|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
914-984 |
8.21e-43 |
|
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: 150.02 E-value: 8.21e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 914 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 984
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| 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 ... |
1001-1066 |
8.36e-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: 149.93 E-value: 8.36e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 1001 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1066
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| 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 ... |
1086-1157 |
3.19e-42 |
|
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: 148.62 E-value: 3.19e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 1086 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1157
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 ... |
1005-1064 |
9.52e-29 |
|
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: 109.55 E-value: 9.52e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 1005 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1064
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
921-979 |
1.22e-26 |
|
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: 103.46 E-value: 1.22e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528303 921 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 979
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1094-1155 |
2.22e-24 |
|
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: 97.23 E-value: 2.22e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 1094 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1155
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1086-1157 |
6.57e-22 |
|
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: 90.58 E-value: 6.57e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 1086 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1157
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-523 |
1.37e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 243 LSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERI 322
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 323 TTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAAL 402
Cdd:COG1196 305 ARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 403 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 482
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462528303 483 vESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:COG1196 455 -EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
915-979 |
2.03e-16 |
|
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: 74.80 E-value: 2.03e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528303 915 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 979
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
270-517 |
5.37e-16 |
|
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: 83.57 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 349
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 350 IANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERH-------GNIEERLRQMEAQ 422
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 423 LEEKNQELQRARQREKMNEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 499
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|....*...
gi 2462528303 500 LVLNIEALRAELDHMRLR 517
Cdd:TIGR02168 913 LRRELEELREKLAQLELR 930
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1086-1157 |
1.10e-15 |
|
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: 72.87 E-value: 1.10e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 1086 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1157
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 ... |
1000-1064 |
3.30e-15 |
|
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: 71.29 E-value: 3.30e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528303 1000 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1064
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 ... |
1000-1064 |
4.71e-15 |
|
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: 70.80 E-value: 4.71e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528303 1000 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1064
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
272-512 |
6.39e-15 |
|
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: 80.10 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIA 351
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 352 NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHG----NIEERLRQMEAQLEEKN 427
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaeleELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 428 QELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAALE--DKNSLLREVESAKKQLEETQHDKDQLVLNIE 505
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEELQEELERLEEALE 464
|
....*..
gi 2462528303 506 ALRAELD 512
Cdd:TIGR02168 465 ELREELE 471
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1000-1064 |
7.65e-13 |
|
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: 64.60 E-value: 7.65e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528303 1000 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1064
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-511 |
1.28e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 192 LEEELGATHKELMILKEQNNQKKTLTDGVLDinheqentpstsgkRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKE 271
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQ--------------ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD------------VREAMAQKEDMEERITTLEKRYLAAQREATSV 339
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 340 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLRQM 419
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----------ELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 420 EAQLEEknqelqrarQREKMNEehnkrlsdtvdklLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE---TQHD 496
Cdd:TIGR02169 895 EAQLRE---------LERKIEE-------------LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELS 952
|
330
....*....|....*
gi 2462528303 497 KDQLVLNIEALRAEL 511
Cdd:TIGR02169 953 LEDVQAELQRVEEEI 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-492 |
1.82e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 187 ERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQ 266
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 267 SQMKERLASLSSHVTELEEDLDTARKDLikseemnTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL 346
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEI-------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 347 ENEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAET-LPEVEAELAQRVAALSKAEERHGNIEERLRQMEaq 422
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESeLEALLNERASLEEALALLRSELEELSEELRELE-- 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528303 423 leEKNQELQRARQ--REKMNEEHNK--RLSDTVDKLLSESNERLQL---HLKERMAALEDKNSLLR-EVESAKKQLEE 492
Cdd:TIGR02168 908 --SKRSELRRELEelREKLAQLELRleGLEVRIDNLQERLSEEYSLtleEAEALENKIEDDEEEARrRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
268-511 |
1.99e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 268 QMKERLASLSSHVTELEEDLD-------TARKDLIKSEEMNtklQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVH 340
Cdd:COG1196 183 ATEENLERLEDILGELERQLEplerqaeKAERYRELKEELK---ELEAELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 341 DLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL----RKAETLPEVEAELAQRVAALSKAEERHGNIEERL 416
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiaRLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 417 RQMEAQLEEKNQELQRARQREkmnEEHNKRLSDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVESAKKQLEETQHD 496
Cdd:COG1196 340 EELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250
....*....|....*
gi 2462528303 497 KDQLVLNIEALRAEL 511
Cdd:COG1196 416 LERLEEELEELEEAL 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-463 |
2.51e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILK-EQNNQKKTLTdgvldinh 225
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLE-------- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 226 eqentpstsgkrssdgslSHEEDLAKVIELQEIISKQSReqsQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQ 305
Cdd:TIGR02168 828 ------------------SLERRIAATERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 306 RDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERL-ELAEQKLQQTLRK 384
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEAL 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 385 AETLPEVEAELAQRVAALSKAEERHGNI-----------EERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLS 448
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFK 1035
|
410
....*....|....*
gi 2462528303 449 DTVDKLlsesNERLQ 463
Cdd:TIGR02168 1036 DTFDQV----NENFQ 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-465 |
5.34e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 156 SEVEVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEELGATHKELMILK----EQNNQKKTLTDGVLDINHEQENTp 231
Cdd:TIGR02168 223 RELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIEELQKELYALANEISRL- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 232 sTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQmkERLASLSSHVTELEEDLDTArkdliksEEMNTKLQRDVREA 311
Cdd:TIGR02168 301 -EQQKQILRERLANLERQLEELEAQLEELESKLDELA--EELAELEEKLEELKEELESL-------EAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 312 MAQKEDMEERITTLEKRYLAAQREATSvhdlndkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKA--ETLP 389
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIAS-------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELE 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 390 EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 465
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-433 |
1.27e-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: 69.32 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168 257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 214 ktltdgvLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARK 292
Cdd:TIGR02168 314 -------LERQLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 293 DLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 373 LAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 433
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-662 |
1.31e-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: 69.32 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNvCREQLLEREEEIAELKAE----RNN 120
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQiaslNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 121 TRLLLEHLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 193
Cdd:TIGR02168 402 IERLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 194 EELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIE------LQEIISKqsREQS 267
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE--LISVDEGYEAAIEaalggrLQAVVVE--NLNA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 268 QMKErLASLSSH----VTELEEDLDTAR--------------------KDLIKSEE-----MNTKLQR-----DVREAMA 313
Cdd:TIGR02168 558 AKKA-IAFLKQNelgrVTFLPLDSIKGTeiqgndreilkniegflgvaKDLVKFDPklrkaLSYLLGGvlvvdDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 314 Q--KEDMEERITTLE-----KRYLAA-QREATSVHDLN-----DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ 380
Cdd:TIGR02168 637 LakKLRPGYRIVTLDgdlvrPGGVITgGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 381 TLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL------ 454
Cdd:TIGR02168 717 LRKELE---ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieq 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 455 -----------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:TIGR02168 794 lkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 524 GRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASV-LANVAQAFESDAdvSD 602
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEY--SL 951
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528303 603 GEDDRDTLLSSVDLLSPSGQADAHTLAMMLQE----QLDAInkeirliqEEKENTEQRAEEIES 662
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAI--------EEYEELKERYDFLTA 1007
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
914-978 |
3.42e-11 |
|
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: 59.93 E-value: 3.42e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 914 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 978
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
246-442 |
4.20e-11 |
|
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: 64.56 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 246 EEDLAKVIELQEIISkqsrEQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:COG1579 3 PEDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 326 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 405
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEK 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462528303 406 EERhgnIEERLRQMEAQLEEKNQElqRARQREKMNEE 442
Cdd:COG1579 144 KAE---LDEELAELEAELEELEAE--REELAAKIPPE 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-512 |
1.05e-10 |
|
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: 66.53 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618 417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 203 LMILKEQNNQKKTLTDGVLDINHE-QENTPSTSGKRSSDGSLSHEEDLakviELQEIISKQ--SREQSQMKERLASLSSH 279
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLR----KLQPEQDLQdvRLHLQQCSQELALKLTA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 280 VTELEEDLdtarkdlikseemntkLQRDVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEnEIANKDSMHR- 358
Cdd:TIGR00618 648 LHALQLTL----------------TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRe 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 359 --QTEDKNRQLQERLELAEQKLQQTLR-KAETLPEVEAEL-AQRVAALSKAEERHGNIEER----------LRQMEAQLE 424
Cdd:TIGR00618 709 leTHIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTEAHFNNNEEvtaalqtgaeLSHLAAEIQ 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 425 EKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNI 504
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
....*...
gi 2462528303 505 EALRAELD 512
Cdd:TIGR00618 869 AKIIQLSD 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-512 |
1.23e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:PRK02224 233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 238 SSDGS--LSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQ 314
Cdd:PRK02224 306 DADAEavEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAE 394
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 395 L--AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------L 464
Cdd:PRK02224 461 VegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraE 540
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462528303 465 HLKERMAALEDKNSLLRevESAKKQLEETQhDKDQLVLNIEALRAELD 512
Cdd:PRK02224 541 ELRERAAELEAEAEEKR--EAAAEAEEEAE-EAREEVAELNSKLAELK 585
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
38-508 |
1.27e-10 |
|
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: 66.22 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 189 CSLLEE--ELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPStsgkRSSDGSLSHEEDLAKVIELQEIISKQSREQ 266
Cdd:TIGR00606 511 ADLDRKlrKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKS----RHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 267 SQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 343
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELA----QRVAALSKAEERHGNIEERLRQ 418
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIIDLKEKE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 419 MEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE------RMAALEDKNSLLREV 483
Cdd:TIGR00606 746 IP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDverkiaQQAAKLQGSDLDRTV 824
|
490 500
....*....|....*....|....*
gi 2462528303 484 ESAKKQLEETQHDKDQLVLNIEALR 508
Cdd:TIGR00606 825 QQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-508 |
1.38e-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: 65.86 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 233 TSGKRSSDG-SLSHEEDLAKVIELQEIISKqsreqsqMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA 311
Cdd:TIGR02169 656 TGGSRAPRGgILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 312 MAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLELAEQKLQQtlrkaETLPEV 391
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNDLEARLSH-----SRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 392 EAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRArqREKMNEEHNKRLS-----DTVDKLLSESN---ERLQ 463
Cdd:TIGR02169 797 QAE-------LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDlkeqiKSIEKEIENLNgkkEELE 867
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462528303 464 LHLKERMAALED----KNSLLREVESAKKQLEETQHDKDQLVLNIEALR 508
Cdd:TIGR02169 868 EELEELEAALRDlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-509 |
4.72e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 249 LAKVIE---LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTL 325
Cdd:PRK04863 337 LNLVQTalrQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 326 EKR---YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-------------QTLRKAetLP 389
Cdd:PRK04863 410 QTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 390 EVEAELAQRVA--ALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLK 467
Cdd:PRK04863 488 EVSRSEAWDVAreLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQE 561
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462528303 468 ERMAALEDKNSllrEVESAKKQLEETQHDKDQLVLNIEALRA 509
Cdd:PRK04863 562 ELEARLESLSE---SVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-515 |
5.51e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSD--------------GSLSHEEDLAkvi 253
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcGRELTEEHRK--- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 254 elqEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqRDVREAMAQKEDMEERITTLEKRYL-AA 332
Cdd:PRK03918 452 ---ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEELeKK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 333 QREATSVHDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALSKAEER 408
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNE 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 409 HgnieERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKN-SLLREVESAK 487
Cdd:PRK03918 604 Y----LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlELSRELAGLR 679
|
410 420
....*....|....*....|....*...
