|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
778-1044 |
2.06e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAgEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 857
Cdd:COG1196 198 LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQ 937
Cdd:COG1196 277 EELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 938 LEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQgAKSLFSTSFSESL 1017
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEE 428
|
250 260
....*....|....*....|....*..
gi 293351385 1018 AAEISSVSRDELMEAIQKQEEINFRLQ 1044
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 ... |
1025-1065 |
2.60e-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: 67.75 E-value: 2.60e-14
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 293351385 1025 SRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1065
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
778-1049 |
3.72e-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: 77.40 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQ-----EFRAQEKVLEETRKQ-KELLCKMEREKSI--- 848
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELeerleEAEEELAEAEAEIEElEAQIEQLKEELKAlre 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEENSELRSCTPCLKAN-------IERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLshERHQFQ 921
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 922 RDKEatQELIEDLRKQLEHLQLLRLEMEQRRGRSsslglqEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQ-IITL 1000
Cdd:TIGR02168 882 RASL--EEALALLRSELEELSEELRELESKRSEL------RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTL 953
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 1001 SIQGAKSLFSTSFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLqDYIDR 1049
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERY-DFLTA 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
780-1045 |
4.24e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 780 RRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKEllckmEREKSIEIENLQARLQQ 859
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 860 LDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLE 939
Cdd:COG1196 307 LEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 940 HLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAA 1019
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260
....*....|....*....|....*.
gi 293351385 1020 EISSVSRDELMEAIQKQEEINFRLQD 1045
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
773-1046 |
9.17e-13 |
|
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: 72.79 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEkVLEETRKQKEllckmereksiEIEN 852
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 853 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE---------------------------EQEN 905
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeiqaelskleeevsriearlreiEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 906 KRKMGDK--LSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRsssLGLQEYNSRARESELEQEVRRLKQDN 983
Cdd:TIGR02169 822 NRLTLEKeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE---LEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 984 RNLKEQNDELNGQIITLSIQ--------GAKSLFSTSFSESLAAEISSVS-----------RDELMEAIQKQEEINFR-L 1043
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRlselkaklEALEEELSEIEDPKGEDEEIPEeelsledvqaeLQRVEEEIRALEPVNMLaI 978
|
...
gi 293351385 1044 QDY 1046
Cdd:TIGR02169 979 QEY 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
778-1038 |
4.05e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ--EKVLEETRKQKELLCKMEREKSIEIENLQA 855
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRelEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 856 RLQQLDEENSELRSCtpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQfQRDKEATQELIEDLR 935
Cdd:COG1196 345 ELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 936 KQLEHLQLLRLEMEQRRGRssslglqeynSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAkslfstsfsE 1015
Cdd:COG1196 421 EELEELEEALAELEEEEEE----------EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA---------E 481
|
250 260
....*....|....*....|...
gi 293351385 1016 SLAAEISSVSRDELMEAIQKQEE 1038
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
778-1046 |
4.17e-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: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAgEQHGRLRQE--NLQL---VHRANALEEQLKEQEFRAQEKVLEETRKQKELlckmeREKSIEIEN 852
Cdd:TIGR02168 198 LERQLKSLERQAEKA-ERYKELKAElrELELallVLRLEELREELEELQEELKEAEEELEELTAEL-----QELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 853 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQ---RLSEEQENKRKMGDKLSHERHQFQRDKEATQE 929
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 930 LIEDLRKQLE-----------HLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQII 998
Cdd:TIGR02168 352 ELESLEAELEeleaeleelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 293351385 999 TLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQ-EEINFRLQDY 1046
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREElEEAEQALDAA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
779-1051 |
5.33e-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: 70.47 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQL--KEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQAR 856
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA-------LAELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 857 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQR---LSEEQENKRKMGDKLSHE--------------RHQ 919
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALREALDELRAEltllneeaanlrerLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 920 FQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLG----------LQEYNS--------RARESELEQEVRRLKQ 981
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleselealLNERASleealallRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 293351385 982 DNRNLKEQNDELNGQI--ITLSIQGAKSLFstsfsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 1051
Cdd:TIGR02168 909 KRSELRRELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
772-981 |
1.33e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 772 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIE 851
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 852 NLQARLQQLDEENSELRsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI 931
Cdd:COG1196 388 LLEALRAAAELAAQLEE-----LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 293351385 932 EDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEY---NSRARESELEQEVRRLKQ 981
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLlllEAEADYEGFLEGVKAALL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
772-1000 |
3.09e-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: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 772 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQlkeQEFRAQEKVLEETRKqkellckmereksiEIE 851
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL---AEYSWDEIDVASAER--------------EIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 852 NLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdklsherhqfqrdkeatqelI 931
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKE-------------------------L 722
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 932 EDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRR-LKQDNRNLKEQNDELNGQIITL 1000
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
778-997 |
3.29e-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: 64.69 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ---------EKVLEETRKQKELLCKMEREKSI 848
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleelEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLsherHQFQRDKEATQ 928
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL----ERLEDRRERLQ 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 293351385 929 ELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSR--ARESELEQEVRRLKQDNRNLKEQNDELNGQI 997
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERleEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
770-1005 |
5.04e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.50 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 770 DIADKVI--FLERRVSELEKDSAAAGEQhgrLRQENLQLVHRANALEEQLkeQEFRAQEKVLEETRKQKELLCKME---- 843
Cdd:COG3206 152 AVANALAeaYLEQNLELRREEARKALEF---LEEQLPELRKELEEAEAAL--EEFRQKNGLVDLSEEAKLLLQQLSeles 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 844 --REKSIEIENLQARLQQLDEENSELRSCTPCLKAN--IERLEEEKQKMLDEIEELTQRLSEEqenkrkmgdklsHERHQ 919
Cdd:COG3206 227 qlAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPN------------HPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 920 fqrdkeATQELIEDLRKQLEH-----LQLLRLEMEQRRGRSSSLG--LQEYNSRARE-SELEQEVRRLKQDNRNLKEQND 991
Cdd:COG3206 295 ------ALRAQIAALRAQLQQeaqriLASLEAELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYE 368
|
250
....*....|....
gi 293351385 992 ELNGQIITLSIQGA 1005
Cdd:COG3206 369 SLLQRLEEARLAEA 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
809-1065 |
9.42e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.84 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 809 RANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM 888
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 889 LDEIEELTQrlseEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQllrLEMEQRRGRSSSLGLQEYNSRAr 968
Cdd:COG4372 114 QEELEELQK----ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ---EELAALEQELQALSEAEAEQAL- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 969 eSELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYID 1048
Cdd:COG4372 186 -DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250
....*....|....*..
gi 293351385 1049 RIIVAILETNPSILEVK 1065
Cdd:COG4372 265 LAILVEKDTEEEELEIA 281
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
809-1054 |
1.14e-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: 61.70 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 809 RANALEEQLKE--QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRsctpclkANIERLEEEKQ 886
Cdd:COG4942 21 AAAEAEAELEQlqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 887 KMLDEIEELTQRLSEE----QENKRKMGDKL---SHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRgrssslg 959
Cdd:COG4942 94 ELRAELEAQKEELAELlralYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 960 lqeynsrareSELEQEVRRLKQDNRNLKEQNDELNGQIITlsiqgakslfstsfSESLAAEISSvSRDELMEAIQKQEEI 1039
Cdd:COG4942 167 ----------AELEAERAELEALLAELEEERAALEALKAE--------------RQKLLARLEK-ELAELAAELAELQQE 221
|
250
....*....|....*
gi 293351385 1040 NFRLQDYIDRIIVAI 1054
Cdd:COG4942 222 AEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
782-1003 |
1.41e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 782 VSELEKDSAAAGEQHGRLRQENLQlvhRANALEEQLKEQEfrAQEKVLEETRKQKEllckmerEKSIEIENLQARLQQLD 861
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAE--EKEEEYAELQEELE-------ELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 862 EENSELrsctpclkanieRLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLsHERHQFQRDKEATQELIEDLRKQLEHL 941
Cdd:COG4717 116 EELEKL------------EKLLQLLPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 293351385 942 QLLRLEMEQRRGRSSSLGLQEynSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
779-1065 |
1.93e-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: 62.01 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVhRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQ 858
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 859 QLDEENSELRSCTPCLKANIERLEEEkqkmldEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQL 938
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 939 EHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIitlsiqgakslfstsfsESLA 1018
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----------------EKLK 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 293351385 1019 AEISSVSR------DELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1065
Cdd:TIGR02169 399 REINELKReldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
779-991 |
2.11e-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: 61.68 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQE--FRAQEKVLEETRKQKELLCKMEREKSieienlqAR 856
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEeaLREQAELNRLKKKYLEALNKKLNEKE-------SQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 857 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEdlrk 936
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE---- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 293351385 937 qlehlqllrLEMEQRRGRSSSLGLQEYNSR-ARESELEQEVRRLKQDNRNLKEQND 991
Cdd:pfam05557 175 ---------LEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIE 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
778-980 |
3.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE-QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQAR 856
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 857 LQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRK 936
Cdd:PRK03918 323 INGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 293351385 937 QLEHLQLLRLEMEQRRGRSSSlglqeynsraRESELEQEVRRLK 980
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKK----------EIKELKKAIEELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
770-966 |
3.64e-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: 60.16 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 770 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ-------EKVL------EETRKQK 836
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqppLALLlspedfLDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 837 ELLCKMEREKSIEIENLQARLQQLDEenselrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHE 916
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAA-----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 293351385 917 RHQFQRDKEATQELIEDLRKQLEHLQllrLEMEQRRGRSSSLGLQEYNSR 966
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLE---AEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
780-981 |
3.64e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 780 RRVSELEKDSAAAGEQHGRLRQENLQLvHRANALEEQLKEQEFRAQEKvLEETRKQKELLCKMEREKSI--EIENLQARL 857
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALeaELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdklsherhQFQRDKEATQELIEDLRKQ 937
Cdd:COG4717 149 EELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEE-------------ELQDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 293351385 938 LEHLQLLRLEMEQRRgrssslglQEYNSRARESELEQEVRRLKQ 981
Cdd:COG4717 212 EEELEEAQEELEELE--------EELEQLENELEAAALEERLKE 247
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
779-1019 |
7.27e-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: 59.99 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLK---------EQEFRAQEKVLEETRKQKELLCKMEREKSIE 849
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKesekekkkaEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 IENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQE 929
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 930 LIEDLRKQL------EHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:pfam02463 438 SIELKQGKLteekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250
....*....|....*.
gi 293351385 1004 GAKSLFSTSFSESLAA 1019
Cdd:pfam02463 518 DGVGGRIISAHGRLGD 533
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
775-1065 |
1.68e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 775 VIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKEllckmerEKSIEIEN 852
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarSELEQLEEELEELNEQLQ-------AAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 853 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIE 932
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 933 DLRKQleHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS 1012
Cdd:COG4372 179 AEAEQ--ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 293351385 1013 FSESLAAEIS-SVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1065
Cdd:COG4372 257 LKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
778-997 |
1.69e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHgRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 857
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRS----CTPC---------------LKANIERLEEEKQKMLDEIEELTQRLsEEQENKRKMGDKLSHERH 918
Cdd:PRK03918 422 KELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 919 QFQRDKEATQEL----IEDLRKQLEHLQLLRLEMEQRRGRSSSLglqeyNSRA-RESELEQEVRRLKQDNRNLKEQNDEL 993
Cdd:PRK03918 501 LAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSL-----KKELeKLEELKKKLAELEKKLDELEEELAEL 575
|
....
