|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
956-1021 |
1.34e-43 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 152.24 E-value: 1.34e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747811797 956 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1021
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
848-918 |
2.49e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 148.87 E-value: 2.49e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747811797 848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1041-1112 |
4.75e-41 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 145.15 E-value: 4.75e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
960-1019 |
9.71e-31 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 115.32 E-value: 9.71e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 960 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1049-1110 |
1.11e-26 |
|
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188895 Cd Length: 62 Bit Score: 103.77 E-value: 1.11e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 1049 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNN 1110
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
855-913 |
4.18e-25 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 99.22 E-value: 4.18e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 747811797 855 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 913
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1041-1112 |
2.14e-19 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 83.26 E-value: 2.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1041-1112 |
2.12e-16 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 74.80 E-value: 2.12e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
955-1019 |
3.83e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 73.98 E-value: 3.83e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 955 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
955-1019 |
4.25e-16 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 73.50 E-value: 4.25e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 955 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
849-913 |
1.21e-15 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 72.48 E-value: 1.21e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 849 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 913
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
955-1019 |
5.78e-14 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 67.68 E-value: 5.78e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 955 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-501 |
6.68e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 301 LEKRYLAAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA 376
Cdd:COG1196 307 LEERRRELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 377 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmAALEEKNTLI 456
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELL 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 747811797 457 QELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGGPFVDGV 501
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-493 |
1.63e-13 |
|
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: 75.48 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAGVRdgaaEEEGTVELgpkRLWkedTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168 182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 246 RERLVtltttvteleedlgTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREatsIHDLNDKLENE 325
Cdd:TIGR02168 252 EEELE--------------ELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANE---ISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 406 LARVRQREKM-------NEDHNKRLSDTVDRLLSESNERLQ----LHLKERMAALEEKNTLIQELESSQRQIEEQhhhKG 474
Cdd:TIGR02168 388 VAQLELQIASlnneierLEARLERLEDRRERLQQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEA---LE 464
|
330
....*....|....*....
gi 747811797 475 RLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168 465 ELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-418 |
1.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 147 EVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEdtg 226
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE--- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEEEEALLELLA 466
|
250 260 270
....*....|....*....|....*....|..
gi 747811797 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-491 |
2.85e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196 157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 335 qceekARHLQELLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 414
Cdd:COG1196 234 -----LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 415 MNEDHNKRLSDTVDRL---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG1196 306 RLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-493 |
4.25e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD--- 425
Cdd:PRK02224 441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErre 519
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747811797 426 TVDRLLSESNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK02224 520 DLEELIAERRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-490 |
5.47e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 307 AAQREATSIHDLNDKLENELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHG 386
Cdd:TIGR02168 863 ELEELIEELESELEALLNERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 387 NIEEHLRQLEGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKN-TLIQELESSQRQ 465
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNlAAIEEYEELKER 1001
|
330 340
....*....|....*....|....*
gi 747811797 466 IEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-439 |
1.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 174 AALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKrlwkedtGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-------LVASDLREADARYYVLGDTLLGRTLVAA 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 334 RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QEL 406
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEY 790
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 747811797 407 ARVRQR-EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196 791 EELEERyDFLSEQREdleearETLEEAIEEIDRETRERFL 830
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
848-912 |
1.26e-10 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 58.01 E-value: 1.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747811797 848 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 912
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-468 |
2.40e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196 408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKR--------LWKEDTGRVEELQELLEKQNFELSQARERLVT 251
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 252 LTTTVTELEEDLGTARR---DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLENELAN 328
Cdd:COG1196 560 AAAIEYLKAAKAGRATFlplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV-AARLEAALRR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 329 KESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELAR 408
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 409 VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEE 468
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-491 |
3.26e-10 |
|
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: 64.70 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 218 KRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 369 AELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkRLSDTVDRLLSESnerlqlhlKERMAA 448
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVD--------KEFAET 383
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 747811797 449 LEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
281-491 |
8.81e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ-ELLEVAEQKLQQTMR 359
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 360 KAE---TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesne 436
Cdd:TIGR02168 770 LEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL------ 843
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 437 rlqlhlKERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02168 844 ------EEQIEELSE------DIESLAAEIEELEELIEELESELEALLNERASLE 886
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-491 |
1.25e-09 |
|
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: 62.82 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483 497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 401 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEK-----NTLIQELES 461
Cdd:pfam05483 647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKhkhqyDKIIEERDS 725
|
490 500 510
....*....|....*....|....*....|....
gi 747811797 462 S----QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam05483 726 ElglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-491 |
1.43e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 115 LEHLECLVSRHERSLRMTVVKRQAqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEE-------AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 275 ELSSKHQRDLREALAQKEDMEE---------------------RITTLEKRYLAAQREATSIHDLNDKLENELANKE--- 330
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaie 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 331 -------------SLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG1196 565 ylkaakagratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 398 QLEEKNQELARVRQREKMNEDHNKRLSdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLS 477
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELL----AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490
....*....|....
gi 747811797 478 EEIEKLRQEVDQLK 491
Cdd:COG1196 721 LEEEALEEQLEAER 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-493 |
1.64e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQrhlnsALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 102 SELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERV 179
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTEL 259
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 260 EEDLGTARRDLIKS----------------EELSSKHQRDLREALAQKEDMEERITTLEKR------YLAAQREATSIHD 317
Cdd:PRK03918 421 IKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKElrelekVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 318 LNDKLEN-----ELANKESLHRQCEEkARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHL 392
Cdd:PRK03918 501 LAEQLKEleeklKKYNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 393 RQL----EGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL--HLKERMAALEEKNTLIQELES--SQR 464
Cdd:PRK03918 580 EELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELEKkySEE 659
|
490 500
....*....|....*....|....*....
gi 747811797 465 QIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKR 688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-409 |
2.07e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 37 REKLLESLRESQETLAatqsRLQDAIHERD-QLQR-HLNSALPQEFATLTRELSmcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168 174 RKETERKLERTRENLD----RLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR02168 248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 275 ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS-----IHDLNDKLENELANKESLHRQCEEKARHLQELLEV 349
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 350 AEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:TIGR02168 473 AEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-495 |
3.19e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKAR 341
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 342 HLQEL----------LEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER----------HGNIEEHLRQLEGQLEE 401
Cdd:PRK03918 239 EIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 402 KNQELARVRQREKMNEDHNKRLSDTVDRL------LSESNERLQLH-----LKERMAALEEKNTlIQELESSQRQIEEQH 470
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLkelekrLEELEERHELYeeakaKKEELERLKKRLT-GLTPEKLEKELEELE 397
|
250 260
....*....|....*....|....*
gi 747811797 471 HHKGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIK 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-470 |
3.92e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 9 NEGDRLGPPHGADADANFEQLmvnmlDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSA------------- 75
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL-----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklekllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 76 --LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKA 153
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAH--QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKED------T 225
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 226 GRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 306 LAAQREATSIHDLND---KLENELANKESLHRQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELAQriAALTKAE 382
Cdd:COG4717 364 QLEELEQEIAALLAEagvEDEEELRAALEQAEEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkrlSDTVDRLLSEsnerlQLHLKERMAALEEK----NTLIQE 458
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQE-----LEELKAELRELAEEwaalKLALEL 501
|
490
....*....|..
gi 747811797 459 LESSQRQIEEQH 470
Cdd:COG4717 502 LEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-491 |
4.22e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS---------ALPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 105 KAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRAALER 178
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 179 VTTLEEQLAGAHQQVSALQQGAGVRDGAAEE----EGTVELGPKRLWKEDTGRV-EELQELLEKQNFELSQARERLVTLT 253
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEElkkaKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLR 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 254 TTVTELEEDLGTARR--------DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK-- 321
Cdd:PRK03918 480 KELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKla 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 322 -LENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:PRK03918 560 eLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 397 GQLEEKNQELarvrqrekmnEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRL 476
Cdd:PRK03918 640 KRLEELRKEL----------EELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
490
....*....|....*
gi 747811797 477 SEEIEKLRQEVDQLK 491
Cdd:PRK03918 710 KKELEKLEKALERVE 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-493 |
8.59e-09 |
|
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: 57.63 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 342 HLQELLEVAE--QKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVrqREKM 415
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 416 NEDHNKRLSDTVDR---LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH-KGRLSEEIEKLRQEVDQLK 491
Cdd:COG1579 83 GNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkKAELDEELAELEAELEELE 162
|
..
