|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
766-1032 |
1.97e-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: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAgEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 845
Cdd:COG1196 198 LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQ 925
Cdd:COG1196 277 EELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 926 LEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQgAKSLFSTSFSESL 1005
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEE 428
|
250 260
....*....|....*....|....*..
gi 564371221 1006 AAEISSVSRDELMEAIQKQEEINFRLQ 1032
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 ... |
1013-1053 |
3.16e-14 |
|
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.
Pssm-ID: 462805 [Multi-domain] Cd Length: 41 Bit Score: 67.36 E-value: 3.16e-14
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 564371221 1013 SRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1053
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-1037 |
3.63e-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: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQ-----EFRAQEKVLEETRKQ-KELLCKMEREKSI--- 836
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELeerleEAEEELAEAEAEIEElEAQIEQLKEELKAlre 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEENSELRSCTPCLKAN-------IERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLshERHQFQ 909
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 910 RDKEatQELIEDLRKQLEHLQLLRLEMEQRRGRSsslglqEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQ-IITL 988
Cdd:TIGR02168 882 RASL--EEALALLRSELEELSEELRELESKRSEL------RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTL 953
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 989 SIQGAKSLFSTSFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLqDYIDR 1037
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERY-DFLTA 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
768-1033 |
4.10e-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: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 768 RRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKEllckmEREKSIEIENLQARLQQ 847
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 848 LDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLE 927
Cdd:COG1196 307 LEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 928 HLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAA 1007
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260
....*....|....*....|....*.
gi 564371221 1008 EISSVSRDELMEAIQKQEEINFRLQD 1033
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
761-1034 |
8.95e-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: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEkVLEETRKQKEllckmereksiEIEN 840
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 841 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE---------------------------EQEN 893
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeiqaelskleeevsriearlreiEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 894 KRKMGDK--LSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRsssLGLQEYNSRARESELEQEVRRLKQDN 971
Cdd:TIGR02169 822 NRLTLEKeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE---LEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 972 RNLKEQNDELNGQIITLSIQ--------GAKSLFSTSFSESLAAEISSVS-----------RDELMEAIQKQEEINFR-L 1031
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRlselkaklEALEEELSEIEDPKGEDEEIPEeelsledvqaeLQRVEEEIRALEPVNMLaI 978
|
...
gi 564371221 1032 QDY 1034
Cdd:TIGR02169 979 QEY 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
766-1026 |
3.92e-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: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ--EKVLEETRKQKELLCKMEREKSIEIENLQA 843
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRelEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 844 RLQQLDEENSELRSCtpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQfQRDKEATQELIEDLR 923
Cdd:COG1196 345 ELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 924 KQLEHLQLLRLEMEQRRGRssslglqeynSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAkslfstsfsE 1003
Cdd:COG1196 421 EELEELEEALAELEEEEEE----------EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA---------E 481
|
250 260
....*....|....*....|...
gi 564371221 1004 SLAAEISSVSRDELMEAIQKQEE 1026
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-1034 |
4.03e-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: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAgEQHGRLRQE--NLQL---VHRANALEEQLKEQEFRAQEKVLEETRKQKELlckmeREKSIEIEN 840
Cdd:TIGR02168 198 LERQLKSLERQAEKA-ERYKELKAElrELELallVLRLEELREELEELQEELKEAEEELEELTAEL-----QELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 841 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQ---RLSEEQENKRKMGDKLSHERHQFQRDKEATQE 917
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 918 LIEDLRKQLE-----------HLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQII 986
Cdd:TIGR02168 352 ELESLEAELEeleaeleelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564371221 987 TLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQ-EEINFRLQDY 1034
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREElEEAEQALDAA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
767-1039 |
5.16e-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: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQL--KEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQAR 844
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA-------LAELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 845 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQR---LSEEQENKRKMGDKLSHE--------------RHQ 907
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALREALDELRAEltllneeaanlrerLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 908 FQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLG----------LQEYNS--------RARESELEQEVRRLKQ 969
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleselealLNERASleealallRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564371221 970 DNRNLKEQNDELNGQI--ITLSIQGAKSLFstsfsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 1039
Cdd:TIGR02168 909 KRSELRRELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
760-969 |
1.29e-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: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 760 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIE 839
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 840 NLQARLQQLDEENSELRsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI 919
Cdd:COG1196 388 LLEALRAAAELAAQLEE-----LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564371221 920 EDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEY---NSRARESELEQEVRRLKQ 969
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLlllEAEADYEGFLEGVKAALL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
760-988 |
2.95e-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: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 760 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQlkeQEFRAQEKVLEETRKqkellckmereksiEIE 839
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL---AEYSWDEIDVASAER--------------EIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 840 NLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdklsherhqfqrdkeatqelI 919
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKE-------------------------L 722
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 920 EDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRR-LKQDNRNLKEQNDELNGQIITL 988
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-985 |
3.27e-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: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ---------EKVLEETRKQKELLCKMEREKSI 836
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleelEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLsherHQFQRDKEATQ 916
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL----ERLEDRRERLQ 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564371221 917 ELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSR--ARESELEQEVRRLKQDNRNLKEQNDELNGQI 985
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERleEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
758-993 |
4.96e-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: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 758 DIADKVI--FLERRVSELEKDSAAAGEQhgrLRQENLQLVHRANALEEQLkeQEFRAQEKVLEETRKQKELLCKME---- 831
Cdd:COG3206 152 AVANALAeaYLEQNLELRREEARKALEF---LEEQLPELRKELEEAEAAL--EEFRQKNGLVDLSEEAKLLLQQLSeles 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 832 --REKSIEIENLQARLQQLDEENSELRSCTPCLKAN--IERLEEEKQKMLDEIEELTQRLSEEqenkrkmgdklsHERHQ 907
Cdd:COG3206 227 qlAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPN------------HPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 908 fqrdkeATQELIEDLRKQLEH-----LQLLRLEMEQRRGRSSSLG--LQEYNSRARE-SELEQEVRRLKQDNRNLKEQND 979
Cdd:COG3206 295 ------ALRAQIAALRAQLQQeaqriLASLEAELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYE 368
|
250
....*....|....
gi 564371221 980 ELNGQIITLSIQGA 993
Cdd:COG3206 369 SLLQRLEEARLAEA 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
797-1053 |
8.96e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.84 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 797 RANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM 876
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 877 LDEIEELTQrlseEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQllrLEMEQRRGRSSSLGLQEYNSRAr 956
Cdd:COG4372 114 QEELEELQK----ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ---EELAALEQELQALSEAEAEQAL- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 957 eSELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYID 1036
Cdd:COG4372 186 -DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250
....*....|....*..
gi 564371221 1037 RIIVAILETNPSILEVK 1053
Cdd:COG4372 265 LAILVEKDTEEEELEIA 281
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
797-1042 |
1.01e-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: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 797 RANALEEQLKE--QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRsctpclkANIERLEEEKQ 874
Cdd:COG4942 21 AAAEAEAELEQlqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 875 KMLDEIEELTQRLSEE----QENKRKMGDKL---SHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRgrssslg 947
Cdd:COG4942 94 ELRAELEAQKEELAELlralYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 948 lqeynsrareSELEQEVRRLKQDNRNLKEQNDELNGQIITlsiqgakslfstsfSESLAAEISSvSRDELMEAIQKQEEI 1027
Cdd:COG4942 167 ----------AELEAERAELEALLAELEEERAALEALKAE--------------RQKLLARLEK-ELAELAAELAELQQE 221
|
250
....*....|....*
gi 564371221 1028 NFRLQDYIDRIIVAI 1042
Cdd:COG4942 222 AEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
770-991 |
1.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 770 VSELEKDSAAAGEQHGRLRQENLQlvhRANALEEQLKEQEfrAQEKVLEETRKQKEllckmerEKSIEIENLQARLQQLD 849
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAE--EKEEEYAELQEELE-------ELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 850 EENSELrsctpclkanieRLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLsHERHQFQRDKEATQELIEDLRKQLEHL 929
Cdd:COG4717 116 EELEKL------------EKLLQLLPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564371221 930 QLLRLEMEQRRGRSSSLGLQEynSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
767-1053 |
1.90e-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: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVhRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQ 846
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 847 QLDEENSELRSCTPCLKANIERLEEEkqkmldEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQL 926
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 927 EHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIitlsiqgakslfstsfsESLA 1006
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----------------EKLK 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 564371221 1007 AEISSVSR------DELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1053
Cdd:TIGR02169 399 REINELKReldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
767-979 |
2.06e-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: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQE--FRAQEKVLEETRKQKELLCKMEREKSieienlqAR 844
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEeaLREQAELNRLKKKYLEALNKKLNEKE-------SQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 845 LQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEdlrk 924
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE---- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564371221 925 qlehlqllrLEMEQRRGRSSSLGLQEYNSR-ARESELEQEVRRLKQDNRNLKEQND 979
Cdd:pfam05557 175 ---------LEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIE 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
766-968 |
3.15e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE-QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQAR 844
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 845 LQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRK 924
Cdd:PRK03918 323 INGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564371221 925 QLEHLQLLRLEMEQRRGRSSSlglqeynsraRESELEQEVRRLK 968
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKK----------EIKELKKAIEELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
758-954 |
3.20e-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: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 758 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ-------EKVL------EETRKQK 824
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqppLALLlspedfLDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 825 ELLCKMEREKSIEIENLQARLQQLDEenselrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHE 904
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAA-----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564371221 905 RHQFQRDKEATQELIEDLRKQLEHLQllrLEMEQRRGRSSSLGLQEYNSR 954
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLE---AEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
768-969 |
3.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 768 RRVSELEKDSAAAGEQHGRLRQENLQLvHRANALEEQLKEQEFRAQEKvLEETRKQKELLCKMEREKSI--EIENLQARL 845
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALeaELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdklsherhQFQRDKEATQELIEDLRKQ 925
Cdd:COG4717 149 EELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEE-------------ELQDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564371221 926 LEHLQLLRLEMEQRRgrssslglQEYNSRARESELEQEVRRLKQ 969
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 ... |
767-1007 |
6.75e-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: 60.37 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLK---------EQEFRAQEKVLEETRKQKELLCKMEREKSIE 837
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKesekekkkaEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 IENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQE 917
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 918 LIEDLRKQL------EHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:pfam02463 438 SIELKQGKLteekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250
....*....|....*.
