQENLQLVhRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQ 840
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 841 QLDEENSELRSCTPCLKANIERLEEEKQKML-DEIEELTQRLSE----EQENKRKMGDrLSHERHQFQRDKEATQELIED 915
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEAEIASlersIAEKERELED-AEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 916 LRKQLEHLQLLRLEVEQRRGRSSslglQEYN-SRARESELEQEVRRLKQDNRNLKEQNDELNGQIitlsiqgakslfsts 994
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELK----EELEdLRAELEEVDKEFAETRDELKDYREKLEKLKREI--------------- 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 284022108 995 fsESLAAEISSVsRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1047
Cdd:TIGR02169 402 --NELKRELDRL-QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
762-963 |
1.91e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 762 RRVSELEKDSAAAGEQHGRLRQENLQLvHRANALEEQLKEQEFRAQEKvLEETRKQKELLCKMEREKSI--EIENLQARL 839
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALeaELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdrlsherhQFQRDKEATQELIEDLRKQ 919
Cdd:COG4717 149 EELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEE-------------ELQDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 284022108 920 LEHLQLLRLEVEQRRgrssslglQEYNSRARESELEQEVRRLKQ 963
Cdd:COG4717 212 EEELEEAQEELEELE--------EELEQLENELEAAALEERLKE 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
752-948 |
3.79e-09 |
|
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: 59.78 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ-------EKVL------EETRKQK 818
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqppLALLlspedfLDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 819 ELLCKMEREKSIEIENLQARLQQLDEenselrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHE 898
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAA-----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 284022108 899 RHQFQRDKEATQELIEDLRKQLEHLQllrLEVEQRRGRSSSLGLQEYNSR 948
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLE---AEAAAAAERTPAAGFAALKGK 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
760-962 |
4.71e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE-QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQAR 838
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 839 LQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRK 918
Cdd:PRK03918 323 INGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 284022108 919 QLEHLQLLRLEVEQRRGRSSSlglqeynsraRESELEQEVRRLK 962
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKK----------EIKELKKAIEELK 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
791-979 |
6.64e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 791 RANALEEQLKEQEfRAQEKVlEETRKQKELLCKMeREKSIEIENLQARLQQLDEENSELRS-----CTPCLKANIERLEE 865
Cdd:COG4913 226 AADALVEHFDDLE-RAHEAL-EDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 866 EKQKMLDEIEELTQRLSEEQENKRKMgdRLSHERHQFQRdkeatqelIEDLRKQLEHLQLLRLEVEQRRGR----SSSLG 941
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARlealLAALG 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 942 LQEYNSRA------------------RESELEQEVRRLKQDNRNLKEQNDELNGQI 979
Cdd:COG4913 373 LPLPASAEefaalraeaaallealeeELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
761-1001 |
9.98e-09 |
|
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: 59.60 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLK---------EQEFRAQEKVLEETRKQKELLCKMEREKSIE 831
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKesekekkkaEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 IENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQE 911
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 912 LIEDLRKQL------EHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 985
Cdd:pfam02463 438 SIELKQGKLteekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250
....*....|....*.
gi 284022108 986 GAKSLFSTSFSESLAA 1001
Cdd:pfam02463 518 DGVGGRIISAHGRLGD 533
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
757-1047 |
1.00e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.38 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 757 VIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKEllckmerEKSIEIEN 834
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarSELEQLEEELEELNEQLQ-------AAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 835 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIE 914
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 915 DLRKQleHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS 994
Cdd:COG4372 179 AEAEQ--ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 284022108 995 FSESLAAEIS-SVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1047
Cdd:COG4372 257 LKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
760-982 |
1.28e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQ---------ENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSI 830
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKElekrleeleERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 EIENLQARLQQLDEENSELrsctpclKANIERLEEEKQKMldeieELTQRLSEEQENKRKMgDRLSHERHQFQRDKEATQ 910
Cdd:PRK03918 406 EISKITARIGELKKEIKEL-------KKAIEELKKAKGKC-----PVCGRELTEEHRKELL-EEYTAELKRIEKELKEIE 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284022108 911 ELIEDLRKQLEHLQ-LLRLEVEQRRGRSSSLGLQEYNSRARESELEqEVRRLKQDNRNLKEQNDELNGQIITL 982
Cdd:PRK03918 473 EKERKLRKELRELEkVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
760-962 |
1.42e-08 |
|
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: 58.24 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKEL-------------LCKMER 826
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELeaqkeelaellraLYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 827 EKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEkqkmLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDK 906
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 907 EATQELIEDLRKQLEHL--QLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLK 962
Cdd:COG4942 195 AERQKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
780-1032 |
1.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 780 RLR--QENLQlvhRANALEEQLKEQefraqekvLEETRKQKEllcKMER--EKSIEIENLQARLQQLDEENselrsctpc 855
Cdd:COG1196 180 KLEatEENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 856 LKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLRLEVEQ 932
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 933 RRGRsssLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLsiQGAKSLFSTSFSESLAAEISsvSRDELM 1012
Cdd:COG1196 317 RLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELL 389
|
250 260
....*....|....*....|
gi 284022108 1013 EAIQKQEEINFRLQDYIDRI 1032
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE 409
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
490-553 |
2.39e-08 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 53.64 E-value: 2.39e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 490 EPGTAQEEGARLRAVFDALDRDGDGFVRIEDFIQFATVYG--AEQVKDLTQYLDPSGLGVISFEDF 553
Cdd:COG5126 60 ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEF 125
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
766-1038 |
2.91e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 766 ELEKDSAAAGEQHgRLRQENLQLVHRANALeeQLKEQEF----RAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQ 841
Cdd:pfam05483 406 ELEELKKILAEDE-KLLDEKKQFEKIAEEL--KGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 842 LDEENSElrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQE---NKRKMGDRLSHERHQFQRDKEATQELIEDLRK 918
Cdd:pfam05483 483 EKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVRE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 919 QL---------------EHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI---- 979
Cdd:pfam05483 556 EFiqkgdevkckldkseENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLnaye 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 980 -----ITLSIQGAKSLF---STSFSESLaaEISSVSRDELMEAIQK-----------QEEINFRLQDYIDRiIVAILE 1038
Cdd:pfam05483 636 ikvnkLELELASAKQKFeeiIDNYQKEI--EDKKISEEKLLEEVEKakaiadeavklQKEIDKRCQHKIAE-MVALME 710
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
754-1008 |
3.36e-08 |
|
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: 57.08 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 754 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKeqefrAQEKVLEETRKQkellckmereksieIE 833
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----ALARRIRALEQE--------------LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEE----QENKRKMGDRLsherHQFQRDKEAT 909
Cdd:COG4942 80 ALEAELAELEKEIAELR-------AELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRL----QYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 910 QELIEDLRKQLEHLQLLRLEVEQRRGRSSSLgLQEYnsRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLsIQGAKS 989
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEAL-LAEL--EEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEE 224
|
250
....*....|....*....
gi 284022108 990 LfsTSFSESLAAEISSVSR 1008
Cdd:COG4942 225 L--EALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
771-963 |
5.60e-08 |
|
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: 56.31 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 771 SAAAGEQHGRLRQENLQLVHRANALEEQLK--EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSE 848
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 849 LRsctpclkANIERLEEEKQKMLDE----------------------------IEELTQRLSEEQENKRKMGDRLSHERH 900
Cdd:COG4942 95 LR-------AELEAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284022108 901 QFQRDKEATQELIEDLRKQLEHLQLLRlevEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQ 963
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
763-982 |
6.06e-08 |
|
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: 56.67 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 763 RVSELEKDSAAAGEQHGRLRQEnLQLVHRANALEEQlKEQEFRAQEKVLEETRKQKE-----LLCKMEREKSIEIENLQ- 836
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQE-LEAARKVKILEEE-RQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERVRl 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 837 ---------ARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLD-EIEELTQRLSEEqENKRKMGDRLSHERHQFQRDK 906
Cdd:pfam17380 454 eeqerqqqvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAMIEE-ERKRKLLEKEMEERQKAIYEE 532
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 907 EATQELIEDLRKQLEhlqllrLEvEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNlKEQNDELNGQIITL 982
Cdd:pfam17380 533 ERRREAEEERRKQQE------ME-ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
755-955 |
6.16e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 755 DKVIFLERRVSELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQLKEQEFRaQEKVLEETRKQKEllckmereksiEIEN 834
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKR-RDKLTEEYAELKE-----------ELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 835 LQARLQQLDEENSELRSCTPCLKANIERLEEEK---QKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQE 911
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREInelKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 284022108 912 LIEDLRKQLEHLQLLRLEVEQRRGRSSSlGLQEYNSRARESELE 955
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKE-EYDRVEKELSKLQRE 491
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
500-557 |
7.90e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.94 E-value: 7.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284022108 500 RLRAVFDALDRDGDGFVRIEDFIQFATVYGA------EQVKDLTQYLDPSGLGVISFEDFYQGI 557
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgeplsdEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
760-1022 |
1.29e-07 |
|
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: 55.80 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSaaagEQHGRLRQENLQLVHRANALEEQLKEQEfraqekvleetrkqkellcKMEREKSIEIENLQARL 839
Cdd:TIGR04523 365 LEEKQNEIEKLK----KENQSYKQEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELtQRLSEEQENKRKMgdrLSHERHQFQRDKEATQELIEDLRKQ 919
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQLKV---LSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 920 LEHL----QLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQD---------NRNLKEQNDELNGQIITLSiQG 986
Cdd:TIGR04523 498 LKKLneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDElnkddfelkKENLEKEIDEKNKEIEELK-QT 576
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 284022108 987 AKSLFSTSFS-----ESLAAEISSVsRDELMEAIQKQEEIN 1022
Cdd:TIGR04523 577 QKSLKKKQEEkqeliDQKEKEKKDL-IKEIEEKEKKISSLE 616
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
776-1023 |
1.44e-07 |
|
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: 55.75 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 776 EQHGRLRQENLQLVHRANALE-EQLKEQEFRAQEKVL----------------EETRKQKELLCKMEREKSIEIENLQAR 838
Cdd:pfam02463 191 DLEELKLQELKLKEQAKKALEyYQLKEKLELEEEYLLyldylklneeridllqELLRDEQEEIESSKQEIEKEEEKLAQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 839 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLD-------------EIEELTQRLSEEQENKRKMGDRLSHERHQFQRD 905
Cdd:pfam02463 271 LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKlerrkvddeeklkESEKEKKKAEKELKKEKEEIEELEKELKELEIK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 906 KEATQELIEDLRKQLEHLQLLRLEV-----EQRRGRSSSLGLQEyNSRARESELEQEVRRLKQ-----DNRNLKEQNDEL 975
Cdd:pfam02463 351 REAEEEEEEELEKLQEKLEQLEEELlakkkLESERLSSAAKLKE-EELELKSEEEKEAQLLLElarqlEDLLKEEKKEEL 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 284022108 976 NGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDELMEaiqKQEEINF 1023
Cdd:pfam02463 430 EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL---KKSEDLL 474
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
762-975 |
1.47e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 762 RRVSELEKDSAAAGEQHGRLRQE----------------NLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKME 825
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKElrelekvlkkeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 826 REksieIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEI--------EELTQRLSE-------------- 883
Cdd:PRK03918 539 GE----IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELeelgfesvEELEERLKElepfyneylelkda 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 884 --EQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEYNSRARE--SELEQEVR 959
Cdd:PRK03918 611 ekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRRE 690
|
250
....*....|....*.
