|
Name |
Accession |
Description |
Interval |
E-value |
| SCAB_CC |
pfam16712 |
Coiled-coil regions of plant-specific actin-binding protein; SCAB_CC is the two coiled-coil, ... |
100-267 |
6.82e-92 |
|
Coiled-coil regions of plant-specific actin-binding protein; SCAB_CC is the two coiled-coil, dimerization domains of plant-specific actin-binding proteins or SCABs, CC1 and CC2, both of which contribute independently to dimerization. CC1 is also required for actin binding, indicating that SCAB1 is a bivalent actin cross-linker. since CC1 adopts an antiparallel helical hairpin that further dimerizes into a four-helix bundle. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement,
Pssm-ID: 465244 [Multi-domain] Cd Length: 168 Bit Score: 277.08 E-value: 6.82e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 100 AASLEKHVLLKKLRDALEALRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDE 179
Cdd:pfam16712 1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 180 ERAFARAEIENAREAVQRVEEALQEHERMSRAAGKQDLEELMKEVQEARRIKMLHQPSKVMDMEHELQALRLQLAEKSKY 259
Cdd:pfam16712 81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160
|
....*...
gi 1229788491 260 SILLQKEL 267
Cdd:pfam16712 161 SLQLLKEL 168
|
|
| SCAB-PH |
pfam17684 |
PH domain of plant-specific actin-binding protein; This family is a PH domain found on ... |
381-488 |
1.20e-76 |
|
PH domain of plant-specific actin-binding protein; This family is a PH domain found on plant-specific actin-binding proteins or SCABs. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement. The Ig-PH fusion domain is at the C-terminus. This domain adopts the PH fold, of seven beta-strands, beta7-beta13 and two alpha-helices, alpha1 and alpha2 arranged into a beta-barrel. The canonical phosphoinositide-binding pocket of the classic PH domain is degenerate in this fused one, and the charge on the pocket suggest that the Ig-PH domain contains a non-canonical binding site for inositol phosphates.
Pssm-ID: 407577 Cd Length: 108 Bit Score: 235.41 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 381 DVEFNVVLTQANGVNHPSELIHVLHVGKMRIKLCKGKNTIAKEYYSSSMQLCGVRGGGNAAAQALFWQAKKDLSFILAFE 460
Cdd:pfam17684 1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80
|
90 100
....*....|....*....|....*...
gi 1229788491 461 SERDRNAAIMLARRFAFDCNIILAGPDD 488
Cdd:pfam17684 81 SERERNAAIMLARRFAFDCNVILAGPDD 108
|
|
| Ig-PH_SCAB1 |
cd13232 |
Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain; SCAB1 is an ... |
366-484 |
2.85e-67 |
|
Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain; SCAB1 is an actin-binding protein that interacts with actin filaments and regulates stomatal movement. SCAB1 is composed of an actin-binding domain, two coiled-coil (CC) domains, and a fused immunoglobulin (Ig) and PH (Ig-PH) domain. SCAB1 homologs are widely present, often in multiple copies (three in Arabidopsis), in plants including eudicots, monocots, ferns and mosses, but are not found in algae and non-plant species. The C-terminal PH domain binds weakly with inositol phosphates via an atypical basic surface patch. SCAB1 forms a dimeric structure via its coiled-coil domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270052 Cd Length: 119 Bit Score: 211.60 E-value: 2.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 366 AAGLGSYVEALVRKHDVEFNVVLTQANGVNHPSELIHVLHVGKMRIKLCKGKNTIAKEYYSSSMQLCGVRGGGNAAAQAL 445
Cdd:cd13232 1 AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGARGGGNAAARAL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1229788491 446 FWQAKKDLSFILAFESERDRNAAIMLARRFAFDCNIILA 484
Cdd:cd13232 81 YWQANKGLSYMLAFESERERNAAIMLARRFASDCNVVLA 119
|
|
| SCAB-Ig |
pfam16709 |
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on ... |
281-378 |
1.91e-62 |
|
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on plant-specific actin-binding proteins or SCABs. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement. The Ig-PH fusion domain is at the C-terminus. This domain is an Ig beta-sandwich fold consisting of two antiparallel beta-sheets built from strands beta1 and beta2 and strands beta3-beta6, respectively.