gi 2462528303 488 KQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-492 |
7.04e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTL---TDGVLDINHEQE 228
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 229 NTpstsgkrsSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQR-- 306
Cdd:PRK03918 304 EY--------LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEle 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 307 --DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLR 383
Cdd:PRK03918 376 rlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKGKCPVCGRELTEEHRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 384 K-AETLPEVEAELAQRVAALSKAEERHGNIEE---------RLRQMEAQLEEKNQELqrarqrEKMNEEHNKRLSDTVDK 453
Cdd:PRK03918 456 EyTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKL------KKYNLEELEKKAEEYEK 529
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462528303 454 LLSESN--ERLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:PRK03918 530 LKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-523 |
7.68e-10 |
|
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: 63.50 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 192 LEEELGATHKELMILK-EQNNQKKTLTDGVLDINH------EQENTPSTSGKRSSDGSLSHEEDLAKviELQEIISKQSR 264
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKdEQNKIKKQLSEKQKELEQnnkkikELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 265 EQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREamaqKEDMEERIttlekrylaaQREATSVHDLND 344
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 345 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE 424
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 425 EKNQELQRARQREKMN-EEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDKNSLL----REVESAKKQLE------ET 493
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNlEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLkekiEKLESEKKEKEskisdlED 545
|
330 340 350
....*....|....*....|....*....|
gi 2462528303 494 QHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:TIGR04523 546 ELNKDDFELKKENLEKEIDEKNKEIEELKQ 575
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-521 |
1.33e-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: 62.77 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 282 ELEEDLDTARKDLIKSE----EMNTKLQRDVREA-MAQK-EDMEERITTLEKRYLAAQreatsVHDLNDKLENEIANKDS 355
Cdd:TIGR02168 176 ETERKLERTRENLDRLEdilnELERQLKSLERQAeKAERyKELKAELRELELALLVLR-----LEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 356 MHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 435
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 436 RekmNEEHNKRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSLLREVEsakKQLEETQHDKDQLVLNIEALRAELDH 513
Cdd:TIGR02168 331 K---LDELAEELAELEEKLeeLKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIER 404
|
....*...
gi 2462528303 514 MRLRGASL 521
Cdd:TIGR02168 405 LEARLERL 412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-492 |
2.61e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 125 LEHLEcLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 417 ERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIE--LQEIISKQSREQSQMKERLAS-LSSHVT 281
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAaaLQNIVVEDDEVAAAAIEYLKAaKAGRAT 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 282 ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERittleKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY-----YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 362 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHgniEERLRQMEAQLEEKNQELQRARQREKMNE 441
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA---LLAEEEEERELAEAEEERLEEELEEEALE 727
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 442 EHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-520 |
2.70e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 305 QRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 385 AETLpevEAELAQRVAALSK------------------AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 446
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528303 447 LSDTVDKlLSESNERLQLHLKERMAALedkNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGAS 520
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-442 |
3.24e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKElnvcreqllereeeiaelKAERNNTRLL 124
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKE------------------KREYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 125 LEHLEclvsrHERSLRmtvvkrqaqspagvssevEVLKALKSLFEHHKALDEKVRERLrvalERCSLLEEELGATHKELM 204
Cdd:TIGR02169 230 KEKEA-----LERQKE------------------AIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 205 ILKEqnNQKKTLTDGVLDINHEQENTpstsgKRSSDGSLSHEEDLA-KVIELQEIISKQ-------SREQSQMKERLASL 276
Cdd:TIGR02169 283 DLGE--EEQLRVKEKIGELEAEIASL-----ERSIAEKERELEDAEeRLAKLEAEIDKLlaeieelEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 277 SSHVTELEEDLDTARKDLiksEEMNTKLQRDVREAMAQKEDME---ERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:TIGR02169 356 TEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 354 DSMHRQTEDKNRQLQERLELAEQKLQQTlrkaetlpeveaelaqrVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 433
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
....*....
gi 2462528303 434 RQREKMNEE 442
Cdd:TIGR02169 496 EAQARASEE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-492 |
4.79e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 336 AtsvhdlnDKLENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEER 415
Cdd:COG4942 99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 416 LRQMEAQLEEKNQELQraRQREKMNEEHNKRlsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:COG4942 169 LEAERAELEALLAELE--EERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
285-515 |
5.55e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 285 EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlndkleNEIankdsmhrqtEDKN 364
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-----------NEI----------SSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMNE 441
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYI 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528303 442 EHNKRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQL---VLNIEALRAELDHMR 515
Cdd:PRK03918 297 KLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKKEELE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
303-494 |
5.69e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 303 KLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTL 382
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 383 RKAETLPEVEA--------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL 454
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462528303 455 LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 494
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
246-521 |
5.94e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqrdvreamaqkedmEERITTL 325
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------------------KEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 326 EKRylaaqreatsvhdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAAL 402
Cdd:PRK03918 244 EKE--------------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 403 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLL 480
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462528303 481 rEVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 521
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
250-442 |
6.00e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKR- 328
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARALYRSg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 329 ----YLAAQREATSVHDLNDKLE--NEI--ANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAET-LPEVEAELAQ 397
Cdd:COG3883 100 gsvsYLDVLLGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEAQQAE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462528303 398 RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 442
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-499 |
7.47e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEELGATHkelmiLKEQNNQKKtltdgvld 222
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAK-------- 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 223 iNHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERlASLSSHVTELEEdldtARK--DLIKSEEM 300
Cdd:PTZ00121 1484 -KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKKAEE----KKKadELKKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 301 ntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQLQERL 371
Cdd:PTZ00121 1558 --KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKV 1635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 372 ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTV 451
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462528303 452 DKLlsesnERLQLHLKERMAALEDknsLLREVESAKKQLEETQHDKDQ 499
Cdd:PTZ00121 1716 KKA-----EELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
265-523 |
9.21e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 265 EQSQMKERLASLSSHVTELEEdldtarkdlikseemntkLQRDVREAMAQKEDMEeRITTLEKRYLAAQREATSVHDLND 344
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER------------------AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 345 KLENEIAnkdsmhrqtEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNieERLRQMEAQLE 424
Cdd:COG4913 280 ALRLWFA---------QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 425 EKNQELQRARQREKmneehnkRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQlv 501
Cdd:COG4913 349 RLERELEERERRRA-------RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR-- 419
|
250 260
....*....|....*....|..
gi 2462528303 502 lNIEALRAELDHMRLRGASLHH 523
Cdd:COG4913 420 -ELRELEAEIASLERRKSNIPA 440
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-436 |
1.23e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 330 lAAQREATSVHDLNDKLENEIANKD------------SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 397
Cdd:COG4942 107 -AELLRALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462528303 398 RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 436
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
250-525 |
1.75e-08 |
|
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: 58.16 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERH 409
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 410 gniEERLRQMEAQLEEKNQELQRA-RQREKMNEEHNKRLSdTVDKLLSESNERL----QLhLKERMAALEDKNSLLREVE 484
Cdd:pfam19220 208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERA-SLRMKLEALTARAaateQL-LAEARNQLRDRDEAIRAAE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462528303 485 SAkkqLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 525
Cdd:pfam19220 283 RR---LKEASIERDTLERRLAGLEADLERRTQQFQEMQRAR 320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-535 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913 281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913 361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913 441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 218 DGVLDINHEQENTPSTSGKRSSDGSLSHEedlakvielqeIISKQSREQSQMKERLASLSSHVT-ELEEDLDTARKD--- 293
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAGK-----------LDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAitr 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 294 --LIKSE----EMNTklQRDVRE-------AMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLEN--EIANKDSMHR 358
Cdd:COG4913 580 agQVKGNgtrhEKDD--RRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 359 QTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRek 438
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR-- 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 439 mneehnkrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAEldHMRLRG 518
Cdd:COG4913 736 ------------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWP 801
|
570
....*....|....*..
gi 2462528303 519 ASLHHGRPHLGSVPDFR 535
Cdd:COG4913 802 AETADLDADLESLPEYL 818
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
156-464 |
2.31e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 156 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPST 233
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 234 SGK---------RSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLaslsshvtelEEDLDTARKDLIKSEEMNTKL 304
Cdd:pfam17380 346 RERelerirqeeRKRELERIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 305 QRDVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:pfam17380 416 QQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 373 LAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 446
Cdd:pfam17380 496 ILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
|
330
....*....|....*...