gi 284022108 960 RLKQDNRNLKEQNDEL 975
Cdd:PRK03918 691 EIKKTLEKLKEELEER 706
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
791-985 |
2.11e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.78 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 791 RANALEEQLKEQEFRAqEKVLEETRKQKELLCKmereksiEIEnLQARlqqldEENSELRSctpclkanieRLEEEKQKM 870
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAEAIKK-------EAL-LEAK-----EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 871 LDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEynsrAR 950
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 284022108 951 E---SELEQEVR-----RLKQDNRNLKEQNDELNGQIITLSIQ 985
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
760-968 |
2.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEkDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 839
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEE--NSELRsctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLR 917
Cdd:COG4913 326 DELEAQirGNGGD--------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 284022108 918 KQLEhlqllrlEVEQRRGRsssLGLQEYNSRARESELEQEVRRLKQDNRNL 968
Cdd:COG4913 398 EELE-------ALEEALAE---AEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
760-988 |
2.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLR---QENLQLVHRANALEEQL--KEQEFRAQEKVLEETRKQKELLCKMEREKSI---E 831
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKekeKELEEVLREINEISSELpeLREELEKLEKEVKELEELKEEIEELEKELESlegS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 IENLQARLQQLDEENSELRSCTPCLKANIERLEE-------------EKQKMLDEIEELTQRLSEEQENKRKMGDRLShE 898
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiklseFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 899 RHQFQRDKEATQELIEDLRKQLEHLQ--------LLRLEVEQRRGRSSSLGLQ--------EYNSRAREsELEQEVRRLK 962
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyeeAKAKKEELERLKKRLTGLTpeklekelEELEKAKE-EIEEEISKIT 411
|
250 260
....*....|....*....|....*.
gi 284022108 963 QDNRNLKEQNDELNGQIITLsiQGAK 988
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEEL--KKAK 435
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
755-1027 |
3.55e-07 |
|
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: 54.59 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 755 DKVIFLERRVSELEKDSAAAGEQHGRLRQEnLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKMEReKS 829
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQlrariEELRAQEAVLEETQERINRARKAAP-LA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 830 IEIENLQARLQQLDEENSELRSCTPCL-KANIERLEEEKQKM-LDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKE 907
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSsIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 908 ATQElIEDLRKQLEHLqllrlevEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQndelngQIITLSIQGA 987
Cdd:TIGR00618 377 LTQH-IHTLQQQKTTL-------TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ------QELQQRYAEL 442
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 284022108 988 KSLFSTSFSESLAAEISsvsrdELMEAIQKQEEINFRLQD 1027
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKI-----HLQESAQSLKEREQQLQT 477
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
760-1008 |
3.71e-07 |
|
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: 54.26 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLvhraNALEEQlKEQ--------EFRAQEKVLEETRKQKEllckmEREKSI- 830
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQ-KEQdwnkelksELKNQEKKLEEIQNQIS-----QNNKIIs 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 ----EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE-EQenkrkmgdrlsherhQFQRD 905
Cdd:TIGR04523 339 qlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDlES---------------KIQNQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 906 KEATQEliedLRKQLEHLQllrleveqrrgrssslglQEYNsraresELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 985
Cdd:TIGR04523 404 EKLNQQ----KDEQIKKLQ------------------QEKE------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260
....*....|....*....|...
gi 284022108 986 gAKSLfsTSFSESLAAEISSVSR 1008
Cdd:TIGR04523 456 -IKNL--DNTRESLETQLKVLSR 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
760-983 |
4.09e-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: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLkeqefRAQEKVLEETRKQKELLckmerekSIEIENLQARL 839
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASL-------NNEIERLEARL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSELRSctpclkaniERLEEEKQKMLDEIEELTQRLSEEQEnkrkmgdrlshERHQFQRDKEATQELIEDLRKQ 919
Cdd:TIGR02168 410 ERLEDRRERLQQ---------EIEELLKKLEEAELKELQAELEELEE-----------ELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 920 LEHLQLLRLEVEQRrgrssslgLQEYNSRARESE-LEQEVRRLKQDNRNLKEQNDELNGQIITLS 983
Cdd:TIGR02168 470 LEEAEQALDAAERE--------LAQLQARLDSLErLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
773-974 |
4.99e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 773 AAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKvLEETRKQKELLCKMEREksIEIENLQARLQQLDEENSELRSC 852
Cdd:pfam13868 56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVER--IQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 853 TPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdrlsheRHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQ 932
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 284022108 933 RRGRsssLGLQEYNSRARESELEQEVRRLKQdNRNLKEQNDE 974
Cdd:pfam13868 206 LRAK---LYQEEQERKERQKEREEAEKKARQ-RQELQQAREE 243
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
763-956 |
5.37e-07 |
|
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: 53.15 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 763 RVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQ 840
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 841 QLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLS-EEQENKR------KMGDRLS-----HERHQFQRDkeA 908
Cdd:pfam19220 129 AETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlLEQENRRlqalseEQAAELAeltrrLAELETQLD--A 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 909 TQELIEDLRKQLEHLQLLR--------LEVEQRRGRSSSLGLQEYNSRARESELEQ 956
Cdd:pfam19220 207 TRARLRALEGQLAAEQAEReraeaqleEAVEAHRAERASLRMKLEALTARAAATEQ 262
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
781-983 |
7.87e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 781 LRQENLQLVHRANALEEQLKEQE---FRAQEKVLEE-TRKQK---ELLCKMEREKSiEIENLQARLQQLDEEN------- 846
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNkniEEQRKKNGENiARKQNkydELVEEAKTIKA-EIEELTDELLNLVMDIedpsaal 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 847 SELRSCTPCLKANIERLEEEkQKMLDEIEEL---TQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIE---DLRKQL 920
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKV-IKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQS 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 921 EHLQLLRLEVEQRRGRssslgLQEYNSRAR--ESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 983
Cdd:PHA02562 337 KKLLELKNKISTNKQS-----LITLVDKAKkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
760-1046 |
8.05e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKELLCKmereksiEIENLQA 837
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAaqAELAQAQEELESLQEEAEELQE-------ELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 838 RLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHE---RHQFQRDKEATQELIE 914
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaldELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 915 DLRKQLEHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS 994
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 284022108 995 FSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEV 1046
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
797-1038 |
1.49e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 797 EQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEE 876
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ----AREELEQLEEELEQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 877 LTQRLSEEQENKRKMGDRLSHER---HQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRR-GRSSSLGLQEYNSRARES 952
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIaELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 953 E---LEQEVRRLKQDNRNLKEQndELNGQIITLSIQGAKSLFSTSFSESL--AAEISSVSRDELMEAIQKQEEINFRLQD 1027
Cdd:COG4372 158 QlesLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAekLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250
....*....|.
gi 284022108 1028 YIDRIIVAILE 1038
Cdd:COG4372 236 SALLDALELEE 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
760-975 |
2.33e-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: 51.88 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQ------ENLQLVHR----ANALE--------EQLKEQEFRAQEKVLEeTRKQKELL 821
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQqldqlkEQLQLLNKllpqANLLAdetladrlEELREELDAAQEAQAF-IQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 822 CKMEREKSI------EIENLQARLQQLDEENSELRSCTPCLKANIERLE----EEKQKMLDE----IEELTQRLSEEQEN 887
Cdd:COG3096 920 AQLEPLVAVlqsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlNEKLRARLEQAEEA 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 888 KRKMGDRLSHERHQFQrdkEATQELIeDLR-----KQLEHLQLLR----LEV------EQR-RGRSSSLGLQEYNSRAR- 950
Cdd:COG3096 1000 RREAREQLRQAQAQYS---QYNQVLA-SLKssrdaKQQTLQELEQeleeLGVqadaeaEERaRIRRDELHEELSQNRSRr 1075
|
250 260 270
....*....|....*....|....*....|....*
gi 284022108 951 ----------ESELEQEVRRLKQDNRNLKEQNDEL 975
Cdd:COG3096 1076 sqlekqltrcEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
801-1010 |
2.55e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 801 EQEFRAQEKVLEETRKQKELLCKmereksiEIENLQARLQQLDEENSELrsctpclKANIERLEEEKQKMLDEIEELTQR 880
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 881 LSEEQEnkrKMGDRLsheRHQFQRDK----------------------------EATQELIEDLRKQLEHLQLLRLEVEQ 932
Cdd:COG3883 81 IEERRE---ELGERA---RALYRSGGsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 933 RRGRSSSLgLQEYNSRARE-----SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVS 1007
Cdd:COG3883 155 KLAELEAL-KAELEAAKAEleaqqAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
...
gi 284022108 1008 RDE 1010
Cdd:COG3883 234 AAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
760-923 |
3.03e-06 |
|
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: 49.54 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ--EKVLEETRKQKELlckmeREKSIEIENLQA 837
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEY-----EALQKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 838 RLQQLDEENSELrsctpclKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELI-EDL 916
Cdd:COG1579 104 RISDLEDEILEL-------MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPEL 176
|
....*..
gi 284022108 917 RKQLEHL 923
Cdd:COG1579 177 LALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
793-1045 |
3.37e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 793 NALEEQLKE---------QEFRAQEKVLE-------ETRKQKELL----CKMEREKS-IEIENLQARLQ----------- 840
Cdd:TIGR04523 127 NKLEKQKKEnkknidkflTEIKKKEKELEklnnkynDLKKQKEELenelNLLEKEKLnIQKNIDKIKNKllklelllsnl 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 841 --------QLDEENSELRSCTPCLKANIERLEEEKQKMLDEI----EELTQRLSEEQENKRKMGDRlsherhqfQRDKEA 908
Cdd:TIGR04523 207 kkkiqknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLKDEQNKIKKQLSEK--------QKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 909 TQELIEDLRKQLEHL--QLLRLEVEQRRGRSSSLG---------LQEYNSRARE-----SELEQEVRRLKQ-------DN 965
Cdd:TIGR04523 279 NNKKIKELEKQLNQLksEISDLNNQKEQDWNKELKselknqekkLEEIQNQISQnnkiiSQLNEQISQLKKeltnsesEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 966 RNLKEQNDELNGQIITLSIQGAKSLFStsfSESLAAEISsvsrdELMEAIQKQEEINFRLQDYIDriivaILETNPSILE 1045
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQE---IKNLESQIN-----DLESKIQNQEKLNQQKDEQIK-----KLQQEKELLE 425
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
755-1026 |
4.03e-06 |
|
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: 51.27 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 755 DKVIFLERRvsELEKDSAAAGeQHGRlrQENLQLVHRANaLEEQLKEQEFRAQE-KVLEETRKQKellckmereksieIE 833
Cdd:pfam15921 561 DKVIEILRQ--QIENMTQLVG-QHGR--TAGAMQVEKAQ-LEKEINDRRLELQEfKILKDKKDAK-------------IR 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLDEENSELrsctpcLKANIERL------EEEKQKMLDEIE----ELTQrLSEEQE----NKRKMGDRLSHER 899
Cdd:pfam15921 622 ELEARVSDLELEKVKL------VNAGSERLravkdiKQERDQLLNEVKtsrnELNS-LSEDYEvlkrNFRNKSEEMETTT 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 900 HQFQRDKEATQELIEDLRKQLEHLQ-----------LLRLEVEQRRGRSSSLG-----LQEYNSRARESE--LEQEVRRL 961
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamGMQKQITAKRGQIDALQskiqfLEEAMTNANKEKhfLKEEKNKL 774
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 962 KQDNRNLKEQNDELNGQIITLSIQgAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQ 1026
Cdd:pfam15921 775 SQELSTVATEKNKMAGELEVLRSQ-ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
500-557 |
4.34e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 45.23 E-value: 4.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284022108 500 RLRAVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDLTQYL----DPSGLGVISFEDFYQGI 557
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELM 62
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
801-1022 |
4.46e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 801 EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSEL-------RSCTPCLKANIERLEEEKQKMLDE 873
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 874 IEELTQRLSEEQENKRKMGDRLSHERHQ-----------FQRDKEATQELIEDLRKQL----EHLQLLRLEVEQRRGRSS 938
Cdd:pfam05483 178 REETRQVYMDLNNNIEKMILAFEELRVQaenarlemhfkLKEDHEKIQHLEEEYKKEIndkeKQVSLLLIQITEKENKMK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 939 SLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI--ITLSIQGAKSLfSTSFSESLaaEISSVSRDELMEAIQ 1016
Cdd:pfam05483 258 DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELedIKMSLQRSMST-QKALEEDL--QIATKTICQLTEEKE 334
|
....*..