Pssm-ID: 465243 Cd Length: 98 Bit Score: 198.32 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 281 YEIDGTESLGSYLHIQPCCDIAPDLSKCSIHWYRIASEGGKKELISGATKSVYAPEPFDVGKILQAEISLDGQSITLTTT 360
Cdd:pfam16709 1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80
|
90
....*....|....*...
gi 1229788491 361 GPIDPAAGLGSYVEALVR 378
Cdd:pfam16709 81 GPIDPAAGLGSYVETLVR 98
|
|
| SCAB1_middle |
cd11675 |
middle domain of the stomatal closure-related actin binding protein1; SCAB1 is a dimeric actin ... |
280-364 |
6.89e-47 |
|
middle domain of the stomatal closure-related actin binding protein1; SCAB1 is a dimeric actin crosslinker conserved in plants. The three-dimensional structure of this domain resembles that of fibronectin type III repeat units and immunoglobulins. It is situated between a coiled-coil dimerization domain and a C-terminal pleckstrin homology-like module. SCAB1 appears to be required for normal actin dynamics in guard cells stomatal movement. The function of the middle domain is not clear.
Pssm-ID: 212565 Cd Length: 85 Bit Score: 157.22 E-value: 6.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 280 LYEIDGTESLGSYLHIQPCCDIAPDLSKCSIHWYRIASEGGKKELISGATKSVYAPEPFDVGKILQAEISLDGQSITLTT 359
Cdd:cd11675 1 LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIVLPGQKESLST 80
|
....*
gi 1229788491 360 TGPID 364
Cdd:cd11675 81 TGPID 85
|
|
| SCAB-ABD |
pfam16711 |
Actin-binding domain of plant-specific actin-binding protein; SCAB-ABD is the actin-binding ... |
55-95 |
2.09e-16 |
|
Actin-binding domain of plant-specific actin-binding protein; SCAB-ABD is the actin-binding domain of plant-specific actin-binding proteins or SCABs. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement. The Ig-PH fusion domain is at the C-terminus. The ABD is structurally independent from the first coiled-coil, CC1, domain which is also involved in binding; the CC1 is likely to function as a dimerization module,
Pssm-ID: 374744 [Multi-domain] Cd Length: 41 Bit Score: 72.94 E-value: 2.09e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1229788491 55 KEVIARETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEEA 95
Cdd:pfam16711 1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
86-282 |
1.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 86 AAAAKLSEEARlREAASLEKHVLLKKlrdalEALRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANF 165
Cdd:PTZ00121 1414 AAAKKKADEAK-KKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 166 LKQASEDAKKLVDEERafARAEIENAREAVQRVEEAlQEHERMSRAAGKQDLEELmKEVQEARRIKMLHQPSKVMDMEHE 245
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAK--KAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEK 1563
|
170 180 190
....*....|....*....|....*....|....*....