gi 747811797 492 GR 493
Cdd:COG1579 163 AE 164
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-491 |
8.93e-09 |
|
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: 60.13 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGVRDGAAEEEGTV----------------ELG-- 216
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLddqlqklladlhkrekELSle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 217 ---PKRLWKEDTG-----------------RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLG--TARRDLIKS- 273
Cdd:pfam15921 397 keqNKRLWDRDTGnsitidhlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslTAQLESTKEm 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 274 -----EELSSKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921 477 lrkvvEELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 336 CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQriaaLTKA-EERHGNIEEhLRQLEGQLEEKNQEL-ARVRQRE 413
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEiNDRRLELQE-FKILKDKKDAKIRELeARVSDLE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 414 ----KMNEDHNKRLSDTVDRllseSNERLQLhLKERMAALEEKNTLIQELESSQRQI----EEQHHHKGRLSEEIEKLRQ 485
Cdd:pfam15921 632 lekvKLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQS 706
|
....*.
gi 747811797 486 EVDQLK 491
Cdd:pfam15921 707 ELEQTR 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-490 |
1.30e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSMCREQLLEREEEISELKAER 108
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 109 NNTRL-----------LLEHLECLVSRHER------SLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRE 170
Cdd:TIGR02168 389 AQLELqiaslnneierLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 171 RLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwKEDTGRVEEL------------------- 231
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL-SGILGVLSELisvdegyeaaieaalggrl 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 232 --------------QELLEKQN------FELSQARERLVTLTTTVTELEED--LGTARrDLIKSEELSSK-------HQR 282
Cdd:TIGR02168 548 qavvvenlnaakkaIAFLKQNElgrvtfLPLDSIKGTEIQGNDREILKNIEgfLGVAK-DLVKFDPKLRKalsyllgGVL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 283 ---DLREALAQ--KEDMEERITTLE-----KRYLAAQREATSIHDLNDKlENELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02168 627 vvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 353 KLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD 428
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747811797 429 RL-----------------LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168 786 ELeaqieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-486 |
1.74e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 280 HQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ 355
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 356 qTMRKAETLPEVEAELAQRIAA---LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG4913 663 -VASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 747811797 433 ESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-486 |
2.51e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 361 AETLpevEAELAQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747811797 423 LSDTVDRlLSESNERLQLHLKERMAALEEKNtliQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-493 |
2.78e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 34 LDEREKLLESLRESQETLAATQSRL-QDAIHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 111 TRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERvTTLEEQLAGAH 190
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 191 QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDL 270
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 271 IKS------------------------EELSSKHQRDLREALAQ--------KEDMEERITTLEKRyLAAQREATSIHDL 318
Cdd:COG1196 515 LLAglrglagavavligveaayeaaleAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAALA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSE 478
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
490 500
....*....|....*....|..
gi 747811797 479 E-------IEKLRQEVDQLKGR 493
Cdd:COG1196 754 EelpeppdLEELERELERLERE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-451 |
3.29e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDgaAEEEGTVElgPKRLWKEDTG----RVEELQEL 234
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 235 LEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATs 314
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 315 ihdlndKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:PTZ00121 1669 ------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 747811797 395 lEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEE 451
Cdd:PTZ00121 1738 -EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-412 |
3.92e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 149 EVLKALKSLFEHHKALDEkVRERLRAALERVTTLEeQLAGAHQQVSALQQGAGVRDGAAEeegtvelgPKRLWKEDTgRV 228
Cdd:COG4913 222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRA--------ALRLWFAQR-RL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 229 EELQELLEKQNFELSQARERlvtltttvteleedlgtarrdlikseelsskhqrdLREALAQKEDMEERITTLEKRYLAA 308
Cdd:COG4913 291 ELLEAELEELRAELARLEAE-----------------------------------LERLEARLDALREELDELEAQIRGN 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 309 QREATsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK-AETLPEVEAELAQRIAALTKAEERHGN 387
Cdd:COG4913 336 GGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALAE 409
|
250 260
....*....|....*....|....*
gi 747811797 388 IEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913 410 AEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-490 |
4.37e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 34 LDEREKLLESLRESQE---TLAATQSRLQDAIHERDQlqrhlnsalpqEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224 236 RDEADEVLEEHEERREeleTLEAEIEDLRETIAETER-----------EREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 111 TRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQL 186
Cdd:PRK02224 305 DDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 187 AGAHQQVSALQ-QGAGVRDGAAEEEGTVELGPkrlwkEDTGRVEELQELLEKqnfELSQARERlvtltttVTELEEDLGT 265
Cdd:PRK02224 373 EEAREAVEDRReEIEELEEEIEELRERFGDAP-----VDLGNAEDFLEELRE---ERDELRER-------EAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 266 ARRDLIKSEEL--------------SSKHQRDLREALAQKEDMEERITTLEkrylaaqreaTSIHDLNDKLE--NELANK 329
Cdd:PRK02224 438 ARERVEEAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAELEDLE----------EEVEEVEERLEraEDLVEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 330 ESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETL----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 406 LARVRQ-REKMNEDHNKRlsDTVDRlLSESNERLQLHLKERMAALEEKNTLIQELESS--QRQIEEQHHHKGRLSEEIEK 482
Cdd:PRK02224 588 IESLERiRTLLAAIADAE--DEIER-LREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQ 664
|
....*...
gi 747811797 483 LRQEVDQL 490
Cdd:PRK02224 665 VEEKLDEL 672
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
278-494 |
4.60e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 278 SKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLEnELANKESLHRQCEEKARHLQellevAEQKLQqt 357
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEP-----------IRELAERYA-AARERLAELEYLRAALRLWF-----AQRRLE-- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 358 mRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ--------LEEKNQELARVRQREKMNEDHNKRLSDTVDR 429
Cdd:COG4913 292 -LLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747811797 430 L---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHhkgRLSEEIEKLRQEVDQLKGRG 494
Cdd:COG4913 371 LglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRK 435
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
848-914 |
4.78e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 50.76 E-value: 4.78e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747811797 848 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 914
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-487 |
9.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 39 KLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSAlpqEFATLTRELSmcreqllEREEEISELKAERNNTRLLLEHL 118
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEA---ELEELEAELA-------ELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 119 eclvsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQ 198
Cdd:COG1196 287 --------QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 199 GAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSS 278
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 279 KHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEVAEQKLQQT 357
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 358 MRKAE----TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRqREKMNEDHNKRLSDTVDRLLSE 433
Cdd:COG1196 519 LRGLAgavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-FLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 747811797 434 SNERLQLHLKERmaALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 487
Cdd:COG1196 598 GAAVDLVASDLR--EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
964-1019 |
9.39e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.99 E-value: 9.39e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 747811797 964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-491 |
9.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL 459
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190
....*....|....*....|....*....|..
gi 747811797 460 ESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-487 |
9.90e-08 |
|
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: 56.77 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHKALDEKVrERLRAAleRVTTLEEQLAGA 189
Cdd:pfam12128 322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKY-NRRRSK--IKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 190 HQQVSALQQGAgVRdGAAEEEGTVElgpkrlwkedtGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLgTARRD 269
Cdd:pfam12128 396 KDKLAKIREAR-DR-QLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA-TATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 270 LIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQELLE 348
Cdd:pfam12128 462 LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAlDELELQLFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 349 VAEQKLQQTMRK---AETL------PEV-----------------------------EAELAQRIAALTKA----EERHG 386
Cdd:pfam12128 542 KEAPDWEQSIGKvisPELLhrtdldPEVwdgsvggelnlygvkldlkridvpewaasEEELRERLDKAEEAlqsaREKQA 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllSESNERLQLHlKERMAALEEKNTLIQELESSQRQI 466
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERKDSANERLNSLEAQLKQL 694
|
490 500
....*....|....*....|....*....