gi 284022108 1017 KQ-EEIN 1022
Cdd:pfam05483 335 AQmEELN 341
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
727-968 |
4.50e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 727 LHQSGTLTMEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEqhgrLRQENLQLVHRANALEEQLKEQEFRA 806
Cdd:COG5022 847 LIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS----LKLVNLELESEIIELKKSLSSDLIEN 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 807 QEKVLEETRKQKELLCKMEREKSIEIE-NLQARLQQLDEENSELRSCTPCLKANIERLEE---EKQKMLDEIEELTQRLS 882
Cdd:COG5022 923 LEFKTELIARLKKLLNNIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEYEDLLKKSTIlvrEGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 883 EEQENKRKM---GDRLSHERHQFQRDKEAT----------------QELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQ 943
Cdd:COG5022 1003 ELSKQYGALqesTKQLKELPVEVAELQSASkiissestelsilkplQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260
....*....|....*....|....*.
gi 284022108 944 EYNSRARESEL-EQEVRRLKQDNRNL 968
Cdd:COG5022 1083 LYQLESTENLLkTINVKDLEVTNRNL 1108
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
752-1020 |
5.41e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.34 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVIFLERRVSELEKdsaaAGEQHGRLRQENL----QLVHRANALEEQLKEQEFRAQEKVLEETRKQkellckmerE 827
Cdd:COG5185 240 DPESELEDLAQTSDKLEK----LVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIAEYTKSI---------D 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 828 KSIEIENLQARLQQLDEENSelrsctpclkanIERLEEEKQKMLDE-IEELTQR---LSEEQENKRKMGDRLSHERHQFQ 903
Cdd:COG5185 307 IKKATESLEEQLAAAEAEQE------------LEESKRETETGIQNlTAEIEQGqesLTENLEAIKEEIENIVGEVELSK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 904 RDKEATQEL--IEDLRKQLEHLQllrleVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI-- 979
Cdd:COG5185 375 SSEELDSFKdtIESTKESLDEIP-----QNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIse 449
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 284022108 980 ITLSIQGAKSLFSTSFSESLAAEISSV--SRDELMEAIQKQEE 1020
Cdd:COG5185 450 LNKVMREADEESQSRLEEAYDEINRSVrsKKEDLNEELTQIES 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
767-968 |
7.94e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 767 LEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEN 846
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 847 SELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLL 926
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 284022108 927 RLEVEQRrGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNL 968
Cdd:COG1196 739 EELLEEE-ELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
826-1033 |
8.74e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.57 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 826 REKSIEIENLQARLQQLDEENSELRSCTPCLKAN-IERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERhQFQR 904
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAEsSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE-QLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 905 dKEATQELIEDLRKQLEHLQLLRLEVEQRRgRSSSLGLQEYNSRARESELEQEVRRLKQdnrNLKEQNDELNGQIITL-S 983
Cdd:COG5185 321 -AEAEQELEESKRETETGIQNLTAEIEQGQ-ESLTENLEAIKEEIENIVGEVELSKSSE---ELDSFKDTIESTKESLdE 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 284022108 984 IQGAKSLFSTSFSESLAAEISSVSRD--ELMEAIQKQEEINFRLQDYIDRII 1033
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQieELQRQIEQATSSNEEVSKLLNELI 447
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
787-963 |
8.78e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 787 QLVHRANALEEQLKEQefRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRsctpclkaniERLEEE 866
Cdd:PRK04863 517 QLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR----------ERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 867 KQKmLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQrrgrssslglqeyn 946
Cdd:PRK04863 585 RQQ-LEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-------------- 649
|
170
....*....|....*..
gi 284022108 947 SRARESELEQEVRRLKQ 963
Cdd:PRK04863 650 LAARKQALDEEIERLSQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1018 |
8.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 860 IERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSH----ERHQFQR-DKEATQELIEDLRKQLEHLQLLRLEVEQrr 934
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEiDVASAEREIAELEAELERLDASSDDLAA-- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 935 grsssLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS------IQGAKSLFSTSFSESLAAEISSVSR 1008
Cdd:COG4913 690 -----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAALGDAVE 764
|
170
....*....|
gi 284022108 1009 DELMEAIQKQ 1018
Cdd:COG4913 765 RELRENLEER 774
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
760-953 |
1.02e-05 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 48.87 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEkdsaaagEQHGRLRQENLQLVHRANALEE--QLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQA 837
Cdd:pfam04849 99 LTERNEALE-------EQLGSAREEILQLRHELSKKDDllQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 838 RLQQLDEENSELRSCTPCLKANIERLEEEKQK-MLDEIEELTQ------RLSEEQENKRKmgdrlSHERHQfqrdKEATQ 910
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEKEQQlMSDCVEQLSEanqqmaELSEELARKME-----ENLRQQ----EEITS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 284022108 911 EL--IEDLRKQL--------EHLQLLRLEVE-QRRGRSSslgLQEYNSRARESE 953
Cdd:pfam04849 243 LLaqIVDLQHKCkelgieneELQQHLQASKEaQRQLTSE---LQELQDRYAECL 293
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
760-960 |
1.10e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQ------ENLQLVH----------------RANALEEQLKEQE-----FRAQEKVLE 812
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSqleqakEGLSALNrllprlnlladetladRVEEIREQLDEAEeakrfVQQHGNALA 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 813 ETRKQKELLckmeREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLE----EEKQKMLDEIEELTQRLSEEQENK 888
Cdd:PRK04863 922 QLEPIVSVL----QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 889 RKMGDRLSHERHQFQ-RDKEATQELIeDLRKQLEHLQLLRLEVEQRRgrsSSLGLQ-----EYNSRARESELEQEVRR 960
Cdd:PRK04863 998 EQERTRAREQLRQAQaQLAQYNQVLA-SLKSSYDAKRQMLQELKQEL---QDLGVPadsgaEERARARRDELHARLSA 1071
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
12-331 |
1.15e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 12 HDQPASGPQRGVMGLVGP---------DAPRGWSEEPEEHAQLQRWPEGPNAPICWPEEVEEPHAPSRWAKEPNAPRCSS 82
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPK 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 83 QEPDeschlAEELEESDSPRCwPQEPDTP--------CHLAKELEEPDAPRClPQEPDTPcylakelEEPNIPRcWPQEP 154
Cdd:PTZ00449 587 HPKD-----PEEPKKPKRPRS-AQRPTRPkspklpelLDIPKSPKRPESPKS-PKRPPPP-------QRPSSPE-RPEGP 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 155 DVPchlaKELEEPDAPRCwPQEPDafchlLKEVEEPDALRcwlqgpdapcHLAKELEDLDSPRcwPQEPDESCHLAKELE 234
Cdd:PTZ00449 652 KII----KSPKPPKSPKP-PFDPK-----FKEKFYDDYLD----------AAAKSKETKTTVV--LDESFESILKETLPE 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 235 EPDAPCHLAKEL-----EEPDAPRCWPQEPDVPcllakkweESDAPCLLTEELEEPDALHCWPQESEAPCLLAKELEEPD 309
Cdd:PTZ00449 710 TPGTPFTTPRPLppklpRDEEFPFEPIGDPDAE--------QPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEED 781
|
330 340
....*....|....*....|..
gi 284022108 310 AShscpqeADTGclsakEPEEP 331
Cdd:PTZ00449 782 IH------AETG-----EPDEA 792
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
760-964 |
1.17e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQE--KVLEETRKQKELLCKMEREK---SIEIEN 834
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEleTLEAEIEDLRETIAETEREReelAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 835 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE----------EQENKRKMGDRLShERHQFQR 904
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqahneEAESLREDADDLE-ERAEELR 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 905 DKEAT-----QELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQD 964
Cdd:PRK02224 363 EEAAEleselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
800-1027 |
1.23e-05 |
|
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: 49.25 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 800 KEQEFRAQEKVLEETRKQKELLckmerekSIEIENLQARLQQLDEENSELRsctpclkanierleeeKQKmldeieeltq 879
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYNDLK----------------KQK---------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 880 rlsEEQENkrkmgdrlshERHQFQRDKEATQELIEDLRKQLEHLQLLRLEveqrrgrssslgLQEYNSRAResELEQEVR 959
Cdd:TIGR04523 169 ---EELEN----------ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN------------LKKKIQKNK--SLESQIS 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 960 RLKQDNRNLKEQNDELNGQIitlsiqgakslfstsfsESLAAEISSVsRDELMEAIQKQEEINFRLQD 1027
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEI-----------------NEKTTEISNT-QTQLNQLKDEQNKIKKQLSE 271
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
782-983 |
1.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 782 RQENLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEnselrsctpcl 856
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET----------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 857 kanIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDR----------LSHERHQFQRDKEATQELIEDLRKQLEhlqll 926
Cdd:PRK02224 267 ---IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQ----- 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 284022108 927 RLEVEQRRGRSSSLGLQEYNSRARE--SELEQEVRRLKQDNRNLKEQNDELNGQIITLS 983
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
752-884 |
1.48e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE----QEFRAQEKVLEETRKQKELLCKMERE 827
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYEALQKEIESLKRRISDLEDEILE 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284022108 828 KSIEIENLQARLQ----QLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEE 884
Cdd:COG1579 115 LMERIEELEEELAeleaELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
760-975 |
1.73e-05 |
|
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: 49.02 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRA---------QEKVLE--ETRKQKELLCKMEREK 828
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkHEAMISdlEERLKKEEKGRQELEK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 829 SIEieNLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEA 908
Cdd:pfam01576 209 AKR--KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 909 tQELIEDLRKQL-EHLQLLRLEVEQRRGrsSSLGLQEYNSRaRESELEQEVRRLKQDNRNLKEQNDEL 975
Cdd:pfam01576 287 -RNKAEKQRRDLgEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
831-979 |
1.75e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 45.32 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 EIENLQARLQQLDEEnselrsctpclkanIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdrlsHERhQFQRDKEATQ 910
Cdd:pfam07926 2 ELSSLQSEIKRLKEE--------------AADAEAQLQKLQEDLEKQAEIAREAQQN---------YER-ELVLHAEDIK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284022108 911 ELiEDLRKQLEHLQL----LRLEVEQRRgrsSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI 979
Cdd:pfam07926 58 AL-QALREELNELKAeiaeLKAEAESAK---AELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
766-1020 |
1.75e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 766 ELEKDSAAAGEQHGRLRQENLQLVHRAnaleEQLKEQEFRAQEKVLEETRKQKellckMEREKSIEIENLQARLQQLDEE 845
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQS----EKDKKNKALAERKDSANERLNS-----LEAQLKQLDKKHQAWLEEQKEQ 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 846 NSELRSCTPC--------------------------LKANIERLEEEKQKMLD--------------EIEELTQRLSEEQ 885
Cdd:pfam12128 709 KREARTEKQAywqvvegaldaqlallkaaiaarrsgAKAELKALETWYKRDLAslgvdpdviaklkrEIRTLERKIERIA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 886 ENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHL--QLLRLEVEQRRgRSSSLGLQEYNSRARESELEQEVRRLKQ 963
Cdd:pfam12128 789 VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELqqQLARLIADTKL-RRAKLEMERKASEKQQVRLSENLRGLRC 867
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 964 DNRNLKEQNDELNGQIITLSIqgakslfstsfSESLAA-EISSVSRDELMEAIQKQEE 1020
Cdd:pfam12128 868 EMSKLATLKEDANSEQAQGSI-----------GERLAQlEDLKLKRDYLSESVKKYVE 914
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
760-926 |
1.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQ--ENLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKmereksiEI 832
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEA-------EL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 833 ENLQarlQQLDEEnseLRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKrkmgdrlshERHQFQRDKEATQEL 912
Cdd:COG4717 173 AELQ---EELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---------EELEEELEQLENELE 237
|
170
....*....|....