gi 2462528303 447 LSDTVDKLLSESNERLQL 464
Cdd:pfam17380 574 EREMMRQIVESEKARAEY 591
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
361-505 |
2.67e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.87 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 361 EDKNRQLQERLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 440
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528303 441 EEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEsakkqlEETQHDKDQLVLNIE 505
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
250-514 |
5.12e-08 |
|
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: 57.49 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 250 AKVIELQEIISKQSR-EQSQMKERLASLSSHVTELEEDLDTARK---DLIKS----EEMNTKLQRDVREAMAQKEDMEER 321
Cdd:pfam01576 327 QEVTELKKALEEETRsHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 322 -------ITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--QTLRKAETLPEVe 392
Cdd:pfam01576 407 rkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 393 aelaqrvaalskaeerhgNIEERLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAA 472
Cdd:pfam01576 486 ------------------NLSTRLRQLE---DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEAL 543
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462528303 473 LEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM 514
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
175-512 |
6.95e-08 |
|
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: 57.05 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 175 DEKVRERLRVALERcSLLEEELGATHKELMiLKEQNNQKKTLTDGVLdiNHE---QENTPSTSGKRSSDGSLSHEEDLAK 251
Cdd:pfam15921 136 ESQSQEDLRNQLQN-TVHELEAAKCLKEDM-LEDSNTQIEQLRKMML--SHEgvlQEIRSILVDFEEASGKKIYEHDSMS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 252 VIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEerITTLEKRYLA 331
Cdd:pfam15921 212 TMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 332 AQREATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLpeveaelaqrvaalskaeerhgn 411
Cdd:pfam15921 290 ARSQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRM----------------------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 412 IEERLRQMEAQLEEKNQELQRAR-------------------------QREK---MNEEHNKRLSD-------TVDKLLS 456
Cdd:pfam15921 340 YEDKIEELEKQLVLANSELTEARterdqfsqesgnlddqlqklladlhKREKelsLEKEQNKRLWDrdtgnsiTIDHLRR 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528303 457 ESNER-----------------LQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam15921 420 ELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-469 |
6.99e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717 167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 200 HKELMILKEQNNQKKT-----LTDGVLDINHEQENTPSTSGKRSSDGSLsheedLAKVIELQEIISKQSREQSQMKERLA 274
Cdd:COG4717 233 ENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFL-----VLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 275 SLSSHVTELE-EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:COG4717 308 QALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 354 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 425
Cdd:COG4717 388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462528303 426 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 469
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-476 |
8.44e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 146 RQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL-MILKEQNNQKKTLTDGVLDIN 224
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 225 H-EQENTPSTSGKRSSDGSLSH-EEDLAKVIE---------LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKD 293
Cdd:TIGR02169 748 SlEQEIENVKSELKELEARIEElEEDLHKLEEalndlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 294 LIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREA----TSVHDLNDKLEN---EIANKDSMHRQTEDKNRQ 366
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleAALRDLESRLGDlkkERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 367 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA----------LSKAEERHGNIEERLRQMEAQLEEKNQELqrarqr 436
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEY------ 981
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462528303 437 ekmnEEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDK 476
Cdd:TIGR02169 982 ----EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-496 |
1.12e-07 |
|
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: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 55 RETQETLALTQGKLHevGHERDSLQRQLNTALpQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLeclvsr 134
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 135 heRSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKK 214
Cdd:COG1196 287 --QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 215 TLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDL 294
Cdd:COG1196 365 EALLEAEAELAEAE-------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 295 IKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA 374
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 375 EQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKN------QELQRARQREKMNEEHNKRLS 448
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAALAAALARGAI 597
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462528303 449 DTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHD 496
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-515 |
1.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 125 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSRE--QSQMKERLASLSSHVTE 282
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 283 LEEDLDTARKDLIKSEEMNTK--------------LQRDVREAMAQ--------KEDMEERITTLEKRyLAAQREATSVH 340
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEaayeaaleaalaaaLQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 341 DLNDKLENEIANKDSMHRQTEDKNRQLQERL-------ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIE 413
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 414 ERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEET 493
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500
....*....|....*....|..
gi 2462528303 494 QHDKDQLVLNIEALRAELDHMR 515
Cdd:COG1196 752 ALEELPEPPDLEELERELERLE 773
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-655 |
1.78e-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: 55.89 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 68 LHEVGHERDSLQRQLNTA-----------------LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLEC 130
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESnelhekqkfylrqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 131 LVSR--HERSLRMTVVKRQAQSPAGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRVALERCSLLEEE 195
Cdd:pfam15921 160 LKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 196 LGATHKELMILKEQNNQKKTL-----TDGV--LDINHEQENTPST---SGKRSSDGSLSHEedlakvielQEIISKQSRE 265
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELllqqhQDRIeqLISEHEVEITGLTekaSSARSQANSIQSQ---------LEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 266 QSQMKER-LASLSSHVTELEEDLDTARKD-------------LIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKRY 329
Cdd:pfam15921 311 QNSMYMRqLSDLESTVSQLRSELREAKRMyedkieelekqlvLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ-----------------ERLELAEQKLQQTLRKA------- 385
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQrleallkamksecqgqmERQMAAIQGKNESLEKVssltaql 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 386 ----ETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE- 460
Cdd:pfam15921 471 estkEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEc 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 461 ---RLQLHLKERM-----------------------AALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM 514
Cdd:pfam15921 551 ealKLQMAEKDKVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 515 RLRGASL-HHGRPHLGSVPDF---RFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQ-TLNEQDWERAQQASVLAN 589
Cdd:pfam15921 631 ELEKVKLvNAGSERLRAVKDIkqeRDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQ 710
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 590 VAQAFESdADVSDGEDDRDTLLSSVDLLSPSGQADA-HTLAMMLQEQLDAINKEIRLIQEEKENTEQ 655
Cdd:pfam15921 711 TRNTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1087-1157 |
1.99e-07 |
|
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: 49.22 E-value: 1.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 1087 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1157
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
315-521 |
2.15e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.69 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 393
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 394 ELAQRVAALSkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLSDTVDKLLSESN--ERLQLHLKERMA 471
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYANSQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 472 ALEDKNSLLREVESAKKQLEETQhdKDQLVLNIEALRAELDHMR--LRGASL 521
Cdd:PRK11281 171 RLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQRksLEGNTQ 220
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-492 |
2.56e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 45 EERDRLLDTLRETQETlaltQGKLHEVGHERDSLQRQLNT--ALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:PRK03918 197 EKEKELEEVLREINEI----SSELPELREELEKLEKEVKEleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 123 LLLEHLECLVSRHE--RSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRErLRVALERCSLLEEELGATH 200
Cdd:PRK03918 273 KEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 201 KELMILKEqnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKV-IELQEIISKQSREQSQMKERLASLSSH 279
Cdd:PRK03918 352 KRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 280 VTELE-----------EDLDTARKDLIK--SEEMNtKLQRDVREAMAQKEDMEERITTLEKrYLAAQREATSVHDLNDKL 346
Cdd:PRK03918 428 IEELKkakgkcpvcgrELTEEHRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 347 EN-----EIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQM-- 419
Cdd:PRK03918 506 KEleeklKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgf 584
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 420 --EAQLEEKNQELqrarqrEKMNEEHNkRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSllrEVESAKKQLEE 492
Cdd:PRK03918 585 esVEELEERLKEL------EPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEK---RLEELRKELEE 651
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
304-662 |
2.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 304 LQRDVREAMAQKEDMEERIttlekrylaaqrEATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLR 383
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEK------------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 384 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL--------- 454
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrdeelrd 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 455 -LSESNERLQLH------LKERMAALEDKNSLLRE--------VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRga 519
Cdd:PRK02224 329 rLEECRVAAQAHneeaesLREDADDLEERAEELREeaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 520 slhhgrphLGSVPDFRFPMADGHTDSYSTSAVLRrpqkGRLAALRDEPSKVQTLNE--------QDWERAQQASVLANVA 591
Cdd:PRK02224 407 --------LGNAEDFLEELREERDELREREAELE----ATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDR 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 592 QAFES-DADVSDGEDDRDTLLSSVDLLSPSGQADAHtlAMMLQEQLDAINKeirLIQEEKENTEQRAEEIES 662
Cdd:PRK02224 475 ERVEElEAELEDLEEEVEEVEERLERAEDLVEAEDR--IERLEERREDLEE---LIAERRETIEEKRERAEE 541
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1009-1064 |
4.80e-07 |
|
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: 48.06 E-value: 4.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 1009 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1064
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
914-980 |
4.90e-07 |
|
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: 48.06 E-value: 4.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 914 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 980
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-492 |
5.73e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 154 VSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMI------LKEQNNQKKTLTDGVLDINHEQ 227
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLeeytaeLKRIEKELKEIEEKERKLRKEL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 228 ENTPSTSGKRSSdgsLSHEEDLAKVI-ELQEIISKQSREQ-SQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLq 305
Cdd:PRK03918 483 RELEKVLKKESE---LIKLKELAEQLkELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL- 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 306 rdvREAMAQKEDMEERITTLEKRYLaaQREATSVHDLNDKLEN--EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLR 383
Cdd:PRK03918 559 ---AELEKKLDELEEELAELLKELE--ELGFESVEELEERLKElePFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 384 K-AETLPEVEaELAQRVAALSK--AEERHGNIEERLRqmeaqleEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesne 460
Cdd:PRK03918 634 ElAETEKRLE-ELRKELEELEKkySEEEYEELREEYL-------ELSRELAGLRAELEELEKRREEIKKTLEKL------ 699
|
330 340 350
....*....|....*....|....*....|..
gi 2462528303 461 rlqlhlKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:PRK03918 700 ------KEELEEREKAKKELEKLEKALERVEE 725
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
36-439 |
7.07e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.15 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220 5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQ-EIISKQ 262
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEgQLAAEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 263 SREQSQMKERLASLSSHVTE---LEEDLDTARKDLIKSEEMNTklqrdvrEAMAQKEDMEERITTLEKRYLAAQREATSV 339
Cdd:pfam19220 223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 340 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 419
Cdd:pfam19220 296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358
|
410 420
....*....|....*....|....*..
gi 2462528303 420 E-------AQLEEKNQELQRARQREKM 439
Cdd:pfam19220 359 TkrfeverAALEQANRRLKEELQRERA 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-453 |
7.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 197 GATHKELmiLKEQNNQKKTLtDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASL 276
Cdd:COG1196 559 AAAAIEY--LKAAKAGRATF-LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 277 SSHVTELEEDLDTARKDL-----------IKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGeggsaggsltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 346 LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNI-----------EE 414
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeyeelEE 795
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462528303 415 RLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 453
Cdd:COG1196 796 RYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
282-474 |
9.45e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 282 ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 362 D--KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLR-QMEAQLEEKNQELQRARQREK 438
Cdd:COG4717 130 LyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462528303 439 MNEEHNKRLSDTVDKLLSE----SNERLQLHLKERMAALE 474
Cdd:COG4717 210 ELEEELEEAQEELEELEEEleqlENELEAAALEERLKEAR 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
354-515 |
1.09e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 354 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQEL-QR 432
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 433 ARQREKmneehNKRLSDTVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRA 509
Cdd:COG3883 92 ARALYR-----SGGSVSYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
....*.
gi 2462528303 510 ELDHMR 515
Cdd:COG3883 165 ELEAAK 170
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-511 |
1.63e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 124 LLEHLECLVSRH--------ERSLRMTVVKRQAQSPAGVsSEVEVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEE 195
Cdd:PRK02224 329 RLEECRVAAQAHneeaeslrEDADDLEERAEELREEAAE-LESELEEAREAVEDRREEIEE-LEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 196 LGATHKEL-MILKEQNNQKKTLTDGVLDINHEQENTPST-----SGKRSSDGSLSHEEDLAKVIElqeiiskQSREQ-SQ 268
Cdd:PRK02224 407 LGNAEDFLeELREERDELREREAELEATLRTARERVEEAealleAGKCPECGQPVEGSPHVETIE-------EDRERvEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 269 MKERLASLSSHVTELEEDLDTArKDLIKSE-EMNTKLQR--DVREAMAQK----EDMEERITTLEKR------------- 328
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERA-EDLVEAEdRIERLEERreDLEELIAERretiEEKRERAEELRERaaeleaeaeekre 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 329 -----YLAAQREATSVHDLNDKLEneiANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 403
Cdd:PRK02224 559 aaaeaEEEAEEAREEVAELNSKLA---ELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 404 kaeERHGNIEERLRqmEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKERMAALEDKNS 478
Cdd:PRK02224 634 ---ERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRERREALENRVE 708
|
490 500 510
....*....|....*....|....*....|...