gi 564371221 992 GAKSLFSTSFSESLAA 1007
Cdd:pfam02463 518 DGVGGRIISAHGRLGD 533
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
766-968 |
1.55e-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: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKEL-------------LCKMER 832
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELeaqkeelaellraLYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 833 EKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEkqkmLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDK 912
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 913 EATQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLK 968
Cdd:COG4942 195 AERQKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
763-1053 |
1.62e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 763 VIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKEllckmerEKSIEIEN 840
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarSELEQLEEELEELNEQLQ-------AAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 841 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIE 920
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 921 DLRKQleHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS 1000
Cdd:COG4372 179 AEAEQ--ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564371221 1001 FSESLAAEIS-SVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK 1053
Cdd:COG4372 257 LKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
786-1038 |
1.93e-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: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 786 RLR--QENLQlvhRANALEEQLKEQefraqekvLEETRKQKEllcKMER--EKSIEIENLQARLQQLDEENselrsctpc 861
Cdd:COG1196 180 KLEatEENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 862 LKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLRLEMEQ 938
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 939 RRGRsssLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLsiQGAKSLFSTSFSESLAAEISsvSRDELM 1018
Cdd:COG1196 317 RLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELL 389
|
250 260
....*....|....*....|
gi 564371221 1019 EAIQKQEEINFRLQDYIDRI 1038
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
808-1014 |
1.95e-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: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 808 QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRL 887
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 888 SEEQENKRKMGDKL--------------SHERHQFQRD-------KEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSL 946
Cdd:COG4942 100 EAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 947 gLQEYnsRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLsIQGAKSLfsTSFSESLAAEISSVSR 1014
Cdd:COG4942 180 -LAEL--EEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEEL--EALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
769-988 |
2.51e-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: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 769 RVSELEKDSAAAGEQHGRLRQEnLQLVHRANALEEQlKEQEFRAQEKVLEETRKQKE-----LLCKMEREKSIEIENLQ- 842
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQE-LEAARKVKILEEE-RQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERVRl 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 843 ---------ARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLD-EIEELTQRLSEEqENKRKMGDKLSHERHQFQRDK 912
Cdd:pfam17380 454 eeqerqqqvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAMIEE-ERKRKLLEKEMEERQKAIYEE 532
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564371221 913 EATQELIEDLRKQLEHLQLLRLEMEQRRgrssslgLQEYNSRARESELEQEVRRLKQDNRNlKEQNDELNGQIITL 988
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRK-------ATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
797-985 |
2.88e-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: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 797 RANALEEQLKEQEfRAQEKVlEETRKQKELLCKMeREKSIEIENLQARLQQLDEENSELRS-----CTPCLKANIERLEE 871
Cdd:COG4913 226 AADALVEHFDDLE-RAHEAL-EDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 872 EKQKMLDEIEELTQRLSEEQENKRKMgdKLSHERHQFQRdkeatqelIEDLRKQLEHLQLLRLEMEQRRGR----SSSLG 947
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARlealLAALG 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564371221 948 LQEYNSRA------------------RESELEQEVRRLKQDNRNLKEQNDELNGQI 985
Cdd:COG4913 373 LPLPASAEefaalraeaaallealeeELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
761-1044 |
3.08e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIfleRRVSELEK-----DSAAAGEQHGRLRQENLQ-LVHRANALEEQLKEQEfraqeKVLEETRKQKELLCKMEREK 834
Cdd:PRK03918 148 EKVV---RQILGLDDyenayKNLGEVIKEIKRRIERLEkFIKRTENIEELIKEKE-----KELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 835 SIEIENLQARLQQLD---EENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGD---------KLS 902
Cdd:PRK03918 220 REELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 903 HERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLglqeynsRARESELEQEVRRLK------QDNRNLKE 976
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEerhelyEEAKAKKE 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 977 QNDELNGQIITLSIqgakslfstsfsESLAAEISSVSR--DELMEAIQKQEEINFRLQDYIDRIIVAILE 1044
Cdd:PRK03918 373 ELERLKKRLTGLTP------------EKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
516-573 |
4.12e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 51.10 E-value: 4.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371221 516 RLRTVFDALDRDGDGFVRIEDFIQFATVYGA------EQVKDLTQYLDPSGLGVISFEDFYQGI 573
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgeplsdEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
768-981 |
6.57e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 768 RRVSELEKDSAAAGEQHGRLRQE----------------NLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKME 831
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKElrelekvlkkeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 832 REksieIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEI--------EELTQRLSE-------------- 889
Cdd:PRK03918 539 GE----IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELeelgfesvEELEERLKElepfyneylelkda 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 890 --EQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARE--SELEQEVR 965
Cdd:PRK03918 611 ekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRRE 690
|
250
....*....|....*.
gi 564371221 966 RLKQDNRNLKEQNDEL 981
Cdd:PRK03918 691 EIKKTLEKLKEELEER 706
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
777-969 |
7.60e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 777 SAAAGEQHGRLRQENLQLVHRANALEEQLK--EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSE 854
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 855 LRsctpclkANIERLEEEKQKMLDE----------------------------IEELTQRLSEEQENKRKMGDKLSHERH 906
Cdd:COG4942 95 LR-------AELEAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564371221 907 QFQRDKEATQELIEDLRKQLEHLQLLRlemEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQ 969
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
766-1028 |
7.78e-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: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSaaagEQHGRLRQENLQLVHRANALEEQLKEQEfraqekvleetrkqkellcKMEREKSIEIENLQARL 845
Cdd:TIGR04523 365 LEEKQNEIEKLK----KENQSYKQEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELtQRLSEEQENKRKmgdKLSHERHQFQRDKEATQELIEDLRKQ 925
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQLK---VLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 926 LEHLQLLRLEMEQR----RGRSSSLGLQEYNSRARESELEQEVRRLKQD---------NRNLKEQNDELNGQIITLSiQG 992
Cdd:TIGR04523 498 LKKLNEEKKELEEKvkdlTKKISSLKEKIEKLESEKKEKESKISDLEDElnkddfelkKENLEKEIDEKNKEIEELK-QT 576
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564371221 993 AKSLFSTSFS-----ESLAAEISSVsRDELMEAIQKQEEIN 1028
Cdd:TIGR04523 577 QKSLKKKQEEkqeliDQKEKEKKDL-IKEIEEKEKKISSLE 616
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
506-569 |
8.27e-08 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 52.10 E-value: 8.27e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564371221 506 EPGTAQEEGARLRTVFDALDRDGDGFVRIEDFIQFATVYG--AEQVKDLTQYLDPSGLGVISFEDF 569
Cdd:COG5126 60 ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEF 125
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
779-980 |
8.40e-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: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 779 AAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKvLEETRKQKELLCKMEREksIEIENLQARLQQLDEENSELRSC 858
Cdd:pfam13868 56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVER--IQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 859 TPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdklsheRHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQ 938
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564371221 939 RRGRsssLGLQEYNSRARESELEQEVRRLKQdNRNLKEQNDE 980
Cdd:pfam13868 206 LRAK---LYQEEQERKERQKEREEAEKKARQ-RQELQQAREE 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
797-991 |
1.02e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 797 RANALEEQLKEQEFRAqEKVLEETRKQKELLCKmereksiEIEnLQARlqqldEENSELRSctpclkanieRLEEEKQKM 876
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAEAIKK-------EAL-LEAK-----EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 877 LDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEynsrAR 956
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564371221 957 E---SELEQEVR-----RLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
760-1000 |
1.11e-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: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 760 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKeqefrAQEKVLEETRKQKELLCKMEREKSIEIE 839
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----ALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 840 NLQARLQQLDEENSEL--------RSCTPCLKANIERLeEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRD 911
Cdd:COG4942 94 ELRAELEAQKEELAELlralyrlgRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 912 KEATQELIEDLRKQLEHLQLLRlemEQRRGRSSSLglqeynsRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:COG4942 173 RAELEALLAELEEERAALEALK---AERQKLLARL-------EKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*....
gi 564371221 992 GAKSLFSTS 1000
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 ... |
782-1036 |
1.72e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 782 EQHGRLRQENLQLVHRANALE-EQLKEQEFRAQEKV-----LEETRKQKELLCKMEREKSIEIEnLQARLQQLDEENSEL 855
Cdd:pfam02463 191 DLEELKLQELKLKEQAKKALEyYQLKEKLELEEEYLlyldyLKLNEERIDLLQELLRDEQEEIE-SSKQEIEKEEEKLAQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 856 RSctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQENKRkmgdklSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLE 935
Cdd:pfam02463 270 VL-------KENKEEEKEKKLQEEELKLLAKEEEELKSEL------LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 936 MEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQ-DNRNLKEQNDELNGQIITLSIQG-AKSLFSTSFSE-SLAAEISSV 1012
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLELARQ 416
|
250 260
....*....|....*....|....
gi 564371221 1013 SRDELMEAIQKQEEINFRLQDYID 1036
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIE 440
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
761-1033 |
1.84e-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: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIFLERRVSELEKDSAAAGEQHGRLRQEnLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKMEReKS 835
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQlrariEELRAQEAVLEETQERINRARKAAP-LA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 836 IEIENLQARLQQLDEENSELRSCTPCL-KANIERLEEEKQKM-LDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKE 913
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSsIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 914 ATQElIEDLRKQLEHLqllrlemEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQndelngQIITLSIQGA 993
Cdd:TIGR00618 377 LTQH-IHTLQQQKTTL-------TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ------QELQQRYAEL 442
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 564371221 994 KSLFSTSFSESLAAEISsvsrdELMEAIQKQEEINFRLQD 1033
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKI-----HLQESAQSLKEREQQLQT 477
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
767-939 |
3.07e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEEtrkqkellckmereksiEIENLQARLQ 846
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 847 QLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENK-RKMGDKLSH---ERHQFQRDKEATQELIEDL 922
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*....
gi 564371221 923 RKQLEHL--QLLRLEMEQR 939
Cdd:COG4717 226 EEELEQLenELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
766-974 |
3.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEkDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 845
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEE--NSELRsctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLR 923
Cdd:COG4913 326 DELEAQirGNGGD--------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564371221 924 KQLEHLQLLRLEMEQRRGRssslglqeynSRARESELEQEVRRLKQDNRNL 974
Cdd:COG4913 398 EELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
772-1044 |
3.21e-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: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 772 ELEKDSAAAGEQHgRLRQENLQLVHRANALeeQLKEQEF----RAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQ 847
Cdd:pfam05483 406 ELEELKKILAEDE-KLLDEKKQFEKIAEEL--KGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 848 LDEENSElrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQE---NKRKMGDKLSHERHQFQRDKEATQELIEDLRK 924
Cdd:pfam05483 483 EKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVRE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 925 QL---------------EHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI---- 985
Cdd:pfam05483 556 EFiqkgdevkckldkseENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLnaye 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 986 -----ITLSIQGAKSLF---STSFSESLaaEISSVSRDELMEAIQK-----------QEEINFRLQDYIDRiIVAILE 1044
Cdd:pfam05483 636 ikvnkLELELASAKQKFeeiIDNYQKEI--EDKKISEEKLLEEVEKakaiadeavklQKEIDKRCQHKIAE-MVALME 710
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
769-945 |
3.38e-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: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 769 RVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQ 846
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 847 QLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLS-EEQENKR--KMGDKLSHERHQFQRDKEATQELIEDLR 923
Cdd:pfam19220 129 AETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlLEQENRRlqALSEEQAAELAELTRRLAELETQLDATR 208
|
170 180
....*....|....*....|..
gi 564371221 924 KQLEHLQLLRLEMEQRRGRSSS 945
Cdd:pfam19220 209 ARLRALEGQLAAEQAERERAEA 230
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
761-961 |
3.62e-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: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIFLERRVSELEKDSAAAGEQHGRLRQEnlqlvhrANALEEQLKEQEFRaQEKVLEETRKQKEllckmereksiEIEN 840
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKR-RDKLTEEYAELKE-----------ELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 841 LQARLQQLDEENSELRSCTPCLKANIERLEEEK---QKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQE 917
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREInelKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564371221 918 LIEDLRKQLEHLQlLRLEMEQRRGRSSSLGLQEYNSRARESELE 961
Cdd:TIGR02169 449 EIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
766-1014 |
3.90e-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: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLvhraNALEEQlKEQ--------EFRAQEKVLEETRKQKEllckmEREKSI- 836
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQ-KEQdwnkelksELKNQEKKLEEIQNQIS-----QNNKIIs 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 ----EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE-EQenkrkmgdklsherhQFQRD 911
Cdd:TIGR04523 339 qlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDlES---------------KIQNQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 912 KEATQEliedLRKQLEHLQllrlemeqrrgrssslglQEYNsraresELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:TIGR04523 404 EKLNQQ----KDEQIKKLQ------------------QEKE------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260
....*....|....*....|...
gi 564371221 992 gAKSLfsTSFSESLAAEISSVSR 1014
Cdd:TIGR04523 456 -IKNL--DNTRESLETQLKVLSR 475
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
787-989 |
3.92e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 787 LRQENLQLVHRANALEEQLKEQE---FRAQEKVLEE-TRKQK---ELLCKMEREKSiEIENLQARLQQLDEEN------- 852
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNkniEEQRKKNGENiARKQNkydELVEEAKTIKA-EIEELTDELLNLVMDIedpsaal 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 853 SELRSCTPCLKANIERLEEEkQKMLDEIEEL---TQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIE---DLRKQL 926
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKV-IKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQS 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 927 EHLQLLRLEMEQRRGRssslgLQEYNSRAR--ESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 989
Cdd:PHA02562 337 KKLLELKNKISTNKQS-----LITLVDKAKkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-930 |
3.95e-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: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLkeqefRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 845
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRS--CTPCLKANIERLEEEKQkMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLR 923
Cdd:TIGR02168 417 ERLQQEIEELLKklEEAELKELQAELEELEE-ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
....*..