gi 284022108 913 IEDLRKQLEHLQLL 926
Cdd:COG4717 238 AAALEERLKEARLL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
760-976 |
2.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVleetrkqkellckmEREKSIEIENLQARL 839
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE--------------DLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSElrsctpclkanierleeekQKMLDEIEELTQRLSEEQENKRkmgDRLSHERHQFQRD-KEATQELIEDLRK 918
Cdd:COG4913 756 AAALGDAVE-------------------RELRENLEERIDALRARLNRAE---EELERAMRAFNREwPAETADLDADLES 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 919 QLEHLQLL-RLEVEqrrgrssslGLQEYNSRARESELEQE-------VRRLKQDNRNLKEQNDELN 976
Cdd:COG4913 814 LPEYLALLdRLEED---------GLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLN 870
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
782-1028 |
2.25e-05 |
|
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: 48.58 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 782 RQENLQLVHRANALEEQLKEQefraQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIE 861
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEM----LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK----LRSRVD 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 862 RLEEEKQKMLDEIEELTQRLSEEQENKRKMGdrlsherhqfQRDKeatqeLIEDLRKQLEHLqllrLEVEQRRGRSSSLG 941
Cdd:pfam15921 528 LKLQELQHLKNEGDHLRNVQTECEALKLQMA----------EKDK-----VIEILRQQIENM----TQLVGQHGRTAGAM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 942 LQEynsrarESELEQEV--RRLK-QDNRNLKEQND----ELNGQIITLSIQGAKslFSTSFSESLAA--EISSvSRDELM 1012
Cdd:pfam15921 589 QVE------KAQLEKEIndRRLElQEFKILKDKKDakirELEARVSDLELEKVK--LVNAGSERLRAvkDIKQ-ERDQLL 659
|
250
....*....|....*..
gi 284022108 1013 EAIQK-QEEINFRLQDY 1028
Cdd:pfam15921 660 NEVKTsRNELNSLSEDY 676
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
760-983 |
2.50e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEqeFRAQEKVLEETRKqkELLCKMEREKSiEIENLQARL 839
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE--LREEAQELREKRD--ELNEKVKELKE-ERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEEL-----TQRLSEEQENK-----RKMGDRLSHERHQFQRDKEAT 909
Cdd:COG1340 88 NELREELDELRK----ELAELNKAGGSIDKLRKEIERLewrqqTEVLSPEEEKElvekiKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 910 QEL--IEDLRKQLEHLqllRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 983
Cdd:COG1340 164 ELRaeLKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
781-970 |
2.70e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 781 LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANI 860
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 861 ERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSL 940
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190
....*....|....*....|....*....|
gi 284022108 941 GLQEYNSRARESELEQEVRRLKQDNRNLKE 970
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
808-1015 |
3.19e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 808 EKVLEETRKqkELLCKMEREKSIEIENLQARLQQLDEENSELRSctpclkaNIERLEEEKQKMLDEIEELTQRLsEEQEN 887
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERI-ERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 888 KrkmgdrlsherhqfqrdkeatqelIEDLRKQlehlqlLRLEVEQRRgrssslglqEYNSRARE-SELEQEVRRLKQDNR 966
Cdd:COG2433 449 E------------------------LSEARSE------ERREIRKDR---------EISRLDREiERLERELEEERERIE 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 284022108 967 NLKEQNDELnGQIITLSIQGAKslfstsfseSLAAEISSVSRDELMEAI 1015
Cdd:COG2433 490 ELKRKLERL-KELWKLEHSGEL---------VPVKVVEKFTKEAIRRLE 528
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
776-984 |
4.16e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 776 EQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLcKMEReksiEIENLQARLQQLDEENSELRSCTPC 855
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQ-LQER----LEEACHKRQLKEREEQKKVQENNLS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 856 LKANIERL---------EEEKQKMLDeieeLTQRLSEEQENK--------RKMGDRLSHERHQFQRDKEATQeliEDLRK 918
Cdd:pfam15558 176 ELLNHQARkvlvdcqakAEELLRRLS----LEQSLQRSQENYeqlveerhRELREKAQKEEEQFQRAKWRAE---EKEEE 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 284022108 919 QLEHLQLLRLEVEQRRGRS---SSLGLQEYNSRARESELEQEvrRLKQDNRNLKEQNDELNGQIITLSI 984
Cdd:pfam15558 249 RQEHKEALAELADRKIQQArqvAHKTVQDKAQRARELNLERE--KNHHILKLKVEKEEKCHREGIKEAI 315
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
753-963 |
4.28e-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: 47.64 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 753 IADKVIFLERRVSelekDSAAAGEQHgrlrQENLQLVHRANAleEQLKEQEFRAQEKVLEETRKQKELLckmEREKSI-- 830
Cdd:COG3096 453 ATEEVLELEQKLS----VADAARRQF----EKAYELVCKIAG--EVERSQAWQTARELLRRYRSQQALA---QRLQQLra 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 ---EIENLQARLQQLDEENSELrsctpCLKANIER-----LEEEKQKMLDEIEELTQRLSEEQENkrkmgdrlsheRHQF 902
Cdd:COG3096 520 qlaELEQRLRQQQNAERLLEEF-----CQRIGQQLdaaeeLEELLAELEAQLEELEEQAAEAVEQ-----------RSEL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 903 QRDKEATQELIEDLRKQ----------LEHL-------------------QLLRLEVEQRRGRSsslglqeyNSRARESE 953
Cdd:COG3096 584 RQQLEQLRARIKELAARapawlaaqdaLERLreqsgealadsqevtaamqQLLEREREATVERD--------ELAARKQA 655
|
250
....*....|
gi 284022108 954 LEQEVRRLKQ 963
Cdd:COG3096 656 LESQIERLSQ 665
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
760-1004 |
5.11e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQhgrLRQENLQLVHRANALEEQ----LKEQEFRAQEKVLEETRKQKEL--LCKMEREKSIEIE 833
Cdd:TIGR00618 716 YDREFNEIENASSSLGSD---LAAREDALNQSLKELMHQartvLKARTEAHFNNNEEVTAALQTGaeLSHLAAEIQFFNR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLDEENSELRSCTP----CLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEAT 909
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKII 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 910 QELiedlrKQLEHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKS 989
Cdd:TIGR00618 873 QLS-----DKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQGLALLVADAYTGSVRP 947
|
250
....*....|....*
gi 284022108 990 LFSTSFSESLAAEIS 1004
Cdd:TIGR00618 948 SATLSGGETFLASLS 962
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
765-975 |
6.36e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 765 SELEkdsaAAGEQHGRLRQENLQLVHrANALEEQLKEQEFRAQEKVLE-ETRKQKELLCKMEREKSIEIENLQARLQQLD 843
Cdd:pfam12128 322 SELE----ALEDQHGAFLDADIETAA-ADQEQLPSWQSELENLEERLKaLTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 844 EENSELRSCTPCLKANIER-LEEEKQKMLDEIEELTQRLSEEQEnkrKMGDRLSHERHQfQRDKEATQELIEDLRKQLEH 922
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEFNEEEY---RLKSRLGELKLR-LNQATATPELLLQLENFDER 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 284022108 923 LQLLRLEVEQRRGRSSSLGLQEYNSRAREselEQEVRRLKQDNRNLKEQNDEL 975
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRR---DQASEALRQASRRLEERQSAL 522
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
793-1022 |
6.36e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 793 NALEEQLKEQEFRAQEKVLEETRKQKELlckmereksieIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLD 872
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDEL-----------NEELKELAEKRDELNAQVKE----LREEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 873 EIEELTQRLSEEQENKRKMGDRLshERHQFQRDKEATQEL-IEDLRKQLEHLqllrleveQRRGRSSSLGLQEynsrarE 951
Cdd:COG1340 72 KVKELKEERDELNEKLNELREEL--DELRKELAELNKAGGsIDKLRKEIERL--------EWRQQTEVLSPEE------E 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 952 SELEQEVRRLKQDNRNLKEQNdELNGQIITLS--IQGAKSLFSTSFSE--SLAAEISSVSrDELMEAIQKQEEIN 1022
Cdd:COG1340 136 KELVEKIKELEKELEKAKKAL-EKNEKLKELRaeLKELRKEAEEIHKKikELAEEAQELH-EEMIELYKEADELR 208
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
752-1020 |
6.88e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLkeQEFRAQEKVLEETRKQKELLCKMEREKSIE 831
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT--SAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 IENlqaRLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIE---ELTQRLSEEQENKRKMGDRLSH-ERHQFQRD-- 905
Cdd:TIGR00618 447 ITC---TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHpNPARQDIDnp 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 906 -------------KEATQELIEDLRKQLEHL--QLLRLEVEQRRGRSSSLGLQEYNSRARES-----ELEQEVRRLKQDN 965
Cdd:TIGR00618 524 gpltrrmqrgeqtYAQLETSEEDVYHQLTSErkQRASLKEQMQEIQQSFSILTQCDNRSKEDipnlqNITVRLQDLTEKL 603
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 284022108 966 RNLKEQNDELN-GQIITLSIQGAK---SLFSTSFSESLAAEISSVSRDELMEAIQKQEE 1020
Cdd:TIGR00618 604 SEAEDMLACEQhALLRKLQPEQDLqdvRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
760-982 |
7.29e-05 |
|
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: 46.94 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQ-------LVHRANALEEQLKEQEFR--AQEKVLEET------------RKQK 818
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKnnseikdLTNQDSVKELIIKNLDNTreSLETQLKVLsrsinkikqnleQKQK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 819 ELlckmeREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMG------ 892
Cdd:TIGR04523 490 EL-----KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeid 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 893 ------DRLSHE-----RHQFQRDKEATQ----------------ELIEDLRKQLEHlqllrLEVEQRRgrsssLGLQEY 945
Cdd:TIGR04523 565 eknkeiEELKQTqkslkKKQEEKQELIDQkekekkdlikeieekeKKISSLEKELEK-----AKKENEK-----LSSIIK 634
|
250 260 270
....*....|....*....|....*....|....*..
gi 284022108 946 NSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITL 982
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
783-979 |
8.17e-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: 46.58 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 783 QENLQLVHRANaleEQLKEQEFRAQEKVLEETRKQKELLCKMereksieienlqaRLQQLDEenselrsctpclkanIER 862
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 863 LEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQR--------DKEATQELiEDLRKQLEHL-----QLLRLE 929
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSqlpvlsdaEREMKKEL-ETINEQLKHLanaikQAKKKM 658
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 284022108 930 VEQRrgRSSSLGLQEYNSRARESELEQEvRRLKQdnrNLKEQNDELNGQI 979
Cdd:pfam10168 659 NYQR--YQIAKSQSIRKKSSLSLSEKQR-KTIKE---ILKQLGSEIDELI 702
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
756-931 |
1.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 756 KVIFLERRVSELEKDSAAAGEQHGRLRQenlqLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMER--EKSIEIE 833
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQ-ENKRKMGDRLSHE----RHQFQRDKEA 908
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRElaglRAELEELEKR 688
|
170 180
....*....|....*....|....*.