gi 2462528303 479 LLREVESAKKQLEETQHDkdqlvlnieaLRAEL 511
Cdd:PRK02224 709 ALEALYDEAEELESMYGD----------LRAEL 731
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1009-1060 |
1.82e-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: 46.08 E-value: 1.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 1009 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1060
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-512 |
1.94e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 192 LEEELGATHKELMILKEQNNQKKtltdgvldinheQENTPSTSGKRSSDGSLSHEEDLAKviELQEIISKQSREQSQMKE 271
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYK------------QEIKNLESQINDLESKIQNQEKLNQ--QKDEQIKKLQQEKELLEK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 272 RLASLSSHVTELEEDLdtarKDLiksEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlnDKLENEIA 351
Cdd:TIGR04523 427 EIERLKETIIKNNSEI----KDL---TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL-------EQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 352 NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERHGNIEERLR--QMEAQLEEKNQE 429
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 430 LQRARQREKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMAA-LED----------------------KNSLLREVES 485
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKISsLEKelekakkeneklssiiknikskKNKLKQEVKQ 649
|
330 340
....*....|....*....|....*..
gi 2462528303 486 AKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:TIGR04523 650 IKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
254-384 |
2.25e-06 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 49.52 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 254 ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA-MAQKEDMEERITTLEKRYLAA 332
Cdd:pfam15619 57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528303 333 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:pfam15619 137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
303-475 |
3.38e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 303 KLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTL 382
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--------NV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 383 RKAETLPEVEAELAQrvaalskAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERL 462
Cdd:COG1579 86 RNNKEYEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 2462528303 463 QLHLKERMAALED 475
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-512 |
3.63e-06 |
|
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: 51.71 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 244 SHEEDLakvIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEErit 323
Cdd:pfam01576 135 KLEEDI---LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 324 tlEKRYLaaQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAET-LPEVEAELAQRV 399
Cdd:pfam01576 209 --AKRKL--EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESER 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 400 AALSKAEERHGNIEERLRQMEAQLEEK------NQELQRARQRE--------------------KMNEEHNKRLSDTVDK 453
Cdd:pfam01576 285 AARNKAEKQRRDLGEELEALKTELEDTldttaaQQELRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQ 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 454 LlsESNERLQLHLKERMAALEDKNSLLR-EVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam01576 365 L--EQAKRNKANLEKAKQALESENAELQaELRTLQQAKQDSEHKRKKLEGQLQELQARLS 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-513 |
5.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 124 LLEHLECLVSRHERSLRMTVVKRQ-AQSPAGVSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEELEELEAELaelQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 200 HKE-----LMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLA 274
Cdd:COG4717 197 LAEeleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 275 SLSSHVTELeedLDTARKDLIKSEEMNTKLQRDVREAMAQKE-DMEERITTLEKRYLAAQREATSVHDLNDKleneIANK 353
Cdd:COG4717 277 GVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDR----IEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 354 DSMHRQTEDKNRQLQerLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEErhgnIEERLRQMEAQLEEKNQELQRA 433
Cdd:COG4717 350 QELLREAEELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 434 RQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAALEDKNSL---LREVESAKKQLEETQHDKDQLVLNIE 505
Cdd:COG4717 422 LEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELaelLQELEELKAELRELAEEWAALKLALE 500
|
....*...
gi 2462528303 506 ALRAELDH 513
Cdd:COG4717 501 LLEEAREE 508
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
254-457 |
6.39e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.46 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 254 ELQEIISKQSREQSQMKERLASLSSHVTELE---------EDLDTARKDLIKSEemntKLQRDVREAMAQKEDMEERITT 324
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAE----KLREALQEALEALSGGEGGALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 325 LekryLA-AQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ----------ERLELAEQKLQ---QTLRK----AE 386
Cdd:COG0497 245 L----LGqALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvtVE 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 387 TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmneEHNKRLSDTVDKLLSE 457
Cdd:COG0497 321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARK------KAAKKLEKAVTAELAD 385
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
175-486 |
6.74e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIE 254
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE---YLESEEINKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 255 LQEIISKQSreqsQMKERLASLSShvteleEDLDTARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTLEKRylaAQR 334
Cdd:PRK01156 541 LKDKHDKYE----EIKNRYKSLKL------EDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESR---LQE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErLELAEQKLQQTLrkaETLPEVEAELAQRVAALSKAEERHGNIEE 414
Cdd:PRK01156 606 IEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIED 681
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 415 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVESA 486
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
255-515 |
7.61e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 255 LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQR 334
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 414
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 415 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 494
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260
....*....|....*....|.
gi 2462528303 495 HDKDQLVLNIEALRAELDHMR 515
Cdd:COG4372 269 VEKDTEEEELEIAALELEALE 289
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-335 |
7.75e-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: 50.45 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 44 LEERDRLLDTLRETQETLALTQGKLHE-----VGHERDSLQRQLnTALPQEFAALTKELNVCREQLLEREEEIAELKAER 118
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALErqkeaIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 119 NNT-RLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEVEV--------LKALKSLFEHHKALDEKVRERLRVALERC 189
Cdd:TIGR02169 289 QLRvKEKIGELEAEIASLERSIA--EKERELEDAEERLAKLEAeidkllaeIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 190 SLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQEntpstsgkrssdgSLSHEEDlakviELQEIISKQSREQSQM 269
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLE---KLKREIN-------------ELKRELD-----RLQEELQRLSEELADL 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
207-499 |
9.02e-06 |
|
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: 49.42 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 207 KEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHE-----EDLAKVIELQEIISKQSREQSQMKERLASLSSHVT 281
Cdd:pfam15905 25 KSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKsqknlKESKDQKELEKEIRALVQERGEQDKRLQALEEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 282 ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEE-----------RITTLEKRYLAAQREAT--SVHDLNDKLEN 348
Cdd:pfam15905 105 KVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAkfsedgtqkkmSSLSMELMKLRNKLEAKmkEVMAKQEGMEG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 349 EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlrKAETLpeveaELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 428
Cdd:pfam15905 185 KLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKND 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 429 ELQRARQREKMNEEHNKRLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREVESAKKQ--LEETQHDKDQ 499
Cdd:pfam15905 258 EIESLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTLNAELEELKEKltLEEQEHQKLQ 327
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
245-516 |
9.66e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 245 HEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITT 324
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 325 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAA 401
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 402 L-----SKAEERHGNIEE----RLR--QMEAQLEEKN-----------QELQRARQREKMNEEHNKRLSDTVDKLlsesN 459
Cdd:pfam07888 256 LgeelsSMAAQRDRTQAElhqaRLQaaQLTLQLADASlalregrarwaQERETLQQSAEADKDRIEKLSAELQRL----E 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 460 ERLQlhlKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRL 516
Cdd:pfam07888 332 ERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-496 |
9.97e-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: 50.22 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128 231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRS-SDGSLSHEEDL--AKVIELQEIISK 261
Cdd:pfam12128 384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEfNEEEYRLKSRLgeLKLRLNQATATP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 262 QSREQ--------SQMKERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRylaaq 333
Cdd:pfam12128 461 ELLLQlenfderiERAREEQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 334 reatsVHDLNDKLENEIAN-KDS---------MHR----------QTEDKNRQLQERLELAEQKLQQTLRKAETLpevEA 393
Cdd:pfam12128 533 -----AGTLLHFLRKEAPDwEQSigkvispelLHRtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEEEL---RE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 394 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllSESNERLQLHlKERMAAL 473
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERK 677
|
490 500
....*....|....*....|...
gi 2462528303 474 EDKNSLLREVESAKKQLEETQHD 496
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQA 700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
115-521 |
1.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 115 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKA--LKSLFEHHKALDEKVR-ERLRVALERCSL 191
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKaEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 192 LEEelgaTHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELqeiisKQSREQSQMKE 271
Cdd:PTZ00121 1324 AEE----AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-----KKKAEEKKKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQrDVREAMAQKEDMEERITTLEKRYLAaqREATSVHDLNDKLEnEIA 351
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE-EAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 352 NKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVE----AELAQRVAALSKAEERHGNIEERLRQMEAQLEE 425
Cdd:PTZ00121 1471 KADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADeakkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 426 --KNQELQRARQR----EKMNEEHNKRLSDTVDKLLSESNER-----LQLHLKERMAALED---------KNSLLREVES 485
Cdd:PTZ00121 1551 lkKAEELKKAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEArieevMKLYEEEKKMKAEEakkaeeakiKAEELKKAEE 1630
|
410 420 430
....*....|....*....|....*....|....*.
gi 2462528303 486 AKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 521
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-525 |
1.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 342 LNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME- 420
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEk 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 421 ---------------AQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVES 485
Cdd:COG4717 124 llqllplyqelealeAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462528303 486 AKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 525
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
365-506 |
1.34e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 47.57 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 365 RQLQERLELAEQKLQQTLRKAETLP----------------EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 428
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 429 ELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEsakkqlEETQHDKDQLVLNIE 505
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
.
gi 2462528303 506 A 506
Cdd:pfam12072 176 E 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-500 |
1.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARK--DLIKSEEMNTKLQRDVREAMAQKEDMEERIT 323
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 324 TLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 403
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 404 KAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEhnKRLSDTVDKLLSESN--ERLQLHLKERMAA--LE 474
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAkkkadEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKkaEEAKKKAEEAKKAdeAK 1476
|
250 260
....*....|....*....|....*.
gi 2462528303 475 DKNSLLREVESAKKQLEETQHDKDQL 500
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEA 1502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-515 |
1.83e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvLDINHEQENTPSTSGKRSSDGSLSHEED 248
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 249 LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQ--RDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 327 KRYlAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAALS 403
Cdd:PTZ00121 1504 KAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 404 KAEE----RHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALE 474
Cdd:PTZ00121 1582 KAEEakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462528303 475 DKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-496 |
2.18e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 247 EDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLI----------KSEEMNTKLQRDVR-EAMAQK 315
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekkmKAEEAKKAEEAKIKaEELKKA 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 316 EDMEERITTLEKRYLAAQREATSVHDLNDklENEIANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVEA 393
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 394 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtVDKLLSESNERLQLHLKERMAAL 473
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVI 1781
|
250 260
....*....|....*....|...