gi 564371221 924 KQLEHLQ 930
Cdd:TIGR02168 496 RLQENLE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
799-1051 |
4.78e-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: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 799 NALEEQLKE---------QEFRAQEKVLE-------ETRKQKELL----CKMEREKS-IEIENLQARLQ----------- 846
Cdd:TIGR04523 127 NKLEKQKKEnkknidkflTEIKKKEKELEklnnkynDLKKQKEELenelNLLEKEKLnIQKNIDKIKNKllklelllsnl 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 847 --------QLDEENSELRSCTPCLKANIERLEEEKQKMLDEI----EELTQRLSEEQENKRKMGDKlsherhqfQRDKEA 914
Cdd:TIGR04523 207 kkkiqknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLKDEQNKIKKQLSEK--------QKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 915 TQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLG---------LQEYNSRARE-----SELEQEVRRLKQ-------DN 971
Cdd:TIGR04523 279 NNKKIKELEKQLNQLksEISDLNNQKEQDWNKELKselknqekkLEEIQNQISQnnkiiSQLNEQISQLKKeltnsesEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 972 RNLKEQNDELNGQIITLSIQGAKSLFStsfSESLAAEISsvsrdELMEAIQKQEEINFRLQDYIDriivaILETNPSILE 1051
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQE---IKNLESQIN-----DLESKIQNQEKLNQQKDEQIK-----KLQQEKELLE 425
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
766-981 |
8.15e-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: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQ------ENLQLVHR----ANALE--------EQLKEQEFRAQEKVLEeTRKQKELL 827
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQqldqlkEQLQLLNKllpqANLLAdetladrlEELREELDAAQEAQAF-IQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 828 CKMEREKSI------EIENLQARLQQLDEENSELRSCTPCLKANIERLE----EEKQKMLDE----IEELTQRLSEEQEN 893
Cdd:COG3096 920 AQLEPLVAVlqsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlNEKLRARLEQAEEA 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 894 KRKMGDKLSHERHQFQrdkEATQELIeDLR-----KQLEHLQLLR----------LEMEQR-RGRSSSLGLQEYNSRAR- 956
Cdd:COG3096 1000 RREAREQLRQAQAQYS---QYNQVLA-SLKssrdaKQQTLQELEQeleelgvqadAEAEERaRIRRDELHEELSQNRSRr 1075
|
250 260 270
....*....|....*....|....*....|....*
gi 564371221 957 ----------ESELEQEVRRLKQDNRNLKEQNDEL 981
Cdd:COG3096 1076 sqlekqltrcEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
766-969 |
1.23e-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: 53.03 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSA--AAGEQHGRLRQENLQLvHRANALEEQLKEQEFRAQEKvlEETRKQKELLCK---MEREKSIEIEN 840
Cdd:COG3096 481 VCKIAGEVERSQAwqTARELLRRYRSQQALA-QRLQQLRAQLAELEQRLRQQ--QNAERLLEEFCQrigQQLDAAEELEE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 841 LQARLQQLDEENSE-LRSCtpclkanIERLEEEKQKmLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI 919
Cdd:COG3096 558 LLAELEAQLEELEEqAAEA-------VEQRSELRQQ-LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564371221 920 EDLRKQLEHLQLLRLEMEQrrgrssslglqeynSRARESELEQEVRRLKQ 969
Cdd:COG3096 630 AAMQQLLEREREATVERDE--------------LAARKQALESQIERLSQ 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
803-1044 |
1.28e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 803 EQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEE 882
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ----AREELEQLEEELEQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 883 LTQRLSEEQENKRKMGDKLSHER---HQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRR-GRSSSLGLQEYNSRARES 958
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIaELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 959 E---LEQEVRRLKQDNRNLKEQndELNGQIITLSIQGAKSLFSTSFSESL--AAEISSVSRDELMEAIQKQEEINFRLQD 1033
Cdd:COG4372 158 QlesLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAekLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250
....*....|.
gi 564371221 1034 YIDRIIVAILE 1044
Cdd:COG4372 236 SALLDALELEE 246
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
766-1052 |
1.78e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKE--QEFRAQEKVLEETRKQKELLCKmereksiEIENLQA 843
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAaqAELAQAQEELESLQEEAEELQE-------ELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 844 RLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHE---RHQFQRDKEATQELIE 920
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaldELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 921 DLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS 1000
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564371221 1001 FSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEV 1052
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
733-974 |
2.68e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 733 LHQSGTLTMEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEqhgrLRQENLQLVHRANALEEQLKEQEFRA 812
Cdd:COG5022 847 LIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS----LKLVNLELESEIIELKKSLSSDLIEN 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 813 QEKVLEETRKQKELLCKMEREKSIEIE-NLQARLQQLDEENSELRSCTPCLKANIERLEE---EKQKMLDEIEELTQRLS 888
Cdd:COG5022 923 LEFKTELIARLKKLLNNIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEYEDLLKKSTIlvrEGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 889 EEQENKRKMGDKLS---HERHQFQRDKEAT----------------QELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQ 949
Cdd:COG5022 1003 ELSKQYGALQESTKqlkELPVEVAELQSASkiissestelsilkplQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260
....*....|....*....|....*.
gi 564371221 950 EYNSRARESEL-EQEVRRLKQDNRNL 974
Cdd:COG5022 1083 LYQLESTENLLkTINVKDLEVTNRNL 1108
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
766-929 |
2.75e-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: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQ--EKVLEETRKQKELlckmeREKSIEIENLQA 843
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEY-----EALQKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 844 RLQQLDEENSElrsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI-EDL 922
Cdd:COG1579 104 RISDLEDEILE-------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPEL 176
|
....*..
gi 564371221 923 RKQLEHL 929
Cdd:COG1579 177 LALYERI 183
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
766-959 |
3.66e-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: 50.02 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEkdsaaagEQHGRLRQENLQLVHRANALEE--QLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQA 843
Cdd:pfam04849 99 LTERNEALE-------EQLGSAREEILQLRHELSKKDDllQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 844 RLQQLDEENSELRSCTPCLKANIERLEEEKQK-MLDEIEELTQ------RLSEEQENKRKmgdklSHERHQfqrdKEATQ 916
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEKEQQlMSDCVEQLSEanqqmaELSEELARKME-----ENLRQQ----EEITS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564371221 917 EL--IEDLRKQL--------EHLQLLRLEME-QRRGRSSslgLQEYNSRARESE 959
Cdd:pfam04849 243 LLaqIVDLQHKCkelgieneELQQHLQASKEaQRQLTSE---LQELQDRYAECL 293
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
761-1032 |
5.75e-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: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIFLERRvsELEKDSAAAGeQHGRlrQENLQLVHRANaLEEQLKEQEFRAQE-KVLEETRKQKellckmereksieIE 839
Cdd:pfam15921 561 DKVIEILRQ--QIENMTQLVG-QHGR--TAGAMQVEKAQ-LEKEINDRRLELQEfKILKDKKDAK-------------IR 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 840 NLQARLQQLDEENSELrsctpcLKANIERL------EEEKQKMLDEIE----ELTQrLSEEQE----NKRKMGDKLSHER 905
Cdd:pfam15921 622 ELEARVSDLELEKVKL------VNAGSERLravkdiKQERDQLLNEVKtsrnELNS-LSEDYEvlkrNFRNKSEEMETTT 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 906 HQFQRDKEATQELIEDLRKQLE-------HLQLLRLEMEQ----RRGRSSSLG-----LQEYNSRARESE--LEQEVRRL 967
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKsmegsdgHAMKVAMGMQKqitaKRGQIDALQskiqfLEEAMTNANKEKhfLKEEKNKL 774
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 968 KQDNRNLKEQNDELNGQIITLSIQgAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQ 1032
Cdd:pfam15921 775 SQELSTVATEKNKMAGELEVLRSQ-ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
773-974 |
5.89e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 773 LEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEN 852
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 853 SELRSCTPcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLL 932
Cdd:COG1196 659 GGSLTGGS-RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564371221 933 RLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNL 974
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
758-1026 |
6.58e-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: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 758 DIADKVIFLERRVSELEKdsaaAGEQHGRLRQENL----QLVHRANALEEQLKEQEFRAQEKVLEETRKQkellckmerE 833
Cdd:COG5185 240 DPESELEDLAQTSDKLEK----LVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIAEYTKSI---------D 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 834 KSIEIENLQARLQQLDEENSelrsctpclkanIERLEEEKQKMLDE-IEELTQR---LSEEQENKRKMGDKLSHERHQFQ 909
Cdd:COG5185 307 IKKATESLEEQLAAAEAEQE------------LEESKRETETGIQNlTAEIEQGqesLTENLEAIKEEIENIVGEVELSK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 910 RDKEATQEL--IEDLRKQLEHLQllrleMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI-- 985
Cdd:COG5185 375 SSEELDSFKdtIESTKESLDEIP-----QNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIse 449
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564371221 986 ITLSIQGAKSLFSTSFSESLAAEISSV--SRDELMEAIQKQEE 1026
Cdd:COG5185 450 LNKVMREADEESQSRLEEAYDEINRSVrsKKEDLNEELTQIES 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
807-1028 |
7.35e-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: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 807 EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSEL-------RSCTPCLKANIERLEEEKQKMLDE 879
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 880 IEELTQRLSEEQENKRKMGDKLSHERHQ-----------FQRDKEATQELIEDLRKQL----EHLQLLRLEMEQRRGRSS 944
Cdd:pfam05483 178 REETRQVYMDLNNNIEKMILAFEELRVQaenarlemhfkLKEDHEKIQHLEEEYKKEIndkeKQVSLLLIQITEKENKMK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 945 SLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI--ITLSIQGAKSLfSTSFSESLaaEISSVSRDELMEAIQ 1022
Cdd:pfam05483 258 DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELedIKMSLQRSMST-QKALEEDL--QIATKTICQLTEEKE 334
|
....*..
gi 564371221 1023 KQ-EEIN 1028
Cdd:pfam05483 335 AQmEELN 341
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
788-1034 |
9.01e-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: 50.12 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 788 RQENLQLVHRANALEEQLKEQefraQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIE 867
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEM----LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK----LRSRVD 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 868 RLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKlsherhqfqrDKeatqeLIEDLRKQLEHLqllrLEMEQRRGRSSSLG 947
Cdd:pfam15921 528 LKLQELQHLKNEGDHLRNVQTECEALKLQMAEK----------DK-----VIEILRQQIENM----TQLVGQHGRTAGAM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 948 LQEynsrarESELEQEV--RRLK-QDNRNLKEQND----ELNGQIITLSIQGAKslFSTSFSESLAA--EISSvSRDELM 1018
Cdd:pfam15921 589 QVE------KAQLEKEIndRRLElQEFKILKDKKDakirELEARVSDLELEKVK--LVNAGSERLRAvkDIKQ-ERDQLL 659
|
250
....*....|....*..