gi 747811797 467 EEQH-----HHKGRLSE---EIEKLRQEV 487
Cdd:pfam12128 695 DKKHqawleEQKEQKREartEKQAYWQVV 723
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
35-492 |
1.97e-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: 55.75 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 35 DEREKLLeSLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR00618 421 DLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 115 LEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618 499 LQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 195 ALQQ-----GAGVRDGAAEEEGTVELGPKRLWKEDTGRvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARrd 269
Cdd:TIGR00618 574 ILTQcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLA-CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA-- 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 270 liksEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQEL--- 346
Cdd:TIGR00618 651 ----LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIena 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 347 -----------LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ---LEEKNQELArvrq 411
Cdd:TIGR00618 727 ssslgsdlaarEDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlREEDTHLLK---- 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 412 rEKMNEDHNKRLSDTVDRLLSEsnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR00618 803 -TLEAEIGQEIPSDEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
.
gi 747811797 492 G 492
Cdd:TIGR00618 880 G 880
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-490 |
2.05e-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: 55.46 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRDGAAEEEGTVELGPKRLwkedtgrvEELQELLEKQNFELSQARE 247
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDeLSQELSDASRKIGEIEKEI--------EQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 248 RLVTLTTTVTELEEDLGTARRDLIKSEELSSKhqrdLREALAQKEDM--EERITTLEKRYlaaqreatsihdlnDKLENE 325
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHK----LEEALNDLEARlsHSRIPEIQAEL--------------SKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-TKAEERHGNIEEH---LRQLEGQLEE 401
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELeaaLRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 402 KNQElaRVRQREKMNEDHNKRlsdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHK---GRLSE 478
Cdd:TIGR02169 887 LKKE--RDELEAQLRELERKI------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQA 958
|
330
....*....|..
gi 747811797 479 EIEKLRQEVDQL 490
Cdd:TIGR02169 959 ELQRVEEEIRAL 970
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
123-493 |
2.41e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 123 SRHERSLRMTVVKRqaqspsgVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE--QLAGAHQQ--VSAL-Q 197
Cdd:PRK04863 275 MRHANERRVHLEEA-------LELRRELYTSRRQLAAEQYRLVEMARE-LAELNEAESDLEQdyQAASDHLNlvQTALrQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 198 QGAGVRdgaAEEEgtvelgpkrlwkedtgrVEELQELLEKQNFELSQARERlvtltttvteleedlgtarrdLIKSEELS 277
Cdd:PRK04863 347 QEKIER---YQAD-----------------LEELEERLEEQNEVVEEADEQ---------------------QEENEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 278 SKHQRDLREALAQKEDMEERITTLEKR---YLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKL 354
Cdd:PRK04863 386 EAAEEEVDELKSQLADYQQALDVQQTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 355 QQTmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE------GQLEEKNQELARVRQREkmnedhnkRLSDTVD 428
Cdd:PRK04863 466 SVA-QAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqrhlaEQLQQLRMRLSELEQRL--------RQQQRAE 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 429 RLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK04863 537 RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-469 |
3.74e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 361 AETLPEVEA--------ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 747811797 433 ESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 469
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-484 |
3.85e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 32 NMLDEREKLLESLRESQETLAATQsRLQDAIHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618 290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 192 QVSA---LQQGAGVRDGAAEEEGTVELGPKRlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:TIGR00618 344 RRLLqtlHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEEK-ARHLQELL 347
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKkAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 348 EVAEQklQQTMRKAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRL 423
Cdd:TIGR00618 498 ELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 424 SDTVDRLLSESNERLQLhlkermaaLEEKNTLIQELESSQRQI-EEQHHHKGRLSEEIEKLR 484
Cdd:TIGR00618 576 TQCDNRSKEDIPNLQNI--------TVRLQDLTEKLSEAEDMLaCEQHALLRKLQPEQDLQD 629
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-493 |
4.93e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 26 FEQLMVNMLDER-EKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRElsmcreqllereeeISEL 104
Cdd:COG4913 285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE--------------IERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 105 KAERNNTRLLLEHLECLVsrheRSLRMTVvkrqaqsPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4913 351 ERELEERERRRARLEALL----AALGLPL-------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 185 QLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpKRLWKEDTG-RVEELQ---ELLE-KQNFELSQ-ARERLvtltttvte 258
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLAL-------RDALAEALGlDEAELPfvgELIEvRPEEERWRgAIERV--------- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 259 leedLGTARRDLIkseeLSSKHQRDLREALAQkEDMEERITTLE-----KRYLAAQREATSI--------HDLNDKLENE 325
Cdd:COG4913 484 ----LGGFALTLL----VPPEHYAAALRWVNR-LHLRGRLVYERvrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 326 LANKESLHR-------QCEEKA------------------RHL-----------QELLEVAEQKLQQTMRKAETLPEVEA 369
Cdd:COG4913 555 LGRRFDYVCvdspeelRRHPRAitragqvkgngtrhekddRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 370 ELAQRIAALTKAEERHGNIEEH------LRQLEGQLEEKNQELARvrqrekmnedhnkrlsdtvdrlLSESNERLQlHLK 443
Cdd:COG4913 635 ALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELER----------------------LDASSDDLA-ALE 691
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 747811797 444 ERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG4913 692 EQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-491 |
5.97e-07 |
|
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: 53.97 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 25 NFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHErdqlqrhlnsalpQEFATLTRELSMcreqllereeeisel 104
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE-------------LEAAKCLKEDML--------------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 105 kaerNNTRLLLEHLECLVSRHE---RSLRMTVVKRQAQSPSGVsSEVEVLKALkslfeHHKALDEKVRERLRAALERVTT 181
Cdd:pfam15921 166 ----EDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKI-YEHDSMSTM-----HFRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 182 LEEQLAGAHQQVSALQqgagvrdgaAEEEGTVELgpkrLWKEDTGRVE--------ELQELLEKQNFELSQARERLVTLT 253
Cdd:pfam15921 236 LKGRIFPVEDQLEALK---------SESQNKIEL----LLQQHQDRIEqlisehevEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELAN-KESL 332
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNlDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 333 HRQCEEKARHLQELLEVAEQKLQ---QTMRKAETLPEVEAEL------AQRIAALTKA--EERHGNIEEHLRQLEGqlee 401
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDHLRRELddrnmeVQRLEALLKAmkSECQGQMERQMAAIQG---- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 402 KNQELARVRQREKMNEDHNKRLSDTVDRLLS-----ESNER----LQLHLKERMAALEEKNTLIQELESS-QRQIEEQHH 471
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmtlESSERtvsdLTASLQEKERAIEATNAEITKLRSRvDLKLQELQH 535
|
490 500
....*....|....*....|
gi 747811797 472 HKGRlSEEIEKLRQEVDQLK 491
Cdd:pfam15921 536 LKNE-GDHLRNVQTECEALK 554
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-451 |
1.07e-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: 51.08 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAeqklqQTMRKAET 363
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 364 LpevEAELAQriaaltkAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLK 443
Cdd:COG1579 94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 747811797 444 ERMAALEE 451
Cdd:COG1579 164 EREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-493 |
1.08e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR------- 334
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKelearie 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 335 QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieehLRQLEGQLEEKNQELARV 409
Cdd:TIGR02169 769 ELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-------LTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 410 RQREKMNEDHNKRLSDTVDRLLSESNERlqlhLKERMAALEEkntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
....