gi 284022108 909 TQEL---IEDLRKQLEHLQLLRLEVE 931
Cdd:PRK03918 689 REEIkktLEKLKEELEEREKAKKELE 714
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
762-974 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 762 RRVSELEKDSAAAGEQHGRLRQ--ENLQLVHRANALEEQLKEQEFRAQE--------KVLEETRKQKELLCKMEREKSIE 831
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEeakkadeaKKAEEKKKADELKKAEELKKAEE 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 IENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKmGDRLSHERHQFQRDKEATQE 911
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284022108 912 LIEDLRKQLEhlqlLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDE 974
Cdd:PTZ00121 1642 EAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
776-932 |
1.06e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 44.67 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 776 EQHGRLRQENLQLVHRANALEEQLKEQEFRA---QEKVLEETRKQKELLCkmeREKSIEIENLQARLQQLDEENSELRSC 852
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAkklEEKAQAALTKGNEELA---REALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 853 TPCLKANIERL-------EEEKQKMLdeIEELTQRlSEEQENKRKMGDRLSHERHQFQR--DKEATQELIEDLRKQLEHL 923
Cdd:pfam04012 113 VEQLRKQLAALetkiqqlKAKKNLLK--ARLKAAK-AQEAVQTSLGSLSTSSATDSFERieEKIEEREARADAAAELASA 189
|
....*....
gi 284022108 924 QLLRLEVEQ 932
Cdd:pfam04012 190 VDLDAKLEQ 198
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
760-1032 |
1.08e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQhgrLRQENLQLV------HRA-NALEEQLKE-QEFRAQekvLEETRKQKELLCKMEREKsie 831
Cdd:PRK11281 126 LESRLAQTLDQLQNAQND---LAEYNSQLVslqtqpERAqAALYANSQRlQQIRNL---LKGGKVGGKALRPSQRVL--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 ienLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEE----QE---NKRKmgdRLSHERHQFQR 904
Cdd:PRK11281 197 ---LQAEQALLNAQNDLQRK----SLEGNTQLQDLLQKQRDYLTARIQRLEHQlqllQEainSKRL---TLSEKTVQEAQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 905 DKEATQELIED--LRKQLEH-LQLLRLEVEQRrgrssslglQEYNSRARES-ELEQEVRRLKQDNRNLKEQNDELNGQII 980
Cdd:PRK11281 267 SQDEAARIQANplVAQELEInLQLSQRLLKAT---------EKLNTLTQQNlRVKNWLDRLTQSERNIKEQISVLKGSLL 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 981 tLS-I--QGAKSLFSTSFSESLAAEISSVsRDELMEAIQKQEEInFRLQDYIDRI 1032
Cdd:PRK11281 338 -LSrIlyQQQQALPSADLIEGLADRIADL-RLEQFEINQQRDAL-FQPDAYIDKL 389
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
768-1026 |
1.16e-04 |
|
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: 46.27 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 768 EKDS--AAAGEQHGRLRQENLQLVHRAnaleeQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEE 845
Cdd:pfam05557 94 EKESqlADAREVISCLKNELSELRRQI-----QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 846 NselrsctpclkANIERLEEEKQKMLDEIEELTQ------RLSEEQENKRKMGDRLSHERhQFQRDKEATQELIEDLRKQ 919
Cdd:pfam05557 169 E-----------QRIKELEFEIQSQEQDSEIVKNskselaRIPELEKELERLREHNKHLN-ENIENKLLLKEEVEDLKRK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 920 LEHL-----QLLRLEVEQRRgrsSSLGLQEYNSRARESELE--------QEVRRLKQDNRNLKEQNDELNGQIITLSIQG 986
Cdd:pfam05557 237 LEREekyreEAATLELEKEK---LEQELQSWVKLAQDTGLNlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 284022108 987 akslfstsfsESLAAEISSVSRD--ELMEAIQKQEEINFRLQ 1026
Cdd:pfam05557 314 ----------RELEQELAQYLKKieDLNKKLKRHKALVRRLQ 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
781-1024 |
1.17e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 781 LRQENLQLVHRANALEEQL-KEQEFRAQEKVLEEtrkQKELLCKMEREKSI-EIENLQARLQQLDEEnselrsctpclka 858
Cdd:PRK04863 839 LRQLNRRRVELERALADHEsQEQQQRSQLEQAKE---GLSALNRLLPRLNLlADETLADRVEEIREQ------------- 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 859 nIERLEEEK------QKMLDEIEELTQRLSEEQENkrkmgdrlsHErhQFQRDKEATQELIEDLRKQLEHLQllrlEVEQ 932
Cdd:PRK04863 903 -LDEAEEAKrfvqqhGNALAQLEPIVSVLQSDPEQ---------FE--QLKQDYQQAQQTQRDAKQQAFALT----EVVQ 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 933 RR---GRSSSLGLQEYNS------RARESELEQEVRRLKQDnrnLKEQNDELngqiitlsiqgakslfsTSFSESLAAEI 1003
Cdd:PRK04863 967 RRahfSYEDAAEMLAKNSdlneklRQRLEQAEQERTRAREQ---LRQAQAQL-----------------AQYNQVLASLK 1026
|
250 260
....*....|....*....|...
gi 284022108 1004 SS--VSRDELMEAIQKQEEINFR 1024
Cdd:PRK04863 1027 SSydAKRQMLQELKQELQDLGVP 1049
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
760-977 |
1.62e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHgRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 839
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 QQLDEENSELRS----CTPC---------------LKANIERLEEEKQK------------------------------M 870
Cdd:PRK03918 422 KELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEieekerklrkelrelekvlkkeseliklkeL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 871 LDEIEELTQRLS-----------EEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSS 939
Cdd:PRK03918 502 AEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 940 LG---LQEYNSRARE---------------SELEQEVRRLKQDNRNLKEQNDELNG 977
Cdd:PRK03918 582 LGfesVEELEERLKElepfyneylelkdaeKELEREEKELKKLEEELDKAFEELAE 637
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
735-1037 |
1.71e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 735 MEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEQHGRLRQE--NLQLVHRANALEEQLKEQE--------- 803
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARlllliaaal 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 804 -------------------------------FRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSC 852
Cdd:COG4717 259 lallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 853 TPCLKANIERLEEEKQKMLDEIEELtQRLSEEQENKRKMGDRLSHERHQFqrdkEATQELIEDLRKQLEHLQLLRLEVEQ 932
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEEL----RAALEQAEEYQELKEELEELEEQLEE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 933 RRGrssslGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSiqgakslfstsfseslaAEISSVSRD-EL 1011
Cdd:COG4717 414 LLG-----ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-----------------AELEQLEEDgEL 471
|
330 340
....*....|....*....|....*.
gi 284022108 1012 MEAIQKQEEINFRLQDYIDRIIVAIL 1037
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKL 497
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
823-930 |
1.71e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 823 KMERE-KSIEIENLQARLQQLDEENSEL-RSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERH 900
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100 110
....*....|....*....|....*....|
gi 284022108 901 QFQRDKEATQELIEDLRKQLEHLQLLRLEV 930
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
760-974 |
1.79e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCK---MEREKSiEIENLQ 836
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkeLEKEEE-REEDER 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 837 ARLQQLDEENSELRsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDL 916
Cdd:pfam13868 157 ILEYLKEKAEREEE-----REAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 917 RKQLEHLQLLRLEVEQRRGRssslgLQEYnsRARESELEQEVRRLKQDNRNLKEQNDE 974
Cdd:pfam13868 232 RQRQELQQAREEQIELKERR-----LAEE--AEREEEEFERMLRKQAEDEEIEQEEAE 282
|
|
| BCAS2 |
pfam05700 |
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ... |
770-882 |
2.03e-04 |
|
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic sequences of unknown function. The mammalian members of this family are annotated as breast carcinoma amplified sequence 2 (BCAS2) proteins. BCAS2 is a putative spliceosome associated protein.
Pssm-ID: 428593 [Multi-domain] Cd Length: 204 Bit Score: 43.73 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 770 DSAAAGEQHGRLRQENLQLV--HRANA--LEEQLKEQEFRAQEKVLEETRKQKELLckmEREKSIEIENLQARLQQLDEE 845
Cdd:pfam05700 98 DNAYAQLEHQRIRIENLELLqkYGANAwrLHNYQLEAILRRLEKELAETKEAIEEV---NRQRKNAQTAAGGELRSLEEK 174
|
90 100 110
....*....|....*....|....*....|....*..
gi 284022108 846 NSELRSctpclkANIErLEEEKQKMLDEIEELTQRLS 882
Cdd:pfam05700 175 WKELVS------KNLE-IEAACEALEAEILELKRQAA 204
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
760-979 |
2.21e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQE--------------NLQLVHRANALEEQLKEqefrAQEKVLEETRKQKEL---LC 822
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSElesvssllneaegkNIKLSKDVSSLESQLQD----TQELLQEETRQKLNLstrLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 823 KMEREKSIEIE----------NLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMg 892
Cdd:pfam01576 493 QLEDERNSLQEqleeeeeakrNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL- 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 893 drlsherhqfQRDKEATQELIEDLRKQLEHLQLL--RLEVEQRR-------GRSSSLGLQEYNSRARESELEQEVRRLK- 962
Cdd:pfam01576 572 ----------EKTKNRLQQELDDLLVDLDHQRQLvsNLEKKQKKfdqmlaeEKAISARYAEERDRAEAEAREKETRALSl 641
|
250 260
....*....|....*....|.
gi 284022108 963 ----QDNRNLKEQNDELNGQI 979
Cdd:pfam01576 642 aralEEALEAKEELERTNKQL 662
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
760-1025 |
2.34e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALE--------------------EQLKEQEFRaqekvLEETRKQKE 819
Cdd:pfam05622 12 LAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLEsgddsgtpggkkylllqkqlEQLQEENFR-----LETARDDYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 820 LLCkMEREKsiEIENLQARLQQLDEENSELRSctpcLKANIERLEE--EKQKMLD-EIEELTQRLSEEQENKRKMgdRLS 896
Cdd:pfam05622 87 IKC-EELEK--EVLELQHRNEELTSLAEEAQA----LKDEMDILREssDKVKKLEaTVETYKKKLEDLGDLRRQV--KLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 897 HERHQFQRdkEATQELIEDLRK------QLE----HLQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNR 966
Cdd:pfam05622 158 EERNAEYM--QRTLQLEEELKKanalrgQLEtykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284022108 967 NLKEQNDEL---NGQIITLSIQGAKSLFSTSFSESLAAEISSVsrdELMEAIQKQEEINFRL 1025
Cdd:pfam05622 236 TLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA---EIREKLIRLQHENKML 294
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
795-979 |
2.78e-04 |
|
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: 44.84 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 795 LEEQLK--EQEFRAQEKVLEETRKQKELLCKMEReksieieNLQARLQQLDEENSELRSctpclkaNIERLEEEKQKMLD 872
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 873 EIEELTQRLSEEQENKRKMGDRLSHERhQFQRDKEATQEliedlrkqlehlQLLRLEVEQRRGRSSSLglqeynsRARES 952
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 284022108 953 ELEQEVRRLKQDNRNLKEQNDELNGQI 979
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
826-1040 |
2.99e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 44.68 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 826 REKSIEIENLQARLQQLDEENSELRSCTPCLKANieRLEEEKQKMLDEIEELTQRLSEEQENKRKMgDRLSHERHQFQ-- 903
Cdd:COG5244 82 KGGLVCESKGMDKDGEIKQENHEDRIHFEESKIR--RLEETIEALKSTEKEEIVELRRENEELDKI-NLSLRERISSEep 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 904 -RDKEATQ-------ELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEynsrARESELEQEVRRLKQDNRNLKEQNDEL 975
Cdd:COG5244 159 eLNKDGSKlsydelkEFVEESRVQVYDMVELVSDISETLNRNGSIQRSS----VRECERSNIHDVLFLVNGILDGVIDEL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 976 NGQIitlsiqgakslfstsfsESLAAEISSvsrdeLMEAIQKQEEINFRLQDYIDRIIVAILETN 1040
Cdd:COG5244 235 NGEL-----------------ERLRRQLVS-----LMSSHGIEVEENSRLKATLEKFQSLELKVN 277
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
858-1032 |
3.03e-04 |
|
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: 45.06 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 858 ANIERLEEEKQKMLDEIEELTQRLSEEQ---ENKRKMGDRLSHERHQFQRDKEATQELIEdlRKQLEHLQLLRLEVEQRR 934
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKRE--YEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 935 GRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLfstsfsESLAAEISSVsRDELMEA 1014
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------GELEAEIASL-ERSIAEK 313
|
170
....*....|....*...