gi 564371221 1019 EAIQK-QEEINFRLQDY 1034
Cdd:pfam15921 660 NEVKTsRNELNSLSEDY 676
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
782-990 |
9.95e-06 |
|
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: 49.26 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 782 EQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLcKMEReksiEIENLQARLQQLDEENSELRSCTPC 861
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQ-LQER----LEEACHKRQLKEREEQKKVQENNLS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 862 LKANIERL---------EEEKQKMLDeieeLTQRLSEEQENK--------RKMGDKLSHERHQFQRDKEATQeliEDLRK 924
Cdd:pfam15558 176 ELLNHQARkvlvdcqakAEELLRRLS----LEQSLQRSQENYeqlveerhRELREKAQKEEEQFQRAKWRAE---EKEEE 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 925 QLEHLQLLRLEMEQRRGRS---SSLGLQEYNSRARESELEQEvrRLKQDNRNLKEQNDELNGQIITLSI 990
Cdd:pfam15558 249 RQEHKEALAELADRKIQQArqvAHKTVQDKAQRARELNLERE--KNHHILKLKVEKEEKCHREGIKEAI 315
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
832-1039 |
1.02e-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: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 832 REKSIEIENLQARLQQLDEENSELRSCTPCLKAN-IERLEEEKQKMLDEIEELTQRLSeEQENKRKMGDKLSHERHQFQR 910
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAEsSKRLNENANNLIKQFENTKEKIA-EYTKSIDIKKATESLEEQLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 911 dKEATQELIEDLRKQLEHLQLLRLEMEQRRgRSSSLGLQEYNSRARESELEQEVRRLKQdnrNLKEQNDELNGQIITL-S 989
Cdd:COG5185 321 -AEAEQELEESKRETETGIQNLTAEIEQGQ-ESLTENLEAIKEEIENIVGEVELSKSSE---ELDSFKDTIESTKESLdE 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564371221 990 IQGAKSLFSTSFSESLAAEISSVSRD--ELMEAIQKQEEINFRLQDYIDRII 1039
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQieELQRQIEQATSSNEEVSKLLNELI 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
766-970 |
1.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQE--KVLEETRKQKELLCKMEREK---SIEIEN 840
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEleTLEAEIEDLRETIAETEREReelAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 841 LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSE----------EQENKRKMGDKLShERHQFQR 910
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqahneEAESLREDADDLE-ERAEELR 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 911 DKEAT-----QELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQD 970
Cdd:PRK02224 363 EEAAEleselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
799-1028 |
1.21e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 799 NALEEQLKEQEFRAQEKVLEETRKQKELlckmereksieIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLD 878
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDEL-----------NEELKELAEKRDELNAQVKE----LREEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 879 EIEELTQRLSEEQENKRKMGDKLshERHQFQRDKEATQEL-IEDLRKQLEhlqllRLEMEQrrgRSSSLGLQEynsrarE 957
Cdd:COG1340 72 KVKELKEERDELNEKLNELREEL--DELRKELAELNKAGGsIDKLRKEIE-----RLEWRQ---QTEVLSPEE------E 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 958 SELEQEVRRLKQDNRNLKEQNdELNGQIITLS--IQGAKSLFSTSFSE--SLAAEISSVSrDELMEAIQKQEEIN 1028
Cdd:COG1340 136 KELVEKIKELEKELEKAKKAL-EKNEKLKELRaeLKELRKEAEEIHKKikELAEEAQELH-EEMIELYKEADELR 208
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
806-1033 |
1.26e-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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 806 KEQEFRAQEKVLEETRKQKELLckmerekSIEIENLQARLQQLDEENSELRsctpclkanierleeeKQKmldeieeltq 885
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYNDLK----------------KQK---------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 886 rlsEEQENkrkmgdklshERHQFQRDKEATQELIEDLRKQLEHLQLLRLEmeqrrgrssslgLQEYNSRAResELEQEVR 965
Cdd:TIGR04523 169 ---EELEN----------ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN------------LKKKIQKNK--SLESQIS 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 966 RLKQDNRNLKEQNDELNGQIitlsiqgakslfstsfsESLAAEISSVsRDELMEAIQKQEEINFRLQD 1033
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEI-----------------NEKTTEISNT-QTQLNQLKDEQNKIKKQLSE 271
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
837-985 |
1.46e-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: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEEnselrsctpclkanIERLEEEKQKMLDEIEELTQRLSEEQENkrkmgdklsHERhQFQRDKEATQ 916
Cdd:pfam07926 2 ELSSLQSEIKRLKEE--------------AADAEAQLQKLQEDLEKQAEIAREAQQN---------YER-ELVLHAEDIK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 917 ELiEDLRKQLEHLQLLRLEME-QRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQI 985
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 ... |
766-981 |
1.72e-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: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRA---------QEKVLE--ETRKQKELLCKMEREK 834
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkHEAMISdlEERLKKEEKGRQELEK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 835 SIEieNLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEA 914
Cdd:pfam01576 209 AKR--KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 915 tQELIEDLRKQL-EHLQLLRLEMEQRRGrsSSLGLQEYNSRaRESELEQEVRRLKQDNRNLKEQNDEL 981
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 |
1.88e-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: 1.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564371221 516 RLRTVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDLTQYL----DPSGLGVISFEDFYQGI 573
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELM 62
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
787-976 |
1.89e-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: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 787 LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANI 866
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 867 ERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSL 946
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190
....*....|....*....|....*....|
gi 564371221 947 GLQEYNSRARESELEQEVRRLKQDNRNLKE 976
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
788-989 |
1.99e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 788 RQENLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEnselrsctpcl 862
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET----------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 863 kanIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDK----------LSHERHQFQRDKEATQELIEDLRKQLEhlqll 932
Cdd:PRK02224 267 ---IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQ----- 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 933 RLEMEQRRGRSSSLGLQEYNSRARE--SELEQEVRRLKQDNRNLKEQNDELNGQIITLS 989
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
766-988 |
2.00e-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: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQ-------LVHRANALEEQLKEQEFR--AQEKVLEET------------RKQK 824
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKnnseikdLTNQDSVKELIIKNLDNTreSLETQLKVLsrsinkikqnleQKQK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 825 ELlckmeREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMG------ 898
Cdd:TIGR04523 490 EL-----KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeid 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 899 ------DKLSHE-----RHQFQRDKEATQ----------------ELIEDLRKQLEHlqllrLEMEQRRgrsssLGLQEY 951
Cdd:TIGR04523 565 eknkeiEELKQTqkslkKKQEEKQELIDQkekekkdlikeieekeKKISSLEKELEK-----AKKENEK-----LSSIIK 634
|
250 260 270
....*....|....*....|....*....|....*..
gi 564371221 952 NSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITL 988
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
772-1026 |
2.01e-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: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 772 ELEKDSAAAGEQHGRLRQENLQLVHRAnaleEQLKEQEFRAQEKVLEETRKQKellckMEREKSIEIENLQARLQQLDEE 851
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQS----EKDKKNKALAERKDSANERLNS-----LEAQLKQLDKKHQAWLEEQKEQ 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 852 NSELRSCTPC--------------------------LKANIERLEEEKQKMLD--------------EIEELTQRLSEEQ 891
Cdd:pfam12128 709 KREARTEKQAywqvvegaldaqlallkaaiaarrsgAKAELKALETWYKRDLAslgvdpdviaklkrEIRTLERKIERIA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 892 ENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHL--QLLRLEMEQRRgRSSSLGLQEYNSRARESELEQEVRRLKQ 969
Cdd:pfam12128 789 VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELqqQLARLIADTKL-RRAKLEMERKASEKQQVRLSENLRGLRC 867
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 970 DNRNLKEQNDELNGQIITLSIqgakslfstsfSESLAA-EISSVSRDELMEAIQKQEE 1026
Cdd:pfam12128 868 EMSKLATLKEDANSEQAQGSI-----------GERLAQlEDLKLKRDYLSESVKKYVE 914
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
766-932 |
2.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQ--ENLQLVHRANALEEQLKE-----QEFRAQEKVLEETRKQKELLCKmereksiEI 838
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEA-------EL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 839 ENLQarlQQLDEEnseLRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKrkmgdklshERHQFQRDKEATQEL 918
Cdd:COG4717 173 AELQ---EELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---------EELEEELEQLENELE 237
|
170
....*....|....
gi 564371221 919 IEDLRKQLEHLQLL 932
Cdd:COG4717 238 AAALEERLKEARLL 251
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
12-328 |
2.27e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 12 HDEPASGPQRGVKGLVGP---------DAPRGWSDEPEEHAQLQRWPEGpnapicwpeEVEEPHAPRRwAEEPSASRCLS 82
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEG---------EVGKKPGPAK-EHKPSKIPTLS 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 83 QEPyESCHLAKELEEPDAPRcSSQEPDAPCHlakdleetdsprcwPLEPDAPchlaKEWEEPDVPRCwPQEPDAPchlak 162
Cdd:PTZ00449 577 KKP-EFPKDPKHPKDPEEPK-KPKRPRSAQR--------------PTRPKSP----KLPELLDIPKS-PKRPESP----- 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 163 ylEEPDAPLCwPQEPDAfcylLKEVEEPDVPRC--RPQEPDAPC--HLAEELED--LDAP--------RCWTQEPNESCN 228
Cdd:PTZ00449 631 --KSPKRPPP-PQRPSS----PERPEGPKIIKSpkPPKSPKPPFdpKFKEKFYDdyLDAAaksketktTVVLDESFESIL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 229 LAKELDEPDTPRCLSQE-----PDAPCLLAKEWEESDAPSCWPQEPDVGPQEPDVGCHlaKEREESDAPCLLTEELKEPD 303
Cdd:PTZ00449 704 KETLPETPGTPFTTPRPlppklPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFH--ETPADTPLPDILAEEFKEED 781
|
330 340
....*....|....*....|....*
gi 564371221 304 AlqcwPQESDAPcllAEELEEPDAP 328
Cdd:PTZ00449 782 I----HAETGEP---DEAMKRPDSP 799
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
766-989 |
2.31e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEqeFRAQEKVLEETRKqkELLCKMEREKSiEIENLQARL 845
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE--LREEAQELREKRD--ELNEKVKELKE-ERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEEL-----TQRLSEEQENK--------RKMGDKLSHERHQFQRDK 912
Cdd:COG1340 88 NELREELDELRK----ELAELNKAGGSIDKLRKEIERLewrqqTEVLSPEEEKElvekikelEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564371221 913 EATQElIEDLRKQLEHLqllRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 989
Cdd:COG1340 164 ELRAE-LKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
766-982 |
2.99e-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: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVleetrkqkellckmEREKSIEIENLQARL 845
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE--------------DLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSElrsctpclkanierleeekQKMLDEIEELTQRLSEEQENKRkmgDKLSHERHQFQRD-KEATQEL---IED 921
Cdd:COG4913 756 AAALGDAVE-------------------RELRENLEERIDALRARLNRAE---EELERAMRAFNREwPAETADLdadLES 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 922 LRKQLEHLQLLRlemeqrrgrssSLGLQEYNSRARESELEQE-------VRRLKQDNRNLKEQNDELN 982
Cdd:COG4913 814 LPEYLALLDRLE-----------EDGLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLN 870
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
814-969 |
3.30e-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: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 814 EKVLEETRKqkELLCKMEREKSIEIENLQARLQQLDEENSELRSctpclkaNIERLEEEKQKMLDEIEELTQRLSEEQEN 893
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 894 KRKMGDKlshERHQFQRDKEAT--QELIEDLRKQLEhlqllRLEMEQRrgrssslglqeynsraresELEQEVRRLKQ 969
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELE-----EERERIE-------------------ELKRKLERLKE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
793-969 |
3.37e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 793 QLVHRANALEEQLKEQefRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRsctpclkaniERLEEE 872
Cdd:PRK04863 517 QLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR----------ERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 873 KQKmLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQrrgrssslglqeyn 952
Cdd:PRK04863 585 RQQ-LEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-------------- 649
|
170
....*....|....*..
gi 564371221 953 SRARESELEQEVRRLKQ 969
Cdd:PRK04863 650 LAARKQALDEEIERLSQ 666
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
766-983 |
3.69e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHgRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARL 845
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRS----CTPC---------------LKANIERLEEEKQK------------------------------M 876
Cdd:PRK03918 422 KELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEieekerklrkelrelekvlkkeseliklkeL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 877 LDEIEELTQRLS-----------EEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSS 945
Cdd:PRK03918 502 AEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564371221 946 LG---LQEYNSRARE---------------SELEQEVRRLKQDNRNLKEQNDELNG 983
Cdd:PRK03918 582 LGfesVEELEERLKElepfyneylelkdaeKELEREEKELKKLEEELDKAFEELAE 637
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
793-957 |
4.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 793 QLVHRANALEEQLKEQEFRAQEKVL--------EETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPC--L 862
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 863 KANIERLEEEKQKMLDEIEELTQRLSEEQENKRKM--GDKLSHERHQFQRDKEATQELIEDLRKqlehLQLLRLEMEQRR 940
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAR 506
|
170
....*....|....*..