gi 747811797 490 LKGR 493
Cdd:TIGR02169 915 KRKR 918
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-493 |
1.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 264 GTARRDLIksEELS--SKHQRDLREALAQKEDMEERITTLEkrylaaqreaTSIHDLNDKLENELANKESLHRQCEEKAR 341
Cdd:TIGR02169 152 PVERRKII--DEIAgvAEFDRKKEKALEELEEVEENIERLD----------LIIDEKRQQLERLRREREKAERYQALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 342 hLQEL--------LEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARvRQRE 413
Cdd:TIGR02169 220 -KREYegyellkeKEALERQKEAIERQLASL---EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 414 KMNEDHNKRLSdtVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169 295 KIGELEAEIAS--LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-486 |
1.38e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGT 212
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 213 VELGPKRLWKEDTGRVEELQELLEKQNF-ELSQARERLVTLTTTVTELEEDLGTARrdliKSEELssKHQRDLREALAQK 291
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKADELK----KAEEL--KKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 292 EDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAEL 371
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVEQLKKKEAEE 1645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 372 AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEE 451
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKAEE 1720
|
330 340 350
....*....|....*....|....*....|....*
gi 747811797 452 kntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:PTZ00121 1721 ---LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-491 |
1.60e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 40 LLESLRESQETLAATQSRL-QDAIHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLE 116
Cdd:COG4717 47 LLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 117 HLECL--VSRHERSL-----RMTVVKRQAQSPSGVSSEVEVLKAlkSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:COG4717 127 LLPLYqeLEALEAELaelpeRLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 190 HQQVSALQQgagvRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQAR----ERLVTLTTTVTELEEDLGT 265
Cdd:COG4717 205 QQRLAELEE----ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllalLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK-----LENELANKESLHRQCEEKA 340
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeelleLLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 341 RHLQelLEVAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKmNEDHN 420
Cdd:COG4717 361 EELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EEELE 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747811797 421 KRLSDTVDRLLSESNERLQLHlkERMAALEEKntlIQELESSQRqIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4717 432 EELEELEEELEELEEELEELR--EELAELEAE---LEQLEEDGE-LAELLQELEELKAELRELAEEWAALK 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-494 |
2.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKV--RERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG 211
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 212 TVELGPKRL--WKEDTGRVEELQELLEKQNFELSQARER-LVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAL 288
Cdd:COG4717 140 ELAELPERLeeLEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 289 AQKEDMEERITTLEKRYLAAQRE-------------------ATSIHDLNDKLEN-----------------ELANKESL 332
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEerlkearlllliaaallalLGLGGSLLSLILTiagvlflvlgllallflLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQR-IAALTKAEERHGNIEEHLRQLE-GQLEEKNQEL---A 407
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQlEELEQEIAALlaeA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 408 RVRQREKMNE--DHNKRLSDTVDRLlSESNERLQLHLKERMAALE--EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:COG4717 380 GVEDEEELRAalEQAEEYQELKEEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAEL 458
|
410
....*....|.
gi 747811797 484 RQEVDQLKGRG 494
Cdd:COG4717 459 EAELEQLEEDG 469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-430 |
2.54e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 388
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 747811797 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-407 |
2.83e-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: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 229 EELQELLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|.
gi 747811797 387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579 149 EELAELEAELEELEAEREELA 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-493 |
2.93e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 153 ALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwKEDTGRVEELQ 232
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 233 ELLE--KQNFELSQARERLVtltttvteleedlgtarrdliKSEELSSKHQrDLREALAQKEDMEERITTLEKRYLAaqR 310
Cdd:PTZ00121 1412 KAAAakKKADEAKKKAEEKK---------------------KADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKA--E 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 311 EATSIHDLNDKLEnELANKESLHRQCEEKARHLQELLEVAEQKLQ-QTMRKAETLPEVE----AELAQRIAALTKAEERH 385
Cdd:PTZ00121 1468 EAKKADEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADeakkAEEAKKADEAKKAEEKK 1546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 386 GniEEHLRQLEGQleEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHLKERMAALEEKntliQELESSQRQ 465
Cdd:PTZ00121 1547 K--ADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMAL-----RKAEEAKKAEEARIEEVMKLYEEE----KKMKAEEAK 1613
|
330 340
....*....|....*....|....*...
gi 747811797 466 IEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-491 |
4.10e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAetlpeveAELAQRIAALtkaEERHGNIEEHLRQLEGQL 399
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAAL---EAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 400 EEKNQELA-RVRQREKMNED-------HNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHH 471
Cdd:COG4942 100 EAQKEELAeLLRALYRLGRQpplalllSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180
....*....|....*....|
gi 747811797 472 HKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4942 175 ELEALLAELEEERAALEALK 194
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
376-493 |
4.73e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.05 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLK---ERMA--ALE 450
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 747811797 451 EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG1842 92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
5.74e-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: 50.72 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGVRDGAAEEEGTVE--LGPKRLWKEDT--GRVEELQELLEkq 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEELREELD-- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 239 nfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEE 383
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEE 1055
|
250 260 270
....*....|....*....|....*....|.
gi 747811797 384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
13-486 |
6.70e-06 |
|
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: 50.61 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 13 RLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCRE 92
Cdd:pfam12128 445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 93 QLLEREEEISELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALD 165
Cdd:pfam12128 525 LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 166 E---KVRERLRAALERVTTLEEQLAGAHQQVSALQqgAGVRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFEL 242
Cdd:pfam12128 604 ErldKAEEALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 243 SQARERLVTLTTTVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDk 321
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK- 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 322 leNELANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEA---ELAQRIAALTK 380
Cdd:pfam12128 758 --RDLASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaisELQQQLARLIA 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 381 -AEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHnkrlsdtvdrlLSESNERLQLHLKERMAALEE-KNTLIQ 457
Cdd:pfam12128 836 dTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDY 904
|
490 500 510
....*....|....*....|....*....|....