gi 284022108 1015 IQKQEEINFRLQDYIDRI 1032
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEI 331
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
763-1020 |
3.20e-04 |
|
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: 44.73 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 763 RVSELEKDSAAAGEQHGRLRQ---ENLQLVHRANALEEQLKEQEfRAQEKV----LEETRKQKELlckMEREK------- 828
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNEnieNKLLLKEEVEDLKRKLEREE-KYREEAatleLEKEKLEQEL---QSWVKlaqdtgl 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 829 --------SIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDR---LSH 897
Cdd:pfam05557 274 nlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllLTK 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 898 ERhQFQR------DKEATQ--------ELIEDLRKQLEHLQLL------RLEVEQRRGRSSSLGLQ-------------- 943
Cdd:pfam05557 354 ER-DGYRailesyDKELTMsnyspqllERIEEAEDMTQKMQAHneemeaQLSVAEEELGGYKQQAQtlerelqalrqqes 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 944 -EYNSRARE--SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS---FSESLAAEISSVSRDElMEAIQK 1017
Cdd:pfam05557 433 lADPSYSKEevDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRKNQ-LEKLQA 511
|
...
gi 284022108 1018 QEE 1020
Cdd:pfam05557 512 EIE 514
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
831-939 |
3.44e-04 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 42.65 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 EIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRlseeqenkrkmgdrlsherhqfQRDKEATQ 910
Cdd:COG3166 46 QIAQQQARNAALQQEIAKLDK----QIAEIKELKKQKAELLARLQVIEQL----------------------QQSRPPWV 99
|
90 100 110
....*....|....*....|....*....|....
gi 284022108 911 ELIEDLRKQL-EHLQLLRLEVEQRR----GRSSS 939
Cdd:COG3166 100 HLLDELARLLpEGVWLTSLSQQGGTltltGVAQS 133
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
762-1045 |
3.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 762 RRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQArlqq 841
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK---- 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 842 lDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERhqfqrdkeatqeliEDLRKQLE 921
Cdd:PTZ00121 1628 -AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE--------------EDEKKAAE 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 922 hlQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAA 1001
Cdd:PTZ00121 1693 --ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 284022108 1002 EISSVSRDELMEAIQKQEEINFRLQdyIDRIIVAILETNPSILE 1045
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
500-529 |
4.20e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 38.70 E-value: 4.20e-04
10 20 30
....*....|....*....|....*....|
gi 284022108 500 RLRAVFDALDRDGDGFVRIEDFIQFATVYG 529
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
798-979 |
4.83e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 798 QLK--EQEFRAQEKVLEETRKQK-ELLCKM-EREKSI-----EIENLQARLQQLDEENSELrsctpclKANIERLEEEK- 867
Cdd:PRK11637 48 QLKsiQQDIAAKEKSVRQQQQQRaSLLAQLkKQEEAIsqasrKLRETQNTLNQLNKQIDEL-------NASIAKLEQQQa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 868 --QKMLDEIEELTQRLSEEQ---------ENKRKmgdrlshERHQ--FQRDKEATQELIEDLRKQLEHLQLLRLEVEQRR 934
Cdd:PRK11637 121 aqERLLAAQLDAAFRQGEHTglqlilsgeESQRG-------ERILayFGYLNQARQETIAELKQTREELAAQKAELEEKQ 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 935 GRSSS-LGLQ-------EYNSRARESELEQEVRRLKQDNRNLKE--QND-ELNGQI 979
Cdd:PRK11637 194 SQQKTlLYEQqaqqqklEQARNERKKTLTGLESSLQKDQQQLSElrANEsRLRDSI 249
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
760-1019 |
4.84e-04 |
|
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: 44.34 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQE--FRAQEKVLEETRKQ-KELLCKMEREKSIEIENLQ 836
Cdd:pfam15921 269 IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQlRSELREAKRMYEDKIEELE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 837 ARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRlsherhqfqrdKEATQELIEDL 916
Cdd:pfam15921 349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR-----------DTGNSITIDHL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 917 RKQLE--HLQLLRLEVEQRRGRSSSLGlqeynsraresELEQEVRRLKQDNRNLKEQNDelngqiITLSIQGAKSLFSTS 994
Cdd:pfam15921 418 RRELDdrNMEVQRLEALLKAMKSECQG-----------QMERQMAAIQGKNESLEKVSS------LTAQLESTKEMLRKV 480
|
250 260
....*....|....*....|....*....
gi 284022108 995 FSE----SLAAEISSVSRDELMEAIQKQE 1019
Cdd:pfam15921 481 VEEltakKMTLESSERTVSDLTASLQEKE 509
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
782-988 |
4.93e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 782 RQENLQLV-HRANALEEQLKEQEFRAQEKVLEETRKQKELlcKMEREKSIEIENLQARL----QQLDEENSELRSCTPCL 856
Cdd:pfam01576 10 KEEELQKVkERQQKAESELKELEKKHQQLCEEKNALQEQL--QAETELCAEAEEMRARLaarkQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 857 KANIERLEEEKQKMLDEIEELTQRLSEEQ-------------ENK-RKMGDR---LSHERHQFQRDKEATQELIEDLRKQ 919
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEaarqklqlekvttEAKiKKLEEDillLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284022108 920 L-------EHLQLLRLEVEQRRGRSSSLGLQEYNSRareSELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAK 988
Cdd:pfam01576 168 LaeeeekaKSLSKLKNKHEAMISDLEERLKKEEKGR---QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
795-917 |
5.13e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.43 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 795 LEEQLKEQEFRAQ-----EKVLEETRKQKEllckMEREKSIEIENLQARLQQLDEENSEL-----RSCTPCLKANIERLE 864
Cdd:pfam02841 178 LQEFLQSKEAVEEailqtDQALTAKEKAIE----AERAKAEAAEAEQELLREKQKEEEQMmeaqeRSYQEHVKQLIEKME 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 284022108 865 EEKQKMLDEIEELTQRLSEEQENKRKMGdrlsherhqFQRDKEATQELIEDLR 917
Cdd:pfam02841 254 AEREQLLAEQERMLEHKLQEQEELLKEG---------FKTEAESLQKEIQDLK 297
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
760-886 |
5.69e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANAleeqlkeqefrAQEKVLEETRKQKELLCKMEREKSiEIENLQARL 839
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE-----------AQQNYERELVLHAEDIKALQALRE-ELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 284022108 840 QQLDEENSELRSCtpcLKANIERLEEEKQKMLDEIEELTQRLSEEQE 886
Cdd:pfam07926 74 AELKAEAESAKAE---LEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| SynN |
smart00503 |
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
831-933 |
6.63e-04 |
|
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p
Pssm-ID: 214699 [Multi-domain] Cd Length: 117 Bit Score: 40.41 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM---LDEIEELTQRLSE--EQENKRKMGDRLSHERHQFQRd 905
Cdd:smart00503 9 KVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLerlIDDIKRLAKEIRAklKELEKENLENRASGSASDRTR- 87
|
90 100
....*....|....*....|....*...
gi 284022108 906 KEATQELIEDLRKQLEHLQLLRLEVEQR 933
Cdd:smart00503 88 KAQTEKLRKKFKEVMNEFQRLQRKYRER 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
752-976 |
7.82e-04 |
|
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: 43.52 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQE---------FRAQEKVLEETRKQKELLC 822
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienlngkKEELEEELEELEAALRDLE 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 823 KMEREKSIEIENLQARLQQldeenselrsctpclkanierLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQF 902
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRE---------------------LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284022108 903 QRDKEATQEL--IEDLRKQLEhlqllRLEVEQRR-GRSSSLGLQEY-NSRARESELEQEVRRLKQDNRNLKEQNDELN 976
Cdd:TIGR02169 941 GEDEEIPEEElsLEDVQAELQ-----RVEEEIRAlEPVNMLAIQEYeEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
760-957 |
8.02e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEfraqekvlEETRKQKELLCKMERE------------ 827
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARAlyrsggsvsyld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 828 -----KSIE--IENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdrlsherh 900
Cdd:COG3883 107 vllgsESFSdfLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAELEAAKAEL--------- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 284022108 901 qfQRDKEATQELIEDLRKQLEHL--QLLRLEVEQRRGRSSSLGLQEYNSRARESELEQE 957
Cdd:COG3883 174 --EAQQAEQEALLAQLSAEEAAAeaQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
761-1019 |
8.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQE-KVLEETRKQKELLCKMEREKSIEIENLQARl 839
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKK- 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 840 qqldeENSELRsctpclKANIERLEEEKQKMldEIEELTQrlsEEQENKRKmgdrlSHERHQFQRDKEATQELIEDLRKQ 919
Cdd:PTZ00121 1711 -----EAEEKK------KAEELKKAEEENKI--KAEEAKK---EAEEDKKK-----AEEAKKDEEEKKKIAHLKKEEEKK 1769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 920 LEHLQLLRLEVEQRrgrssslGLQEYNSRaRESELEQEVRRLKQDNRNLKEQNDELNgqiitLSIQGAKSLFSTSFSEsl 999
Cdd:PTZ00121 1770 AEEIRKEKEAVIEE-------ELDEEDEK-RRMEVDKKIKDIFDNFANIIEGGKEGN-----LVINDSKEMEDSAIKE-- 1834
|
250 260
....*....|....*....|
gi 284022108 1000 aAEISSVSRDELMEAIQKQE 1019
Cdd:PTZ00121 1835 -VADSKNMQLEEADAFEKHK 1853
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
496-559 |
1.10e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 40.16 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284022108 496 EEGARLRAVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDltqyLDPSGLGVISFEDFYQGIVA 559
Cdd:COG5126 2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSE----ADTDGDGRISREEFVAGMES 61
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
758-934 |
1.11e-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: 43.04 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 758 IFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKM---------EREK 828
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKdeleskeekEKEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 829 SIEIENLQARLQQLDEENSELRSCTpCLKANIERLEEEKQKML------DEIEELTQRLSEEQENKR------KMGDRLS 896
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERI-KEEAEILLKYEEEPEELlleeadEKEKEENNKEEEEERNKRlllakeELGKVNL 977
|
170 180 190
....*....|....*....|....*....|....*....