gi 1229788491 246 LQALRLQLAEKSKYSILLQKELA--ISKKAMGDSSSLYE 282
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYE 1602
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-273 |
5.22e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 60 RETAQLLEQQKRLS-VRDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRDALEALRGRVAGRNKD------DVE 132
Cdd:COG1196 219 KEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 133 EAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAfARAEIENAREAVQRVEEALQEHERMSRAA 212
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229788491 213 GKQDLEELMKEVQEARRIKMLHQpsKVMDMEHELQALRLQLAEKSKYSILLQKELAISKKA 273
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAA--QLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-256 |
2.68e-06 |
|
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: 50.06 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 58 IARETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEE-----ARLREAASLEKhvLLKKLRDALEALRgrvagRNKDDVE 132
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaEAEAEIEELEA--QIEQLKEELKALR-----EALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 133 EAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKklvdEERAFARAEIENAREAVQRVEEALQEHErmsraA 212
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEALL-----N 880
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1229788491 213 GKQDLEELMKEVQEARRIKMlhqpSKVMDMEHELQALRLQLAEK 256
Cdd:TIGR02168 881 ERASLEEALALLRSELEELS----EELRELESKRSELRRELEEL 920
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SCAB_CC |
pfam16712 |
Coiled-coil regions of plant-specific actin-binding protein; SCAB_CC is the two coiled-coil, ... |
100-267 |
6.82e-92 |
|
Coiled-coil regions of plant-specific actin-binding protein; SCAB_CC is the two coiled-coil, dimerization domains of plant-specific actin-binding proteins or SCABs, CC1 and CC2, both of which contribute independently to dimerization. CC1 is also required for actin binding, indicating that SCAB1 is a bivalent actin cross-linker. since CC1 adopts an antiparallel helical hairpin that further dimerizes into a four-helix bundle. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement,
Pssm-ID: 465244 [Multi-domain] Cd Length: 168 Bit Score: 277.08 E-value: 6.82e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 100 AASLEKHVLLKKLRDALEALRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDE 179
Cdd:pfam16712 1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 180 ERAFARAEIENAREAVQRVEEALQEHERMSRAAGKQDLEELMKEVQEARRIKMLHQPSKVMDMEHELQALRLQLAEKSKY 259
Cdd:pfam16712 81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160
|
....*...
gi 1229788491 260 SILLQKEL 267
Cdd:pfam16712 161 SLQLLKEL 168
|
|
| SCAB-PH |
pfam17684 |
PH domain of plant-specific actin-binding protein; This family is a PH domain found on ... |
381-488 |
1.20e-76 |
|
PH domain of plant-specific actin-binding protein; This family is a PH domain found on plant-specific actin-binding proteins or SCABs. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement. The Ig-PH fusion domain is at the C-terminus. This domain adopts the PH fold, of seven beta-strands, beta7-beta13 and two alpha-helices, alpha1 and alpha2 arranged into a beta-barrel. The canonical phosphoinositide-binding pocket of the classic PH domain is degenerate in this fused one, and the charge on the pocket suggest that the Ig-PH domain contains a non-canonical binding site for inositol phosphates.
Pssm-ID: 407577 Cd Length: 108 Bit Score: 235.41 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 381 DVEFNVVLTQANGVNHPSELIHVLHVGKMRIKLCKGKNTIAKEYYSSSMQLCGVRGGGNAAAQALFWQAKKDLSFILAFE 460
Cdd:pfam17684 1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80
|
90 100
....*....|....*....|....*...
gi 1229788491 461 SERDRNAAIMLARRFAFDCNIILAGPDD 488
Cdd:pfam17684 81 SERERNAAIMLARRFAFDCNVILAGPDD 108
|
|
| Ig-PH_SCAB1 |
cd13232 |
Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain; SCAB1 is an ... |
366-484 |
2.85e-67 |
|
Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain; SCAB1 is an actin-binding protein that interacts with actin filaments and regulates stomatal movement. SCAB1 is composed of an actin-binding domain, two coiled-coil (CC) domains, and a fused immunoglobulin (Ig) and PH (Ig-PH) domain. SCAB1 homologs are widely present, often in multiple copies (three in Arabidopsis), in plants including eudicots, monocots, ferns and mosses, but are not found in algae and non-plant species. The C-terminal PH domain binds weakly with inositol phosphates via an atypical basic surface patch. SCAB1 forms a dimeric structure via its coiled-coil domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270052 Cd Length: 119 Bit Score: 211.60 E-value: 2.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 366 AAGLGSYVEALVRKHDVEFNVVLTQANGVNHPSELIHVLHVGKMRIKLCKGKNTIAKEYYSSSMQLCGVRGGGNAAAQAL 445
Cdd:cd13232 1 AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGARGGGNAAARAL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1229788491 446 FWQAKKDLSFILAFESERDRNAAIMLARRFAFDCNIILA 484
Cdd:cd13232 81 YWQANKGLSYMLAFESERERNAAIMLARRFASDCNVVLA 119
|
|
| SCAB-Ig |
pfam16709 |
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on ... |
281-378 |
1.91e-62 |
|
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on plant-specific actin-binding proteins or SCABs. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement. The Ig-PH fusion domain is at the C-terminus. This domain is an Ig beta-sandwich fold consisting of two antiparallel beta-sheets built from strands beta1 and beta2 and strands beta3-beta6, respectively.