gi 293351385 994 NGQI 997
Cdd:PRK03918 576 LKEL 579
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
778-980 |
1.73e-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: 57.85 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKEL-------------LCKMER 844
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELeaqkeelaellraLYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 845 EKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEkqkmLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDK 924
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 925 EATQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLK 980
Cdd:COG4942 195 AERQKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
798-1050 |
1.99e-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: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 798 RLR--QENLQlvhRANALEEQLKEQefraqekvLEETRKQKEllcKMER--EKSIEIENLQARLQQLDEENselrsctpc 873
Cdd:COG1196 180 KLEatEENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 874 LKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLRLEMEQ 950
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 951 RRGRsssLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLsiQGAKSLFSTSFSESLAAEISsvSRDELM 1030
Cdd:COG1196 317 RLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELL 389
|
250 260
....*....|....*....|
gi 293351385 1031 EAIQKQEEINFRLQDYIDRI 1050
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
820-1026 |
2.10e-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: 57.47 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 820 QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRL 899
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 900 SEEQENKRKMGDKL--------------SHERHQFQRD-------KEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSL 958
Cdd:COG4942 100 EAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 959 gLQEYnsRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLsIQGAKSLfsTSFSESLAAEISSVSR 1026
Cdd:COG4942 180 -LAEL--EEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEEL--EALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
781-1000 |
2.62e-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: 58.21 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 781 RVSELEKDSAAAGEQHGRLRQEnLQLVHRANALEEQlKEQEFRAQEKVLEETRKQKE-----LLCKMEREKSIEIENLQ- 854
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQE-LEAARKVKILEEE-RQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERVRl 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 855 ---------ARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLD-EIEELTQRLSEEqENKRKMGDKLSHERHQFQRDK 924
Cdd:pfam17380 454 eeqerqqqvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAMIEE-ERKRKLLEKEMEERQKAIYEE 532
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 293351385 925 EATQELIEDLRKQLEHLQLLRLEMEQRRgrssslgLQEYNSRARESELEQEVRRLKQDNRNlKEQNDELNGQIITL 1000
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRK-------ATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
809-997 |
3.05e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 809 RANALEEQLKEQEfRAQEKVlEETRKQKELLCKMeREKSIEIENLQARLQQLDEENSELRS-----CTPCLKANIERLEE 883
Cdd:COG4913 226 AADALVEHFDDLE-RAHEAL-EDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 884 EKQKMLDEIEELTQRLSEEQENKRKMgdKLSHERHQFQRdkeatqelIEDLRKQLEHLQLLRLEMEQRRGR----SSSLG 959
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARlealLAALG 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 293351385 960 LQEYNSRA------------------RESELEQEVRRLKQDNRNLKEQNDELNGQI 997
Cdd:COG4913 373 LPLPASAEefaalraeaaallealeeELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
773-1056 |
3.29e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIfleRRVSELEK-----DSAAAGEQHGRLRQENLQ-LVHRANALEEQLKEQEfraqeKVLEETRKQKELLCKMEREK 846
Cdd:PRK03918 148 EKVV---RQILGLDDyenayKNLGEVIKEIKRRIERLEkFIKRTENIEELIKEKE-----KELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 847 SIEIENLQARLQQLD---EENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGD---------KLS 914
Cdd:PRK03918 220 REELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 915 HERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLglqeynsRARESELEQEVRRLK------QDNRNLKE 988
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEerhelyEEAKAKKE 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 989 QNDELNGQIITLSIqgakslfstsfsESLAAEISSVSR--DELMEAIQKQEEINFRLQDYIDRIIVAILE 1056
Cdd:PRK03918 373 ELERLKKRLTGLTP------------EKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
516-573 |
3.74e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 51.10 E-value: 3.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 293351385 516 RLRTVFDALDRDGDGFVRIEDFIQFATVYGA------EQVKDLTQYLDPSGLGVISFEDFYQGI 573
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgeplsdEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
780-993 |
7.07e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 780 RRVSELEKDSAAAGEQHGRLRQE----------------NLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKME 843
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKElrelekvlkkeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 844 REksieIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEI--------EELTQRLSE-------------- 901
Cdd:PRK03918 539 GE----IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELeelgfesvEELEERLKElepfyneylelkda 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 902 --EQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARE--SELEQEVR 977
Cdd:PRK03918 611 ekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRRE 690
|
250
....*....|....*.
gi 293351385 978 RLKQDNRNLKEQNDEL 993
Cdd:PRK03918 691 EIKKTLEKLKEELEER 706
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
506-569 |
7.68e-08 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 52.49 E-value: 7.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 293351385 506 EPGTAQEEGARLRTVFDALDRDGDGFVRIEDFIQFATVYG--AEQVKDLTQYLDPSGLGVISFEDF 569
Cdd:COG5126 60 ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEF 125
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
778-1040 |
7.89e-08 |
|
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: 56.57 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSaaagEQHGRLRQENLQLVHRANALEEQLKEQEfraqekvleetrkqkellcKMEREKSIEIENLQARL 857
Cdd:TIGR04523 365 LEEKQNEIEKLK----KENQSYKQEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELtQRLSEEQENKRKmgdKLSHERHQFQRDKEATQELIEDLRKQ 937
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQLK---VLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 938 LEHLQLLRLEMEQR----RGRSSSLGLQEYNSRARESELEQEVRRLKQD---------NRNLKEQNDELNGQIITLSiQG 1004
Cdd:TIGR04523 498 LKKLNEEKKELEEKvkdlTKKISSLKEKIEKLESEKKEKESKISDLEDElnkddfelkKENLEKEIDEKNKEIEELK-QT 576
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 293351385 1005 AKSLFSTSFS-----ESLAAEISSVsRDELMEAIQKQEEIN 1040
Cdd:TIGR04523 577 QKSLKKKQEEkqeliDQKEKEKKDL-IKEIEEKEKKISSLE 616
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
789-981 |
8.27e-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: 55.54 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 789 SAAAGEQHGRLRQENLQLVHRANALEEQLK--EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSE 866
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 867 LRsctpclkANIERLEEEKQKMLDE----------------------------IEELTQRLSEEQENKRKMGDKLSHERH 918
Cdd:COG4942 95 LR-------AELEAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 293351385 919 QFQRDKEATQELIEDLRKQLEHLQLLRlemEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQ 981
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
791-992 |
8.37e-08 |
|
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: 55.31 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 791 AAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKvLEETRKQKELLCKMEREksIEIENLQARLQQLDEENSELRSC 870
Cdd:pfam13868 56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVER--IQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 871 TPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdklsheRHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQ 950
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 293351385 951 RRGRsssLGLQEYNSRARESELEQEVRRLKQdNRNLKEQNDE 992
Cdd:pfam13868 206 LRAK---LYQEEQERKERQKEREEAEKKARQ-RQELQQAREE 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
809-1003 |
1.04e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 809 RANALEEQLKEQEFRAqEKVLEETRKQKELLCKmereksiEIEnLQARlqqldEENSELRSctpclkanieRLEEEKQKM 888
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAEAIKK-------EAL-LEAK-----EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 889 LDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEynsrAR 968
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 293351385 969 E---SELEQEVR-----RLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
772-1012 |
1.18e-07 |
|
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: 55.16 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 772 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKeqefrAQEKVLEETRKQKELLCKMEREKSIEIE 851
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----ALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 852 NLQARLQQLDEENSEL--------RSCTPCLKANIERLeEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRD 923
Cdd:COG4942 94 ELRAELEAQKEELAELlralyrlgRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 924 KEATQELIEDLRKQLEHLQLLRlemEQRRGRSSSLglqeynsRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:COG4942 173 RAELEALLAELEEERAALEALK---AERQKLLARL-------EKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*....
gi 293351385 1004 GAKSLFSTS 1012
Cdd:COG4942 243 TPAAGFAAL 251
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
794-1048 |
1.84e-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: 55.36 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 794 EQHGRLRQENLQLVHRANALE-EQLKEQEFRAQEKV-----LEETRKQKELLCKMEREKSIEIEnLQARLQQLDEENSEL 867
Cdd:pfam02463 191 DLEELKLQELKLKEQAKKALEyYQLKEKLELEEEYLlyldyLKLNEERIDLLQELLRDEQEEIE-SSKQEIEKEEEKLAQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 868 RSctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQENKRkmgdklSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLE 947
Cdd:pfam02463 270 VL-------KENKEEEKEKKLQEEELKLLAKEEEELKSEL------LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 948 MEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQ-DNRNLKEQNDELNGQIITLSIQG-AKSLFSTSFSE-SLAAEISSV 1024
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLELARQ 416
|
250 260
....*....|....*....|....
gi 293351385 1025 SRDELMEAIQKQEEINFRLQDYID 1048
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIE 440
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
773-1045 |
1.85e-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: 55.36 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIFLERRVSELEKDSAAAGEQHGRLRQEnLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKMEReKS 847
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQlrariEELRAQEAVLEETQERINRARKAAP-LA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 848 IEIENLQARLQQLDEENSELRSCTPCL-KANIERLEEEKQKM-LDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKE 925
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSsIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 926 ATQElIEDLRKQLEHLqllrlemEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQndelngQIITLSIQGA 1005
Cdd:TIGR00618 377 LTQH-IHTLQQQKTTL-------TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ------QELQQRYAEL 442
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 293351385 1006 KSLFSTSFSESLAAEISsvsrdELMEAIQKQEEINFRLQD 1045
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKI-----HLQESAQSLKEREQQLQT 477
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
779-951 |
3.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEEtrkqkellckmereksiEIENLQARLQ 858
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 859 QLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENK-RKMGDKLSH---ERHQFQRDKEATQELIEDL 934
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*....
gi 293351385 935 RKQLEHL--QLLRLEMEQR 951
Cdd:COG4717 226 EEELEQLenELEAAALEER 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
784-1056 |
3.09e-07 |
|
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: 54.73 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 784 ELEKDSAAAGEQHgRLRQENLQLVHRANALeeQLKEQEF----RAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQ 859
Cdd:pfam05483 406 ELEELKKILAEDE-KLLDEKKQFEKIAEEL--KGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 860 LDEENSElrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQE---NKRKMGDKLSHERHQFQRDKEATQELIEDLRK 936
Cdd:pfam05483 483 EKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVRE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 937 QL---------------EHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI---- 997
Cdd:pfam05483 556 EFiqkgdevkckldkseENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLnaye 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 998 -----ITLSIQGAKSLF---STSFSESLaaEISSVSRDELMEAIQK-----------QEEINFRLQDYIDRiIVAILE 1056
Cdd:pfam05483 636 ikvnkLELELASAKQKFeeiIDNYQKEI--EDKKISEEKLLEEVEKakaiadeavklQKEIDKRCQHKIAE-MVALME 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
778-986 |
3.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEkDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 857
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEE--NSELRsctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLR 935
Cdd:COG4913 326 DELEAQirGNGGD--------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 293351385 936 KQLEHLQLLRLEMEQRRGRssslglqeynSRARESELEQEVRRLKQDNRNL 986
Cdd:COG4913 398 EELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
781-957 |
3.71e-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: 53.92 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 781 RVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQ 858
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 859 QLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLS-EEQENKR--KMGDKLSHERHQFQRDKEATQELIEDLR 935
Cdd:pfam19220 129 AETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlLEQENRRlqALSEEQAAELAELTRRLAELETQLDATR 208
|
170 180
....*....|....*....|..
gi 293351385 936 KQLEHLQLLRLEMEQRRGRSSS 957
Cdd:pfam19220 209 ARLRALEGQLAAEQAERERAEA 230
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
773-973 |
3.73e-07 |
|
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: 54.69 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIFLERRVSELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQLKEQEFRaQEKVLEETRKQKEllckmereksiEIEN 852
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKR-RDKLTEEYAELKE-----------ELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 853 LQARLQQLDEENSELRSCTPCLKANIERLEEEK---QKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQE 929
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREInelKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 293351385 930 LIEDLRKQLEHLQlLRLEMEQRRGRSSSLGLQEYNSRARESELE 973
Cdd:TIGR02169 449 EIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
778-1026 |
3.95e-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: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLvhraNALEEQlKEQ--------EFRAQEKVLEETRKQKEllckmEREKSI- 848
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQ-KEQdwnkelksELKNQEKKLEEIQNQIS-----QNNKIIs 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 ----EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE-EQenkrkmgdklsherhQFQRD 923
Cdd:TIGR04523 339 qlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDlES---------------KIQNQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 924 KEATQEliedLRKQLEHLQllrlemeqrrgrssslglQEYNsraresELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:TIGR04523 404 EKLNQQ----KDEQIKKLQ------------------QEKE------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260
....*....|....*....|...
gi 293351385 1004 gAKSLfsTSFSESLAAEISSVSR 1026
Cdd:TIGR04523 456 -IKNL--DNTRESLETQLKVLSR 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
778-942 |
3.97e-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: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLkeqefRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 857
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRS--CTPCLKANIERLEEEKQkMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLR 935
Cdd:TIGR02168 417 ERLQQEIEELLKklEEAELKELQAELEELEE-ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
....*..