gi 564371221 941 GRSSSLGLQEYNSRARE 957
Cdd:COG4717 507 EEYREERLPPVLERASE 523
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
789-985 |
5.28e-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: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 789 QENLQLVHRANaleEQLKEQEFRAQEKVLEETRKQKELLCKMereksieienlqaRLQQLDEenselrsctpclkanIER 868
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 869 LEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQR--------DKEATQELiEDLRKQLEHL----QLLRLEM 936
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSqlpvlsdaEREMKKEL-ETINEQLKHLanaiKQAKKKM 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564371221 937 EQRRgRSSSLGLQEYNSRARESELEQEvRRLKQdnrNLKEQNDELNGQI 985
Cdd:pfam10168 659 NYQR-YQIAKSQSIRKKSSLSLSEKQR-KTIKE---ILKQLGSEIDELI 702
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
766-1038 |
6.97e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQhgrLRQENLQLV------HRA-NALEEQLKE-QEFRAQekvLEETRKQKELLCKMEREKsie 837
Cdd:PRK11281 126 LESRLAQTLDQLQNAQND---LAEYNSQLVslqtqpERAqAALYANSQRlQQIRNL---LKGGKVGGKALRPSQRVL--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 ienLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEE----QE---NKRKmgdKLSHERHQFQR 910
Cdd:PRK11281 197 ---LQAEQALLNAQNDLQRK----SLEGNTQLQDLLQKQRDYLTARIQRLEHQlqllQEainSKRL---TLSEKTVQEAQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 911 DKEATQELIED--LRKQLEHlqllRLEMEQRRGRSSslglQEYNSRARES-ELEQEVRRLKQDNRNLKEQNDELNGQIIt 987
Cdd:PRK11281 267 SQDEAARIQANplVAQELEI----NLQLSQRLLKAT----EKLNTLTQQNlRVKNWLDRLTQSERNIKEQISVLKGSLL- 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564371221 988 LS-I--QGAKSLFSTSFSESLAAEISSVsRDELMEAIQKQEEInFRLQDYIDRI 1038
Cdd:PRK11281 338 LSrIlyQQQQALPSADLIEGLADRIADL-RLEQFEINQQRDAL-FQPDAYIDKL 389
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
766-977 |
7.27e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQ------ENLQLVH----------------RANALEEQLKEQE-----FRAQEKVLE 818
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSqleqakEGLSALNrllprlnlladetladRVEEIREQLDEAEeakrfVQQHGNALA 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 819 ETRKQKELLckmeREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLE----EEKQKMLDEIEELTQRLSEEQENK 894
Cdd:PRK04863 922 QLEPIVSVL----QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 895 RKMGDKLSHERHQFQ-RDKEATQELI---------EDLRKQLEH-LQLLRL----EMEQR-RGRSSSLGLQEYNSRARES 958
Cdd:PRK04863 998 EQERTRAREQLRQAQaQLAQYNQVLAslkssydakRQMLQELKQeLQDLGVpadsGAEERaRARRDELHARLSANRSRRN 1077
|
250
....*....|....*....
gi 564371221 959 ELEQEVRRLKQDNRNLKEQ 977
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKK 1096
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
768-980 |
8.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 768 RRVSELEKDSAAAGEQHGRLRQ--ENLQLVHRANALEEQLKEQEFRAQE--------KVLEETRKQKELLCKMEREKSIE 837
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEeakkadeaKKAEEKKKADELKKAEELKKAEE 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 IENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKmGDKLSHERHQFQRDKEATQE 917
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564371221 918 LIEDLRKQLEhlqlLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDE 980
Cdd:PTZ00121 1642 EAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
801-985 |
9.82e-05 |
|
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: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 801 LEEQLK--EQEFRAQEKVLEETRKQKELLCKMEReksieieNLQARLQQLDEENSELRSctpclkaNIERLEEEKQKMLD 878
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 879 EIEELTQRLSEEQENkRKMGDKLSHERHQFQRDKEATQEliedlrkqlehlQLLRLEMEQRRGRSSSLglqeynsRARES 958
Cdd:pfam09726 466 TVQQLEKRLKAEQEA-RASAEKQLAEEKKRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 564371221 959 ELEQEVRRLKQDNRNLKEQNDELNGQI 985
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
766-980 |
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 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCK---MEREKSiEIENLQ 842
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkeLEKEEE-REEDER 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 843 ARLQQLDEENSELRsctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDL 922
Cdd:pfam13868 157 ILEYLKEKAEREEE-----REAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 923 RKQLEHLQLLRLEMEQRRGRssslgLQEYnsRARESELEQEVRRLKQDNRNLKEQNDE 980
Cdd:pfam13868 232 RQRQELQQAREEQIELKERR-----LAEE--AEREEEEFERMLRKQAEDEEIEQEEAE 282
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
762-968 |
1.26e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 762 KVIFLERRVSELEKDSAAAGEQHGRLRQenlqLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMER--EKSIEIE 839
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 840 NLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQ-ENKRKMGDKLSHE----RHQFQRDKEA 914
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRElaglRAELEELEKR 688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564371221 915 TQEL---IEDLRKQLEhlqllrlEMEQRRGRSSSLGlqeyNSRARESELEQEVRRLK 968
Cdd:PRK03918 689 REEIkktLEKLKEELE-------EREKAKKELEKLE----KALERVEELREKVKKYK 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
741-1043 |
1.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 741 MEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEQHGRLRQE--NLQLVHRANALEEQLKEQE--------- 809
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARlllliaaal 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 810 -------------------------------FRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSC 858
Cdd:COG4717 259 lallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 859 TPCLKANIERLEEEKQKMLDEIEELtQRLSEEQENKRKMGDKLSHERHQFqrdkEATQELIEDLRKQLEHLQLLRLEMEQ 938
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEEL----RAALEQAEEYQELKEELEELEEQLEE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 939 RRGrssslGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSiqgakslfstsfseslaAEISSVSRD-EL 1017
Cdd:COG4717 414 LLG-----ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-----------------AELEQLEEDgEL 471
|
330 340
....*....|....*....|....*.
gi 564371221 1018 MEAIQKQEEINFRLQDYIDRIIVAIL 1043
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKL 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
768-981 |
1.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 768 RRVSELEKDSAAAGEQHGRLRQENLQLvhRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQArlqq 847
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK---- 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 848 lDEENSELRsctpclKANIERLEEEKQKmldEIEELTQRlseeQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLE 927
Cdd:PTZ00121 1655 -AEEENKIK------AAEEAKKAEEDKK---KAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564371221 928 hlqlLRLEMEQRRGRSSSLGLQEYNSRARESEL---EQEVRRLKQDNRNLKEQNDEL 981
Cdd:PTZ00121 1721 ----LKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
771-981 |
1.67e-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: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 771 SELEkdsaAAGEQHGRLRQENLQLVHrANALEEQLKEQEFRAQEKVLE-ETRKQKELLCKMEREKSIEIENLQARLQQLD 849
Cdd:pfam12128 322 SELE----ALEDQHGAFLDADIETAA-ADQEQLPSWQSELENLEERLKaLTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 850 EENSELRSCTPCLKANIER-LEEEKQKMLDEIEELTQRLSEEQEnkrKMGDKLSHERHQfQRDKEATQELIEDLRKQLEH 928
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEFNEEEY---RLKSRLGELKLR-LNQATATPELLLQLENFDER 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564371221 929 LQLLRLEMEQRRGRSSSLGLQEYNSRAREselEQEVRRLKQDNRNLKEQNDEL 981
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRR---DQASEALRQASRRLEERQSAL 522
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
837-945 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRlseeqenkrkmgdklsherhqfQRDKEATQ 916
Cdd:COG3166 46 QIAQQQARNAALQQEIAKLDK----QIAEIKELKKQKAELLARLQVIEQL----------------------QQSRPPWV 99
|
90 100 110
....*....|....*....|....*....|....
gi 564371221 917 ELIEDLRKQL-EHLQLLRLEMEQRR----GRSSS 945
Cdd:COG3166 100 HLLDELARLLpEGVWLTSLSQQGGTltltGVAQS 133
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
758-1026 |
1.82e-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: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 758 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLkeQEFRAQEKVLEETRKQKELLCKMEREKSIE 837
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT--SAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 IENlqaRLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIE---ELTQRLSEEQENKRKMGDKLSH-ERHQFQRD-- 911
Cdd:TIGR00618 447 ITC---TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHpNPARQDIDnp 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 912 -------------KEATQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLGLQEYNSRARES-----ELEQEVRRLKQDN 971
Cdd:TIGR00618 524 gpltrrmqrgeqtYAQLETSEEDVYHQLTSErkQRASLKEQMQEIQQSFSILTQCDNRSKEDipnlqNITVRLQDLTEKL 603
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 972 RNLKEQNDELN-GQIITLSIQGAK---SLFSTSFSESLAAEISSVSRDELMEAIQKQEE 1026
Cdd:TIGR00618 604 SEAEDMLACEQhALLRKLQPEQDLqdvRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
807-985 |
2.10e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 807 EQEFRAQEKVLEETRKQKELLCKmereksiEIENLQARLQQLDEENSELrsctpclKANIERLEEEKQKMLDEIEELTQR 886
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 887 LSEEQEnkrKMGDKLSHerhqFQRDKEATQEL--------IEDLrkqLEHLQLLRLEMEQRRGRssslgLQEYNS----- 953
Cdd:COG3883 81 IEERRE---ELGERARA----LYRSGGSVSYLdvllgsesFSDF---LDRLSALSKIADADADL-----LEELKAdkael 145
|
170 180 190
....*....|....*....|....*....|..
gi 564371221 954 RARESELEQEVRRLKQDNRNLKEQNDELNGQI 985
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
766-1031 |
2.15e-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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALE--------------------EQLKEQEFRaqekvLEETRKQKE 825
Cdd:pfam05622 12 LAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLEsgddsgtpggkkylllqkqlEQLQEENFR-----LETARDDYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 826 LLCkMEREKsiEIENLQARLQQLDEENSELRSctpcLKANIERLEE--EKQKMLD-EIEELTQRLSEEQENKRKMgdKLS 902
Cdd:pfam05622 87 IKC-EELEK--EVLELQHRNEELTSLAEEAQA----LKDEMDILREssDKVKKLEaTVETYKKKLEDLGDLRRQV--KLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 903 HERHQFQRdkEATQELIEDLRK------QLE----HLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNR 972
Cdd:pfam05622 158 EERNAEYM--QRTLQLEEELKKanalrgQLEtykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564371221 973 NLKEQNDEL---NGQIITLSIQGAKSLFSTSFSESLAAEISSVsrdELMEAIQKQEEINFRL 1031
Cdd:pfam05622 236 TLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA---EIREKLIRLQHENKML 294
|
|
| BCAS2 |
pfam05700 |
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ... |
776-888 |
2.29e-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: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 776 DSAAAGEQHGRLRQENLQLV--HRANA--LEEQLKEQEFRAQEKVLEETRKQKELLckmEREKSIEIENLQARLQQLDEE 851
Cdd:pfam05700 98 DNAYAQLEHQRIRIENLELLqkYGANAwrLHNYQLEAILRRLEKELAETKEAIEEV---NRQRKNAQTAAGGELRSLEEK 174
|
90 100 110
....*....|....*....|....*....|....*..
gi 564371221 852 NSELRSctpclkANIErLEEEKQKMLDEIEELTQRLS 888
Cdd:pfam05700 175 WKELVS------KNLE-IEAACEALEAEILELKRQAA 204
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
774-1032 |
2.39e-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: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 774 EKDS--AAAGEQHGRLRQENLQLVHRAnaleeQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQA-------- 843
Cdd:pfam05557 94 EKESqlADAREVISCLKNELSELRRQI-----QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKqqsslaea 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 844 --RLQQLDEENSELRSCTPCLKANIERLEE--EKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELI 919
Cdd:pfam05557 169 eqRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 920 eDLRKQLEHLQlLRLEMEQRRGRSSSLGLQeynsraRESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGakslfst 999
Cdd:pfam05557 249 -TLELEKEKLE-QELQSWVKLAQDTGLNLR------SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
250 260 270
....*....|....*....|....*....|....*
gi 564371221 1000 sfsESLAAEISSVSRD--ELMEAIQKQEEINFRLQ 1032
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 ... |
766-985 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQE--------------NLQLVHRANALEEQLKEqefrAQEKVLEETRKQKEL---LC 828
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSElesvssllneaegkNIKLSKDVSSLESQLQD----TQELLQEETRQKLNLstrLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 829 KMEREKSIEIE----------NLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMg 898
Cdd:pfam01576 493 QLEDERNSLQEqleeeeeakrNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL- 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 899 dklsherhqfQRDKEATQELIEDLRKQLEHLQLL--RLEMEQRR-------GRSSSLGLQEYNSRARESELEQEVRRLK- 968
Cdd:pfam01576 572 ----------EKTKNRLQQELDDLLVDLDHQRQLvsNLEKKQKKfdqmlaeEKAISARYAEERDRAEAEAREKETRALSl 641
|
250 260
....*....|....*....|.
gi 564371221 969 ----QDNRNLKEQNDELNGQI 985
Cdd:pfam01576 642 aralEEALEAKEELERTNKQL 662
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
782-938 |
2.70e-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: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 782 EQHGRLRQENLQLVHRANALEEQLKEQEFRA---QEKVLEETRKQKELLCkmeREKSIEIENLQARLQQLDEENSELRSC 858
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAkklEEKAQAALTKGNEELA---REALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 859 TPCLKANIERL-------EEEKQKMLdeIEELTQRlSEEQENKRKMGDKLSHERHQFQR--DKEATQELIEDLRKQLEHL 929
Cdd:pfam04012 113 VEQLRKQLAALetkiqqlKAKKNLLK--ARLKAAK-AQEAVQTSLGSLSTSSATDSFERieEKIEEREARADAAAELASA 189
|
....*....