Pssm-ID: 465243 Cd Length: 98 Bit Score: 198.32 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 281 YEIDGTESLGSYLHIQPCCDIAPDLSKCSIHWYRIASEGGKKELISGATKSVYAPEPFDVGKILQAEISLDGQSITLTTT 360
Cdd:pfam16709 1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80
|
90
....*....|....*...
gi 1229788491 361 GPIDPAAGLGSYVEALVR 378
Cdd:pfam16709 81 GPIDPAAGLGSYVETLVR 98
|
|
| SCAB1_middle |
cd11675 |
middle domain of the stomatal closure-related actin binding protein1; SCAB1 is a dimeric actin ... |
280-364 |
6.89e-47 |
|
middle domain of the stomatal closure-related actin binding protein1; SCAB1 is a dimeric actin crosslinker conserved in plants. The three-dimensional structure of this domain resembles that of fibronectin type III repeat units and immunoglobulins. It is situated between a coiled-coil dimerization domain and a C-terminal pleckstrin homology-like module. SCAB1 appears to be required for normal actin dynamics in guard cells stomatal movement. The function of the middle domain is not clear.
Pssm-ID: 212565 Cd Length: 85 Bit Score: 157.22 E-value: 6.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 280 LYEIDGTESLGSYLHIQPCCDIAPDLSKCSIHWYRIASEGGKKELISGATKSVYAPEPFDVGKILQAEISLDGQSITLTT 359
Cdd:cd11675 1 LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIVLPGQKESLST 80
|
....*
gi 1229788491 360 TGPID 364
Cdd:cd11675 81 TGPID 85
|
|
| SCAB-ABD |
pfam16711 |
Actin-binding domain of plant-specific actin-binding protein; SCAB-ABD is the actin-binding ... |
55-95 |
2.09e-16 |
|
Actin-binding domain of plant-specific actin-binding protein; SCAB-ABD is the actin-binding domain of plant-specific actin-binding proteins or SCABs. SCAB proteins bind, bundle and stabilize actin filaments and regulate stomatal movement. The Ig-PH fusion domain is at the C-terminus. The ABD is structurally independent from the first coiled-coil, CC1, domain which is also involved in binding; the CC1 is likely to function as a dimerization module,
Pssm-ID: 374744 [Multi-domain] Cd Length: 41 Bit Score: 72.94 E-value: 2.09e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1229788491 55 KEVIARETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEEA 95
Cdd:pfam16711 1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
86-282 |
1.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 86 AAAAKLSEEARlREAASLEKHVLLKKlrdalEALRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANF 165
Cdd:PTZ00121 1414 AAAKKKADEAK-KKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 166 LKQASEDAKKLVDEERafARAEIENAREAVQRVEEAlQEHERMSRAAGKQDLEELmKEVQEARRIKMLHQPSKVMDMEHE 245
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAK--KAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEK 1563
|
170 180 190
....*....|....*....|....*....|....*....