gi 293351385 936 KQLEHLQ 942
Cdd:TIGR02168 496 RLQENLE 502
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
799-1001 |
3.98e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 799 LRQENLQLVHRANALEEQLKEQE---FRAQEKVLEE-TRKQK---ELLCKMEREKSiEIENLQARLQQLDEEN------- 864
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNkniEEQRKKNGENiARKQNkydELVEEAKTIKA-EIEELTDELLNLVMDIedpsaal 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 865 SELRSCTPCLKANIERLEEEkQKMLDEIEEL---TQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIE---DLRKQL 938
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKV-IKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQS 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 939 EHLQLLRLEMEQRRGRssslgLQEYNSRAR--ESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 1001
Cdd:PHA02562 337 KKLLELKNKISTNKQS-----LITLVDKAKkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
811-1063 |
4.85e-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: 53.87 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 811 NALEEQLKE---------QEFRAQEKVLE-------ETRKQKELL----CKMEREKS-IEIENLQARLQ----------- 858
Cdd:TIGR04523 127 NKLEKQKKEnkknidkflTEIKKKEKELEklnnkynDLKKQKEELenelNLLEKEKLnIQKNIDKIKNKllklelllsnl 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 859 --------QLDEENSELRSCTPCLKANIERLEEEKQKMLDEI----EELTQRLSEEQENKRKMGDKlsherhqfQRDKEA 926
Cdd:TIGR04523 207 kkkiqknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLKDEQNKIKKQLSEK--------QKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 927 TQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLG---------LQEYNSRARE-----SELEQEVRRLKQ-------DN 983
Cdd:TIGR04523 279 NNKKIKELEKQLNQLksEISDLNNQKEQDWNKELKselknqekkLEEIQNQISQnnkiiSQLNEQISQLKKeltnsesEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 984 RNLKEQNDELNGQIITLSIQGAKSLFStsfSESLAAEISsvsrdELMEAIQKQEEINFRLQDYIDriivaILETNPSILE 1063
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQE---IKNLESQIN-----DLESKIQNQEKLNQQKDEQIK-----KLQQEKELLE 425
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
778-993 |
8.63e-07 |
|
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: 53.42 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQ------ENLQLVHR----ANALE--------EQLKEQEFRAQEKVLEeTRKQKELL 839
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQqldqlkEQLQLLNKllpqANLLAdetladrlEELREELDAAQEAQAF-IQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 840 CKMEREKSI------EIENLQARLQQLDEENSELRSCTPCLKANIERLE----EEKQKMLDE----IEELTQRLSEEQEN 905
Cdd:COG3096 920 AQLEPLVAVlqsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlNEKLRARLEQAEEA 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 906 KRKMGDKLSHERHQFQrdkEATQELIeDLR-----KQLEHLQLLR----------LEMEQR-RGRSSSLGLQEYNSRAR- 968
Cdd:COG3096 1000 RREAREQLRQAQAQYS---QYNQVLA-SLKssrdaKQQTLQELEQeleelgvqadAEAEERaRIRRDELHEELSQNRSRr 1075
|
250 260 270
....*....|....*....|....*....|....*
gi 293351385 969 ----------ESELEQEVRRLKQDNRNLKEQNDEL 993
Cdd:COG3096 1076 sqlekqltrcEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
778-981 |
1.28e-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: 52.65 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSA--AAGEQHGRLRQENLQLvHRANALEEQLKEQEFRAQEKvlEETRKQKELLCK---MEREKSIEIEN 852
Cdd:COG3096 481 VCKIAGEVERSQAwqTARELLRRYRSQQALA-QRLQQLRAQLAELEQRLRQQ--QNAERLLEEFCQrigQQLDAAEELEE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 853 LQARLQQLDEENSE-LRSCtpclkanIERLEEEKQKmLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI 931
Cdd:COG3096 558 LLAELEAQLEELEEqAAEA-------VEQRSELRQQ-LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 293351385 932 EDLRKQLEHLQLLRLEMEQrrgrssslglqeynSRARESELEQEVRRLKQ 981
Cdd:COG3096 630 AAMQQLLEREREATVERDE--------------LAARKQALESQIERLSQ 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
815-1056 |
1.31e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 815 EQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEE 894
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ----AREELEQLEEELEQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 895 LTQRLSEEQENKRKMGDKLSHER---HQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRR-GRSSSLGLQEYNSRARES 970
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIaELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 971 E---LEQEVRRLKQDNRNLKEQndELNGQIITLSIQGAKSLFSTSFSESL--AAEISSVSRDELMEAIQKQEEINFRLQD 1045
Cdd:COG4372 158 QlesLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAekLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250
....*....|.
gi 293351385 1046 YIDRIIVAILE 1056
Cdd:COG4372 236 SALLDALELEE 246
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
778-1064 |
1.85e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKELLCKmereksiEIENLQA 855
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAaqAELAQAQEELESLQEEAEELQE-------ELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 856 RLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHE---RHQFQRDKEATQELIE 932
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaldELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 933 DLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS 1012
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 293351385 1013 FSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEV 1064
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
745-986 |
2.67e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 745 LHQSGTLTMEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEqhgrLRQENLQLVHRANALEEQLKEQEFRA 824
Cdd:COG5022 847 LIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS----LKLVNLELESEIIELKKSLSSDLIEN 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 825 QEKVLEETRKQKELLCKMEREKSIEIE-NLQARLQQLDEENSELRSCTPCLKANIERLEE---EKQKMLDEIEELTQRLS 900
Cdd:COG5022 923 LEFKTELIARLKKLLNNIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEYEDLLKKSTIlvrEGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 901 EEQENKRKMGDKLS---HERHQFQRDKEAT----------------QELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQ 961
Cdd:COG5022 1003 ELSKQYGALQESTKqlkELPVEVAELQSASkiissestelsilkplQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260
....*....|....*....|....*.
gi 293351385 962 EYNSRARESEL-EQEVRRLKQDNRNL 986
Cdd:COG5022 1083 LYQLESTENLLkTINVKDLEVTNRNL 1108
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
778-941 |
2.79e-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: 49.92 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ--EKVLEETRKQKELlckmeREKSIEIENLQA 855
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEY-----EALQKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 856 RLQQLDEENSElrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI-EDL 934
Cdd:COG1579 104 RISDLEDEILE-------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPEL 176
|
....*..
gi 293351385 935 RKQLEHL 941
Cdd:COG1579 177 LALYERI 183
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
778-971 |
3.25e-06 |
|
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: 50.41 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEkdsaaagEQHGRLRQENLQLVHRANALEE--QLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQA 855
Cdd:pfam04849 99 LTERNEALE-------EQLGSAREEILQLRHELSKKDDllQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 856 RLQQLDEENSELRSCTPCLKANIERLEEEKQK-MLDEIEELTQ------RLSEEQENKRKmgdklSHERHQfqrdKEATQ 928
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEKEQQlMSDCVEQLSEanqqmaELSEELARKME-----ENLRQQ----EEITS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 293351385 929 EL--IEDLRKQL--------EHLQLLRLEME-QRRGRSSslgLQEYNSRARESE 971
Cdd:pfam04849 243 LLaqIVDLQHKCkelgieneELQQHLQASKEaQRQLTSE---LQELQDRYAECL 293
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
785-986 |
6.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 785 LEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEN 864
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 865 SELRSCTPcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLL 944
Cdd:COG1196 659 GGSLTGGS-RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 293351385 945 RLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNL 986
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
773-1044 |
6.13e-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: 50.50 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIFLERRvsELEKDSAAAGeQHGRlrQENLQLVHRANaLEEQLKEQEFRAQE-KVLEETRKQKellckmereksieIE 851
Cdd:pfam15921 561 DKVIEILRQ--QIENMTQLVG-QHGR--TAGAMQVEKAQ-LEKEINDRRLELQEfKILKDKKDAK-------------IR 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 852 NLQARLQQLDEENSELrsctpcLKANIERL------EEEKQKMLDEIE----ELTQrLSEEQE----NKRKMGDKLSHER 917
Cdd:pfam15921 622 ELEARVSDLELEKVKL------VNAGSERLravkdiKQERDQLLNEVKtsrnELNS-LSEDYEvlkrNFRNKSEEMETTT 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 918 HQFQRDKEATQELIEDLRKQLE-------HLQLLRLEMEQ----RRGRSSSLG-----LQEYNSRARESE--LEQEVRRL 979
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKsmegsdgHAMKVAMGMQKqitaKRGQIDALQskiqfLEEAMTNANKEKhfLKEEKNKL 774
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 980 KQDNRNLKEQNDELNGQIITLSIQgAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQ 1044
Cdd:pfam15921 775 SQELSTVATEKNKMAGELEVLRSQ-ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
770-1038 |
6.67e-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: 49.96 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 770 DIADKVIFLERRVSELEKdsaaAGEQHGRLRQENL----QLVHRANALEEQLKEQEFRAQEKVLEETRKQkellckmerE 845
Cdd:COG5185 240 DPESELEDLAQTSDKLEK----LVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIAEYTKSI---------D 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 846 KSIEIENLQARLQQLDEENSelrsctpclkanIERLEEEKQKMLDE-IEELTQR---LSEEQENKRKMGDKLSHERHQFQ 921
Cdd:COG5185 307 IKKATESLEEQLAAAEAEQE------------LEESKRETETGIQNlTAEIEQGqesLTENLEAIKEEIENIVGEVELSK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 922 RDKEATQEL--IEDLRKQLEHLQllrleMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI-- 997
Cdd:COG5185 375 SSEELDSFKdtIESTKESLDEIP-----QNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIse 449
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 293351385 998 ITLSIQGAKSLFSTSFSESLAAEISSV--SRDELMEAIQKQEE 1038
Cdd:COG5185 450 LNKVMREADEESQSRLEEAYDEINRSVrsKKEDLNEELTQIES 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
819-1040 |
7.39e-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: 50.11 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 819 EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSEL-------RSCTPCLKANIERLEEEKQKMLDE 891
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 892 IEELTQRLSEEQENKRKMGDKLSHERHQ-----------FQRDKEATQELIEDLRKQL----EHLQLLRLEMEQRRGRSS 956
Cdd:pfam05483 178 REETRQVYMDLNNNIEKMILAFEELRVQaenarlemhfkLKEDHEKIQHLEEEYKKEIndkeKQVSLLLIQITEKENKMK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 957 SLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI--ITLSIQGAKSLfSTSFSESLaaEISSVSRDELMEAIQ 1034
Cdd:pfam05483 258 DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELedIKMSLQRSMST-QKALEEDL--QIATKTICQLTEEKE 334
|
....*..
gi 293351385 1035 KQ-EEIN 1040
Cdd:pfam05483 335 AQmEELN 341
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
800-1046 |
9.61e-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: 49.73 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 800 RQENLQLVHRANALEEQLKEQefraQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIE 879
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEM----LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK----LRSRVD 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 880 RLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKlsherhqfqrDKeatqeLIEDLRKQLEHLqllrLEMEQRRGRSSSLG 959
Cdd:pfam15921 528 LKLQELQHLKNEGDHLRNVQTECEALKLQMAEK----------DK-----VIEILRQQIENM----TQLVGQHGRTAGAM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 960 LQEynsrarESELEQEV--RRLK-QDNRNLKEQND----ELNGQIITLSIQGAKslFSTSFSESLAA--EISSvSRDELM 1030
Cdd:pfam15921 589 QVE------KAQLEKEIndRRLElQEFKILKDKKDakirELEARVSDLELEKVK--LVNAGSERLRAvkDIKQ-ERDQLL 659
|
250
....*....|....*..