gi 747811797 458 ELESSQRQIEE-----QHHHKGRLSEEIEKLRQE 486
Cdd:pfam12128 905 LSESVKKYVEHfknviADHSGSGLAETWESLREE 938
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1042-1113 |
7.96e-06 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 44.59 E-value: 7.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1113
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
964-1015 |
9.51e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.15 E-value: 9.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 747811797 964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1015
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-493 |
9.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 24 ANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-DRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 104 LKAERNNTRLLLEHLE-------CLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRA 174
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 175 ALERVTTLEEQLAGAHQQ-VSALQQGAGVRDGA--AEEEGTVELGPKRLWKEDTGRV-----------EELQELLEKQNF 240
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERyATAIEVAAGNRLNNvvVEDDAVAKEAIELLKRRKAGRAtflplnkmrdeRRDLSILSEDGV 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 241 --------ELSQARERLVTLTTTVTELEEDLGTARRDLIKSE------EL-------------SSKHQRDLREALAQKED 293
Cdd:TIGR02169 599 igfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegELfeksgamtggsraPRGGILFSRSEPAELQR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR-------QCEEKARHLQELLEVAEQKLQQTMRKAET--- 363
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 364 -LPEVEAELAQRIAALTKAEERHGNIEEHLRQleGQLEEKNQELARVRQREKMNEdhnKRLSDtVDRLLSESNERLQLhL 442
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE---ARLRE-IEQKLNRLTLEKEY-L 831
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 747811797 443 KERMAALEEKNTLIQELESS-QRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-485 |
1.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 42 ESLRESQETLAATQSRLQDAIHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224 390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTVELGPKRLwKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERL-EE---RREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 247 ERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEkrylaaqreatsihdlndKLENEL 326
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE------------------RIRTLL 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 327 ANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER 676
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747811797 407 ARVRQREKMNEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKntlIQELESSQRQIEEQHHHKGRLSEEiekLRQ 485
Cdd:PRK02224 677 DDLQAEIGAVENELEELEE----------------LRERREALENR---VEALEALYDEAEELESMYGDLRAE---LRQ 733
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-493 |
1.06e-05 |
|
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: 49.69 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 360 -------KAETLPEVEAELAQRIAALTKAeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD---- 428
Cdd:pfam05622 81 arddyriKCEELEKEVLELQHRNEELTSL-------AEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDlrrq 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747811797 429 -RLLSESNerlqLHLKERMAALEEK----NTLIQELESSQRQIEEQHHhkgRLSEEI---EKLRQEVDQLKGR 493
Cdd:pfam05622 154 vKLLEERN----AEYMQRTLQLEEElkkaNALRGQLETYKRQVQELHG---KLSEESkkaDKLEFEYKKLEEK 219
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1042-1112 |
1.26e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 1.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747811797 1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1112
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-493 |
2.09e-05 |
|
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: 48.90 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 42 ESLRESQETLAATqsRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECL 121
Cdd:TIGR02168 220 AELRELELALLVL--RLEELREELEELQEELK-EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 122 VSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG 201
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 202 VRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQnfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQ 281
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 282 RDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE--KARH--------LQELLEVAE 351
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSglsgilgvLSELISVDE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 352 Q-------------------------KLQQTMRKAET------------------------------------LPEVEAE 370
Cdd:TIGR02168 534 GyeaaieaalggrlqavvvenlnaakKAIAFLKQNELgrvtflpldsikgteiqgndreilkniegflgvakdLVKFDPK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 371 L-------------------AQRIAALTKAEER-----------HG---------------------NIEEHLRQLEGQL 399
Cdd:TIGR02168 614 LrkalsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpGGvitggsaktnssilerrreieELEEKIEELEEKI 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 400 EEKNQELARVR----QREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQH----- 470
Cdd:TIGR02168 694 AELEKALAELRkeleELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerlee 772
|
570 580
....*....|....*....|....*
gi 747811797 471 --HHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168 773 aeEELAEAEAEIEELEAQIEQLKEE 797
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-463 |
2.60e-05 |
|
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: 46.60 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQ 463
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-489 |
4.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 169 RERLRAALERVTTLEEQLAGAHQQVSALQ-QGAGVRDGAAEEEGTVELGPKRL-WKEDTGRVEELQ---ELLEKQNFELS 243
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIdVASAEREIAELEaelERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 244 QARERLVTLTTTVTELEEDLGTARRDLIKSEelssKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLE 323
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 324 NELAnkeslhRQCEEKARHLQELLEVAEQKLQQTMR------------------------------KAETLPEVEAELAQ 373
Cdd:COG4913 765 RELR------ENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadleslpeylalldrlEEDGLPEYEERFKE 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 374 riaALTKAEER-----HGNIEEHLRQLEGQLEEKNQELARVRqrekMNEDHnkrlsdtvdrllsesneRLQLHLKERmaA 448
Cdd:COG4913 839 ---LLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKRIP----FGPGR-----------------YLRLEARPR--P 892
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 747811797 449 LEEKNTLIQELESSQRQI-----EEQHHHKGRLSEEIEKLRQEVDQ 489
Cdd:COG4913 893 DPEVREFRQELRAVTSGAslfdeELSEARFAALKRLIERLRSEEEE 938
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
232-482 |
5.64e-05 |
|
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: 47.43 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 232 QELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaQKEDMEERITTLEKRYLAAqrE 311
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAM--E 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 312 ATSIHDLnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRiaaltkaeerhgnieeH 391
Cdd:pfam17380 374 ISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR----------------E 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 392 LRQLEgqlEEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHL---KERMAALEEKNTLI--QELESSQRQI 466
Cdd:pfam17380 437 VRRLE---EERAREMERVRLEEQERQQQVERL-----RQQEEERKRKKLELekeKRDRKRAEEQRRKIleKELEERKQAM 508
|
250
....*....|....*.
gi 747811797 467 EEQHHHKGRLSEEIEK 482
Cdd:pfam17380 509 IEEERKRKLLEKEMEE 524
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
270-491 |
7.16e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 270 LIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIH-----------------DLNDKLENELANKES- 331
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnkllklelllsnlkkkiQKNKSLESQISELKKq 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 332 ---LHRQCEEKARHLQEL---LEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLE----E 401
Cdd:TIGR04523 227 nnqLKDNIEKKQQEINEKtteISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 402 KNQELAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRL 476
Cdd:TIGR04523 304 KEQDWNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
250
....*....|....*
gi 747811797 477 SEEIEKLRQEVDQLK 491
Cdd:TIGR04523 383 KQEIKNLESQINDLE 397
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
295-491 |
7.60e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 295 EERITTLEKRYLAAQREATSIHD----LNDKL---ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLP-- 365
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDniekKQQEInekTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkq 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 366 --EVEAELA----QRIAALTKA-EERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDHNKRlsdTVDRLLS 432
Cdd:TIGR04523 290 lnQLKSEISdlnnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELE 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747811797 433 ESNERLQLHLKERMAALEEKNTL---IQELESS-----------QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLesqINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
318-493 |
7.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 318 LNDKLENElanKESLHRQCEEKARHLQELLEVAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 398 QLEEKNQELARVRQREKMnEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ-------- 469
Cdd:COG4717 117 ELEKLEKLLQLLPLYQEL-EALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELleqlslat 190
|
170 180
....*....|....*....|....
gi 747811797 470 HHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEE 214
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
8.94e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169 760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 185 QLAGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLG 264
Cdd:TIGR02169 830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESR--------------LG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKAR 341
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEE 965
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 747811797 342 HLQELLEV---AEQKLQQTMR-------KAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169 966 EIRALEPVnmlAIQEYEEVLKrldelkeKRAKLEEERKAILERIEEYEK 1014
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
291-491 |
9.09e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 291 KEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEV 367
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 368 EAELAQRIAALTKAEERHGNIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE 436
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747811797 437 rlqlhLKERMAALE----EKNTLIQELES--------------------SQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523 522 -----LKEKIEKLEsekkEKESKISDLEDelnkddfelkkenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-486 |
1.20e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 274 EELSSKHQRDLREALAQKE---DMEERITTLEKRY--LAAQREA--TSIHDLNDKLENELANKESLHRQCEEKArhlQEL 346
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIknLDNTRESleTQLKVLSRSINKIKQNLEQKQKELKSKE---KEL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 347 LEVAEQKLQqtmrkaetLPEVEAELAQRIAALTKAEErhgNIEEHLRQLEGQLEEKNQELarvrqrEKMNEDHNKRLSDT 426
Cdd:TIGR04523 499 KKLNEEKKE--------LEEKVKDLTKKISSLKEKIE---KLESEKKEKESKISDLEDEL------NKDDFELKKENLEK 561
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747811797 427 VDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQ----RQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKkdliKEIEEKEKKISSLEKELEKAKKE 625
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
1.33e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 747811797 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
263-491 |
1.82e-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: 46.12 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 263 LGTARRDLIKSEELsskhqRDLREALAQKEDMEERITTLEKRYLAAQREAtsihdlndKLENELANKESLHRQCEEKARH 342
Cdd:pfam02463 162 AAGSRLKRKKKEAL-----KKLIEETENLAELIIDLEELKLQELKLKEQA--------KKALEYYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 343 LQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQeLARVRQREKMNEDHNKR 422
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLER 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747811797 423 LSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
222-491 |
1.90e-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: 45.73 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 222 KEDTGRVEELQELLEKQNFELSQARErlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREaLAQKEDMEERITTL 301
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIID---------------LEELKLQELKLKEQAKKALEYYQL-KEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 302 EKRYLAAQREATSIHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEA 369
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 370 ELAQRIaaLTKAEERHGNIEEHLRQLEGQLEEKNQELARV-RQREKMNE---------DHNKRLSDTVDRLLSESNERLQ 439
Cdd:pfam02463 310 VDDEEK--LKESEKEKKKAEKELKKEKEEIEELEKELKELeIKREAEEEeeeeleklqEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 747811797 440 LHLKERMAALEEKNTLIQE------LESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEaqllleLARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-417 |
2.38e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaaeeegtvelgpkrlwkedtgRVEELQE 233
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 234 LLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:COG4372 67 ELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERHGNIEEHLR 393
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNAEKEEELA 203
|
250 260
....*....|....*....|....