gi 284022108 897 HERHQFQRDKEA-TQELIEDLRKQLEHLQLLRLEVEQRR 934
Cdd:pfam02463 978 MAIEEFEEKEERyNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
786-884 |
1.15e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 786 LQLVHRANALEEQLKEqefrAQEKvLEETRKQKELLCKmereksiEIENLQARLQQLDEENSELRSCTPCLKANIERLEE 865
Cdd:COG4026 124 LQNIPEYNELREELLE----LKEK-IDEIAKEKEKLTK-------ENEELESELEELREEYKKLREENSILEEEFDNIKS 191
|
90
....*....|....*....
gi 284022108 866 EKQKMLDEIEELTQRLSEE 884
Cdd:COG4026 192 EYSDLKSRFEELLKKRLLE 210
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
800-963 |
1.37e-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: 42.63 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 800 KEQEFRAQEKVLEETRKQKELLCKMEREKSIEienlQARLQQLDEENSELRSctpclkaniERLEEEKQKMLDEIEELTQ 879
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEE----QRRLQQEQLERAEKMR---------EELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 880 RLSEEQ----ENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEYNSRARESELE 955
Cdd:pfam15709 395 RLEEERqrqeEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE 474
|
....*...
gi 284022108 956 QEVRRLKQ 963
Cdd:pfam15709 475 ERLEYQRQ 482
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
754-972 |
1.43e-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: 42.65 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 754 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLvhranALEEQLKEQEFR---AQEKVLEETRKQKELLCKMERE--- 827
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL-----QTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHpnp 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 828 ---KSIEIENLQARLQQLDEENSELRS--------CTPCLKaNIERLEEEKQKMLDEIEELTQ---RLSEEQENKRKMGD 893
Cdd:TIGR00618 516 arqDIDNPGPLTRRMQRGEQTYAQLETseedvyhqLTSERK-QRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 894 RLsheRHQFQRDKEATQELIEDLRKQLEHLQ----LLRLEVEQRRgRSSSLGLQEYNSRARESELEQE-----VRRLKQD 964
Cdd:TIGR00618 595 RL---QDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRLHLQQ-CSQELALKLTALHALQLTLTQErvrehALSIRVL 670
|
....*...
gi 284022108 965 NRNLKEQN 972
Cdd:TIGR00618 671 PKELLASR 678
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
801-1031 |
1.47e-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: 42.42 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 801 EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEnselrsctpclkanieRLEEEKQKMLDEIEElTQR 880
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQE----------------RLRQEKEEKAREVER-RRK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 881 LSEEQENKRKMGDRLS-----HERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRS---SSLGLQEYNSRARES 952
Cdd:pfam17380 318 LEEAEKARQAEMDRQAaiyaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRElerLQMERQQKNERVRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 953 ELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDEL-----MEAIQKQEEINFRLQD 1027
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQerqqqVERLRQQEEERKRKKL 477
|
....
gi 284022108 1028 YIDR 1031
Cdd:pfam17380 478 ELEK 481
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
808-918 |
1.60e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.59 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 808 EKVLEETRKQKELLCKMEREKSI---EIENLQARLQQLDEEnselrsctpcLKANIERL-EEEKQKMLDEIEELTQRLSE 883
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKrqaELQKLEKELQALQEK----------LQKEAATLsEEERQKKERELQKKQQELQR 101
|
90 100 110
....*....|....*....|....*....|....*
gi 284022108 884 EQENKRKMgdrlsherhQFQRDKEATQELIEDLRK 918
Cdd:COG2825 102 KQQEAQQD---------LQKRQQELLQPILEKIQK 127
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
828-1022 |
1.63e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 828 KSIEIENLQARLQQLDEENSELRSCTPCLK---------ANIERLE--------EEKQKMLDEIEELTQRLSEEQ----- 885
Cdd:pfam10174 301 KESELLALQTKLETLTNQNSDCKQHIEVLKesltakeqrAAILQTEvdalrlrlEEKESFLNKKTKQLQDLTEEKstlag 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 886 --ENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRS-SSLG---------------LQEYNS 947
Cdd:pfam10174 381 eiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdTALTtleealsekeriierLKEQRE 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 948 RARESELEqEVRRLKQDNRNLKEQNDELngqiitlsiQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEIN 1022
Cdd:pfam10174 461 REDRERLE-ELESLKKENKDLKEKVSAL---------QPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
774-922 |
1.72e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 774 AGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENselrsct 853
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE------- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 854 pclkaniERLEEEKQKMLDEIEELTQRLSE-EQENKRKMGdrlsherhqfQRDKEATQELIEDLRKQLEH 922
Cdd:PRK12705 105 -------NQLEEREKALSARELELEELEKQlDNELYRVAG----------LTPEQARKLLLKLLDAELEE 157
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
761-952 |
1.73e-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: 42.25 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHgRLRQENLQLVHRANA---LEEQLKEQEFRAQEKVLEETRKQKE-------LLCKMEREKS- 829
Cdd:pfam15709 344 EMRRLEVERKRREQEEQR-RLQQEQLERAEKMREeleLEQQRRFEEIRLRKQRLEEERQRQEeeerkqrLQLQAAQERAr 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 830 IEIENLQARLQQLDEENSElrsctpclkANIERLEEEKQKMldeiEELTQRLSEEQenKRKMGdrlsherhqfqrdkEAT 909
Cdd:pfam15709 423 QQQEEFRRKLQELQRKKQQ---------EEAERAEAEKQRQ----KELEMQLAEEQ--KRLME--------------MAE 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 284022108 910 QELIEDLRKQLEHLQLLRLEVEQRRGR---SSSLGLQEYNSRARES 952
Cdd:pfam15709 474 EERLEYQRQKQEAEEKARLEAEERRQKeeeAARLALEEAMKQAQEQ 519
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
760-1030 |
1.88e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQEnlqlVHRANALEEQL---KEQEFRAQEKVLEETRKQKELLCkmereksiEIENLQ 836
Cdd:pfam05622 150 LRRQVKLLEERNAEYMQRTLQLEEE----LKKANALRGQLetyKRQVQELHGKLSEESKKADKLEF--------EYKKLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 837 ARLQQLDEENselrsctpclkaniERLEEEKQKMLDEIEELtqRLSEEQENKRKMGDRLsHERHQFQRDKEATQELIEDL 916
Cdd:pfam05622 218 EKLEALQKEK--------------ERLIIERDTLRETNEEL--RCAQLQQAELSQADAL-LSPSSDPGDNLAAEIMPAEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 917 RKQLEHLQL----LRLEVE-QRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGqiiTLSIQGAKSLF 991
Cdd:pfam05622 281 REKLIRLQHenkmLRLGQEgSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQK---ALQEQGSKAED 357
|
250 260 270
....*....|....*....|....*....|....*....
gi 284022108 992 STSFSESLAAEIssvsrDELMEAiqkQEEINfRLQDYID 1030
Cdd:pfam05622 358 SSLLKQKLEEHL-----EKLHEA---QSELQ-KKKEQIE 387
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
752-1019 |
2.15e-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: 42.34 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 752 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKqkellCKMEREKSIE 831
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK-----LIQDQQEQIQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 I----------------ENLQARLQ---QLDEENSELRSCTPCLKANIER---LEEEKQKMLDEIEELTQRLSEE----- 884
Cdd:TIGR00606 861 HlksktnelkseklqigTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELISSKETSnkkaq 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 885 ---QENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGR-SSSLGLQEYN---SRARESELEQE 957
Cdd:TIGR00606 941 dkvNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKiNEDMRLMRQDidtQKIQERWLQDN 1020
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284022108 958 VRRLKQDN--RNLKEQNDELNGQIITLSIQGAKSLFstsfsESLAAEISSVSRDELMEAIQKQE 1019
Cdd:TIGR00606 1021 LTLRKRENelKEVEEELKQHLKEMGQMQVLQMKQEH-----QKLEENIDLIKRNHVLALGRQKG 1079
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
755-982 |
2.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 755 DKVIFLERRVSELEKDSAAAGEQHGRLRQ------ENLQLVHRANALEEQLKEQEFRAQEK--VLEETRKQKELL----- 821
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKreRAEELRERAAELeaeae 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 822 -------CKMER--EKSIEIENLQARLQQLDEENSELRSCTPCLKA---NIERLEE--EKQKMLDEIEELT-QRLSEEQE 886
Cdd:PRK02224 555 ekreaaaEAEEEaeEAREEVAELNSKLAELKERIESLERIRTLLAAiadAEDEIERlrEKREALAELNDERrERLAEKRE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 887 NKRKMGDRLSHER-HQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSlGLQEYNS-RARESELEQEVRRLkqd 964
Cdd:PRK02224 635 RKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEELEElRERREALENRVEAL--- 710
|
250
....*....|....*...
gi 284022108 965 nRNLKEQNDELNGQIITL 982
Cdd:PRK02224 711 -EALYDEAEELESMYGDL 727
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
776-973 |
2.99e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.20 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 776 EQHGRLRQENLQLVhraNALEEQLKEQEFR---AQEKVLEetrkqkellckmereksieienlqarLQQLDEENSELRSC 852
Cdd:pfam15742 96 ELEVLKQAQSIKSQ---NSLQEKLAQEKSRvadAEEKILE--------------------------LQQKLEHAHKVCLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 853 TPCLKANiERLEEEKQKMLDEIEELTQRLSEEQEnKRKMGDRLSHERHQ---FQRDKEATQELI---EDLRKQLEHLQLL 926
Cdd:pfam15742 147 DTCILEK-KQLEERIKEASENEAKLKQQYQEEQQ-KRKLLDQNVNELQQqvrSLQDKEAQLEMTnsqQQLRIQQQEAQLK 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 284022108 927 RLEVEQRRG---RSSSLGLQEynsraRESELEQEVRRLKQDNRNLKEQND 973
Cdd:pfam15742 225 QLENEKRKSdehLKSNQELSE-----KLSSLQQEKEALQEELQQVLKQLD 269
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
755-921 |
3.13e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 755 DKVIFLERRVSELEKDSaaagEQHGR-LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIE 833
Cdd:COG5185 406 EILATLEDTLKAADRQI----EELQRqIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 834 NLQARLQQLdeeNSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEqenKRKMGDRLSHERHQFQRDKEATQELI 913
Cdd:COG5185 482 DLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF---MRARGYAHILALENLIPASELIQASN 555
|
....*...
gi 284022108 914 EDLRKQLE 921
Cdd:COG5185 556 AKTDGQAA 563
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
780-971 |
3.31e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 780 RLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSI--EIENLQARLQQlDEENSELRsctpclk 857
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEkaERDELRAKLYQ-EEQERKER------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 858 aniERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdrlshERHQFQRDKEATQELiedLRKQLEHLQLLRLEVEQRRgrs 937
Cdd:pfam13868 221 ---QKEREEAEKKARQRQELQQAREEQIELKERR------LAEEAEREEEEFERM---LRKQAEDEEIEQEEAEKRR--- 285
|
170 180 190
....*....|....*....|....*....|....
gi 284022108 938 sslglqeynsrARESELEQEVRRLKQDNRNLKEQ 971
Cdd:pfam13868 286 -----------MKRLEHRRELEKQIEEREEQRAA 308
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
765-943 |
3.32e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 765 SELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQLKEQEFRAQEKVLEETRKQKEllcKMEREKSIEIENLQARLQQLDE 844
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAK-------YNRRRSKIKEQNNRDIAGIKDKLAKIRE---ARDRQLAVAEDDLQALESELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 845 E-NSELRSCTPCLKANIERLEEEKQKMLDEI---EELTQ---------RLSEEQENKRKMGDRLSHERHQFQRDKEatqe 911
Cdd:pfam12128 427 QlEAGKLEFNEEEYRLKSRLGELKLRLNQATatpELLLQlenfderieRAREEQEAANAEVERLQSELRQARKRRD---- 502
|
170 180 190
....*....|....*....|....*....|..