gi 293351385 1031 EAIQK-QEEINFRLQDY 1046
Cdd:pfam15921 660 NEVKTsRNELNSLSEDY 676
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
844-1051 |
1.03e-05 |
|
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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 844 REKSIEIENLQARLQQLDEENSELRSCTPCLKAN-IERLEEEKQKMLDEIEELTQRLSeEQENKRKMGDKLSHERHQFQR 922
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAEsSKRLNENANNLIKQFENTKEKIA-EYTKSIDIKKATESLEEQLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 923 dKEATQELIEDLRKQLEHLQLLRLEMEQRRgRSSSLGLQEYNSRARESELEQEVRRLKQdnrNLKEQNDELNGQIITL-S 1001
Cdd:COG5185 321 -AEAEQELEESKRETETGIQNLTAEIEQGQ-ESLTENLEAIKEEIENIVGEVELSKSSE---ELDSFKDTIESTKESLdE 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 293351385 1002 IQGAKSLFSTSFSESLAAEISSVSRD--ELMEAIQKQEEINFRLQDYIDRII 1051
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQieELQRQIEQATSSNEEVSKLLNELI 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
778-982 |
1.04e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQE--KVLEETRKQKELLCKMEREK---SIEIEN 852
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEleTLEAEIEDLRETIAETEREReelAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 853 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE----------EQENKRKMGDKLShERHQFQR 922
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqahneEAESLREDADDLE-ERAEELR 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 923 DKEAT-----QELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQD 982
Cdd:PRK02224 363 EEAAEleselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
794-1002 |
1.07e-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: 48.88 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 794 EQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLcKMEReksiEIENLQARLQQLDEENSELRSCTPC 873
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQ-LQER----LEEACHKRQLKEREEQKKVQENNLS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 874 LKANIERL---------EEEKQKMLDeieeLTQRLSEEQENK--------RKMGDKLSHERHQFQRDKEATQeliEDLRK 936
Cdd:pfam15558 176 ELLNHQARkvlvdcqakAEELLRRLS----LEQSLQRSQENYeqlveerhRELREKAQKEEEQFQRAKWRAE---EKEEE 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 937 QLEHLQLLRLEMEQRRGRS---SSLGLQEYNSRARESELEQEvrRLKQDNRNLKEQNDELNGQIITLSI 1002
Cdd:pfam15558 249 RQEHKEALAELADRKIQQArqvAHKTVQDKAQRARELNLERE--KNHHILKLKVEKEEKCHREGIKEAI 315
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
818-1045 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 818 KEQEFRAQEKVLEETRKQKELLckmerekSIEIENLQARLQQLDEENSELRsctpclkanierleeeKQKmldeieeltq 897
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYNDLK----------------KQK---------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 898 rlsEEQENkrkmgdklshERHQFQRDKEATQELIEDLRKQLEHLQLLRLEmeqrrgrssslgLQEYNSRAResELEQEVR 977
Cdd:TIGR04523 169 ---EELEN----------ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN------------LKKKIQKNK--SLESQIS 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 978 RLKQDNRNLKEQNDELNGQIitlsiqgakslfstsfsESLAAEISSVsRDELMEAIQKQEEINFRLQD 1045
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEI-----------------NEKTTEISNT-QTQLNQLKDEQNKIKKQLSE 271
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
811-1040 |
1.37e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 811 NALEEQLKEQEFRAQEKVLEETRKQKELlckmereksieIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLD 890
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDEL-----------NEELKELAEKRDELNAQVKE----LREEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 891 EIEELTQRLSEEQENKRKMGDKLshERHQFQRDKEATQEL-IEDLRKQLEhlqllRLEMEQrrgRSSSLGLQEynsrarE 969
Cdd:COG1340 72 KVKELKEERDELNEKLNELREEL--DELRKELAELNKAGGsIDKLRKEIE-----RLEWRQ---QTEVLSPEE------E 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 970 SELEQEVRRLKQDNRNLKEQNdELNGQIITLS--IQGAKSLFSTSFSE--SLAAEISSVSrDELMEAIQKQEEIN 1040
Cdd:COG1340 136 KELVEKIKELEKELEKAKKAL-EKNEKLKELRaeLKELRKEAEEIHKKikELAEEAQELH-EEMIELYKEADELR 208
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
849-997 |
1.51e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 45.71 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEEnselrsctpclkanIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdklsHERhQFQRDKEATQ 928
Cdd:pfam07926 2 ELSSLQSEIKRLKEE--------------AADAEAQLQKLQEDLEKQAEIAREAQQN---------YER-ELVLHAEDIK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 929 ELiEDLRKQLEHLQLLRLEME-QRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI 997
Cdd:pfam07926 58 AL-QALREELNELKAEIAELKaEAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
778-993 |
1.74e-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: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRA---------QEKVLE--ETRKQKELLCKMEREK 846
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkHEAMISdlEERLKKEEKGRQELEK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 847 SIEieNLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEA 926
Cdd:pfam01576 209 AKR--KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 927 tQELIEDLRKQL-EHLQLLRLEMEQRRGrsSSLGLQEYNSRaRESELEQEVRRLKQDNRNLKEQNDEL 993
Cdd:pfam01576 287 -RNKAEKQRRDLgEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
516-573 |
1.85e-05 |
|
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: 43.31 E-value: 1.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 293351385 516 RLRTVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDLTQYL----DPSGLGVISFEDFYQGI 573
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELM 62
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
800-1001 |
1.90e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 800 RQENLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEnselrsctpcl 874
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET----------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 875 kanIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDK----------LSHERHQFQRDKEATQELIEDLRKQLEhlqll 944
Cdd:PRK02224 267 ---IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQ----- 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 945 RLEMEQRRGRSSSLGLQEYNSRARE--SELEQEVRRLKQDNRNLKEQNDELNGQIITLS 1001
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
799-988 |
1.94e-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: 48.35 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 799 LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANI 878
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 879 ERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSL 958
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190
....*....|....*....|....*....|
gi 293351385 959 GLQEYNSRARESELEQEVRRLKQDNRNLKE 988
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
778-1000 |
2.02e-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: 48.86 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQ-------LVHRANALEEQLKEQEFR--AQEKVLEET------------RKQK 836
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKnnseikdLTNQDSVKELIIKNLDNTreSLETQLKVLsrsinkikqnleQKQK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 837 ELlckmeREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMG------ 910
Cdd:TIGR04523 490 EL-----KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeid 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 911 ------DKLSHE-----RHQFQRDKEATQ----------------ELIEDLRKQLEHlqllrLEMEQRRgrsssLGLQEY 963
Cdd:TIGR04523 565 eknkeiEELKQTqkslkKKQEEKQELIDQkekekkdlikeieekeKKISSLEKELEK-----AKKENEK-----LSSIIK 634
|
250 260 270
....*....|....*....|....*....|....*..
gi 293351385 964 NSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITL 1000
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-944 |
2.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQ--ENLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKmereksiEI 850
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEA-------EL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 851 ENLQarlQQLDEEnseLRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKrkmgdklshERHQFQRDKEATQEL 930
Cdd:COG4717 173 AELQ---EELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---------EELEEELEQLENELE 237
|
170
....*....|....
gi 293351385 931 IEDLRKQLEHLQLL 944
Cdd:COG4717 238 AAALEERLKEARLL 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
784-1038 |
2.14e-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: 48.68 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 784 ELEKDSAAAGEQHGRLRQENLQLVHRAnaleEQLKEQEFRAQEKVLEETRKQKellckMEREKSIEIENLQARLQQLDEE 863
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQS----EKDKKNKALAERKDSANERLNS-----LEAQLKQLDKKHQAWLEEQKEQ 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 864 NSELRSCTPC--------------------------LKANIERLEEEKQKMLD--------------EIEELTQRLSEEQ 903
Cdd:pfam12128 709 KREARTEKQAywqvvegaldaqlallkaaiaarrsgAKAELKALETWYKRDLAslgvdpdviaklkrEIRTLERKIERIA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 904 ENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHL--QLLRLEMEQRRgRSSSLGLQEYNSRARESELEQEVRRLKQ 981
Cdd:pfam12128 789 VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELqqQLARLIADTKL-RRAKLEMERKASEKQQVRLSENLRGLRC 867
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 982 DNRNLKEQNDELNGQIITLSIqgakslfstsfSESLAA-EISSVSRDELMEAIQKQEE 1038
Cdd:pfam12128 868 EMSKLATLKEDANSEQAQGSI-----------GERLAQlEDLKLKRDYLSESVKKYVE 914
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
12-328 |
2.34e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 12 HDEPASGPQRGVKGLVGP---------DAPRGWSDEPEEHAQLQRWPEGpnapicwpeEVEEPHAPRRwAEEPSASRCLS 82
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEG---------EVGKKPGPAK-EHKPSKIPTLS 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 83 QEPyESCHLAKELEEPDAPRcSSQEPDAPCHlakdleetdsprcwPLEPDAPchlaKEWEEPDVPRCwPQEPDAPchlak 162
Cdd:PTZ00449 577 KKP-EFPKDPKHPKDPEEPK-KPKRPRSAQR--------------PTRPKSP----KLPELLDIPKS-PKRPESP----- 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 163 ylEEPDAPLCwPQEPDAfcylLKEVEEPDVPRC--RPQEPDAPC--HLAEELED--LDAP--------RCWTQEPNESCN 228
Cdd:PTZ00449 631 --KSPKRPPP-PQRPSS----PERPEGPKIIKSpkPPKSPKPPFdpKFKEKFYDdyLDAAaksketktTVVLDESFESIL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 229 LAKELDEPDTPRCLSQE-----PDAPCLLAKEWEESDAPSCWPQEPDVGPQEPDVGCHlaKEREESDAPCLLTEELKEPD 303
Cdd:PTZ00449 704 KETLPETPGTPFTTPRPlppklPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFH--ETPADTPLPDILAEEFKEED 781
|
330 340
....*....|....*....|....*
gi 293351385 304 AlqcwPQESDAPcllAEELEEPDAP 328
Cdd:PTZ00449 782 I----HAETGEP---DEAMKRPDSP 799
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
778-1001 |
2.58e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEqeFRAQEKVLEETRKqkELLCKMEREKSiEIENLQARL 857
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE--LREEAQELREKRD--ELNEKVKELKE-ERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEEL-----TQRLSEEQENK--------RKMGDKLSHERHQFQRDK 924
Cdd:COG1340 88 NELREELDELRK----ELAELNKAGGSIDKLRKEIERLewrqqTEVLSPEEEKElvekikelEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 293351385 925 EATQElIEDLRKQLEHLqllRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 1001
Cdd:COG1340 164 ELRAE-LKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
778-994 |
3.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVleetrkqkellckmEREKSIEIENLQARL 857
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE--------------DLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSElrsctpclkanierleeekQKMLDEIEELTQRLSEEQENKRkmgDKLSHERHQFQRD-KEATQEL---IED 933
Cdd:COG4913 756 AAALGDAVE-------------------RELRENLEERIDALRARLNRAE---EELERAMRAFNREwPAETADLdadLES 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 934 LRKQLEHLQLLRlemeqrrgrssSLGLQEYNSRARESELEQE-------VRRLKQDNRNLKEQNDELN 994
Cdd:COG4913 814 LPEYLALLDRLE-----------EDGLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLN 870
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
805-981 |
3.50e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 805 QLVHRANALEEQLKEQefRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRsctpclkaniERLEEE 884
Cdd:PRK04863 517 QLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR----------ERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 885 KQKmLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQrrgrssslglqeyn 964
Cdd:PRK04863 585 RQQ-LEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-------------- 649
|
170
....*....|....*..
gi 293351385 965 SRARESELEQEVRRLKQ 981
Cdd:PRK04863 650 LAARKQALDEEIERLSQ 666
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
826-981 |
3.64e-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: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 826 EKVLEETRKqkELLCKMEREKSIEIENLQARLQQLDEENSELRSctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQEN 905
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 906 KRKMGDKlshERHQFQRDKEAT--QELIEDLRKQLEhlqllRLEMEQRrgrssslglqeynsraresELEQEVRRLKQ 981
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELE-----EERERIE-------------------ELKRKLERLKE 500
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
801-997 |
5.31e-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: 47.35 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 801 QENLQLVHRANaleEQLKEQEFRAQEKVLEETRKQKELLCKMereksieienlqaRLQQLDEenselrsctpclkanIER 880
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 881 LEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQR--------DKEATQELiEDLRKQLEHL----QLLRLEM 948
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSqlpvlsdaEREMKKEL-ETINEQLKHLanaiKQAKKKM 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 293351385 949 EQRRgRSSSLGLQEYNSRARESELEQEvRRLKQdnrNLKEQNDELNGQI 997
Cdd:pfam10168 659 NYQR-YQIAKSQSIRKKSSLSLSEKQR-KTIKE---ILKQLGSEIDELI 702
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
778-1050 |
7.06e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQhgrLRQENLQLV------HRA-NALEEQLKE-QEFRAQekvLEETRKQKELLCKMEREKsie 849
Cdd:PRK11281 126 LESRLAQTLDQLQNAQND---LAEYNSQLVslqtqpERAqAALYANSQRlQQIRNL---LKGGKVGGKALRPSQRVL--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 ienLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEE----QE---NKRKmgdKLSHERHQFQR 922
Cdd:PRK11281 197 ---LQAEQALLNAQNDLQRK----SLEGNTQLQDLLQKQRDYLTARIQRLEHQlqllQEainSKRL---TLSEKTVQEAQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 923 DKEATQELIED--LRKQLEHlqllRLEMEQRRGRSSslglQEYNSRARES-ELEQEVRRLKQDNRNLKEQNDELNGQIIt 999
Cdd:PRK11281 267 SQDEAARIQANplVAQELEI----NLQLSQRLLKAT----EKLNTLTQQNlRVKNWLDRLTQSERNIKEQISVLKGSLL- 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 293351385 1000 LS-I--QGAKSLFSTSFSESLAAEISSVsRDELMEAIQKQEEInFRLQDYIDRI 1050
Cdd:PRK11281 338 LSrIlyQQQQALPSADLIEGLADRIADL-RLEQFEINQQRDAL-FQPDAYIDKL 389
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
778-989 |
7.37e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQ------ENLQLVH----------------RANALEEQLKEQE-----FRAQEKVLE 830
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSqleqakEGLSALNrllprlnlladetladRVEEIREQLDEAEeakrfVQQHGNALA 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 831 ETRKQKELLckmeREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLE----EEKQKMLDEIEELTQRLSEEQENK 906
Cdd:PRK04863 922 QLEPIVSVL----QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 907 RKMGDKLSHERHQFQ-RDKEATQELI---------EDLRKQLEH-LQLLRL----EMEQR-RGRSSSLGLQEYNSRARES 970
Cdd:PRK04863 998 EQERTRAREQLRQAQaQLAQYNQVLAslkssydakRQMLQELKQeLQDLGVpadsGAEERaRARRDELHARLSANRSRRN 1077
|
250
....*....|....*....