gi 747811797 394 QLEGQLEEKNQELARVRQREKMNE 417
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSL 227
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
136-490 |
2.54e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 136 RQAQSPSGVSSEVEVLKALKSLFEHHKAL----------DEKVRERLRAALERV----TTLEEQLAGAHQQVSALQQGAG 201
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMisdleerlkkEEKGRQELEKAKRKLegesTDLQEQIAELQAQIAELRAQLA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 202 VRD-------GAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNfelsQARERLVTLTTTVTELEEDLGTARRDLIKS- 273
Cdd:pfam01576 240 KKEeelqaalARLEEETAQKNNALKKIRELEAQISELQEDLESER----AARNKAEKQRRDLGEELEALKTELEDTLDTt 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 274 ---EELSSKHQRDLREAlaqKEDMEERITTLEKRYLA-AQREATSIHDLNDKLENELANKESLHRQ---CEEKARHLQEL 346
Cdd:pfam01576 316 aaqQELRSKREQEVTEL---KKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAkqaLESENAELQAE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 347 LEV--------------AEQKLQQTMRKAETLPEVEAELAQRIA-----------ALTKAEERHGNIEEHLRQLEGQL-- 399
Cdd:pfam01576 393 LRTlqqakqdsehkrkkLEGQLQELQARLSESERQRAELAEKLSklqselesvssLLNEAEGKNIKLSKDVSSLESQLqd 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 400 ------EEKNQELA---RVRQ--------REKMNEDHNKRLS-----DTVDRLLSESNERLQLHLKERMAALEEKNTLIQ 457
Cdd:pfam01576 473 tqellqEETRQKLNlstRLRQledernslQEQLEEEEEAKRNverqlSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552
|
410 420 430
....*....|....*....|....*....|...
gi 747811797 458 ELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
135-484 |
2.58e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRdgAAEEEgtV 213
Cdd:pfam09731 88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ--AVKAH--T 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 214 ELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 294 MEERITTLEKRYLAA-----QREATSIH-DLNDKL-ENELANKESLHRQCEekarHLQELLEVAEQKLQqTMRKAETLpE 366
Cdd:pfam09731 240 SLAKLVDQYKELVASerivfQQELVSIFpDIIPVLkEDNLLSNDDLNSLIA----HAHREIDQLSKKLA-ELKKREEK-H 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 367 VEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTVDRLLSES 434
Cdd:pfam09731 314 IERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVLVEQEIEL 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 747811797 435 NERLQLHLKERMAalEEKNTL---IQELESSQRQIEEQhhHKGRLSEEIEKLR 484
Cdd:pfam09731 393 QREFLQDIKEKVE--EERAGRllkLNELLANLKGLEKA--TSSHSEVEDENRK 441
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
325-486 |
2.72e-04 |
|
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: 45.11 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 325 ELANKESLHRQCEEKARHLQELLEVAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEEHLRQLEG-QLEEKN 403
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 404 QELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKermAALEEKntlIQElESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELE---AARKVK---ILE-EERQRKIQQQKVEMEQIRAEQEEA 432
|
...
gi 747811797 484 RQE 486
Cdd:pfam17380 433 RQR 435
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
222-490 |
2.73e-04 |
|
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: 44.95 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 222 KEDTGRVEELQELLEKQNFELS-QARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRdlREALAQKEDMEERITT 300
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE--TGIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 301 LEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveaelaqr 374
Cdd:COG5185 352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD------------ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 375 iaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSEsnerlqlhLKERMAALEEK 452
Cdd:COG5185 420 ----RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRS--------VRSKKEDLNEE 486
|
250 260 270
....*....|....*....|....*....|....*...
gi 747811797 453 NTLIQELESSQRQIEEQhhHKGRLSEEIEKLRQEVDQL 490
Cdd:COG5185 487 LTQIESRVSTLKATLEK--LRAKLERQLEGVRSKLDQV 522
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-466 |
3.12e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 366 EVEA-ELAQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRqrekmnedhnKRLSDTVDRLLSESN--ERLQLHL 442
Cdd:PRK11281 108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAAL 165
|
170 180
....*....|....*....|....
gi 747811797 443 KERMAALEEKNTLIQELESSQRQI 466
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKAL 189
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
347-589 |
3.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 347 LEVAEQKLQQTMRKAETlpeVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRL-- 423
Cdd:COG3883 18 IQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERAra 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 424 --------------------SDTVDRL-----LSESNERLQLHLKERMAALEE-KNTLIQELESSQRQIEEQHHHKGRLS 477
Cdd:COG3883 95 lyrsggsvsyldvllgsesfSDFLDRLsalskIADADADLLEELKADKAELEAkKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 478 EEIEKLRQEVDQLKGRGGPFVDGVHSRSHMGSAADVRFSLGTTTHAPPGvhRRYSALREESAKDWETSPLPGMLAPAAGP 557
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA--AAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250 260 270
....*....|....*....|....*....|..
gi 747811797 558 AFDSDPEISDVDEDEPGGLVGSADVVSPSGHS 589
Cdd:COG3883 253 GAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
316-486 |
3.96e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 316 HDLNDKLENELANKESLHRQCEEKARHLQEL-LEVA--EQKLQQTMR-KAETLPEVEaELAQRIAALTKAEERHGNIEEH 391
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSkGKVAqlEEKLVSTEKeKIEEKSETE-KLLEYITELSCVSEQVEKYKLD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 392 LRQLEGQLEEKNQELARVRQREKMNEDHnkrLSDTVDRLlsesNERLQL--HLKERMAALEE--KNTLIQELESSQRQIE 467
Cdd:pfam15905 245 IAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDL----NEKCKLleSEKEELLREYEekEQTLNAELEELKEKLT 317
|
170
....*....|....*....
gi 747811797 468 EQhhhkgrlSEEIEKLRQE 486
Cdd:pfam15905 318 LE-------EQEHQKLQQK 329
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
338-493 |
4.08e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.20 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:cd00176 40 KKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 418 DH---NKRLSDTVDRLLSESN-------ERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQ 485
Cdd:cd00176 114 DAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNE 193
|
....*...
gi 747811797 486 EVDQLKGR 493
Cdd:cd00176 194 RWEELLEL 201
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
267-491 |
4.37e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 267 RRDLI-KSEELSSKhqrdLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQE 345
Cdd:COG1340 45 RDELNaQVKELREE----AQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 346 LlevaeQKLQQTMrkaETLPEVEAELAQRIAALTK-AEERhgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLS 424
Cdd:COG1340 121 L-----EWRQQTE---VLSPEEEKELVEKIKELEKeLEKA-----KKALEKNEKLKELRAELKELRKEA---EEIHKKIK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747811797 425 DTVDRLLSESNERLQLhLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG1340 185 ELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
227-493 |
4.88e-04 |
|
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: 44.43 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTarrdlikseelsskhqrdLREALAQKEDMEERITtlEKRYL 306
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTT------------------LEEALSEKERIIERLK--EQRER 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 385
Cdd:pfam10174 462 EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLk 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 386 ------------GNIEEHLRQLEGQLEEKNQELAR-----------VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:pfam10174 542 kahnaeeavrtnPEINDRIRLLEQEVARYKEESGKaqaeverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVA 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 747811797 443 KERMAALEEKNTLIQELESSQRQIEE-----QHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNladnsQQLQLEELMGALEKTRQELDATKAR 677
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
297-491 |
5.47e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.06 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 297 RITTLEKRYLAAQREATSIHDLNDKLENELANKESlhrqcEEKARHLQELLEVAEQKLQQTMRKAETL------------ 364
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDAS-----KQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 365 -----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTvDRLLSESnerLQ 439
Cdd:pfam12795 76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 440 LHLKERMAALEEK----------NTLIQELESSQRQIEEQHHHkgRLSEEIEKLRQEVDQLK 491
Cdd:pfam12795 152 WALQAELAALKAQidmleqellsNNNRQDLLKARRDLLTLRIQ--RLEQQLQALQELLNEKR 211
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
283-439 |
6.15e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtm 358
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEIQENKILIEKLRG---------- 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 359 rKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERL 438
Cdd:PRK01156 651 -KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL 725
|
.