gi 284022108 912 liedlrKQLEHLQLLRLEVEQRRGRSSSLGLQ 943
Cdd:pfam12128 503 ------QASEALRQASRRLEERQSALDELELQ 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
831-1031 |
3.35e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 831 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEK------QKMLDEIE--ELTQRLSEEQENKRKMgDRLSHERHQF 902
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKReyEGYELLKEKEALERQK-EAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 903 QRDKEATQELIEDLRKQLEHL------------------------QLLRLEVEQRRGRSSslgLQEYNSRAResELEQEV 958
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvkeKIGELEAEIASLERS---IAEKERELE--DAEERL 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284022108 959 RRLKQDNRNLKEQNDELNGQIITLSIQgakslfstsfSESLAAEISSvSRDELMEAIQKQEEINFRLQDYIDR 1031
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKR----------RDKLTEEYAE-LKEELEDLRAELEEVDKEFAETRDE 386
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
795-922 |
3.51e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.87 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 795 LEEQLKEQEFRAQEKVLE---ETRKQKELLCKMEREKSIEIENLQARLQQ----LDEENSELRSctpcLKANIERLEEEK 867
Cdd:pfam12072 40 IEEAKKEAETKKKEALLEakeEIHKLRAEAERELKERRNELQRQERRLLQkeetLDRKDESLEK----KEESLEKKEKEL 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 868 QKMLDEIEELTQRLSEEQENKRKMGDRLSherhQFQRDkEATQELIEDLRKQLEH 922
Cdd:pfam12072 116 EAQQQQLEEKEEELEELIEEQRQELERIS----GLTSE-EAKEILLDEVEEELRH 165
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
771-934 |
3.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 771 SAAAGEQHGRLRQENLQLV-----HRANALEEQLKEQEfraqekVLEETRKQKELLCKMEREKSIEIENLQARLQqldee 845
Cdd:PRK04863 270 VAADYMRHANERRVHLEEAlelrrELYTSRRQLAAEQY------RLVEMARELAELNEAESDLEQDYQAASDHLN----- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 846 nselrsctpcLKANIERLEEEKQKMLDEIEELTQRLsEEQENKRKMGDRLSHERhqfQRDKEATQELIEDLRKQLEHLQl 925
Cdd:PRK04863 339 ----------LVQTALRQQEKIERYQADLEELEERL-EEQNEVVEEADEQQEEN---EARAEAAEEEVDELKSQLADYQ- 403
|
....*....
gi 284022108 926 LRLEVEQRR 934
Cdd:PRK04863 404 QALDVQQTR 412
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
786-933 |
3.81e-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: 40.29 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 786 LQLVH-RANALEEQLKE--QEFRAQEKVLEETRKQKEllckmerEKSIEIENLQARLQQLDEE----------------- 845
Cdd:COG1579 12 LQELDsELDRLEHRLKElpAELAELEDELAALEARLE-------AAKTELEDLEKEIKRLELEieevearikkyeeqlgn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 846 ---NSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEH 922
Cdd:COG1579 85 vrnNKEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|.
gi 284022108 923 LQLLRLEVEQR 933
Cdd:COG1579 161 LEAEREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
776-983 |
3.85e-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: 41.57 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 776 EQHGR-LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRK-----QKELLCKMEREKSIEIENLQARLQ--QLDEENS 847
Cdd:TIGR00606 308 HNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlqlQADRHQEHIRARDSLIQSLATRLEldGFERGPF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 848 ELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ--- 924
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqle 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 284022108 925 -----LLRLEVEQRRGRsSSLGLQEYNS-----RARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 983
Cdd:TIGR00606 468 gssdrILELDQELRKAE-RELSKAEKNSltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT 535
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
793-1028 |
4.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 793 NALEEQLKEQ--EFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKM 870
Cdd:PRK01156 186 DYLEEKLKSSnlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 871 ---LDEIEELTQRLSE-EQENKRKMGDRLSHERHQ------FQRDKEATQELIEDLR----------KQLEHLQLLRLEV 930
Cdd:PRK01156 262 esdLSMELEKNNYYKElEERHMKIINDPVYKNRNYindyfkYKNDIENKKQILSNIDaeinkyhaiiKKLSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 931 EQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELngqiitlsiqgakslfstsfsESLAAEISSVSRDE 1010
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI---------------------ERMSAFISEILKIQ 400
|
250 260
....*....|....*....|.
gi 284022108 1011 LM--EAIQKQ-EEINFRLQDY 1028
Cdd:PRK01156 401 EIdpDAIKKElNEINVKLQDI 421
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
761-963 |
4.73e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEqLKEQEFRAQEKVLEETRKQ-------------KELLCKME-- 825
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-LELQLFPQAGTLLHFLRKEapdweqsigkvisPELLHRTDld 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 826 -------------------REKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELT-------- 878
Cdd:pfam12128 567 pevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASreetfart 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 879 ---------QRLSEEQENKRkmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRRGRSSSLGLQEYnSRA 949
Cdd:pfam12128 647 alknarldlRRLFDEKQSEK---DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY-WQV 722
|
250
....*....|....
gi 284022108 950 RESELEQEVRRLKQ 963
Cdd:pfam12128 723 VEGALDAQLALLKA 736
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
832-970 |
4.81e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 832 IENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKmgdrlsherhqfQRDKEATQE 911
Cdd:PRK00409 522 IASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ------------QAIKEAKKE 585
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 284022108 912 lIEDLRKQLEHLQllrleveqrrgrssslglQEYNSRARESELEQEVRRLKQDNRNLKE 970
Cdd:PRK00409 586 -ADEIIKELRQLQ------------------KGGYASVKAHELIEARKRLNKANEKKEK 625
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
796-895 |
4.86e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 796 EEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQL-DEENSELRSctpclKANIERLEEekqkmldEI 874
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRK-----DREISRLDR-------EI 474
|
90 100
....*....|....*....|.
gi 284022108 875 EELTQRLSEEQENKRKMGDRL 895
Cdd:COG2433 475 ERLERELEEERERIEELKRKL 495
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
866-975 |
5.13e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 866 EKQKML-DEIEELTQRlseEQENKRKMGDRLSHERHQFQRDKEATQELIEdLRKQLEHLQLLRLEVEqrrgrssslglqe 944
Cdd:pfam13851 26 ELIKSLkEEIAELKKK---EERNEKLMSEIQQENKRLTEPLQKAQEEVEE-LRKQLENYEKDKQSLK------------- 88
|
90 100 110
....*....|....*....|....*....|.
gi 284022108 945 yNSRARESELEQEVRRLKQDNRNLKEQNDEL 975
Cdd:pfam13851 89 -NLKARLKVLEKELKDLKWEHEVLEQRFEKV 118
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
860-933 |
5.18e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 40.69 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 860 IERLEEEKQ---KMLDEIEELTQRlseEQENKRKMGD---RLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQR 933
Cdd:PRK11091 77 VEQLEESRQrlsRLVAKLEEMRER---DLELNVQLKDniaQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQ 153
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
760-890 |
5.92e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALE----------EQLKEQ--EFRAQEKVLEEtrKQKELLCKMErE 827
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQRLSEElaDLNAAIAGIEA--KINELEEEKE-D 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 828 KSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEEL--TQRLSEEQENKRK 890
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGR 510
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
796-917 |
7.62e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.48 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 796 EEQLKEQEFRAQEKVLEETRKQKELLCKmEREKSieienLQARLQQLDEEnselrsctpclkanierLEEEKQKMLDEIE 875
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLE-DQERS-----YEEHLRQLKEK-----------------MEEERENLLKEQE 258
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 284022108 876 ELTQRLSEEQENKRKMGdrlsherhqFQRDKEATQELIEDLR 917
Cdd:cd16269 259 RALESKLKEQEALLEEG---------FKEQAELLQEEIRSLK 291
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
761-873 |
7.76e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 38.98 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 761 ERRVSELEKDSAAAGEQHGR-LRQENLQLVHRANALEEQLKEQEFR--AQEKVLEETRKQKELL-----CKMEREKSIEI 832
Cdd:pfam14988 84 EREIQDLEEEKEKVRAETAEkDREAHLQFLKEKALLEKQLQELRILelGERATRELKRKAQALKlaakqALSEFCRSIKR 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 284022108 833 EN--LQARLQQLDEEnselrscTPCLKANIERLEEEKQKMLDE 873
Cdd:pfam14988 164 ENrqLQKELLQLIQE-------TQALEAIKSKLENRKQRLKEE 199
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
805-982 |
8.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 805 RAQEKVLEETRKQKEllckmerekSIEIENLQARLQQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLsEE 884
Cdd:PRK02224 183 SDQRGSLDQLKAQIE---------EKEEKDLHERLNGLESELAELD-------EEIERYEEQREQARETRDEADEVL-EE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 885 QENKRKMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEVEQRR-GRSSSLGLQEYNSRA----------RESE 953
Cdd:PRK02224 246 HEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERdDLLAEAGLDDADAEAvearreeledRDEE 325
|
170 180
....*....|....*....|....*....
gi 284022108 954 LEQEVRRLKQDNRNLKEQNDELNGQIITL 982
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDL 354
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
899-1043 |
8.31e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 38.93 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 899 RHQFQRDKEATQELIEDLRKQLEHLQllrleveqrrgrsSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQ 978
Cdd:cd21116 79 IELADNLIKGDQGAKQQLLQGLEALQ-------------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQ 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284022108 979 IITLsiQGAKSLFSTsFSESLAAEISSVsrdelmEAIQKQEEInfrLQDYIDRIIVAILETNPSI 1043
Cdd:cd21116 146 VAVL--NALKNQLNS-LAEQIDAAIDAL------EKLSNDWQT---LDSDIKELITDLEDAESSI 198
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
770-890 |
8.34e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 770 DSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKE-----LLCKMEREKSIEIENLQARLQQLDE 844
Cdd:PRK09510 56 DPGAVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlekerLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 284022108 845 ENSELRSCTPCLKANIE--RLEEEKQKMLDE---IEELTQRLSEEQENKRK 890
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEakRAAAAAKKAAAEakkKAEAEAAKKAAAEAKKK 186
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
948-979 |
8.91e-03 |
|
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 35.21 E-value: 8.91e-03
10 20 30
....*....|....*....|....*....|..
gi 284022108 948 RARESELEQEVRRLKQDNRNLKEQNDELNGQI 979
Cdd:cd14686 20 KERIEELEEEVEELEEENEELKAELEELRAEV 51
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
760-975 |
9.54e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 760 LERRVSELEKDSAAAGEQHGRLRQENLQL----------------------------VHRANALEEQLKEQEFRAQEKV- 810
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELeekykelsasseelseekdallaqraahEARIRELEEDIKTLTQRVLEREt 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 811 -LEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQ---- 885
Cdd:pfam07888 151 eLERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkea 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284022108 886 ENKRKMGD-RLSHER-HQFQRDKEATQELIEDLRKQLEH----LQLLRLEVEQRRGRSSSLGLQEYNSRARESELEQEVR 959
Cdd:pfam07888 231 ENEALLEElRSLQERlNASERKVEGLGEELSSMAAQRDRtqaeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQ 310
|
250
....*....|....*..
gi 284022108 960 RLKQ-DNRNLKEQNDEL 975
Cdd:pfam07888 311 QSAEaDKDRIEKLSAEL 327
|
|
| |