gi 293351385 971 ELEQEVRRLKQDNRNLKEQ 989
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKK 1096
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
780-992 |
8.72e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 780 RRVSELEKDSAAAGEQHGRLRQ--ENLQLVHRANALEEQLKEQEFRAQE--------KVLEETRKQKELLCKMEREKSIE 849
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEeakkadeaKKAEEKKKADELKKAEELKKAEE 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 IENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKmGDKLSHERHQFQRDKEATQE 929
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 293351385 930 LIEDLRKQLEhlqlLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDE 992
Cdd:PTZ00121 1642 EAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
813-997 |
1.08e-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: 46.38 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 813 LEEQLK--EQEFRAQEKVLEETRKQKELLCKMEReksieieNLQARLQQLDEENSELRSctpclkaNIERLEEEKQKMLD 890
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 891 EIEELTQRLSEEQENkRKMGDKLSHERHQFQRDKEATQEliedlrkqlehlQLLRLEMEQRRGRSSSLglqeynsRARES 970
Cdd:pfam09726 466 TVQQLEKRLKAEQEA-RASAEKQLAEEKKRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 293351385 971 ELEQEVRRLKQDNRNLKEQNDELNGQI 997
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
778-992 |
1.09e-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: 45.68 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCK---MEREKSiEIENLQ 854
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkeLEKEEE-REEDER 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 855 ARLQQLDEENSELRsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDL 934
Cdd:pfam13868 157 ILEYLKEKAEREEE-----REAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 935 RKQLEHLQLLRLEMEQRRGRssslgLQEYnsRARESELEQEVRRLKQDNRNLKEQNDE 992
Cdd:pfam13868 232 RQRQELQQAREEQIELKERR-----LAEE--AEREEEEFERMLRKQAEDEEIEQEEAE 282
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
753-1055 |
1.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 753 MEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEQHGRLRQE--NLQLVHRANALEEQLKEQE--------- 821
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARlllliaaal 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 822 -------------------------------FRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSC 870
Cdd:COG4717 259 lallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 871 TPCLKANIERLEEEKQKMLDEIEELtQRLSEEQENKRKMGDKLSHERHQFqrdkEATQELIEDLRKQLEHLQLLRLEMEQ 950
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEEL----RAALEQAEEYQELKEELEELEEQLEE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 951 RRGrssslGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSiqgakslfstsfseslaAEISSVSRD-EL 1029
Cdd:COG4717 414 LLG-----ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-----------------AELEQLEEDgEL 471
|
330 340
....*....|....*....|....*.
gi 293351385 1030 MEAIQKQEEINFRLQDYIDRIIVAIL 1055
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
774-980 |
1.36e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 774 KVIFLERRVSELEKDSAAAGEQHGRLRQenlqLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMER--EKSIEIE 851
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 852 NLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQ-ENKRKMGDKLSHE----RHQFQRDKEA 926
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRElaglRAELEELEKR 688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 293351385 927 TQEL---IEDLRKQLEhlqllrlEMEQRRGRSSSLGlqeyNSRARESELEQEVRRLK 980
Cdd:PRK03918 689 REEIkktLEKLKEELE-------EREKAKKELEKLE----KALERVEELREKVKKYK 734
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
780-993 |
1.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 780 RRVSELEKDSAAAGEQHGRLRQENLQLvhRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQArlqq 859
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK---- 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 860 lDEENSELRsctpclKANIERLEEEKQKmldEIEELTQRlseeQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLE 939
Cdd:PTZ00121 1655 -AEEENKIK------AAEEAKKAEEDKK---KAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 293351385 940 hlqlLRLEMEQRRGRSSSLGLQEYNSRARESEL---EQEVRRLKQDNRNLKEQNDEL 993
Cdd:PTZ00121 1721 ----LKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
783-993 |
1.70e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 783 SELEkdsaAAGEQHGRLRQENLQLVHrANALEEQLKEQEFRAQEKVLE-ETRKQKELLCKMEREKSIEIENLQARLQQLD 861
Cdd:pfam12128 322 SELE----ALEDQHGAFLDADIETAA-ADQEQLPSWQSELENLEERLKaLTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 862 EENSELRSCTPCLKANIER-LEEEKQKMLDEIEELTQRLSEEQEnkrKMGDKLSHERHQfQRDKEATQELIEDLRKQLEH 940
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEFNEEEY---RLKSRLGELKLR-LNQATATPELLLQLENFDER 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 293351385 941 LQLLRLEMEQRRGRSSSLGLQEYNSRAREselEQEVRRLKQDNRNLKEQNDEL 993
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRR---DQASEALRQASRRLEERQSAL 522
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
849-957 |
1.77e-04 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 43.42 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRlseeqenkrkmgdklsherhqfQRDKEATQ 928
Cdd:COG3166 46 QIAQQQARNAALQQEIAKLDK----QIAEIKELKKQKAELLARLQVIEQL----------------------QQSRPPWV 99
|
90 100 110
....*....|....*....|....*....|....
gi 293351385 929 ELIEDLRKQL-EHLQLLRLEMEQRR----GRSSS 957
Cdd:COG3166 100 HLLDELARLLpEGVWLTSLSQQGGTltltGVAQS 133
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
770-1038 |
1.81e-04 |
|
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: 45.73 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 770 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLkeQEFRAQEKVLEETRKQKELLCKMEREKSIE 849
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT--SAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 IENlqaRLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIE---ELTQRLSEEQENKRKMGDKLSH-ERHQFQRD-- 923
Cdd:TIGR00618 447 ITC---TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHpNPARQDIDnp 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 924 -------------KEATQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLGLQEYNSRARES-----ELEQEVRRLKQDN 983
Cdd:TIGR00618 524 gpltrrmqrgeqtYAQLETSEEDVYHQLTSErkQRASLKEQMQEIQQSFSILTQCDNRSKEDipnlqNITVRLQDLTEKL 603
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 984 RNLKEQNDELN-GQIITLSIQGAK---SLFSTSFSESLAAEISSVSRDELMEAIQKQEE 1038
Cdd:TIGR00618 604 SEAEDMLACEQhALLRKLQPEQDLqdvRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
778-1043 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALE--------------------EQLKEQEFRaqekvLEETRKQKE 837
Cdd:pfam05622 12 LAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLEsgddsgtpggkkylllqkqlEQLQEENFR-----LETARDDYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 838 LLCkMEREKsiEIENLQARLQQLDEENSELRSctpcLKANIERLEE--EKQKMLD-EIEELTQRLSEEQENKRKMgdKLS 914
Cdd:pfam05622 87 IKC-EELEK--EVLELQHRNEELTSLAEEAQA----LKDEMDILREssDKVKKLEaTVETYKKKLEDLGDLRRQV--KLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 915 HERHQFQRdkEATQELIEDLRK------QLE----HLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNR 984
Cdd:pfam05622 158 EERNAEYM--QRTLQLEEELKKanalrgQLEtykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 293351385 985 NLKEQNDEL---NGQIITLSIQGAKSLFSTSFSESLAAEISSVsrdELMEAIQKQEEINFRL 1043
Cdd:pfam05622 236 TLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA---EIREKLIRLQHENKML 294
|
|
| BCAS2 |
pfam05700 |
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ... |
788-900 |
2.32e-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: 43.34 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 788 DSAAAGEQHGRLRQENLQLV--HRANA--LEEQLKEQEFRAQEKVLEETRKQKELLckmEREKSIEIENLQARLQQLDEE 863
Cdd:pfam05700 98 DNAYAQLEHQRIRIENLELLqkYGANAwrLHNYQLEAILRRLEKELAETKEAIEEV---NRQRKNAQTAAGGELRSLEEK 174
|
90 100 110
....*....|....*....|....*....|....*..
gi 293351385 864 NSELRSctpclkANIErLEEEKQKMLDEIEELTQRLS 900
Cdd:pfam05700 175 WKELVS------KNLE-IEAACEALEAEILELKRQAA 204
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
786-1044 |
2.45e-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: 45.12 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 786 EKDS--AAAGEQHGRLRQENLQLVHRAnaleeQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQA-------- 855
Cdd:pfam05557 94 EKESqlADAREVISCLKNELSELRRQI-----QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKqqsslaea 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 856 --RLQQLDEENSELRSCTPCLKANIERLEE--EKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI 931
Cdd:pfam05557 169 eqRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 932 eDLRKQLEHLQlLRLEMEQRRGRSSSLGLQeynsraRESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGakslfst 1011
Cdd:pfam05557 249 -TLELEKEKLE-QELQSWVKLAQDTGLNLR------SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
250 260 270
....*....|....*....|....*....|....*
gi 293351385 1012 sfsESLAAEISSVSRD--ELMEAIQKQEEINFRLQ 1044
Cdd:pfam05557 314 ---RELEQELAQYLKKieDLNKKLKRHKALVRRLQ 345
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
778-997 |
2.51e-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: 45.17 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQE--------------NLQLVHRANALEEQLKEqefrAQEKVLEETRKQKEL---LC 840
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSElesvssllneaegkNIKLSKDVSSLESQLQD----TQELLQEETRQKLNLstrLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 841 KMEREKSIEIE----------NLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMg 910
Cdd:pfam01576 493 QLEDERNSLQEqleeeeeakrNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL- 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 911 dklsherhqfQRDKEATQELIEDLRKQLEHLQLL--RLEMEQRR-------GRSSSLGLQEYNSRARESELEQEVRRLK- 980
Cdd:pfam01576 572 ----------EKTKNRLQQELDDLLVDLDHQRQLvsNLEKKQKKfdqmlaeEKAISARYAEERDRAEAEAREKETRALSl 641
|
250 260
....*....|....*....|.
gi 293351385 981 ----QDNRNLKEQNDELNGQI 997
Cdd:pfam01576 642 aralEEALEAKEELERTNKQL 662
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
819-997 |
2.69e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 819 EQEFRAQEKVLEETRKQKELLCKmereksiEIENLQARLQQLDEENSELrsctpclKANIERLEEEKQKMLDEIEELTQR 898
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 899 LSEEQEnkrKMGDKLSHerhqFQRDKEATQEL--------IEDLrkqLEHLQLLRLEMEQRRGRssslgLQEYNS----- 965
Cdd:COG3883 81 IEERRE---ELGERARA----LYRSGGSVSYLdvllgsesFSDF---LDRLSALSKIADADADL-----LEELKAdkael 145
|
170 180 190
....*....|....*....|....*....|..