gi 747811797 439 Q 439
Cdd:PRK01156 726 E 726
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
851-909 |
6.53e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 39.62 E-value: 6.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747811797 851 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 909
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-478 |
8.09e-04 |
|
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: 43.88 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpkRLWKEDTGRVEELQELLEKQNFELSQ 244
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ--------HELDTVVSKIELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 245 ARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 325 ELankESLHRQCEEKARHLQELlevaEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:TIGR00606 942 KV---NDIKEKVKNIHGYMKDI----ENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 405 E-------LARVRQREKMNEdhnkrLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELES----SQRQIEEQ-HHH 472
Cdd:TIGR00606 1013 QerwlqdnLTLRKRENELKE-----VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVlalgRQKGYEKEiKHF 1087
|
....*.
gi 747811797 473 KGRLSE 478
Cdd:TIGR00606 1088 KKELRE 1093
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
286-493 |
8.22e-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: 43.80 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 286 EALAQKEDMEERITTLEKRY----LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrKA 361
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----KQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 362 ETLPEVEAElaqriaaltkaeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDtVDRLLSESNERLQlh 441
Cdd:TIGR00618 260 QLLKQLRAR------------------IEELRAQEAVLEETQERINRARKAAPLAA-HIKAVTQ-IEQQAQRIHTELQ-- 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 747811797 442 lkERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00618 318 --SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
388-491 |
9.17e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 388 IEEHLRQLEGQLEEKNQELARVRQREK-MNEDHNKRLSDTVDRLLSEsNERLQLHLKERMAALEEkntLIQELESSQRQI 466
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELtEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457
|
90 100
....*....|....*....|....*
gi 747811797 467 EEQHhhkgRLSEEIEKLRQEVDQLK 491
Cdd:COG2433 458 RREI----RKDREISRLDREIERLE 478
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
274-412 |
1.18e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 274 EELSSKHQR-----DLREALAQ-KEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ--- 344
Cdd:COG0497 209 EELEEERRRlsnaeKLREALQEaLEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRryl 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 345 -------ELLEVAEQKLQ---QTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:COG0497 289 dslefdpERLEEVEERLAllrRLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368
|
..
gi 747811797 411 QR 412
Cdd:COG0497 369 KK 370
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
850-914 |
1.74e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 38.02 E-value: 1.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747811797 850 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 914
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
326-487 |
2.00e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 326 LANKESLHRQCEEKARHLQELLEVAEQKLQQT---------MRKAEtlpeVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:COG1842 50 IANQKRLERQLEELEAEAEKWEEKARLALEKGredlarealERKAE----LEAQAEALEAQLAQLEEQVEKLKEALRQLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 397 GQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL---ESSQRQIEEQhHHK 473
Cdd:COG1842 126 SKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELaagDSLDDELAEL-EAD 203
|
170
....*....|....
gi 747811797 474 GRLSEEIEKLRQEV 487
Cdd:COG1842 204 SEVEDELAALKAKM 217
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
964-1019 |
2.20e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 747811797 964 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1042-1081 |
2.75e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.63 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 747811797 1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1081
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
230-452 |
2.78e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 230 ELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQK----EDMEERITTLEKRY 305
Cdd:pfam05483 545 NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnkniEELHQENKALKKKG 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI--AALTKAEE 383
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkRCQHKIAE 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 384 RHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALE 450
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILK 784
|
..
gi 747811797 451 EK 452
Cdd:pfam05483 785 DK 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-377 |
3.09e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747811797 305 YLaaqreatsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAA 377
Cdd:COG1579 112 IL----------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
267-483 |
3.37e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.86 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 267 RRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQEL 346
Cdd:pfam06008 25 TKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK---ATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 347 LEVAEQKLQQTMRKAETLPEVEAELAQRIAAltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 426
Cdd:pfam06008 102 NEKVATLGENDFALPSSDLSRMLAEAQRMLG----EIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 427 VDRLLSESNERLQ---LHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:pfam06008 178 LRDSLAEYEAKLSdlrELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
104-490 |
3.42e-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: 41.73 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 104 LKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLraaLERVTTLE 183
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL---QEQLRDKD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 184 EQLAGAHQQVSALQQGAGVRDGA--------AEEEGTVELGPKRLWKEDTGRVEELqELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNTDTAlttleealSEKERIIERLKEQREREDRERLEEL-ESLKKENKDLKEKVSALQPELTE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 256 VTELEEDL----------GTARRDLIKSEELSSKHQRD--------------LREALAQKEDMEERITTLEK-------- 303
Cdd:pfam10174 494 KESSLIDLkehasslassGLKKDSKLKSLEIAVEQKKEecsklenqlkkahnAEEAVRTNPEINDRIRLLEQevarykee 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 304 ---------RYLAAQREATSihDLNDKlENELANKESLH-RQCEEKARHLQELlevaeQKLQQTMRKAETlpeVEAELAQ 373
Cdd:pfam10174 574 sgkaqaeveRLLGILREVEN--EKNDK-DKKIAELESLTlRQMKEQNKKVANI-----KHGQQEMKKKGA---QLLEEAR 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 374 RIAALTKAEERHGNIEEhlrqLEGQLEEKNQELARVRQR----EKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAAL 449
Cdd:pfam10174 643 RREDNLADNSQQLQLEE----LMGALEKTRQELDATKARlsstQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAI 718
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 747811797 450 EEKNTLIQELESSQRQieeqhhhKGRLSEEIEKLRQEVDQL 490
Cdd:pfam10174 719 SEKDANIALLELSSSK-------KKKTQEEVMALKREKDRL 752
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-385 |
3.54e-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: 41.59 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 28 QLMVNMLDEREKLLESLRESQETLAATQSRLQDAihERDQLQRHLNSALPQEfATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREKAERYQALLKEKREY--EGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 108 RNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLE 183
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 184 EQLAGAHQQVSALQqgAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQARERLVTLTTTVTELeedL 263
Cdd:TIGR02169 343 REIEEERKRRDKLT--EEYAELKEELEDLRA------------ELEEVDKEFAETRDELKDYREKLEKLKREINEL---K 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 264 GTARRDLIKSEELSSKhQRDLREALAQKED----MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:TIGR02169 406 RELDRLQEELQRLSEE-LADLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 747811797 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI-------AALTKAEERH 385
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERY 537
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
262-493 |
3.84e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY------LAAQREA--TSIhdlnDKLENELANKESLH 333
Cdd:pfam06160 87 ALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLANRFSygPAI----DELEKQLAEIEEEF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 334 RQCEE--------KARHLQELLEVAEQKLQQTMRK--------AETLPEVEAELAQRIAALTKAEER--HGNIEEHLRQL 395
Cdd:pfam06160 163 SQFEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelKTELPDQLEELKEGYREMEEEGYAleHLNVDKEIQQL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 396 EGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQLH-----LKERMAALEEKNTLIQ-ELES-SQ 463
Cdd:pfam06160 243 EEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknlpeIEDYLEHAEEQNKELKeELERvQQ 319
|
250 260 270
....*....|....*....|....*....|...