gi 2462528303 474 EDKnsLLREVESAKKQLEETQHD 496
Cdd:PTZ00121 1782 EEE--LDEEDEKRRMEVDKKIKD 1802
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
250-485 |
2.24e-05 |
|
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: 48.89 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 330 LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKAEERH 409
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKV-------NDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQ 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528303 410 GNIEERLRQMEAQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVES 485
Cdd:TIGR00606 994 EKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
400-517 |
2.39e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 400 AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--ALE 474
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462528303 475 DKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 517
Cdd:COG1842 92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-511 |
3.13e-05 |
|
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: 48.18 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 34 SHFEQLMVSMleerDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTK-ELNVCREQLLEREEeia 112
Cdd:pfam05483 296 KELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfEATTCSLEELLRTE--- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 113 ELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRqaqspagvSSEVEVLKALKSLFEHHKALDEKvrerlrvalERCSLL 192
Cdd:pfam05483 369 QQRLEKNEDQLKIITME-LQKKSSELEEMTKFKN--------NKEVELEELKKILAEDEKLLDEK---------KQFEKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 193 EEELGATHKELMILKEQNNQKktltdgVLDInhEQENTPSTSgkrssdgslSHEEDLAKVIELQEIISKQSREQSQMKER 272
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKE------IHDL--EIQLTAIKT---------SEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 273 LASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTLEKRYLAAQREATSVHD----LNDKLEN 348
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLELKKHQE-------DIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 349 EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK---AEERHGNIEE-RLRQMEAQLE 424
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 425 EKNQEL-------QRARQREKMNEEH-------NKRLSDTVDKLLSESNERLQLHLKERMAALEDK----NSLLREVESA 486
Cdd:pfam05483 647 SAKQKFeeiidnyQKEIEDKKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHkhqyDKIIEERDSE 726
|
490 500
....*....|....*....|....*....
gi 2462528303 487 ----KKQLEETQHDKDQLVLNIEALRAEL 511
Cdd:pfam05483 727 lglyKNKEQEQSSAKAALEIELSNIKAEL 755
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
177-512 |
3.20e-05 |
|
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: 47.93 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTsgKRSSDGS--------LSH-EE 247
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLA--NRFSYGPaidelekqLAEiEE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 248 DLAKVIEL---------QEIISKQSRE----QSQMK--------------ERLASLSSHVTELEED------------LD 288
Cdd:pfam06160 161 EFSQFEELtesgdyleaREVLEKLEEEtdalEELMEdipplyeelktelpDQLEELKEGYREMEEEgyalehlnvdkeIQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 289 TARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIANKDSMHRQTEDKN 364
Cdd:pfam06160 241 QLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKK----YVEKNLPEIEDYLEHAEEQNKELKEEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--EKNQE-----LQRARQRE 437
Cdd:pfam06160 315 ERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEeiEEEQEefkesLQSLRKDE 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528303 438 KmneEHNKRLsDTVDKLLSESNERLQlhlKERMAALEDknSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam06160 395 L---EAREKL-DEFKLELREIKRLVE---KSNLPGLPE--SYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLD 460
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-474 |
3.47e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921 401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKE-------------------QNNQKK--------TL 216
Cdd:pfam15921 480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSrvdlklqelqhlknegdhlRNVQTEcealklqmAE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 217 TDGVLDINHEQ-ENTPSTSGK--RSSDGSLSHEEDLAKVI-----ELQEIISKQSREQSQMKERLASLSS---------- 278
Cdd:pfam15921 560 KDKVIEILRQQiENMTQLVGQhgRTAGAMQVEKAQLEKEIndrrlELQEFKILKDKKDAKIRELEARVSDlelekvklvn 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 279 -------HVTELEEDLD-------TARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKRYLAAQREATSVHDLND 344
Cdd:pfam15921 640 agserlrAVKDIKQERDqllnevkTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 345 KLE----NEIANKDSMHRQTEDKNRQ---LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLR 417
Cdd:pfam15921 717 SMEgsdgHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR 796
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 418 QMEAQLEEKNQELQRARQREKMneehnkRLSDTVDKLLSESNERLQLHLKERMAALE 474
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
321-517 |
4.21e-05 |
|
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: 46.53 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 321 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL------------ 388
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 389 -----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLLSESnerLQ 463
Cdd:pfam12795 76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 464 LHLKERMAALEDKNSLLRE--------VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 517
Cdd:pfam12795 152 WALQAELAALKAQIDMLEQellsnnnrQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-437 |
4.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAmaqKEDMEERITTLEKRYL 330
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 331 AAQR------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAET----- 387
Cdd:COG3883 94 ALYRsggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAakael 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528303 388 -------------LPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 437
Cdd:COG3883 174 eaqqaeqeallaqLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1087-1157 |
5.79e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.26 E-value: 5.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 1087 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1157
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
46-519 |
6.27e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNL-----ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 126 EHLEC----LVSRHERSLRMTVVKRQAQSPagVSSEVEVLKALKSLFEHHKAL-----------------DEKVRERLRV 184
Cdd:PRK01156 235 NNLKSalneLSSLEDMKNRYESEIKTAESD--LSMELEKNNYYKELEERHMKIindpvyknrnyindyfkYKNDIENKKQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 185 ALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIELQEIisKQSR 264
Cdd:PRK01156 313 ILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS--YLKSIESLKKKIEEYSK--NIER 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 265 EQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKR--------YLAAQREA 336
Cdd:PRK01156 389 MSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgtTLGEEKSN 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 337 TSVHDLNDK---LENEIANKDSMHRQTEDKNRQLQERLE-LAEQKLQQTLRKAETLPEVEAELAQ---RVAALSKAEERH 409
Cdd:PRK01156 469 HIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEYNKIESARADLEDikiKINELKDKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 410 GNIEERLRQMEAQ-LEEKNQELQRA-RQREKMNEEHNKRLSDTVDKLLSESNERLQlhlkERMAALEDKNS----LLREV 483
Cdd:PRK01156 549 EEIKNRYKSLKLEdLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLESRLQ----EIEIGFPDDKSyidkSIREI 624
|
490 500 510
....*....|....*....|....*....|....*.
gi 2462528303 484 ESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGA 519
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-510 |
7.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 236 KRSSDGSLSHEEDLAKVIELQEIiSKQSREQSQMKERlASLSSHVTELEEDLDTARK--DLIKSEEMNTKLQRDVREAMA 313
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKK-AEEAKKAEEAKKK-AEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 314 QKEDMEERITTLEKRYLAAQREATSVHDLND-KLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAETLP 389
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEKKKAEeakKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 390 EVE------------AELAQRVAALSKAEERHGNIE-----ERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD 452
Cdd:PTZ00121 1588 KAEearieevmklyeEEKKMKAEEAKKAEEAKIKAEelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528303 453 KLLSESNERLQLHLKERMAALEDKNSLLREVESAKKqLEETQHDKDQLVLNIEALRAE 510
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKKAEELKKA 1724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-517 |
7.60e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 346 LENEIANKDSMHRQTEDknrqLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEE 425
Cdd:PRK03918 174 IKRRIERLEKFIKRTEN----IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 426 KNQEL----QRARQREKMNEEHNKRLSDtvdklLSESNERLQlHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLV 501
Cdd:PRK03918 250 LEGSKrkleEKIRELEERIEELKKEIEE-----LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170
....*....|....*.
gi 2462528303 502 LNIEALRAELDHMRLR 517
Cdd:PRK03918 324 NGIEERIKELEEKEER 339
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
360-663 |
9.29e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 360 TEDKNRQLqERLEL-AEQKLQ-QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ-ELQRARQR 436
Cdd:COG1196 195 LGELERQL-EPLERqAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAElEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 437 EKMNEEhnkrlsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRL 516
Cdd:COG1196 274 LELEEL---------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 517 RGASLhhgrphlgsvpdfrfpmadghTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQA--SVLANVAQAF 594
Cdd:COG1196 345 ELEEA---------------------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLE 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528303 595 ESDADVSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 663
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
261-521 |
9.64e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 261 KQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQReatsvh 340
Cdd:TIGR00618 283 QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH------ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 341 dLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS-------------KA 405
Cdd:TIGR00618 357 -IRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdlqgqlahakkqqEL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 406 EERHGNIEERLRQMEAQLEE-KNQELQRARQR---EKMNEEHNKRLSDTVDKLLSESNERLQLH------LKERMAALED 475
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKlEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGSCIHPNP 515
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462528303 476 KNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 521
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL 561
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
163-430 |
1.06e-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: 46.74 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 163 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTDGVLDINHEQENTPS------ 232
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEKESSLIDLKEHASSlassgl 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 233 --TSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlaSLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVRE 310
Cdd:pfam10174 514 kkDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNP---EINDRIRLLEQEVARYKEESGKAQAEVERLLGILRE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 311 AMAQKEDMEERITTLEKRYLAAQREATsVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPE 390
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLRQMKEQN-KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ 669
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462528303 391 VEAELAQRVAALSKA-EERHGNIE----ERLRQMEAQLEEKNQEL 430
Cdd:pfam10174 670 ELDATKARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
244-429 |
1.11e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.51 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 244 SHEEDLAKVIELQEIISKQ----SREQSQMKERLASLSSHVTELEEDLDTARKDliKSEEMNTKlqrdvreamaqkedme 319
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLmseiQQENKRLTEPLQKAQEEVEELRKQLENYEKD--KQSLKNLK---------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 320 ERITTLEKRYLAAQREATSVHDLNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQR 398
Cdd:pfam13851 92 ARLKVLEKELKDLKWEHEVLEQRFEKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEV 168
|
170 180 190
....*....|....*....|....*....|.
gi 2462528303 399 VAALSKAEERHGNIEERLRQMeaqLEEKNQE 429
Cdd:pfam13851 169 LAAANLDPDALQAVTEKLEDV---LESKNQL 196
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-435 |
1.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717 228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 204 MILKEQNNQKKTltdgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTEL 283
Cdd:COG4717 305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 284 EEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDK 363
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEE 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 364 NRQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALSKAEERHGnieeRLRQMEAQLEEKNQELQRARQ 435
Cdd:COG4717 448 LEELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
154-517 |
1.13e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 154 VSSEVEVLKALKSLFEHHKALD--EKVRERLRVALERCSLLEEELGATHKELMilkEQNNQKKTLTDGVldinheqENTP 231
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEaqRKAIQELQFENEKVSLKLEEEIQENKDLI---KENNATRHLCNLL-------KETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 232 STSGKRSSDGSLSHEEDLAKVIELQEIISKqsreqsqmkerlasLSSHVTELEEDLDTARKdlikseEMNTKLQRDVREA 311
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEK--------------MILAFEELRVQAENARL------EMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 312 MAQKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpev 391
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHL--- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 392 EAELAQRVAALSKAEERHGNIEERLR-----------QMEAQLEEKN--------------------QELQRA-RQREKM 439
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNkakaahsfvvtefeattcslEELLRTeQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 440 NEEHNKRLSDTVDKLLSESNERLQL------HLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDH 513
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
....
gi 2462528303 514 MRLR 517
Cdd:pfam05483 455 LEIQ 458
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-494 |
1.30e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 260 SKQSREQSQMKERLAslsshvTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKED---MEERITTLEKRYLAAQREA 336
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRA------DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 337 TSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA----------ELAQRVAALSKAE 406
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAarkaeeerkaEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 407 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESA 486
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
....*...