gi 293351385 966 RARESELEQEVRRLKQDNRNLKEQNDELNGQI 997
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
781-1038 |
2.88e-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: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 781 RVSELEKDSAAAGEQHGRLRQ---ENLQLVHRANALEEQLKEQEfRAQEKV----LEETRKQKELlckMEREK------- 846
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNEnieNKLLLKEEVEDLKRKLEREE-KYREEAatleLEKEKLEQEL---QSWVKlaqdtgl 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 847 --------SIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDK---LSH 915
Cdd:pfam05557 274 nlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllLTK 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 916 ER---------------------HQFQRDKEAT------QELIEDLRKQLEHLQ-----------LLRLEMEQRRGRSSs 957
Cdd:pfam05557 354 ERdgyrailesydkeltmsnyspQLLERIEEAEdmtqkmQAHNEEMEAQLSVAEeelggykqqaqTLERELQALRQQES- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 958 lglQEYNSRARE--SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS---FSESLAAEISSVSRDElMEA 1032
Cdd:pfam05557 433 ---LADPSYSKEevDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRKNQ-LEK 508
|
....*.
gi 293351385 1033 IQKQEE 1038
Cdd:pfam05557 509 LQAEIE 514
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
794-950 |
3.00e-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: 43.51 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 794 EQHGRLRQENLQLVHRANALEEQLKEQEFRA---QEKVLEETRKQKELLCkmeREKSIEIENLQARLQQLDEENSELRSC 870
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAkklEEKAQAALTKGNEELA---REALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 871 TPCLKANIERL-------EEEKQKMLdeIEELTQRlSEEQENKRKMGDKLSHERHQFQR--DKEATQELIEDLRKQLEHL 941
Cdd:pfam04012 113 VEQLRKQLAALetkiqqlKAKKNLLK--ARLKAAK-AQEAVQTSLGSLSTSSATDSFERieEKIEEREARADAAAELASA 189
|
....*....
gi 293351385 942 QLLRLEMEQ 950
Cdd:pfam04012 190 VDLDAKLEQ 198
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
816-997 |
3.55e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 816 QLK--EQEFRAQEKVLEETRKQK-ELLCKM-EREKSI-----EIENLQARLQQLDEENSELrsctpclKANIERLEEEK- 885
Cdd:PRK11637 48 QLKsiQQDIAAKEKSVRQQQQQRaSLLAQLkKQEEAIsqasrKLRETQNTLNQLNKQIDEL-------NASIAKLEQQQa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 886 --QKMLDEIEELTQRLSEEQ---------ENKRKmgdklshERHQ--FQRDKEATQELIEDLRKQLEHLQLLRLEMEQRR 952
Cdd:PRK11637 121 aqERLLAAQLDAAFRQGEHTglqlilsgeESQRG-------ERILayFGYLNQARQETIAELKQTREELAAQKAELEEKQ 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 293351385 953 GRSSS-LGLQ-------EYNSRARESELEQEVRRLKQDNRNLKE--QND-ELNGQI 997
Cdd:PRK11637 194 SQQKTlLYEQqaqqqklEQARNERKKTLTGLESSLQKDQQQLSElrANEsRLRDSI 249
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
800-1006 |
3.74e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 800 RQENLQLV-HRANALEEQLKEQEFRAQEKVLEETRKQKELlcKMEREKSIEIENLQARL----QQLDEENSELRSCTPCL 874
Cdd:pfam01576 10 KEEELQKVkERQQKAESELKELEKKHQQLCEEKNALQEQL--QAETELCAEAEEMRARLaarkQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 875 KANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMG-DKLSHE----------------RHQFQRDKEATQELIEDLRKQ 937
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlEKVTTEakikkleedillledqNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 938 L-------EHLQLLRL-------EMEQRRGRssslglqEYNSRareSELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:pfam01576 168 LaeeeekaKSLSKLKNkheamisDLEERLKK-------EEKGR---QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQ 237
|
...
gi 293351385 1004 GAK 1006
Cdd:pfam01576 238 LAK 240
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
844-1058 |
3.87e-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: 44.29 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 844 REKSIEIENLQARLQQLDEENSELRSCTPCLKANieRLEEEKQKMLDEIEELTQRLSEEQENKRKMgDKLSHERHQFQ-- 921
Cdd:COG5244 82 KGGLVCESKGMDKDGEIKQENHEDRIHFEESKIR--RLEETIEALKSTEKEEIVELRRENEELDKI-NLSLRERISSEep 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 922 -RDKEATQ-------ELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEynsrARESELEQEVRRLKQDNRNLKEQNDEL 993
Cdd:COG5244 159 eLNKDGSKlsydelkEFVEESRVQVYDMVELVSDISETLNRNGSIQRSS----VRECERSNIHDVLFLVNGILDGVIDEL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 994 NGQIitlsiqgakslfstsfsESLAAEISSvsrdeLMEAIQKQEEINFRLQDYIDRIIVAILETN 1058
Cdd:COG5244 235 NGEL-----------------ERLRRQLVS-----LMSSHGIEVEENSRLKATLEKFQSLELKVN 277
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
813-935 |
6.41e-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: 43.04 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 813 LEEQLKEQEFRAQ-----EKVLEETRKQKEllckMEREKSIEIENLQARLQQLDEENSEL-----RSCTPCLKANIERLE 882
Cdd:pfam02841 178 LQEFLQSKEAVEEailqtDQALTAKEKAIE----AERAKAEAAEAEQELLREKQKEEEQMmeaqeRSYQEHVKQLIEKME 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 293351385 883 EEKQKMLDEIEELTQRLSEEQENKRKMGdklsherhqFQRDKEATQELIEDLR 935
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 ... |
778-904 |
7.96e-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: 40.70 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANAleeqlkeqefrAQEKVLEETRKQKELLCKMEREKSiEIENLQARL 857
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE-----------AQQNYERELVLHAEDIKALQALRE-ELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 293351385 858 QQLDEENSELRSCtpcLKANIERLEEEKQKMLDEIEELTQRLSEEQE 904
Cdd:pfam07926 74 AELKAEAESAKAE---LEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
779-966 |
8.23e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQE-KVLEETRKQKELLCKMEREKSIEIENLQARL 857
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 858 QQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQrlseEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQ 937
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK----DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170 180
....*....|....*....|....*....
gi 293351385 938 LEHLQLLRLEMEQRRGRSSSLGLQEYNSR 966
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
841-947 |
8.35e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 841 KMERE-KSIEIENLQARLQQLDEENSEL-RSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERH 918
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 293351385 919 QFQRDKEATQELIEDLRKQLEHLQLLRLE 947
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
792-932 |
8.45e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 792 AGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCT 871
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEERE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 872 PCLKANIERLEEEKQKMLDEIEELTQrLSEEQENK---RKMGDKLSHERHQF-QRDKEATQELIE 932
Cdd:PRK12705 112 KALSARELELEELEKQLDNELYRVAG-LTPEQARKlllKLLDAELEEEKAQRvKKIEEEADLEAE 175
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
776-952 |
8.93e-04 |
|
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: 43.42 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 776 IFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKM---------EREK 846
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKdeleskeekEKEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 847 SIEIENLQARLQQLDEENSELRSCTpCLKANIERLEEEKQKML------DEIEELTQRLSEEQENKR------KMGDKLS 914
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERI-KEEAEILLKYEEEPEELlleeadEKEKEENNKEEEEERNKRlllakeELGKVNL 977
|
170 180 190
....*....|....*....|....*....|....*....
gi 293351385 915 HERHQFQRDKEA-TQELIEDLRKQLEHLQLLRLEMEQRR 952
Cdd:pfam02463 978 MAIEEFEEKEERyNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
778-1048 |
9.26e-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: 43.14 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQEnlqlVHRANALEEQL---KEQEFRAQEKVLEETRKQKELLCkmereksiEIENLQ 854
Cdd:pfam05622 150 LRRQVKLLEERNAEYMQRTLQLEEE----LKKANALRGQLetyKRQVQELHGKLSEESKKADKLEF--------EYKKLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 855 ARLQQLDEENselrsctpclkaniERLEEEKQKMLDEIEELtqRLSEEQENKRKMGDKLsHERHQFQRDKEATQELIEDL 934
Cdd:pfam05622 218 EKLEALQKEK--------------ERLIIERDTLRETNEEL--RCAQLQQAELSQADAL-LSPSSDPGDNLAAEIMPAEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 935 RKQLEHLQL----LRL-EMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGqiiTLSIQGAKSLF 1009
Cdd:pfam05622 281 REKLIRLQHenkmLRLgQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQK---ALQEQGSKAED 357
|
250 260 270
....*....|....*....|....*....|....*....
gi 293351385 1010 STSFSESLAAEIssvsrDELMEAiqkQEEINfRLQDYID 1048
Cdd:pfam05622 358 SSLLKQKLEEHL-----EKLHEA---QSELQ-KKKEQIE 387
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
516-545 |
9.37e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 37.54 E-value: 9.37e-04
10 20 30
....*....|....*....|....*....|
gi 293351385 516 RLRTVFDALDRDGDGFVRIEDFIQFATVYG 545
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
876-1050 |
9.94e-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: 43.13 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 876 ANIERLEEEKQKMLDEIEELTQRLSEEQ---ENKRKMGDKLSHERHQFQRDKEATQELIEdlRKQLEHLQLLRLEMEQRR 952
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKRE--YEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 953 GRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLfstsfsESLAAEISSVsRDELMEA 1032
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------GELEAEIASL-ERSIAEK 313
|
170
....*....|....*...
gi 293351385 1033 IQKQEEINFRLQDYIDRI 1050
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEI 331
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
770-1037 |
1.02e-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: 43.50 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 770 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKqkellCKMEREKSIE 849
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK-----LIQDQQEQIQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 I----------------ENLQARLQ---QLDEENSELRSCTPCLKANIER---LEEEKQKMLDEIEELTQRLSEE----- 902
Cdd:TIGR00606 861 HlksktnelkseklqigTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELISSKETSnkkaq 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 903 ---QENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGR-SSSLGLQEYN---SRARESELEQE 975
Cdd:TIGR00606 941 dkvNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKiNEDMRLMRQDidtQKIQERWLQDN 1020
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 293351385 976 VRRLKQDN--RNLKEQNDELNGQIITLSIQGAKSLFstsfsESLAAEISSVSRDELMEAIQKQE 1037
Cdd:TIGR00606 1021 LTLRKRENelKEVEEELKQHLKEMGQMQVLQMKQEH-----QKLEENIDLIKRNHVLALGRQKG 1079
|
|
| SynN |
smart00503 |
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
849-951 |
1.13e-03 |
|
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: 40.02 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM---LDEIEELTQRLSE--EQENKRKMGDKLSHERHQFQRd 923
Cdd:smart00503 9 KVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLerlIDDIKRLAKEIRAklKELEKENLENRASGSASDRTR- 87
|
90 100
....*....|....*....|....*...
gi 293351385 924 KEATQELIEDLRKQLEHLQLLRLEMEQR 951
Cdd:smart00503 88 KAQTEKLRKKFKEVMNEFQRLQRKYRER 115
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
773-949 |
1.14e-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: 43.02 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIFLERRVSELEKDSaaagEQHGR-LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIE 851
Cdd:COG5185 406 EILATLEDTLKAADRQI----EELQRqIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 852 NLQARLQQLdeeNSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEqenKRKMGDKLSHERHQFQRDKEATQELI 931
Cdd:COG5185 482 DLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF---MRARGYAHILALENLIPASELIQASN 555
|
170
....*....|....*...
gi 293351385 932 EDLRKQLEHLQLLRLEME 949
Cdd:COG5185 556 AKTDGQAANLRTAVIDEL 573
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
819-1049 |
1.15e-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: 42.80 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 819 EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEnselrsctpclkanieRLEEEKQKMLDEIEElTQR 898
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQE----------------RLRQEKEEKAREVER-RRK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 899 LSEEQENKRKMGDKLS-----HERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRS---SSLGLQEYNSRARES 970
Cdd:pfam17380 318 LEEAEKARQAEMDRQAaiyaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRElerLQMERQQKNERVRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 971 ELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDEL-----MEAIQKQEEINFRLQD 1045
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQerqqqVERLRQQEEERKRKKL 477
|
....