gi 564371221 930 QLLRLEMEQ 938
Cdd:pfam04012 190 VDLDAKLEQ 198
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
769-1026 |
2.86e-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: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 769 RVSELEKDSAAAGEQHGRLRQ---ENLQLVHRANALEEQLKEQEfRAQEKV----LEETRKQKELlckMEREK------- 834
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNEnieNKLLLKEEVEDLKRKLEREE-KYREEAatleLEKEKLEQEL---QSWVKlaqdtgl 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 835 --------SIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDK---LSH 903
Cdd:pfam05557 274 nlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllLTK 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 904 ER---------------------HQFQRDKEAT------QELIEDLRKQLEHLQ-----------LLRLEMEQRRGRSSs 945
Cdd:pfam05557 354 ERdgyrailesydkeltmsnyspQLLERIEEAEdmtqkmQAHNEEMEAQLSVAEeelggykqqaqTLERELQALRQQES- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 946 lglQEYNSRARE--SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTS---FSESLAAEISSVSRDElMEA 1020
Cdd:pfam05557 433 ---LADPSYSKEevDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRKNQ-LEK 508
|
....*.
gi 564371221 1021 IQKQEE 1026
Cdd:pfam05557 509 LQAEIE 514
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
804-985 |
3.36e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 804 QLK--EQEFRAQEKVLEETRKQK-ELLCKM-EREKSI-----EIENLQARLQQLDEENSELrsctpclKANIERLEEEK- 873
Cdd:PRK11637 48 QLKsiQQDIAAKEKSVRQQQQQRaSLLAQLkKQEEAIsqasrKLRETQNTLNQLNKQIDEL-------NASIAKLEQQQa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 874 --QKMLDEIEELTQRLSEEQ---------ENKRKmgdklshERHQ--FQRDKEATQELIEDLRKQLEHLQLLRLEMEQRR 940
Cdd:PRK11637 121 aqERLLAAQLDAAFRQGEHTglqlilsgeESQRG-------ERILayFGYLNQARQETIAELKQTREELAAQKAELEEKQ 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564371221 941 GRSSS-LGLQ-------EYNSRARESELEQEVRRLKQDNRNLKE--QND-ELNGQI 985
Cdd:PRK11637 194 SQQKTlLYEQqaqqqklEQARNERKKTLTGLESSLQKDQQQLSElrANEsRLRDSI 249
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
832-1046 |
3.66e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 44.68 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 832 REKSIEIENLQARLQQLDEENSELRSCTPCLKANieRLEEEKQKMLDEIEELTQRLSEEQENKRKMgDKLSHERHQFQ-- 909
Cdd:COG5244 82 KGGLVCESKGMDKDGEIKQENHEDRIHFEESKIR--RLEETIEALKSTEKEEIVELRRENEELDKI-NLSLRERISSEep 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 910 -RDKEATQ-------ELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEynsrARESELEQEVRRLKQDNRNLKEQNDEL 981
Cdd:COG5244 159 eLNKDGSKlsydelkEFVEESRVQVYDMVELVSDISETLNRNGSIQRSS----VRECERSNIHDVLFLVNGILDGVIDEL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 982 NGQIitlsiqgakslfstsfsESLAAEISSvsrdeLMEAIQKQEEINFRLQDYIDRIIVAILETN 1046
Cdd:COG5244 235 NGEL-----------------ERLRRQLVS-----LMSSHGIEVEENSRLKATLEKFQSLELKVN 277
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
788-994 |
3.69e-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: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 788 RQENLQLV-HRANALEEQLKEQEFRAQEKVLEETRKQKELlcKMEREKSIEIENLQARL----QQLDEENSELRSCTPCL 862
Cdd:pfam01576 10 KEEELQKVkERQQKAESELKELEKKHQQLCEEKNALQEQL--QAETELCAEAEEMRARLaarkQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 863 KANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMG-DKLSHE----------------RHQFQRDKEATQELIEDLRKQ 925
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlEKVTTEakikkleedillledqNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 926 L-------EHLQLLRL-------EMEQRRGRssslglqEYNSRareSELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:pfam01576 168 LaeeeekaKSLSKLKNkheamisDLEERLKK-------EEKGR---QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQ 237
|
...
gi 564371221 992 GAK 994
Cdd:pfam01576 238 LAK 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
689-977 |
5.73e-04 |
|
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: 43.94 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 689 VVMVIGSEEHFEDYGEGSEAELSPETLCNGEL--DCEDPAFLTPRYLHQSGTLTMEAledpppepvECPEEDIADKVIFL 766
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtaHCDKLLLENKELTQEASDMTLEL---------KKHQEDIINCKKQE 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSI--EIENLQAR 844
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLkkQIENKNKN 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 845 LQQLDEENSELRSCTPC-------LKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQE 917
Cdd:pfam05483 610 IEELHQENKALKKKGSAenkqlnaYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 918 LIEDLRKQLEH--LQLLRLeMEQRRG--------RSSSLGLqeYNSRARESE-----LEQEVRRLKQDNRNLKEQ 977
Cdd:pfam05483 690 LQKEIDKRCQHkiAEMVAL-MEKHKHqydkiieeRDSELGL--YKNKEQEQSsakaaLEIELSNIKAELLSLKKQ 761
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
801-923 |
6.49e-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: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 801 LEEQLKEQEFRAQ-----EKVLEETRKQKEllckMEREKSIEIENLQARLQQLDEENSEL-----RSCTPCLKANIERLE 870
Cdd:pfam02841 178 LQEFLQSKEAVEEailqtDQALTAKEKAIE----AERAKAEAAEAEQELLREKQKEEEQMmeaqeRSYQEHVKQLIEKME 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564371221 871 EEKQKMLDEIEELTQRLSEEQENKRKMGdklsherhqFQRDKEATQELIEDLR 923
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 ... |
766-892 |
7.94e-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: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANAleeqlkeqefrAQEKVLEETRKQKELLCKMEREKSiEIENLQARL 845
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE-----------AQQNYERELVLHAEDIKALQALRE-ELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 564371221 846 QQLDEENSELRSCtpcLKANIERLEEEKQKMLDEIEELTQRLSEEQE 892
Cdd:pfam07926 74 AELKAEAESAKAE---LEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
767-954 |
7.99e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQE-KVLEETRKQKELLCKMEREKSIEIENLQARL 845
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 846 QQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQrlseEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQ 925
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK----DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170 180
....*....|....*....|....*....
gi 564371221 926 LEHLQLLRLEMEQRRGRSSSLGLQEYNSR 954
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
829-935 |
8.24e-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: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 829 KMERE-KSIEIENLQARLQQLDEENSEL-RSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERH 906
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 564371221 907 QFQRDKEATQELIEDLRKQLEHLQLLRLE 935
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
764-940 |
8.30e-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: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 764 IFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKM---------EREK 834
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKdeleskeekEKEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 835 SIEIENLQARLQQLDEENSELRSCTpCLKANIERLEEEKQKML------DEIEELTQRLSEEQENKR------KMGDKLS 902
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERI-KEEAEILLKYEEEPEELlleeadEKEKEENNKEEEEERNKRlllakeELGKVNL 977
|
170 180 190
....*....|....*....|....*....|....*....
gi 564371221 903 HERHQFQRDKEA-TQELIEDLRKQLEHLQLLRLEMEQRR 940
Cdd:pfam02463 978 MAIEEFEEKEERyNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
780-920 |
8.34e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 780 AGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCT 859
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEERE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 860 PCLKANIERLEEEKQKMLDEIEELTQrLSEEQENK---RKMGDKLSHERHQF-QRDKEATQELIE 920
Cdd:PRK12705 112 KALSARELELEELEKQLDNELYRVAG-LTPEQARKlllKLLDAELEEEKAQRvKKIEEEADLEAE 175
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
516-545 |
9.27e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 37.54 E-value: 9.27e-04
10 20 30
....*....|....*....|....*....|
gi 564371221 516 RLRTVFDALDRDGDGFVRIEDFIQFATVYG 545
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
766-1036 |
9.62e-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: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQEnlqlVHRANALEEQL---KEQEFRAQEKVLEETRKQKELLCkmereksiEIENLQ 842
Cdd:pfam05622 150 LRRQVKLLEERNAEYMQRTLQLEEE----LKKANALRGQLetyKRQVQELHGKLSEESKKADKLEF--------EYKKLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 843 ARLQQLDEENselrsctpclkaniERLEEEKQKMLDEIEELtqRLSEEQENKRKMGDKLsHERHQFQRDKEATQELIEDL 922
Cdd:pfam05622 218 EKLEALQKEK--------------ERLIIERDTLRETNEEL--RCAQLQQAELSQADAL-LSPSSDPGDNLAAEIMPAEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 923 RKQLEHLQL----LRL-EMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGqiiTLSIQGAKSLF 997
Cdd:pfam05622 281 REKLIRLQHenkmLRLgQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQK---ALQEQGSKAED 357
|
250 260 270
....*....|....*....|....*....|....*....
gi 564371221 998 STSFSESLAAEIssvsrDELMEAiqkQEEINfRLQDYID 1036
Cdd:pfam05622 358 SSLLKQKLEEHL-----EKLHEA---QSELQ-KKKEQIE 387
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1038 |
9.89e-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: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 864 ANIERLEEEKQKMLDEIEELTQRLSEEQ---ENKRKMGDKLSHERHQFQRDKEATQELIEdlRKQLEHLQLLRLEMEQRR 940
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKRE--YEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 941 GRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLfstsfsESLAAEISSVsRDELMEA 1020
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------GELEAEIASL-ERSIAEK 313
|
170
....*....|....*...
gi 564371221 1021 IQKQEEINFRLQDYIDRI 1038
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEI 331
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
758-1025 |
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: 43.11 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 758 DIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKqkellCKMEREKSIE 837
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK-----LIQDQQEQIQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 I----------------ENLQARLQ---QLDEENSELRSCTPCLKANIER---LEEEKQKMLDEIEELTQRLSEE----- 890
Cdd:TIGR00606 861 HlksktnelkseklqigTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELISSKETSnkkaq 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 891 ---QENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGR-SSSLGLQEYN---SRARESELEQE 963
Cdd:TIGR00606 941 dkvNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKiNEDMRLMRQDidtQKIQERWLQDN 1020
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371221 964 VRRLKQDN--RNLKEQNDELNGQIITLSIQGAKSLFstsfsESLAAEISSVSRDELMEAIQKQE 1025
Cdd:TIGR00606 1021 LTLRKRENelKEVEEELKQHLKEMGQMQVLQMKQEH-----QKLEENIDLIKRNHVLALGRQKG 1079
|
|
| SynN |
smart00503 |
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
837-939 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM---LDEIEELTQRLSE--EQENKRKMGDKLSHERHQFQRd 911
Cdd:smart00503 9 KVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLerlIDDIKRLAKEIRAklKELEKENLENRASGSASDRTR- 87
|
90 100
....*....|....*....|....*...
gi 564371221 912 KEATQELIEDLRKQLEHLQLLRLEMEQR 939
Cdd:smart00503 88 KAQTEKLRKKFKEVMNEFQRLQRKYRER 115
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
29-516 |
1.04e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 29 PDAPRGWSDEPEEHAQLQRWPEGPNAPICWPEEVEEPHAPRRwAEEPSASRCLSQEPYESCHLA----KELEEPDAPRCS 104
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQrprrRAARPTVGSLTS 2697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 105 SQEPDAPchlakdlEETDSPRCWPLEPDAPCHLAKEWEEPDVPRCWPQEPDAPCHLAKYLEEPDAPLCWPQEPDAfcyll 184
Cdd:PHA03247 2698 LADPPPP-------PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----- 2765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 185 keVEEPDVPRCRPQEP------DAPCHLAEELEDLDAPRCWTQEPNESCNLAKELDEPDTPRCLSQEPDAPCLLAKEWEE 258
Cdd:PHA03247 2766 --PPAPAPPAAPAAGPprrltrPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 259 SDAPSCWPQEPDVGPqepdvGCHLAKEREESDAPCLLTEELKEPDALQCWPQESDAPCLLA---EELEEPDAPHCCSQEV 335
Cdd:PHA03247 2844 GPPPPSLPLGGSVAP-----GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAlppDQPERPPQPQAPPPPQ 2918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 336 DTECLSAKESEEPDASHlwPGEPDAPclLVKEPEEADAPHCWPEEPeepdalnAPCFWANEPDEPDAPRCWSEEPQVLCL 415
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPP--PPRPQPP--LAPTTDPAGAGEPSGAVP-------QPWLGALVPGRVAVPRFRVPQPAPSRE 2987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 416 WPEEQNTTQCWQEEPDASCFWS-----EDREEPKVSCLQFKEPekpkvacswPEELEDCCPTRGLPLEPLLAEGELLQAC 490
Cdd:PHA03247 2988 APASSTPPLTGHSLSRVSSWASslalhEETDPPPVSLKQTLWP---------PDDTEDSDADSLFDSDSERSDLEALDPL 3058
|
490 500
....*....|....*....|....*.