gi 2462528303 487 KKQLEETQ 494
Cdd:PTZ00121 1308 KKKAEEAK 1315
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-512 |
1.39e-04 |
|
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: 44.92 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 380 QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE----EHNKRLSDTVDKLL 455
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleieEVEARIKKYEEQLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528303 456 SESNER----LQL---HLKERMAALEDK-NSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:COG1579 84 NVRNNKeyeaLQKeieSLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
177-512 |
1.42e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTsgKRSSDGS--------LSH-EE 247
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLA--NRFSFGPaldelekqLENlEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 248 DLAKVIEL---------QEIISKQSREQSQMKERLASLSSHVTELE-------EDLDTARKDLIKS-------------E 298
Cdd:PRK04778 180 EFSQFVELtesgdyveaREILDQLEEELAALEQIMEEIPELLKELQtelpdqlQELKAGYRELVEEgyhldhldiekeiQ 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 299 EMNTKLQR--------DVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIANKDSMHRQTEDKNRQ 366
Cdd:PRK04778 260 DLKEQIDEnlalleelDLDEAEEKNEEIQERIDQLydilEREVKARK----YVEKNSDTLPDFLEHAKEQNKELKEEIDR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 367 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--EKNQE-----LQRARQREKm 439
Cdd:PRK04778 336 VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQEklsemLQGLRKDEL- 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528303 440 neEHNKRLsDTVDKLLSESNERLQlhlKERMAALEDknSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:PRK04778 415 --EAREKL-ERYRNKLHEIKRYLE---KSNLPGLPE--DYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLE 479
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
264-435 |
1.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 264 REQSQMKERLASLSSHVTELEEDLDTARKDLIK----------SEEMNTKLQR------DVREAMAQKEDMEERITTLEK 327
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 328 R------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE-LAQ 397
Cdd:COG3206 248 QlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEaLQA 327
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462528303 398 RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 435
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
127-484 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 127 HLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMIL 206
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 207 KEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEdLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEED 286
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL-KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 287 LDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 366
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 367 LQERLELAEQKLQQTLRKAETLPEVEaeLAQRVAALSKAEERHGNIEERLRQMEAQLEEK-----NQELQRARQREKMNE 441
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEEL--LLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlMAIEEFEEKEERYNK 992
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462528303 442 EH--NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVE 484
Cdd:pfam02463 993 DEleKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVF 1037
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
249-508 |
1.82e-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: 45.97 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 249 LAKVIE-LQEIISKQSREQSQMKERLASLS-------SHVTELEEDLdtARKDLIkSEEMNTKLQRDVREAMAQKEDMEE 320
Cdd:pfam10174 399 LQKKIEnLQEQLRDKDKQLAGLKERVKSLQtdssntdTALTTLEEAL--SEKERI-IERLKEQREREDRERLEELESLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 321 RITTLEKRYLAAQREAT----SVHDLNDK---LENEIANKDSMHRQTEDKNRQLQE---RLELAEQKLQQTLRKAETLPE 390
Cdd:pfam10174 476 ENKDLKEKVSALQPELTekesSLIDLKEHassLASSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVRTNPE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 391 V-------EAELAQRVAALSKAEERHGNIEERLRQME----------AQLEE------KNQELQRARQREKMNEEHNKRL 447
Cdd:pfam10174 556 IndrirllEQEVARYKEESGKAQAEVERLLGILREVEnekndkdkkiAELESltlrqmKEQNKKVANIKHGQQEMKKKGA 635
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 448 SDTVDKLLSESNER---LQLHLKERMAALEDKNSllrEVESAKKQLEETQ---HDKDQLVLNIEALR 508
Cdd:pfam10174 636 QLLEEARRREDNLAdnsQQLQLEELMGALEKTRQ---ELDATKARLSSTQqslAEKDGHLTNLRAER 699
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
160-664 |
1.85e-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: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 160 VLKALKSLFEHHKALDEK--VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELlrDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 238 SSDGSLS----HEEDLAKVIELQEIISKQSREQSQMKERL----ASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVR 309
Cdd:pfam02463 308 RKVDDEEklkeSEKEKKKAEKELKKEKEEIEELEKELKELeikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 310 EAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSM--HRQTEDKNRQLQERLELAEQKLqqtlrkaeT 387
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEELEKQEL--------K 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 388 LPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdTVDKLLSESNERLQLHLK 467
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG--VGGRIISAHGRLGDLGVA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 468 ERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPhLGSVPDFRFPMADGHTDSYs 547
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEA- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 548 TSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLAnvAQAFESDADVSDGEDDRDTLLSSVDLLSPSGQADaht 627
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE--GLAEKSEVKASLSELTKELLEIQELQEKAESELA--- 690
|
490 500 510
....*....|....*....|....*....|....*..
gi 2462528303 628 LAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRV 664
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV 727
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
364-502 |
1.91e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 364 NRQLQERLELAEQKLQQtlrkaetlpeVEAELAqRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-------- 435
Cdd:COG1566 78 PTDLQAALAQAEAQLAA----------AEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavs 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 436 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 502
Cdd:COG1566 147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTI 210
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
917-975 |
2.02e-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: 40.78 E-value: 2.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 917 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 975
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
245-460 |
2.10e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 245 HEEDLAKVIELQEI-----ISKQSREQSQMKERLASLSSHVTELEEDLDTARK-------DLIKSEEMNT-KLQRDVREA 311
Cdd:PRK05771 26 HELGVVHIEDLKEElsnerLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 312 MAQKEDMEERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEQKLQQTLRK------- 384
Cdd:PRK05771 106 EEEISELENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 385 ------AETLPEVEAELAQrvAALSKAE-ERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDKLLS 456
Cdd:PRK05771 181 vvvvvlKELSDEVEEELKK--LGFERLElEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEI 258
|
....
gi 2462528303 457 ESNE 460
Cdd:PRK05771 259 ELER 262
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-438 |
2.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 266 QSQMKERLASLSSHVTELEEDLDTARKDLIKSEE--MNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 343
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 344 DKLENEIA-NKDSMHRQTEDKN-RQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKAEERHGNIEERLRQME 420
Cdd:COG3206 243 AALRAQLGsGPDALPELLQSPViQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170
....*....|....*...
gi 2462528303 421 AQLEEKNQELQRARQREK 438
Cdd:COG3206 323 EALQAREASLQAQLAQLE 340
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
365-510 |
2.23e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 365 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQELQRARQREKMNEEHN 444
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 445 KRLSDTVDKllseSNERLQLHLKERmaaledkNSLLREVESAKKQLEETQHDKDQLVLNIEALRAE 510
Cdd:PRK12704 99 DRKLELLEK----REEELEKKEKEL-------EQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1009-1064 |
2.38e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 40.33 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 1009 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1064
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
251-422 |
2.49e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKR 328
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 329 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEE 407
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
170
....*....|....*
gi 2462528303 408 RHGNIEERLRQMEAQ 422
Cdd:COG3206 366 LYESLLQRLEEARLA 380
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
343-447 |
2.85e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 343 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-----AALSKAEERHGNIEERLR 417
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELR 594
|
90 100 110
....*....|....*....|....*....|...
gi 2462528303 418 QMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 447
Cdd:PRK00409 595 QLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
260-492 |
2.97e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 44.83 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 260 SKQSREQSQMKERLASLSShVTELEEDLdtARKDLIKseemntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATS- 338
Cdd:pfam15066 288 SGASQENCKTPDTEQSFES-LQPLEEDM--ALNEVLQ------KLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKq 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 339 ------VHDLNDKLENEIANKDSMHRQTEDKNRQLQ---ERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERH 409
Cdd:pfam15066 359 qvfvdiINKLKENVEELIEDKYNVILEKNDINKTLQnlqEILANTQKHLQESRKEKETL---QLELKKIKVNYVHLQERY 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 410 GN-IEERLR------QMEAQLEEKNQELQRARQrekMNEEHNKRLSDTVDKLLSESNERLQ--LHLKERMAALEDKNslL 480
Cdd:pfam15066 436 ITeMQQKNKsvsqclEMDKTLSKKEEEVERLQQ---LKGELEKATTSALDLLKREKETREQefLSLQEEFQKHEKEN--L 510
|
250
....*....|..
gi 2462528303 481 REVESAKKQLEE 492
Cdd:pfam15066 511 EERQKLKSRLEK 522
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
281-512 |
3.58e-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: 44.96 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 281 TELEEDLDTARKDLIKSEEMNTKLQrdVREAMAQKEDMEERI----TTLEKRYLAAQREATSVHDLNDKLENEIANKDSM 356
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIE--ETENLAELIIDLEELklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 357 HRQTEDKNRQLQERLElaeqklQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRqmeAQLEEKNQELQRARQR 436
Cdd:pfam02463 234 LNEERIDLLQELLRDE------QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL---KLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 437 EKMNEEHNKRlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam02463 305 LERRKVDDEE----KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
268-431 |
3.66e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.64 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 268 QMKERLASLSSHVTELEEDLDTARKDLIK---------SEEMNTKLQrDVREAMAQK-EDMEERIT-TLEKrylAAQREA 336
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDrleketealRERLQKDLE-EVRAKLEPYlEELQAKLGqNVEE---LRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 337 TSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTLrkAETLPEVEAELAQRVAALSK-----AEERHGN 411
Cdd:pfam01442 77 PYTEELRKRLNADA---EELQEKLAPYGEELRERLEQNVDALRARL--APYAEELRQKLAERLEELKEslapyAEEVQAQ 151
|
170 180
....*....|....*....|
gi 2462528303 412 IEERLRQMEAQLEEKNQELQ 431
Cdd:pfam01442 152 LSQRLQELREKLEPQAEDLR 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-353 |
4.42e-04 |
|
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: 43.98 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIEL 255
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM----EERITTLEKRYLA 331
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAE 217
|
170 180
....*....|....*....|..
gi 2462528303 332 AQREATSVHDLNDKLENEIANK 353
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
254-501 |
4.79e-04 |
|
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: 44.56 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 254 ELQEIiskqSREQSQMKERLASLSSHVTELEEDLDTARKDLikseemnTKLQRDVREAMA-QKEDMEERITTLEKRYLAA 332
Cdd:COG3096 837 ELAAL----RQRRSELERELAQHRAQEQQLRQQLDQLKEQL-------QLLNKLLPQANLlADETLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 333 QREATSVHDLNDKLEnEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALS--------- 403
Cdd:COG3096 906 QEAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSyedavgllg 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 404 --------------KAEERHGNIEERLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 465
Cdd:COG3096 981 ensdlneklrarleQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIR 1060
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462528303 466 LKERMAALEDKNSLLREVEsakKQLEETQHDKDQLV 501
Cdd:COG3096 1061 RDELHEELSQNRSRRSQLE---KQLTRCEAEMDSLQ 1093
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
366-511 |
5.67e-04 |
|
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: 42.99 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 366 QLQERLELAE--QKLQQTLRKAETLP----EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR--- 436
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 437 ----------EKMNEEHNKRLSDTVDKLLsESNERLQlHLKERMAALEDK-NSLLREVESAKKQLEETQHDKDQLVLNIE 505
Cdd:COG1579 85 vrnnkeyealQKEIESLKRRISDLEDEIL-ELMERIE-ELEEELAELEAElAELEAELEEKKAELDEELAELEAELEELE 162
|
....*.