gi 293351385 1046 YIDR 1049
Cdd:pfam17380 478 ELEK 481
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
846-1040 |
1.21e-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: 42.89 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 846 KSIEIENLQARLQQLDEENSELRSCTPCLK---------ANIERLE--------EEKQKMLDEIEELTQRLSEEQ----- 903
Cdd:pfam10174 301 KESELLALQTKLETLTNQNSDCKQHIEVLKesltakeqrAAILQTEvdalrlrlEEKESFLNKKTKQLQDLTEEKstlag 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 904 --ENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRS-SSLG---------------LQEYNS 965
Cdd:pfam10174 381 eiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdTALTtleealsekeriierLKEQRE 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 966 RARESELEqEVRRLKQDNRNLKEQNDELngqiitlsiQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEIN 1040
Cdd:pfam10174 461 REDRERLE-ELESLKKENKDLKEKVSAL---------QPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
29-516 |
1.24e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 29 PDAPRGWSDEPEEHAQLQRWPEGPNAPICWPEEVEEPHAPRRwAEEPSASRCLSQEPYESCHLA----KELEEPDAPRCS 104
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQrprrRAARPTVGSLTS 2697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 105 SQEPDAPchlakdlEETDSPRCWPLEPDAPCHLAKEWEEPDVPRCWPQEPDAPCHLAKYLEEPDAPLCWPQEPDAfcyll 184
Cdd:PHA03247 2698 LADPPPP-------PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----- 2765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 185 keVEEPDVPRCRPQEP------DAPCHLAEELEDLDAPRCWTQEPNESCNLAKELDEPDTPRCLSQEPDAPCLLAKEWEE 258
Cdd:PHA03247 2766 --PPAPAPPAAPAAGPprrltrPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 259 SDAPSCWPQEPDVGPqepdvGCHLAKEREESDAPCLLTEELKEPDALQCWPQESDAPCLLA---EELEEPDAPHCCSQEV 335
Cdd:PHA03247 2844 GPPPPSLPLGGSVAP-----GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAlppDQPERPPQPQAPPPPQ 2918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 336 DTECLSAKESEEPDASHlwPGEPDAPclLVKEPEEADAPHCWPEEPeepdalnAPCFWANEPDEPDAPRCWSEEPQVLCL 415
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPP--PPRPQPP--LAPTTDPAGAGEPSGAVP-------QPWLGALVPGRVAVPRFRVPQPAPSRE 2987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 416 WPEEQNTTQCWQEEPDASCFWS-----EDREEPKVSCLQFKEPekpkvacswPEELEDCCPTRGLPLEPLLAEGELLQAC 490
Cdd:PHA03247 2988 APASSTPPLTGHSLSRVSSWASslalhEETDPPPVSLKQTLWP---------PDDTEDSDADSLFDSDSERSDLEALDPL 3058
|
490 500
....*....|....*....|....*.
gi 293351385 491 PGPPPDPglaLSLPSEPGTAqEEGAR 516
Cdd:PHA03247 3059 PPEPHDP---FAHEPDPATP-EAGAR 3080
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
804-902 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 804 LQLVHRANALEEQLKEqefrAQEKvLEETRKQKELLCKmereksiEIENLQARLQQLDEENSELRSCTPCLKANIERLEE 883
Cdd:COG4026 124 LQNIPEYNELREELLE----LKEK-IDEIAKEKEKLTK-------ENEELESELEELREEYKKLREENSILEEEFDNIKS 191
|
90
....*....|....*....
gi 293351385 884 EKQKMLDEIEELTQRLSEE 902
Cdd:COG4026 192 EYSDLKSRFEELLKKRLLE 210
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
884-993 |
1.29e-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: 41.05 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 884 EKQKML-DEIEELTQRlseEQENKRKMgDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEqrrgrssslglqe 962
Cdd:pfam13851 26 ELIKSLkEEIAELKKK---EERNEKLM-SEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLK------------- 88
|
90 100 110
....*....|....*....|....*....|.
gi 293351385 963 yNSRARESELEQEVRRLKQDNRNLKEQNDEL 993
Cdd:pfam13851 89 -NLKARLKVLEKELKDLKWEHEVLEQRFEKV 118
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
512-575 |
1.59e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 293351385 512 EEGARLRTVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDltqyLDPSGLGVISFEDFYQGIVA 575
Cdd:COG5126 2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSE----ADTDGDGRISREEFVAGMES 61
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
773-1000 |
1.68e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 773 DKVIFLERRVSELEKDSAAAGEQHGRLRQ------ENLQLVHRANALEEQLKEQEFRAQEK--VLEETRKQKELL----- 839
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKreRAEELRERAAELeaeae 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 840 -------CKMER--EKSIEIENLQARLQQLDEENSELRSCTPCLKA---NIERLEE--EKQKMLDEIEELT-QRLSEEQE 904
Cdd:PRK02224 555 ekreaaaEAEEEaeEAREEVAELNSKLAELKERIESLERIRTLLAAiadAEDEIERlrEKREALAELNDERrERLAEKRE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 905 NKRKMGDKLSHER-HQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSlGLQEYNS-RARESELEQEVRRLkqd 982
Cdd:PRK02224 635 RKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEELEElRERREALENRVEAL--- 710
|
250
....*....|....*...
gi 293351385 983 nRNLKEQNDELNGQIITL 1000
Cdd:PRK02224 711 -EALYDEAEELESMYGDL 727
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
811-1046 |
1.82e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 811 NALEEQLKEQ--EFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKM 888
Cdd:PRK01156 186 DYLEEKLKSSnlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 889 ---LDEIEELTQRLSE-EQENKRKMGDKLSHERHQ------FQRDKEATQELIEDLR----------KQLEHLQLLRLEM 948
Cdd:PRK01156 262 esdLSMELEKNNYYKElEERHMKIINDPVYKNRNYindyfkYKNDIENKKQILSNIDaeinkyhaiiKKLSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 949 EQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELngqiitlsiqgakslfstsfsESLAAEISSVSRDE 1028
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI---------------------ERMSAFISEILKIQ 400
|
250 260
....*....|....*....|.
gi 293351385 1029 LM--EAIQKQ-EEINFRLQDY 1046
Cdd:PRK01156 401 EIdpDAIKKElNEINVKLQDI 421
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
778-975 |
1.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEfraqekvlEETRKQKELLCKMERE------------ 845
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARAlyrsggsvsyld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 846 -----KSIE--IENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdklsherh 918
Cdd:COG3883 107 vllgsESFSdfLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAELEAAKAEL--------- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 919 qfQRDKEATQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLGLQEYNSRARESELEQE 975
Cdd:COG3883 174 --EAQQAEQEALLAQLSAEEAAAeaQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
826-936 |
1.97e-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: 40.20 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 826 EKVLEETRKQKELLCKMEREKSI---EIENLQARLQQLDEEnselrsctpcLKANIERL-EEEKQKMLDEIEELTQRLSE 901
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKrqaELQKLEKELQALQEK----------LQKEAATLsEEERQKKERELQKKQQELQR 101
|
90 100 110
....*....|....*....|....*....|....*
gi 293351385 902 EQENKRKMgdklsherhQFQRDKEATQELIEDLRK 936
Cdd:COG2825 102 KQQEAQQD---------LQKRQQELLQPILEKIQK 127
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
792-1042 |
2.03e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 792 AGEQ-HGRLRQENLQLVHRANALEEQ---LKEQEFRAQEKVLEETRKQKELLCKMEReksieIENLQARLQQLDEENSEL 867
Cdd:TIGR00618 532 RGEQtYAQLETSEEDVYHQLTSERKQrasLKEQMQEIQQSFSILTQCDNRSKEDIPN-----LQNITVRLQDLTEKLSEA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 868 RSCTPCLKaniERLEEEKQKMLDEieeltQRLSEEQENKRKMGDKLSHERHQFQrdKEATQEliedlrKQLEHLQLLRlE 947
Cdd:TIGR00618 607 EDMLACEQ---HALLRKLQPEQDL-----QDVRLHLQQCSQELALKLTALHALQ--LTLTQE------RVREHALSIR-V 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 948 MEQRRGRSSSLGLQEYNSRARE-----SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKslfsTSFSESLAAEIS 1022
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQltywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD----LAAREDALNQSL 745
|
250 260
....*....|....*....|
gi 293351385 1023 SVSRDELMEAIQKQEEINFR 1042
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFN 765
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
794-991 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 794 EQHGRLRQENLQLVhraNALEEQLKEQEFR---AQEKVLEetrkqkellckmereksieienlqarLQQLDEENSELRSC 870
Cdd:pfam15742 96 ELEVLKQAQSIKSQ---NSLQEKLAQEKSRvadAEEKILE--------------------------LQQKLEHAHKVCLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 871 TPCLKANiERLEEEKQKMLDEIEELTQRLSEEQEnKRKMGDKLSHERHQ---FQRDKEATQELI---EDLRKQLEHLQLL 944
Cdd:pfam15742 147 DTCILEK-KQLEERIKEASENEAKLKQQYQEEQQ-KRKLLDQNVNELQQqvrSLQDKEAQLEMTnsqQQLRIQQQEAQLK 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 293351385 945 RLEMEQRRG---RSSSLGLQEynsraRESELEQEVRRLKQDNRNLKEQND 991
Cdd:pfam15742 225 QLENEKRKSdehLKSNQELSE-----KLSSLQQEKEALQEELQQVLKQLD 269
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
784-1003 |
2.73e-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: 41.88 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 784 ELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFraQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQ---- 859
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL--ALKLTALHALQLTLTQERVREHALSIRVLPKELLAsrql 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 860 -LDEENSELRSCTPC--------------------------------------LKANIERLEEEKQKMLDEIEELTQRLS 900
Cdd:TIGR00618 681 aLQKMQSEKEQLTYWkemlaqcqtllrelethieeydrefneienassslgsdLAAREDALNQSLKELMHQARTVLKART 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 901 EEQENKR-------KMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEY----NSRARE 969
Cdd:TIGR00618 761 EAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEeqflSRLEEK 840
|
250 260 270
....*....|....*....|....*....|....
gi 293351385 970 SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 1003
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| Sec2p |
pfam06428 |
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ... |
879-957 |
2.86e-03 |
|
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.
Pssm-ID: 428938 [Multi-domain] Cd Length: 92 Bit Score: 37.93 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 879 ERLEEEKQKMLDEIEELTQRLSEEQEnkrKMGDKLSHERHQFQRDKEATQE-------LIEDLRKQLEHLQLLRLEMEQR 951
Cdd:pfam06428 10 LEAEKEKKKLEKELEDLTASLFEEAN---KMVAAARREKHAVEIKNDQLKEqlkeketLLESLQEQLKELKQVMQKMEEE 86
|
....*.
gi 293351385 952 RGRSSS 957
Cdd:pfam06428 87 QDDQTN 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
772-990 |
3.13e-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: 41.49 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 772 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLvhranALEEQLKEQEFR---AQEKVLEETRKQKELLCKMERE--- 845
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL-----QTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHpnp 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 846 ---KSIEIENLQARLQQLDEENSELRS--------CTPCLKaNIERLEEEKQKMLDEIEELTQ---RLSEEQENKRKMGD 911
Cdd:TIGR00618 516 arqDIDNPGPLTRRMQRGEQTYAQLETseedvyhqLTSERK-QRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 912 KLsheRHQFQRDKEATQELIEDLRKQLEHLQ----LLRLEMEQRRgRSSSLGLQEYNSRARESELEQE-----VRRLKQD 982
Cdd:TIGR00618 595 RL---QDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRLHLQQ-CSQELALKLTALHALQLTLTQErvrehALSIRVL 670
|
....*...
gi 293351385 983 NRNLKEQN 990
Cdd:TIGR00618 671 PKELLASR 678
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
794-1001 |
3.23e-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: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 794 EQHGR-LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRK-----QKELLCKMEREKSIEIENLQARLQ--QLDEENS 865
Cdd:TIGR00606 308 HNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlqlQADRHQEHIRARDSLIQSLATRLEldGFERGPF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 866 ELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQ--- 942
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqle 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 943 -----LLRLEMEQRRGRsSSLGLQEYNS-----RARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 1001
Cdd:TIGR00606 468 gssdrILELDQELRKAE-RELSKAEKNSltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT 535
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
779-981 |
3.33e-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: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEqLKEQEFRAQEKVLEETRKQ-------------KELLCKME-- 843
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-LELQLFPQAGTLLHFLRKEapdweqsigkvisPELLHRTDld 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 844 -------------------REKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELT-------- 896
Cdd:pfam12128 567 pevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASreetfart 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 897 ---------QRLSEEQENKRkmgDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYnSRA 967
Cdd:pfam12128 647 alknarldlRRLFDEKQSEK---DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY-WQV 722
|
250
....*....|....
gi 293351385 968 RESELEQEVRRLKQ 981
Cdd:pfam12128 723 VEGALDAQLALLKA 736
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
814-913 |
3.62e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 814 EEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQL-DEENSELRSctpclKANIERLEEekqkmldEI 892
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRK-----DREISRLDR-------EI 474
|
90 100
....*....|....*....|.