gi 564371221 491 PGPPPDPglaLSLPSEPGTAqEEGAR 516
Cdd:PHA03247 3059 PPEPHDP---FAHEPDPATP-EAGAR 3080
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
807-1037 |
1.10e-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: 43.19 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 807 EQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEEnselrsctpclkanieRLEEEKQKMLDEIEElTQR 886
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQE----------------RLRQEKEEKAREVER-RRK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 887 LSEEQENKRKMGDKLS-----HERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRS---SSLGLQEYNSRARES 958
Cdd:pfam17380 318 LEEAEKARQAEMDRQAaiyaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRElerLQMERQQKNERVRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 959 ELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDEL-----MEAIQKQEEINFRLQD 1033
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQerqqqVERLRQQEEERKRKKL 477
|
....
gi 564371221 1034 YIDR 1037
Cdd:pfam17380 478 ELEK 481
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
761-937 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIFLERRVSELEKDSaaagEQHGR-LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIE 839
Cdd:COG5185 406 EILATLEDTLKAADRQI----EELQRqIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 840 NLQARLQQLdeeNSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEqenKRKMGDKLSHERHQFQRDKEATQELI 919
Cdd:COG5185 482 DLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF---MRARGYAHILALENLIPASELIQASN 555
|
170
....*....|....*...
gi 564371221 920 EDLRKQLEHLQLLRLEME 937
Cdd:COG5185 556 AKTDGQAANLRTAVIDEL 573
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
834-1028 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 834 KSIEIENLQARLQQLDEENSELRSCTPCLK---------ANIERLE--------EEKQKMLDEIEELTQRLSEEQ----- 891
Cdd:pfam10174 301 KESELLALQTKLETLTNQNSDCKQHIEVLKesltakeqrAAILQTEvdalrlrlEEKESFLNKKTKQLQDLTEEKstlag 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 892 --ENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRS-SSLG---------------LQEYNS 953
Cdd:pfam10174 381 eiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdTALTtleealsekeriierLKEQRE 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 954 RARESELEqEVRRLKQDNRNLKEQNDELngqiitlsiQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEIN 1028
Cdd:pfam10174 461 REDRERLE-ELESLKKENKDLKEKVSAL---------QPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
872-981 |
1.25e-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: 41.43 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 872 EKQKML-DEIEELTQRlseEQENKRKMgDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEqrrgrssslglqe 950
Cdd:pfam13851 26 ELIKSLkEEIAELKKK---EERNEKLM-SEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLK------------- 88
|
90 100 110
....*....|....*....|....*....|.
gi 564371221 951 yNSRARESELEQEVRRLKQDNRNLKEQNDEL 981
Cdd:pfam13851 89 -NLKARLKVLEKELKDLKWEHEVLEQRFEKV 118
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
792-890 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 792 LQLVHRANALEEQLKEqefrAQEKvLEETRKQKELLCKmereksiEIENLQARLQQLDEENSELRSCTPCLKANIERLEE 871
Cdd:COG4026 124 LQNIPEYNELREELLE----LKEK-IDEIAKEKEKLTK-------ENEELESELEELREEYKKLREENSILEEEFDNIKS 191
|
90
....*....|....*....
gi 564371221 872 EKQKMLDEIEELTQRLSEE 890
Cdd:COG4026 192 EYSDLKSRFEELLKKRLLE 210
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
512-575 |
1.64e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371221 512 EEGARLRTVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDltqyLDPSGLGVISFEDFYQGIVA 575
Cdd:COG5126 2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSE----ADTDGDGRISREEFVAGMES 61
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
799-1034 |
1.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 799 NALEEQLKEQ--EFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKM 876
Cdd:PRK01156 186 DYLEEKLKSSnlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 877 ---LDEIEELTQRLSE-EQENKRKMGDKLSHERHQ------FQRDKEATQELIEDLR----------KQLEHLQLLRLEM 936
Cdd:PRK01156 262 esdLSMELEKNNYYKElEERHMKIINDPVYKNRNYindyfkYKNDIENKKQILSNIDaeinkyhaiiKKLSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 937 EQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELngqiitlsiqgakslfstsfsESLAAEISSVSRDE 1016
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI---------------------ERMSAFISEILKIQ 400
|
250 260
....*....|....*....|.
gi 564371221 1017 LM--EAIQKQ-EEINFRLQDY 1034
Cdd:PRK01156 401 EIdpDAIKKElNEINVKLQDI 421
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
761-988 |
1.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 761 DKVIFLERRVSELEKDSAAAGEQHGRLRQ------ENLQLVHRANALEEQLKEQEFRAQEK--VLEETRKQKELL----- 827
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKreRAEELRERAAELeaeae 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 828 -------CKMER--EKSIEIENLQARLQQLDEENSELRSCTPCLKA---NIERLEE--EKQKMLDEIEELT-QRLSEEQE 892
Cdd:PRK02224 555 ekreaaaEAEEEaeEAREEVAELNSKLAELKERIESLERIRTLLAAiadAEDEIERlrEKREALAELNDERrERLAEKRE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 893 NKRKMGDKLSHER-HQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSlGLQEYNS-RARESELEQEVRRLkqd 970
Cdd:PRK02224 635 RKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEELEElRERREALENRVEAL--- 710
|
250
....*....|....*...
gi 564371221 971 nRNLKEQNDELNGQIITL 988
Cdd:PRK02224 711 -EALYDEAEELESMYGDL 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
766-963 |
1.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEfraqekvlEETRKQKELLCKMERE------------ 833
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARAlyrsggsvsyld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 834 -----KSIE--IENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMgdklsherh 906
Cdd:COG3883 107 vllgsESFSdfLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAELEAAKAEL--------- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 907 qfQRDKEATQELIEDLRKQLEHL--QLLRLEMEQRRGRSSSLGLQEYNSRARESELEQE 963
Cdd:COG3883 174 --EAQQAEQEALLAQLSAEEAAAeaQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
814-924 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 814 EKVLEETRKQKELLCKMEREKSI---EIENLQARLQQLDEEnselrsctpcLKANIERL-EEEKQKMLDEIEELTQRLSE 889
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKrqaELQKLEKELQALQEK----------LQKEAATLsEEERQKKERELQKKQQELQR 101
|
90 100 110
....*....|....*....|....*....|....*
gi 564371221 890 EQENKRKMgdklsherhQFQRDKEATQELIEDLRK 924
Cdd:COG2825 102 KQQEAQQD---------LQKRQQELLQPILEKIQK 127
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
780-1030 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 780 AGEQ-HGRLRQENLQLVHRANALEEQ---LKEQEFRAQEKVLEETRKQKELLCKMEReksieIENLQARLQQLDEENSEL 855
Cdd:TIGR00618 532 RGEQtYAQLETSEEDVYHQLTSERKQrasLKEQMQEIQQSFSILTQCDNRSKEDIPN-----LQNITVRLQDLTEKLSEA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 856 RSCTPCLKaniERLEEEKQKMLDEieeltQRLSEEQENKRKMGDKLSHERHQFQrdKEATQEliedlrKQLEHLQLLRlE 935
Cdd:TIGR00618 607 EDMLACEQ---HALLRKLQPEQDL-----QDVRLHLQQCSQELALKLTALHALQ--LTLTQE------RVREHALSIR-V 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 936 MEQRRGRSSSLGLQEYNSRARE-----SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKslfsTSFSESLAAEIS 1010
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQltywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD----LAAREDALNQSL 745
|
250 260
....*....|....*....|
gi 564371221 1011 SVSRDELMEAIQKQEEINFR 1030
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFN 765
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
782-979 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 782 EQHGRLRQENLQLVhraNALEEQLKEQEFR---AQEKVLEetrkqkellckmereksieienlqarLQQLDEENSELRSC 858
Cdd:pfam15742 96 ELEVLKQAQSIKSQ---NSLQEKLAQEKSRvadAEEKILE--------------------------LQQKLEHAHKVCLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 859 TPCLKANiERLEEEKQKMLDEIEELTQRLSEEQEnKRKMGDKLSHERHQ---FQRDKEATQELI---EDLRKQLEHLQLL 932
Cdd:pfam15742 147 DTCILEK-KQLEERIKEASENEAKLKQQYQEEQQ-KRKLLDQNVNELQQqvrSLQDKEAQLEMTnsqQQLRIQQQEAQLK 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564371221 933 RLEMEQRRG---RSSSLGLQEynsraRESELEQEVRRLKQDNRNLKEQND 979
Cdd:pfam15742 225 QLENEKRKSdehLKSNQELSE-----KLSSLQQEKEALQEELQQVLKQLD 269
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
772-991 |
2.74e-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: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 772 ELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFraQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQ---- 847
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL--ALKLTALHALQLTLTQERVREHALSIRVLPKELLAsrql 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 848 -LDEENSELRSCTPC--------------------------------------LKANIERLEEEKQKMLDEIEELTQRLS 888
Cdd:TIGR00618 681 aLQKMQSEKEQLTYWkemlaqcqtllrelethieeydrefneienassslgsdLAAREDALNQSLKELMHQARTVLKART 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 889 EEQENKR-------KMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEY----NSRARE 957
Cdd:TIGR00618 761 EAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEeqflSRLEEK 840
|
250 260 270
....*....|....*....|....*....|....
gi 564371221 958 SELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQ 991
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| Sec2p |
pfam06428 |
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ... |
867-945 |
2.91e-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: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 867 ERLEEEKQKMLDEIEELTQRLSEEQEnkrKMGDKLSHERHQFQRDKEATQE-------LIEDLRKQLEHLQLLRLEMEQR 939
Cdd:pfam06428 10 LEAEKEKKKLEKELEDLTASLFEEAN---KMVAAARREKHAVEIKNDQLKEqlkeketLLESLQEQLKELKQVMQKMEEE 86
|
....*.
gi 564371221 940 RGRSSS 945
Cdd:pfam06428 87 QDDQTN 92
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
767-969 |
3.17e-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: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEqLKEQEFRAQEKVLEETRKQ-------------KELLCKME-- 831
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-LELQLFPQAGTLLHFLRKEapdweqsigkvisPELLHRTDld 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 832 -------------------REKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELT-------- 884
Cdd:pfam12128 567 pevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASreetfart 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 885 ---------QRLSEEQENKRkmgDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYnSRA 955
Cdd:pfam12128 647 alknarldlRRLFDEKQSEK---DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY-WQV 722
|
250
....*....|....
gi 564371221 956 RESELEQEVRRLKQ 969
Cdd:pfam12128 723 VEGALDAQLALLKA 736
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
782-989 |
3.21e-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: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 782 EQHGR-LRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRK-----QKELLCKMEREKSIEIENLQARLQ--QLDEENS 853
Cdd:TIGR00606 308 HNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlqlQADRHQEHIRARDSLIQSLATRLEldGFERGPF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 854 ELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQ--- 930
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqle 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 931 -----LLRLEMEQRRGRsSSLGLQEYNS-----RARESELEQEVRRLKQDNRNLKEQNDELNGQIITLS 989
Cdd:TIGR00606 468 gssdrILELDQELRKAE-RELSKAEKNSltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT 535
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
760-978 |
3.33e-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: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 760 ADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLvhranALEEQLKEQEFR---AQEKVLEETRKQKELLCKMERE--- 833
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL-----QTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIHpnp 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 834 ---KSIEIENLQARLQQLDEENSELRS--------CTPCLKaNIERLEEEKQKMLDEIEELTQ---RLSEEQENKRKMGD 899
Cdd:TIGR00618 516 arqDIDNPGPLTRRMQRGEQTYAQLETseedvyhqLTSERK-QRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 900 KLsheRHQFQRDKEATQELIEDLRKQLEHLQ----LLRLEMEQRRgRSSSLGLQEYNSRARESELEQE-----VRRLKQD 970
Cdd:TIGR00618 595 RL---QDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRLHLQQ-CSQELALKLTALHALQLTLTQErvrehALSIRVL 670
|
....*...