gi 2462528303 506 ALRAEL 511
Cdd:COG1579 163 AEREEL 168
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
326-492 |
8.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 326 EKRYLAAQREAtsvhdlndkLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 405
Cdd:PRK04863 507 EQRHLAEQLQQ---------LRMRLSELEQRLRQQQRAERLLAE----FCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 406 EERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE----RLQLHLKERMAALEDknsllR 481
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDvteyMQQLLERERELTVER-----D 648
|
170
....*....|.
gi 2462528303 482 EVESAKKQLEE 492
Cdd:PRK04863 649 ELAARKQALDE 659
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
134-471 |
1.01e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 134 RHERSLRMTVvkRQAQSPAGVSSEVEVLKAlKSLFEHHKALDEKVRERLRvalERCSLLEEELGATHKELMILKEQNNQK 213
Cdd:pfam02029 13 RRAREERRRQ--KEEEEPSGQVTESVEPNE-HNSYEEDSELKPSGQGGLD---EEEAFLDRTAKREERRQKRLQEALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 214 K----TLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQ--SQMKERLASLSSHVTELEEDL 287
Cdd:pfam02029 87 KefdpTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENkwSTEVRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 288 DTARKDLIKSEEM---NTKLQRDVREAMAQKEDMEERITTLekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 364
Cdd:pfam02029 167 EEVPTENFAKEEVkdeKIKKEKKVKYESKVFLDQKRGHPEV-----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 365 RQLQerlelAEQKLQQTLRKAETLPEVEAE-LAQRVA-ALSKAEERHGNIEERLRQMEaqlEEKNQELQRARQREKMNEE 442
Cdd:pfam02029 242 VFLE-----AEQKLEELRRRRQEKESEEFEkLRQKQQeAELELEELKKKREERRKLLE---EEEQRRKQEEAERKLREEE 313
|
330 340
....*....|....*....|....*....
gi 2462528303 443 HNKRLSDTVDKLLSESNERLQLHLKERMA 471
Cdd:pfam02029 314 EKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
193-516 |
1.02e-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: 43.19 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 193 EEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSgkrssdgsLSHEEdlaKVIELQEIISKQ---SREQSQM 269
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--------AEAEQ---RIKELEFEIQSQeqdSEIVKNS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 270 KERLASLSshvtELEedldtarKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEkRYLAAQREATSVHDLNDKLENE 349
Cdd:pfam05557 193 KSELARIP----ELE-------KELERLREHNKHLNENIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 350 I---ANKDSMH----RQTEDKNRQ----LQERLELAEQK---LQQTLRKAETLPEVEAELAQ---RVAALSKAEERHGNI 412
Cdd:pfam05557 261 LqswVKLAQDTglnlRSPEDLSRRieqlQQREIVLKEENsslTSSARQLEKARRELEQELAQylkKIEDLNKKLKRHKAL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 413 EERLRQ-----------MEAQLEEKNQELQRARQREKMNEEhNKRLSDTVDK---LLSESNERLQLHLKERMAALEDKNS 478
Cdd:pfam05557 341 VRRLQRrvllltkerdgYRAILESYDKELTMSNYSPQLLER-IEEAEDMTQKmqaHNEEMEAQLSVAEEELGGYKQQAQT 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462528303 479 LLREVESAKKQleETQHDKDQLVLNIEALRAELDHMRL 516
Cdd:pfam05557 420 LERELQALRQQ--ESLADPSYSKEEVDSLRRKLETLEL 455
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-425 |
1.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 161 LKALKSLFEHHKALDEKVR----ERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTpstsgk 236
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL------ 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 237 rssdgslshEEDLAKVieLQEIISKQSREQSQMKERLASLSSHVTELEEdLDTARKDLIKSEEMNTKLQRDVREAMAQKE 316
Cdd:PRK03918 569 ---------EEELAEL--LKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 317 DMEERITTLEKRYLAAQREATsvhdlndklENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAEL- 395
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYS---------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERe 707
|
250 260 270
....*....|....*....|....*....|..
gi 2462528303 396 --AQRVAALSKAEERHGNIEERLRQMEAQLEE 425
Cdd:PRK03918 708 kaKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-492 |
1.14e-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: 43.24 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 193 EEELGATHKELMILKEQNNQ-KKTLTDgvldinHEQENTPSTSGKRSSDGSLSHEEDL------------AKVIELQEII 259
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKaESELKE------LEKKHQQLCEEKNALQEQLQAETELcaeaeemrarlaARKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 260 --------SKQSREQSQMKERlASLSSHVTELEEDLD---TARK------------------DLIKSEEMNTKLQRdvre 310
Cdd:pfam01576 78 helesrleEEEERSQQLQNEK-KKMQQHIQDLEEQLDeeeAARQklqlekvtteakikkleeDILLLEDQNSKLSK---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 311 amaQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQtEDKNRQLQERL---------ELAEQKLQQT 381
Cdd:pfam01576 153 ---ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-EEKGRQELEKAkrklegestDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 382 LRKAETLPEVEAELAQRVAALSKAEE---RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEs 458
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE- 307
|
330 340 350
....*....|....*....|....*....|....
gi 2462528303 459 nerLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:pfam01576 308 ---LEDTLDTTAAQQELRSKREQEVTELKKALEE 338
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
350-511 |
1.15e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 350 IANKdsmhRQTEDKNRQLQERLELAEQKLQQTLRK---------AETLPEVEAELAQRVAALSKAEERHGNIEERLRQME 420
Cdd:COG1842 50 IANQ----KRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 421 AQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAK---KQLEETQHDK 497
Cdd:COG1842 126 SKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDsldDELAELEADS 204
|
170
....*....|....*..
gi 2462528303 498 ---DQLvlniEALRAEL 511
Cdd:COG1842 205 eveDEL----AALKAKM 217
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
344-492 |
1.21e-03 |
|
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: 41.59 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAE----------------TLPEVEAELAQRVAALSKAEE 407
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNeelarealaekkslekQAEALETQLAQQRSAVEQLRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 408 RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAK 487
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190
|
....*
gi 2462528303 488 KQLEE 492
Cdd:pfam04012 191 DLDAK 195
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
291-494 |
1.24e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 291 RKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY----LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 366
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 367 LQERLELAEQKLQQtlrkaetlpevEAELAQRVAAlskaeerhgniEERLRQMEAQLEEKNQELQRARQREKMnEEHNKR 446
Cdd:TIGR00618 245 LTQKREAQEEQLKK-----------QQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPL-AAHIKA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462528303 447 LSDtVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 494
Cdd:TIGR00618 302 VTQ-IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
|
| F-BAR_PACSIN1 |
cd07680 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
324-445 |
1.36e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153364 [Multi-domain] Cd Length: 258 Bit Score: 41.96 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 324 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 390
Cdd:cd07680 61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 391 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 445
Cdd:cd07680 141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
236-522 |
1.38e-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: 43.02 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 236 KRSSDGSLSHEEDLAKviELQEIISKQSREQSQMKErLASLSSHVTELEEDLDTARKDLIKseemntklqrdVREAMAQK 315
Cdd:COG3096 281 RELSERALELRRELFG--ARRQLAEEQYRLVEMARE-LEELSARESDLEQDYQAASDHLNL-----------VQTALRQQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 316 EDME---ERITTLEKRyLAAQREAtsVHDLNDKLENEIANK-------DSMHRQTEDKNRQL--QERLELAEQKLQQTLR 383
Cdd:COG3096 347 EKIEryqEDLEELTER-LEEQEEV--VEEAAEQLAEAEARLeaaeeevDSLKSQLADYQQALdvQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 384 KAETLPEvEAELAQRvaalskaeerhgNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNkrlsdtvdkllSESNERLQ 463
Cdd:COG3096 424 KARALCG-LPDLTPE------------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAAR-----------RQFEKAYE 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528303 464 LHLK-----ERMAALEDKNSLLREVESAKKQLEetqhdkdqlvlNIEALRAELDHMRLRGASLH 522
Cdd:COG3096 480 LVCKiagevERSQAWQTARELLRRYRSQQALAQ-----------RLQQLRAQLAELEQRLRQQQ 532
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
358-507 |
1.46e-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: 43.02 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 358 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQRE 437
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 438 KMNEEHNKRLSdtvdKLLSESNERLQlHLKERMAALEDKNSLLREVESAKKQLEETqhdKDQLVLNIEAL 507
Cdd:COG3096 602 PAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERL 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
223-510 |
1.50e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 223 INHEQENTPST-----SGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASlSSHVTELEEdldtARK--DLI 295
Cdd:PTZ00121 1066 VGQDEGLKPSYkdfdfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK-AEDARKAEE----ARKaeDAR 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 296 KSEEMNtKLQRDVREAMAQKED----MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERL 371
Cdd:PTZ00121 1141 KAEEAR-KAEDAKRVEIARKAEdarkAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE-RKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 372 ELAEQKLQQTLRKAETLPEvEAELAQRVAALSKAEERHGNIEERL-----RQMEAQLEE--KNQELQRARQREKMNEehn 444
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKK-DAEEAKKAEEERNNEEIRKFEEARMahfarRQAAIKAEEarKADELKKAEEKKKADE--- 1294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 445 KRLSDTVDKLlsesnERLQLHLKERMAALEDKnsllREVESAKKQLEETQHDKDQLVLNIEALRAE 510
Cdd:PTZ00121 1295 AKKAEEKKKA-----DEAKKKAEEAKKADEAK----KKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
246-513 |
1.61e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEemntklQRDVREAMAQKEDMEERITTL 325
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDCQRELEKL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 326 --EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ--------------KLQQTLRKAETLP 389
Cdd:TIGR00606 332 nkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfserqiknfhtlVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 390 EVEAELAQRvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNErlqLHLKER 469
Cdd:TIGR00606 412 QLCADLQSK---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE---LRKAER 485
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462528303 470 MAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDH 513
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
222-476 |
1.63e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 222 DINHEQENTPSTSGKRSSDGSLSHEED--LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEE 299
Cdd:PLN02939 70 DENGQLENTSLRTVMELPQKSTSSDDDhnRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 300 MNTKLQRDVREAMAQKEDMEERITTLEKRY--------LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERL 371
Cdd:PLN02939 150 ARLQALEDLEKILTEKEALQGKINILEMRLsetdarikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 372 ELAEQKLQQTLRK--AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE------------------EKNQELQ 431
Cdd:PLN02939 227 ELDVLKEENMLLKddIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIvaqedvsklsplqydcwwEKVENLQ 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528303 432 RARQREKMNEEH-------NKRLSDTVDKL---LSESN------ERLQLhLKERMAALEDK 476
Cdd:PLN02939 307 DLLDRATNQVEKaalvldqNQDLRDKVDKLeasLKEANvskfssYKVEL-LQQKLKLLEER 366
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
254-512 |
1.73e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 42.30 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 254 ELQEIISKQSREQSQMKERLASLSSHVTELEEDLdtarkdLIKSEEMNTKLQRDV----REAMAQKEDMEERITTLEkRY 329
Cdd:pfam03999 6 HLHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDA------LSEENDKEQRILQSIadlrAEAAILCLYMRNRLLHEE-RD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 330 LAAQREATSVH----DLNDKLENEIANKDSMHRQTEDKNRQLQERL-ELAEQKLQQTlrkAETLPEVE--AELAQRVAAL 402
Cdd:pfam03999 79 PFEPKKGMSLLqkekKLDTQLEHLRKEKAPRLAEIKELLEQLQQLCeELGEEPLPLL---IDPLPSLEelESFRKHLENL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 403 SKA-EERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEH-NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLL 480
Cdd:pfam03999 156 RNEkERRLEEVNELKKQIKLLMEELDLVPGTDFEEDLLCESEdNFCLSRENIDKLRKLIKQLEEQKAEREEKIDDLREKI 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462528303 481 REV-----ESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam03999 236 LELwnrlqVPQEEQESFVRENNSLSQDTIDALREELQ 272
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1009-1056 |
1.78e-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: 38.05 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462528303 1009 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1056
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
267-442 |
1.81e-03 |
|
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.