gi 747811797 464 RQI---EEQHHHKGrLSEEIEKLRQEVDQLKGR 493
Cdd:pfam06160 320 SYTlneNELERVRG-LEKQLEELEKRYDEIVER 351
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
273-410 |
3.99e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 273 SEELSSKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039 45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747811797 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
266-491 |
4.72e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 266 ARRDLIKSEELSSKHQRDLREA-------LAQKEDMEERITTLEKRYL-------AAQREATSIHDLNDKLENELANKES 331
Cdd:pfam01576 796 AVKQLKKLQAQMKDLQRELEEArasrdeiLAQSKESEKKLKNLEAELLqlqedlaASERARRQAQQERDELADEIASGAS 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 332 LHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT---KAEERHGNIEEHLRQlegQLEEKNQEL-A 407
Cdd:pfam01576 876 GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELkA 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 408 RVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 487
Cdd:pfam01576 953 KLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRM 1032
|
....
gi 747811797 488 DQLK 491
Cdd:pfam01576 1033 KQLK 1036
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
169-493 |
4.94e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRD-----GAAEEEGTVELGPKRLW----------KEDTGR----V 228
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVeMAReleelSARESDLEQDYQAASDHlnlvqtalrqQEKIERyqedL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 229 EELQELLEKQNFELSQARERLVTLTttvteleedlgtARRDLIKSEELSSKHQ-RDLREALaqkeDMEERITTLEKRYLA 307
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAE------------ARLEAAEEEVDSLKSQlADYQQAL----DVQQTRAIQYQQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 308 AQREATSIHDLNDKlenELANKESLHRQCEEKARHLQELLEVAEQKLQqTMRKAETLPEVEAELAQRIAALTKAEERHGN 387
Cdd:COG3096 421 ALEKARALCGLPDL---TPENAEDYLAAFRAKEQQATEEVLELEQKLS-VADAARRQFEKAYELVCKIAGEVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 388 IEEHLRQ------LEGQLEEKNQELARVRQREKMNEDhnkrlsdtVDRLLSESNERLQLHLKERMAALEEKNTLIQELES 461
Cdd:COG3096 497 ARELLRRyrsqqaLAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350
....*....|....*....|....*....|..
gi 747811797 462 SQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-412 |
4.99e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQ 244
Cdd:COG3206 170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 245 ARERLVTLTTTVteleedlgtARRDLIKSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206 238 AEARLAALRAQL---------GSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 325 ELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:COG3206 299 QIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
....*...
gi 747811797 405 ELARVRQR 412
Cdd:COG3206 366 LYESLLQR 373
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
30-415 |
5.47e-03 |
|
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: 40.44 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220 15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG--TVELGpkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam19220 154 ALQRAEGELATARERLALLEQENRRLQALSEEQAaeLAELT--RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 256 VTELEEDLGTARRDL-IKSEELSSKH---QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKES 331
Cdd:pfam19220 232 LEEAVEAHRAERASLrMKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 332 LHrQCEEKARhlQELLEVAEqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEEHLRQLEGQ-------LEEKNQ 404
Cdd:pfam19220 312 QF-QEMQRAR--AELEERAE-----MLTKA---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANR 374
|
410
....*....|.
gi 747811797 405 ELARVRQREKM 415
Cdd:pfam19220 375 RLKEELQRERA 385
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-490 |
6.21e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 271 IKSEELSSKHQRDLREALAQKEDMEERITTLEK-------RYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL 343
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 344 QELLEVAEQKLQ--------------QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELarv 409
Cdd:TIGR04523 200 ELLLSNLKKKIQknkslesqiselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI---ISQLNEQISQLKKELTN 353
|
.
gi 747811797 490 L 490
Cdd:TIGR04523 354 S 354
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
320-491 |
6.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKA-EERHGNIEEHLRQL--E 396
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 397 GQ--------LEEKNQE--LARVRQREKMNEDHNKRLSDTVDrlLSESNERLQLHLKERMAALEE-KNTLIQELESSQRQ 465
Cdd:COG3883 99 GGsvsyldvlLGSESFSdfLDRLSALSKIADADADLLEELKA--DKAELEAKKAELEAKLAELEAlKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 747811797 466 IEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-491 |
6.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaAEEEGTVELGPKrlwKEDTGRVEELQELLE-- 236
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK--------AEEERKAEEARK---AEDAKKAEAVKKAEEak 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 237 KQNFELSQA-RERLVTLTTTVTELEEDLGTARRDLIKSEElsSKHQRDLREALAQKEDMEERITTLEKRYLAAQR---EA 312
Cdd:PTZ00121 1237 KDAEEAKKAeEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEA 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 313 TSIHDLNDKLENELANKESLHRQCEE-----------------KARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI 375
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEakkaaeaakaeaeaaadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 376 AALTKAEERHGNIEEHLRQLEgqlEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNErlqlhlKERMAALEEK 452
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAA---AKKKADEAKKKAEEKKKADEAKKKAEeakKADEAKKKAEE------AKKAEEAKKK 1465
|
330 340 350
....*....|....*....|....*....|....*....
gi 747811797 453 NTLIQELESSQRQIEEQHHHKgRLSEEIEKLRQEVDQLK 491
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAK 1503
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
35-490 |
6.85e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQ---LQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 112 RLLLEHLECLVS-RHERSLRMTVVKRQAQSPSGVSSEVEVLKalkslfEHHKALDEKVR--ERLRAALErvtTLEEQLAG 188
Cdd:pfam05557 97 SQLADAREVISClKNELSELRRQIQRAELELQSTNSELEELQ------ERLDLLKAKASeaEQLRQNLE---KQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 189 AHQQVSALQQGAGVRDGAAEEEGTVelgpkrlwKEDTGRVEELQELLEKQNFELSQARErlvtltttvteleedlgTARR 268
Cdd:pfam05557 168 AEQRIKELEFEIQSQEQDSEIVKNS--------KSELARIPELEKELERLREHNKHLNE-----------------NIEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 269 DLIKSEELSskhqrDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKarhLQELLE 348
Cdd:pfam05557 223 KLLLKEEVE-----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQL---QQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 349 VAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDH 419
Cdd:pfam05557 295 LKEENsslTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAilesydKELTMSNY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 420 NKRLSDTVdRLLSESNERLQLHLKE---RMAALEEK--------NTLIQELESSQRQieEQHHHKGRLSEEIEKLRQEVD 488
Cdd:pfam05557 375 SPQLLERI-EEAEDMTQKMQAHNEEmeaQLSVAEEElggykqqaQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLE 451
|
..
gi 747811797 489 QL 490
Cdd:pfam05557 452 TL 453
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
964-1008 |
7.00e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.51 E-value: 7.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 747811797 964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1008
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
274-490 |
8.33e-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: 40.42 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 274 EELSSKHQRDLREALAQKEDMEERITTLEKRY---LAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQEllev 349
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemLGLAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEE---- 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 350 aEQKLQQTMRKAETLPEVeaeLAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELArVRQREKMNEDHNKRLsdtvdR 429
Cdd:TIGR00606 770 -QETLLGTIMPEEESAKV---CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-VQQVNQEKQEKQHEL-----D 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747811797 430 LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-485 |
8.62e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEeegtvelgpkrlwkedtgRVEELQELLEKQNFELSQA 245
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------------------ALEKARALCGLPDLTPENA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 246 RERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQR--DLREALA---QKEDMEERITTL-----EKRYLAAQREAtsi 315
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayELVCKIAgevERSQAWQTARELlrryrSQQALAQRLQQ--- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 316 hdlndkLENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL 395
Cdd:COG3096 517 ------LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747811797 396 EGQLEEKNQELarvRQREKMNEDHNKRLSdtvdRLLSESNERLQlHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGR 475
Cdd:COG3096 587 LEQLRARIKEL---AARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAAR---KQA 655
|
330
....*....|
gi 747811797 476 LSEEIEKLRQ 485
Cdd:COG3096 656 LESQIERLSQ 665
|
|
| |