gi 564371221 971 NRNLKEQN 978
Cdd:TIGR00618 671 PKELLASR 678
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
802-901 |
3.39e-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: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 802 EEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQL-DEENSELRSctpclKANIERLEEekqkmldEI 880
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRK-----DREISRLDR-------EI 474
|
90 100
....*....|....*....|.
gi 564371221 881 EELTQRLSEEQENKRKMGDKL 901
Cdd:COG2433 475 ERLERELEEERERIEELKRKL 495
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
866-939 |
4.21e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 41.08 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 866 IERLEEEKQ---KMLDEIEELTQRlseEQENKRKMGD---KLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQR 939
Cdd:PRK11091 77 VEQLEESRQrlsRLVAKLEEMRER---DLELNVQLKDniaQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQ 153
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
838-976 |
4.30e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 IENLQARLQQLDEENSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKmgdklsherhqfQRDKEATQE 917
Cdd:PRK00409 522 IASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ------------QAIKEAKKE 585
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 918 lIEDLRKQLEHLQllrlemeqrrgrssslglQEYNSRARESELEQEVRRLKQDNRNLKE 976
Cdd:PRK00409 586 -ADEIIKELRQLQ------------------KGGYASVKAHELIEARKRLNKANEKKEK 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
792-939 |
4.47e-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: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 792 LQLVH-RANALEEQLKE--QEFRAQEKVLEETRKQKEllckmerEKSIEIENLQARLQQLDEE----------------- 851
Cdd:COG1579 12 LQELDsELDRLEHRLKElpAELAELEDELAALEARLE-------AAKTELEDLEKEIKRLELEieevearikkyeeqlgn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 852 ---NSELRSctpcLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEH 928
Cdd:COG1579 85 vrnNKEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|.
gi 564371221 929 LQLLRLEMEQR 939
Cdd:COG1579 161 LEAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
837-1026 |
4.54e-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: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLdEIEELTQRLsEEQENKRKMGDKLSHErhqfqRDKEATQ 916
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-REYEGYELLKEKEALE-----RQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 917 ELIEDLRKQLEHLQLLRLEMEQRRG-----------RSSSLGLQEYNS-RARESELEQEVRRLKQDNRNLKEQNDELNGQ 984
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEeieqlleelnkKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564371221 985 IITLSIQ-GAKSLFSTSFSESLAAEisSVSRDELMEAIQKQEE 1026
Cdd:TIGR02169 324 LAKLEAEiDKLLAEIEELEREIEEE--RKRRDKLTEEYAELKE 364
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
837-1027 |
5.36e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 837 EIENLQARLQQLDEENSELRSctpclkanierLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQ 916
Cdd:PRK01156 340 DYIKKKSRYDDLNNQILELEG-----------YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 917 ELIEDLRKQL------------------EHLQLLRLEMEQRRGRS------SSLG-------LQEYN---SRARE--SEL 960
Cdd:PRK01156 409 KELNEINVKLqdisskvsslnqriralrENLDELSRNMEMLNGQSvcpvcgTTLGeeksnhiINHYNekkSRLEEkiREI 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564371221 961 EQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLfstsfsESLAAEISSVSRD--ELMEAIQKQEEI 1027
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKI------ESARADLEDIKIKinELKDKHDKYEEI 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
766-922 |
5.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEK-----DSAAAGEQHGRLRQENLQLvhranaLEEQLKE--QEFRAQEKVLEETRKQ-KELLCKMEREKSIE 837
Cdd:PRK03918 590 LEERLKELEPfyneyLELKDAEKELEREEKELKK------LEEELDKafEELAETEKRLEELRKElEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 838 IEN----LQARLQQLDEENSELRSCTPCLKANIERLEEEKQKM---LDEIEELTQRLSEEQENKRKMGD-KLSHERHQFQ 909
Cdd:PRK03918 664 LREeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELREKVKKyKALLKERALS 743
|
170
....*....|...
gi 564371221 910 RDKEATQELIEDL 922
Cdd:PRK03918 744 KVGEIASEIFEEL 756
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
844-981 |
5.65e-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: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 844 RLQQLDEENSELRsctpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKrkmgDKLSHERHQFQRDKEATQELIEDLR 923
Cdd:COG1579 11 DLQELDSELDRLE-------HRLKELPAELAELEDELAALEARLEAAKTEL----EDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371221 924 KQLEH------LQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDEL 981
Cdd:COG1579 80 EQLGNvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
797-1035 |
5.66e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 797 RANALEEQLKEQEFRAQekvLEETRKQKELlckmEREKSIEIENLQARLQQLDeenselrsctpclkaNIERLEEEKQKM 876
Cdd:PRK11281 28 RAASNGDLPTEADVQAQ---LDALNKQKLL----EAEDKLVQQDLEQTLALLD---------------KIDRQKEETEQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 877 LDEIEELTQRLSEEQENKRKMGDKLSherhqfqrdkeatqeliEDLRKQLEHLQLLRLEMEQRRgRSSSLG-----LQEY 951
Cdd:PRK11281 86 KQQLAQAPAKLRQAQAELEALKDDND-----------------EETRETLSTLSLRQLESRLAQ-TLDQLQnaqndLAEY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 952 NS----------RAReSELEQEVRRLKQDNRNLK-----------EQNDELNGQIITLSIQGA---KSLFSTSFSESLAA 1007
Cdd:PRK11281 148 NSqlvslqtqpeRAQ-AALYANSQRLQQIRNLLKggkvggkalrpSQRVLLQAEQALLNAQNDlqrKSLEGNTQLQDLLQ 226
|
250 260
....*....|....*....|....*...
gi 564371221 1008 EIssvsRDELMEAIQKQEEINFRLQDYI 1035
Cdd:PRK11281 227 KQ----RDYLTARIQRLEHQLQLLQEAI 250
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
777-940 |
5.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 777 SAAAGEQHGRLRQENLQLV-----HRANALEEQLKEQEfraqekVLEETRKQKELLCKMEREKSIEIENLQARLQqldee 851
Cdd:PRK04863 270 VAADYMRHANERRVHLEEAlelrrELYTSRRQLAAEQY------RLVEMARELAELNEAESDLEQDYQAASDHLN----- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 852 nselrsctpcLKANIERLEEEKQKMLDEIEELTQRLsEEQENKRKMGDKLSHERhqfQRDKEATQELIEDLRKQLEHLQl 931
Cdd:PRK04863 339 ----------LVQTALRQQEKIERYQADLEELEERL-EEQNEVVEEADEQQEEN---EARAEAAEEEVDELKSQLADYQ- 403
|
....*....
gi 564371221 932 LRLEMEQRR 940
Cdd:PRK04863 404 QALDVQQTR 412
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
877-1049 |
6.43e-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: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 877 LDEIE-ELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQllrlemeqrrgrsSSLGLQEYNSRA 955
Cdd:cd21116 50 LNEIKpKLLSLPNDIIGYNNTFQSYYPDLIELADNLIKGDQGAKQQLLQGLEALQ-------------SQVTKKQTSVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 956 RESELEQEVRRLKQDNRNLKEQNDELNGQIITLsiQGAKSLFSTsFSESLAAEISSVsrdelmEAIQKQEEInfrLQDYI 1035
Cdd:cd21116 117 FINELTTFKNDLDDDSRNLQTDATKAQAQVAVL--NALKNQLNS-LAEQIDAAIDAL------EKLSNDWQT---LDSDI 184
|
170
....*....|....
gi 564371221 1036 DRIIVAILETNPSI 1049
Cdd:cd21116 185 KELITDLEDAESSI 198
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
766-896 |
6.82e-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: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 766 LERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALE----------EQLKEQ--EFRAQEKVLEEtrKQKELLCKMErE 833
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQRLSEElaDLNAAIAGIEA--KINELEEEKE-D 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371221 834 KSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEEL--TQRLSEEQENKRK 896
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGR 510
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
767-935 |
7.14e-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: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALeeQLKEQEFRAQekvLEETRKQKELL---CKMEREK-SIEIENLQ 842
Cdd:pfam17078 65 ERRLKDLEDQLSELKNSYEELTESNKQLKKRLENS--SASETTLEAE---LERLQIQYDALvdsQNEYKDHyQQEINTLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 843 ARLQQLdeenselrsctpclkanieRLEEEKQkmldeIEELTQRLSEEQENKRKMGDKLSHERHQFqrdKEATQELIEDL 922
Cdd:pfam17078 140 ESLEDL-------------------KLENEKQ-----LENYQQRISSNDKDIDTKLDSYNNKFKNL---DNIYVNKNNKL 192
|
170
....*....|....
gi 564371221 923 RKQLEHL-QLLRLE 935
Cdd:pfam17078 193 LTKLDSLaQLLDLP 206
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
954-985 |
7.81e-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: 7.81e-03
10 20 30
....*....|....*....|....*....|..
gi 564371221 954 RARESELEQEVRRLKQDNRNLKEQNDELNGQI 985
Cdd:cd14686 20 KERIEELEEEVEELEEENEELKAELEELRAEV 51
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
836-1033 |
7.93e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 836 IEIENLQARLQQLDEENSELRSCTpclkANIERLEEEKQKMLDEIEELTQRLSEEQENKR---KMGDKLSHERHQFQRDK 912
Cdd:PRK01156 159 LEINSLERNYDKLKDVIDMLRAEI----SNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 913 EATQELIEDLRKQLEHLQllRLEMEQRRGRSSSLGLQEYNSRAreSELEQEVRRLKQD----NRNLKEQNDELNGQIITL 988
Cdd:PRK01156 235 NNLKSALNELSSLEDMKN--RYESEIKTAESDLSMELEKNNYY--KELEERHMKIINDpvykNRNYINDYFKYKNDIENK 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564371221 989 S--IQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 1033
Cdd:PRK01156 311 KqiLSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE 357
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
767-879 |
7.95e-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: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 767 ERRVSELEKDSAAAGEQHGR-LRQENLQLVHRANALEEQLKEQEFR--AQEKVLEETRKQKELL-----CKMEREKSIEI 838
Cdd:pfam14988 84 EREIQDLEEEKEKVRAETAEkDREAHLQFLKEKALLEKQLQELRILelGERATRELKRKAQALKlaakqALSEFCRSIKR 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564371221 839 EN--LQARLQQLDEEnselrscTPCLKANIERLEEEKQKMLDE 879
Cdd:pfam14988 164 ENrqLQKELLQLIQE-------TQALEAIKSKLENRKQRLKEE 199
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
801-928 |
8.36e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 38.71 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 801 LEEQLKEQEFRAQEKVLE---ETRKQKELLCKMEREKSIEIENLQARLQQ----LDEENSELRSctpcLKANIERLEEE- 872
Cdd:pfam12072 40 IEEAKKEAETKKKEALLEakeEIHKLRAEAERELKERRNELQRQERRLLQkeetLDRKDESLEK----KEESLEKKEKEl 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 564371221 873 --KQKMLDEIEELTQRLSEEQENKRKMGDKLSHErhqfqrdkEATQELIEDLRKQLEH 928
Cdd:pfam12072 116 eaQQQQLEEKEEELEELIEEQRQELERISGLTSE--------EAKEILLDEVEEELRH 165
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
802-923 |
9.22e-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: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371221 802 EEQLKEQEFRAQEKVLEETRKQKELLCKmEREKSieienLQARLQQLDEEnselrsctpclkanierLEEEKQKMLDEIE 881
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLE-DQERS-----YEEHLRQLKEK-----------------MEEERENLLKEQE 258
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564371221 882 ELTQRLSEEQENKRKMGdklsherhqFQRDKEATQELIEDLR 923
Cdd:cd16269 259 RALESKLKEQEALLEEG---------FKEQAELLQEEIRSLK 291
|
|
| bZIP_plant_BZIP46 |
cd14707 |
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ... |
953-981 |
9.50e-03 |
|
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. 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: 269855 [Multi-domain] Cd Length: 55 Bit Score: 35.37 E-value: 9.50e-03
10 20 30
....*....|....*....|....*....|...
gi 564371221 953 SRAR----ESELEQEVRRLKQDNRNLKEQNDEL 981
Cdd:cd14707 16 SRARkqayTNELELEVAHLKEENARLKRQQEEL 48
|
|
| |