gi 293351385 893 EELTQRLSEEQENKRKMGDKL 913
Cdd:COG2433 475 ERLERELEEERERIEELKRKL 495
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
878-951 |
4.16e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 41.08 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 878 IERLEEEKQ---KMLDEIEELTQRlseEQENKRKMGD---KLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQR 951
Cdd:PRK11091 77 VEQLEESRQrlsRLVAKLEEMRER---DLELNVQLKDniaQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQ 153
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
850-988 |
4.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 IENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKmgdklsherhqfQRDKEATQE 929
Cdd:PRK00409 522 IASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ------------QAIKEAKKE 585
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 930 lIEDLRKQLEHLQllrlemeqrrgrssslglQEYNSRARESELEQEVRRLKQDNRNLKE 988
Cdd:PRK00409 586 -ADEIIKELRQLQ------------------KGGYASVKAHELIEARKRLNKANEKKEK 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
804-951 |
4.53e-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: 39.91 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 804 LQLVH-RANALEEQLKE--QEFRAQEKVLEETRKQKEllckmerEKSIEIENLQARLQQLDEE----------------- 863
Cdd:COG1579 12 LQELDsELDRLEHRLKElpAELAELEDELAALEARLE-------AAKTELEDLEKEIKRLELEieevearikkyeeqlgn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 864 ---NSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEH 940
Cdd:COG1579 85 vrnNKEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|.
gi 293351385 941 LQLLRLEMEQR 951
Cdd:COG1579 161 LEAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1038 |
4.64e-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: 41.21 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLdEIEELTQRLsEEQENKRKMGDKLSHErhqfqRDKEATQ 928
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-REYEGYELLKEKEALE-----RQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 929 ELIEDLRKQLEHLQLLRLEMEQRRG-----------RSSSLGLQEYNS-RARESELEQEVRRLKQDNRNLKEQNDELNGQ 996
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEeieqlleelnkKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 293351385 997 IITLSIQ-GAKSLFSTSFSESLAAEisSVSRDELMEAIQKQEE 1038
Cdd:TIGR02169 324 LAKLEAEiDKLLAEIEELEREIEEE--RKRRDKLTEEYAELKE 364
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
856-993 |
5.73e-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: 39.52 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 856 RLQQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKrkmgDKLSHERHQFQRDKEATQELIEDLR 935
Cdd:COG1579 11 DLQELDSELDRLE-------HRLKELPAELAELEDELAALEARLEAAKTEL----EDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 293351385 936 KQLEH------LQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDEL 993
Cdd:COG1579 80 EQLGNvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
809-1047 |
5.73e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 809 RANALEEQLKEQEFRAQekvLEETRKQKELlckmEREKSIEIENLQARLQQLDeenselrsctpclkaNIERLEEEKQKM 888
Cdd:PRK11281 28 RAASNGDLPTEADVQAQ---LDALNKQKLL----EAEDKLVQQDLEQTLALLD---------------KIDRQKEETEQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 889 LDEIEELTQRLSEEQENKRKMGDKLSherhqfqrdkeatqeliEDLRKQLEHLQLLRLEMEQRRgRSSSLG-----LQEY 963
Cdd:PRK11281 86 KQQLAQAPAKLRQAQAELEALKDDND-----------------EETRETLSTLSLRQLESRLAQ-TLDQLQnaqndLAEY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 964 NS----------RAReSELEQEVRRLKQDNRNLK-----------EQNDELNGQIITLSIQGA---KSLFSTSFSESLAA 1019
Cdd:PRK11281 148 NSqlvslqtqpeRAQ-AALYANSQRLQQIRNLLKggkvggkalrpSQRVLLQAEQALLNAQNDlqrKSLEGNTQLQDLLQ 226
|
250 260
....*....|....*....|....*...
gi 293351385 1020 EIssvsRDELMEAIQKQEEINFRLQDYI 1047
Cdd:PRK11281 227 KQ----RDYLTARIQRLEHQLQLLQEAI 250
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
778-934 |
5.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEK-----DSAAAGEQHGRLRQENLQLvhranaLEEQLKE--QEFRAQEKVLEETRKQ-KELLCKMEREKSIE 849
Cdd:PRK03918 590 LEERLKELEPfyneyLELKDAEKELEREEKELKK------LEEELDKafEELAETEKRLEELRKElEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 850 IEN----LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM---LDEIEELTQRLSEEQENKRKMGD-KLSHERHQFQ 921
Cdd:PRK03918 664 LREeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELREKVKKyKALLKERALS 743
|
170
....*....|...
gi 293351385 922 RDKEATQELIEDL 934
Cdd:PRK03918 744 KVGEIASEIFEEL 756
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
849-1039 |
5.82e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 EIENLQARLQQLDEENSELRSctpclkanierLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQ 928
Cdd:PRK01156 340 DYIKKKSRYDDLNNQILELEG-----------YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 929 ELIEDLRKQL------------------EHLQLLRLEMEQRRGRS------SSLG-------LQEYN---SRARE--SEL 972
Cdd:PRK01156 409 KELNEINVKLqdisskvsslnqriralrENLDELSRNMEMLNGQSvcpvcgTTLGeeksnhiINHYNekkSRLEEkiREI 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 293351385 973 EQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLfstsfsESLAAEISSVSRD--ELMEAIQKQEEI 1039
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKI------ESARADLEDIKIKinELKDKHDKYEEI 551
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
789-952 |
5.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 789 SAAAGEQHGRLRQENLQLV-----HRANALEEQLKEQEfraqekVLEETRKQKELLCKMEREKSIEIENLQARLQqldee 863
Cdd:PRK04863 270 VAADYMRHANERRVHLEEAlelrrELYTSRRQLAAEQY------RLVEMARELAELNEAESDLEQDYQAASDHLN----- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 864 nselrsctpcLKANIERLEEEKQKMLDEIEELTQRLsEEQENKRKMGDKLSHERhqfQRDKEATQELIEDLRKQLEHLQl 943
Cdd:PRK04863 339 ----------LVQTALRQQEKIERYQADLEELEERL-EEQNEVVEEADEQQEEN---EARAEAAEEEVDELKSQLADYQ- 403
|
....*....
gi 293351385 944 LRLEMEQRR 952
Cdd:PRK04863 404 QALDVQQTR 412
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
889-1061 |
6.52e-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: 39.32 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 889 LDEIE-ELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQllrlemeqrrgrsSSLGLQEYNSRA 967
Cdd:cd21116 50 LNEIKpKLLSLPNDIIGYNNTFQSYYPDLIELADNLIKGDQGAKQQLLQGLEALQ-------------SQVTKKQTSVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 968 RESELEQEVRRLKQDNRNLKEQNDELNGQIITLsiQGAKSLFSTsFSESLAAEISSVsrdelmEAIQKQEEInfrLQDYI 1047
Cdd:cd21116 117 FINELTTFKNDLDDDSRNLQTDATKAQAQVAVL--NALKNQLNS-LAEQIDAAIDAL------EKLSNDWQT---LDSDI 184
|
170
....*....|....
gi 293351385 1048 DRIIVAILETNPSI 1061
Cdd:cd21116 185 KELITDLEDAESSI 198
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
778-908 |
7.15e-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: 40.44 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 778 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALE----------EQLKEQ--EFRAQEKVLEEtrKQKELLCKMErE 845
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQRLSEElaDLNAAIAGIEA--KINELEEEKE-D 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 293351385 846 KSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEEL--TQRLSEEQENKRK 908
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGR 510
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
779-947 |
7.23e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.34 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALeeQLKEQEFRAQekvLEETRKQKELL---CKMEREK-SIEIENLQ 854
Cdd:pfam17078 65 ERRLKDLEDQLSELKNSYEELTESNKQLKKRLENS--SASETTLEAE---LERLQIQYDALvdsQNEYKDHyQQEINTLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 855 ARLQQLdeenselrsctpclkanieRLEEEKQkmldeIEELTQRLSEEQENKRKMGDKLSHERHQFqrdKEATQELIEDL 934
Cdd:pfam17078 140 ESLEDL-------------------KLENEKQ-----LENYQQRISSNDKDIDTKLDSYNNKFKNL---DNIYVNKNNKL 192
|
170
....*....|....
gi 293351385 935 RKQLEHL-QLLRLE 947
Cdd:pfam17078 193 LTKLDSLaQLLDLP 206
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
779-891 |
7.90e-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: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 779 ERRVSELEKDSAAAGEQHGR-LRQENLQLVHRANALEEQLKEQEFR--AQEKVLEETRKQKELL-----CKMEREKSIEI 850
Cdd:pfam14988 84 EREIQDLEEEKEKVRAETAEkDREAHLQFLKEKALLEKQLQELRILelGERATRELKRKAQALKlaakqALSEFCRSIKR 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 293351385 851 EN--LQARLQQLDEEnselrscTPCLKANIERLEEEKQKMLDE 891
Cdd:pfam14988 164 ENrqLQKELLQLIQE-------TQALEAIKSKLENRKQRLKEE 199
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
848-1045 |
8.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 848 IEIENLQARLQQLDEENSELRSCTpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKR---KMGDKLSHERHQFQRDK 924
Cdd:PRK01156 159 LEINSLERNYDKLKDVIDMLRAEI----SNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 925 EATQELIEDLRKQLEHLQllRLEMEQRRGRSSSLGLQEYNSRAreSELEQEVRRLKQD----NRNLKEQNDELNGQIITL 1000
Cdd:PRK01156 235 NNLKSALNELSSLEDMKN--RYESEIKTAESDLSMELEKNNYY--KELEERHMKIINDpvykNRNYINDYFKYKNDIENK 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 293351385 1001 S--IQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 1045
Cdd:PRK01156 311 KqiLSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE 357
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
813-940 |
8.55e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 38.71 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 813 LEEQLKEQEFRAQEKVLE---ETRKQKELLCKMEREKSIEIENLQARLQQ----LDEENSELRSctpcLKANIERLEEE- 884
Cdd:pfam12072 40 IEEAKKEAETKKKEALLEakeEIHKLRAEAERELKERRNELQRQERRLLQkeetLDRKDESLEK----KEESLEKKEKEl 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 293351385 885 --KQKMLDEIEELTQRLSEEQENKRKMGDKLSHErhqfqrdkEATQELIEDLRKQLEH 940
Cdd:pfam12072 116 eaQQQQLEEKEEELEELIEEQRQELERISGLTSE--------EAKEILLDEVEEELRH 165
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
966-997 |
8.71e-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: 35.60 E-value: 8.71e-03
10 20 30
....*....|....*....|....*....|..
gi 293351385 966 RARESELEQEVRRLKQDNRNLKEQNDELNGQI 997
Cdd:cd14686 20 KERIEELEEEVEELEEENEELKAELEELRAEV 51
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
814-935 |
9.10e-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: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 814 EEQLKEQEFRAQEKVLEETRKQKELLCKmEREKSieienLQARLQQLDEEnselrsctpclkanierLEEEKQKMLDEIE 893
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLE-DQERS-----YEEHLRQLKEK-----------------MEEERENLLKEQE 258
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 293351385 894 ELTQRLSEEQENKRKMGdklsherhqFQRDKEATQELIEDLR 935
Cdd:cd16269 259 RALESKLKEQEALLEEG---------FKEQAELLQEEIRSLK 291
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
689-989 |
9.85e-03 |
|
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: 40.09 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 689 VVMVIGSEEHFEDYGEGSEAELSPETLCNGELDCEDPAFLtpspakrLSSRKVARylhQSGTLTMEAledpppepvECPE 768
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL-------LENKELTQ---EASDMTLEL---------KKHQ 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 769 EDIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSI 848
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 849 --EIENLQARLQQLDEENSELRSCTPC-------LKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQ 919
Cdd:pfam05483 600 kkQIENKNKNIEELHQENKALKKKGSAenkqlnaYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293351385 920 FQRDKEATQELIEDLRKQLEH--LQLLRLeMEQRRG--------RSSSLGLqeYNSRARESE-----LEQEVRRLKQDNR 984
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHkiAEMVAL-MEKHKHqydkiieeRDSELGL--YKNKEQEQSsakaaLEIELSNIKAELL 756
|
....*
gi 293351385 985 NLKEQ 989
Cdd:pfam05483 757 SLKKQ 761
|
|
| |