Pssm-ID: 407241 [Multi-domain] Cd Length: 360 Bit Score: 42.10 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 267 SQMKERLASLSSHVTELEEDLDTARKDLIKSeemntkLQRDVREAMAQKEDMEERITTLekrYLAAQREATSVHDLNDKL 346
Cdd:pfam17097 114 SVSDPKYASLEDEVSQLEDDTLTVLNQEIDQ------IKGDILQVAQEIADKQDQVNEL---CLETSNELDECWELLNEL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 347 ENeiankdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEveaelaqrvaalSKAEERHgnIEERLRQMEAQLEEK 426
Cdd:pfam17097 185 ER-------LRDQRITVEEQTSNEKDTELDPVEETYEEWKSLQE------------SLQQLEH--LKEELDQLQKQKDSL 243
|
170
....*....|....*.
gi 2462528303 427 NQELQRARQREKMNEE 442
Cdd:pfam17097 244 EKVDKSSINRTQNDEE 259
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
237-525 |
2.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 237 RSSDGSLSHEEDLAKvielqeiiSKQSREQSQmkERLASLSSHVTELEEdldtARKDL-IKSEEMNTKLQRdVREAMAQK 315
Cdd:PRK04863 283 VHLEEALELRRELYT--------SRRQLAAEQ--YRLVEMARELAELNE----AESDLeQDYQAASDHLNL-VQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 316 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL---QERLELAE------QKLQQTLRKAE 386
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQtraiqyQQAVQALERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 387 TL---PEVEAElaqrvaalskaeerhgNIEERLRQMEAQLEEKNQELQRARQREKMNEEHN----------KRLSDTVD- 452
Cdd:PRK04863 428 QLcglPDLTAD----------------NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvRKIAGEVSr 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 453 -----------------KLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PRK04863 492 seawdvarellrrlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330
....*....|
gi 2462528303 516 LRGASLHHGR 525
Cdd:PRK04863 572 ESVSEARERR 581
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
916-978 |
2.33e-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: 37.63 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528303 916 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 978
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
250-488 |
2.87e-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: 42.04 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 250 AKVIELQEIISKQSREQSQM----KERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQ----RDVREAMAQKEDMEEr 321
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 322 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 379
Cdd:pfam05557 78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 380 QTLRKAETLPEVEA---ELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARqrekmneEHNKRLSDTVDK--L 454
Cdd:pfam05557 157 NLEKQQSSLAEAEQrikELEFEIQSQEQDSEIVKNSKSEL----ARIPELEKELERLR-------EHNKHLNENIENklL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462528303 455 LSESNERLQLHL------KERMAALEDKNS-LLREVESAKK 488
Cdd:pfam05557 226 LKEEVEDLKRKLereekyREEAATLELEKEkLEQELQSWVK 266
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1087-1151 |
3.11e-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: 3.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528303 1087 VLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1151
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
337-511 |
3.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 337 TSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA-EERHGNIEER 415
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEE----LNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 416 LRQM----------EAQLEEKNQE--LQRARQREKMNEEHNKRLSDtvdklLSESNERLQLHLKERMAALEDKNSLLREV 483
Cdd:COG3883 92 ARALyrsggsvsylDVLLGSESFSdfLDRLSALSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180
....*....|....*....|....*...
gi 2462528303 484 ESAKKQLEETQHDKDQLVLNIEALRAEL 511
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
365-513 |
3.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERlrqmeaqlEEKNQELQRARQREKMNEEHN 444
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528303 445 KRLSDTVDKLLSESNerlqlHLKERMAALEDKNSLLREVESAKKQLEETQHdKDQLvlnIEALRAELDH 513
Cdd:PRK12705 98 EKLDNLENQLEEREK-----ALSARELELEELEKQLDNELYRVAGLTPEQA-RKLL---LKLLDAELEE 157
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
342-512 |
3.49e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 342 LNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAetLPEVEAELAQRVAALSK-----AEERHGNIEERL 416
Cdd:pfam01442 2 LEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKD--LEEVRAKLEPYLEELQAklgqnVEELRQRLEPYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 417 RQMEAQLEEKNQELQRaRQREKMnEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALedKNSLLREVESAKKQLEET 493
Cdd:pfam01442 80 EELRKRLNADAEELQE-KLAPYG-EELRERLEQNVDALrarLAPYAEELRQKLAERLEEL--KESLAPYAEEVQAQLSQR 155
|
170 180
....*....|....*....|
gi 2462528303 494 QHD-KDQLVLNIEALRAELD 512
Cdd:pfam01442 156 LQElREKLEPQAEDLREKLD 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-499 |
3.59e-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: 41.70 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 268 QMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM-------EERITTLEKRYL-------AAQ 333
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLqlqedlaASE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 334 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS---KAEERHG 410
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTS 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 411 NIEERLRQmeaQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAledkNSLLREVESAKK- 488
Cdd:pfam01576 934 QKSESARQ---QLERQNKELKaKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAA----NKLVRRTEKKLKe 1006
|
250
....*....|....
gi 2462528303 489 ---QLEETQHDKDQ 499
Cdd:pfam01576 1007 vllQVEDERRHADQ 1020
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-488 |
3.72e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 112 AELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspagvssevEVLKALKSLFEHHKaldeKVRERL 182
Cdd:PRK04863 803 ATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELERALADHESQEQ----QQRSQL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 183 RVALERCSLLEEELGathkELMILKEQnnqkkTLTDGVLDInheqentpstsgkrssdgslshEEDLAKVIELQEIISKQ 262
Cdd:PRK04863 868 EQAKEGLSALNRLLP----RLNLLADE-----TLADRVEEI----------------------REQLDEAEEAKRFVQQH 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 263 SREQSQMKERLASLSSHvtelEEDLDTarkdlikseemntkLQRDVREAMAQKEDMEERITTLEkrYLAAQREATSVHDL 342
Cdd:PRK04863 917 GNALAQLEPIVSVLQSD----PEQFEQ--------------LKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 343 NDKLEneiankdsmhrQTEDKNRQLQERLELAEqklQQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQ 422
Cdd:PRK04863 977 AEMLA-----------KNSDLNEKLRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQE 1038
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 423 LEEKNQEL---------QRARQREkmnEEHNKRLSDT------VDKLLSESNERLQlHLKERMAALEDKNSLLRE-VESA 486
Cdd:PRK04863 1039 LKQELQDLgvpadsgaeERARARR---DELHARLSANrsrrnqLEKQLTFCEAEMD-NLTKKLRKLERDYHEMREqVVNA 1114
|
..
gi 2462528303 487 KK 488
Cdd:PRK04863 1115 KA 1116
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-511 |
4.87e-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: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 256 QEIISKQSREQSQMKERLASLSSHVTELE--------------EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEER 321
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEkkhqqlceeknalqEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 322 ITTLEKRYLAAQRE----ATSVHDLNDKLENEIANKDSMHRQ---TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 394
Cdd:pfam01576 84 LEEEEERSQQLQNEkkkmQQHIQDLEEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 395 LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekmnEEHNKRLSDTVDKLLSESNERLQLHLKERMAALE 474
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQE----LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462528303 475 DKNsllREVESAKKQLEETQHDKDQLVLNIEALRAEL 511
Cdd:pfam01576 240 KKE---EELQAALARLEEETAQKNNALKKIRELEAQI 273
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-277 |
5.40e-03 |
|
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: 40.52 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHHKALdekvRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528303 202 ELM-ILKEQNNQKKTLTDGVldinHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLS 277
Cdd:COG4942 175 ELEaLLAELEEERAALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DUF1978 |
pfam09321 |
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ... |
264-472 |
6.65e-03 |
|
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified.
Pssm-ID: 312723 [Multi-domain] Cd Length: 244 Bit Score: 39.91 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 264 REQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEE--RITTLEKRYLAAQREATSVHD 341
Cdd:pfam09321 11 KEFREMLERLSDYRKVVFWLSENGVIDLPNDPGKWGLSGIPCRDALSEISRHELWEKkaHLKHLESLYTQARDRFEKQSS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 342 LNDKLENEIANKDSMhRQTEDKNRQLQERLELAEQKLQQtlRKAETL-PEVEAELAQRVAALSKAEERHGNIEERLRQME 420
Cdd:pfam09321 91 KKNQKELEEAEQEYL-SSWEDVKDQEIERVQERLQALQA--LYPEVSvSEEETEGQETVTPTVDLETALGRIEESYRECV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462528303 421 AQLEE--KNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAA 472
Cdd:pfam09321 168 RDQEDywKEEESKEVEMSAEFREEGGKKKSEEFQEQLGSLERFLKEHSEELEVL 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
226-515 |
8.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 226 EQENTPSTSGKRSSDGSLSHE----EDLAKVIELQEIISKQSREQSQMKE--RLASLSSHVTELEEdLDTARK--DLIKS 297
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEarkaEDARKAEEARKAEDAKRVEIARKAEdaRKAEEARKAEDAKK-AEAARKaeEVRKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 298 EEMntKLQRDVREAMAQKEDMEERITTLEKRYLAAQReATSVHDLndklenEIANKDSMHRQTEDKNRQLQERLELAEQK 377
Cdd:PTZ00121 1191 EEL--RKAEDARKAEAARKAEEERKAEEARKAEDAKK-AEAVKKA------EEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528303 378 LQQTLRKAETlpeVEAELAQRVAALSKAEERHGNIE----ERLRQMEaQLEEKNQELQRARQREKMNEEHNKRlSDTVDK 453
Cdd:PTZ00121 1262 MAHFARRQAA---IKAEEARKADELKKAEEKKKADEakkaEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKK-ADAAKK 1336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528303 454 LLSESNERLQLHLKERMAALEdknsllrEVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD-------EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
|
| |