gi 1229788491 246 LQALRLQLAEKSKYSILLQKELA--ISKKAMGDSSSLYE 282
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYE 1602
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-273 |
5.22e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 60 RETAQLLEQQKRLS-VRDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRDALEALRGRVAGRNKD------DVE 132
Cdd:COG1196 219 KEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 133 EAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAfARAEIENAREAVQRVEEALQEHERMSRAA 212
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229788491 213 GKQDLEELMKEVQEARRIKMLHQpsKVMDMEHELQALRLQLAEKSKYSILLQKELAISKKA 273
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAA--QLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-266 |
6.52e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 44 EAKDDPKVISMKEVIARETAQLLEQQKRLSVRDlaskferglAAAAKLSEEARLREAASLEKHVLLKKLRDALEALRGRV 123
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK---------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 124 AGRNKDDVEEAIAMVEAL----------AVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAFARAEIENARE 193
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLkkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229788491 194 AvQRVEEALQEHERMSRAAgkqdlEELMKEvQEARRIKMLHQPSKVMDMEHELQALRLQLAEKSKYSILLQKE 266
Cdd:PTZ00121 1701 A-KKAEELKKKEAEEKKKA-----EELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
125-272 |
1.32e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 125 GRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAK----KLVDEERAFARAEIENAREAVQRVEE 200
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQeeedKLLEEAEKEAQQAIKEAKKEADEIIK 591
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229788491 201 ALQEHERMSRAAGK-QDLEELMKEVQEARRIKMLHQPsKVMDMEHELQAlrlqlAEKSKYSILLQKELAISKK 272
Cdd:PRK00409 592 ELRQLQKGGYASVKaHELIEARKRLNKANEKKEKKKK-KQKEKQEELKV-----GDEVKYLSLGQKGEVLSIP 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-256 |
2.68e-06 |
|
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: 50.06 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 58 IARETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEE-----ARLREAASLEKhvLLKKLRDALEALRgrvagRNKDDVE 132
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaEAEAEIEELEA--QIEQLKEELKALR-----EALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 133 EAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKklvdEERAFARAEIENAREAVQRVEEALQEHErmsraA 212
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEALL-----N 880
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1229788491 213 GKQDLEELMKEVQEARRIKMlhqpSKVMDMEHELQALRLQLAEK 256
Cdd:TIGR02168 881 ERASLEEALALLRSELEELS----EELRELESKRSELRRELEEL 920
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-255 |
3.01e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 57 VIARETAQLLEQqkrlsVRDLASKFErglAAAAKLSEEARLREAASLEKHVL-LKKLRDALEALRGRVAG------RNKD 129
Cdd:COG4913 245 EDAREQIELLEP-----IRELAERYA---AARERLAELEYLRAALRLWFAQRrLELLEAELEELRAELARleaeleRLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 130 DVEEAIAMVEALAVQLTQREGELIQE-KAEVKKLANFLKQASEDAKKL-----------VDEERAFA--RAEIENAREAV 195
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLeallaalglplPASAEEFAalRAEAAALLEAL 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229788491 196 QRVEEALQEHERMSRAA---GKQDLEELMKEVQEARRikmlhqpsKVMDMEHELQALRLQLAE 255
Cdd:COG4913 397 EEELEALEEALAEAEAAlrdLRRELRELEAEIASLER--------RKSNIPARLLALRDALAE 451
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
40-274 |
4.46e-06 |
|
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: 49.35 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 40 NQIVEAKDDPKVIS---MKEVIARETAQLLEQQKRLSVRDLASKfeRGLAAAAKLSEEARLREAASLEKHVLLKKLRD-A 115
Cdd:pfam17380 272 NQLLHIVQHQKAVSerqQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEMDRQAAIYAEQERMAMERErE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 116 LEALRGRVAGRNKDDV-EEAIAM-------VEALAVQlTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAFARAE 187
Cdd:pfam17380 350 LERIRQEERKRELERIrQEEIAMeisrmreLERLQME-RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 188 IENARE-AVQRVEEALQ---EHERMSRAAGKQDLEELMKEVQEARRIKM----------LHQPSKVMDMEHELQALRLQL 253
Cdd:pfam17380 429 QEEARQrEVRRLEEERAremERVRLEEQERQQQVERLRQQEEERKRKKLelekekrdrkRAEEQRRKILEKELEERKQAM 508
|
250 260
....*....|....*....|.
gi 1229788491 254 AEKSKYSILLQKELAISKKAM 274
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAI 529
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-258 |
6.09e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 84 GLAAAAKLseEARLREAASLEKHV-----LLKKLRDALEALRGRVAGRNK--------DDVEEAIAMVEALAVQLTQRE- 149
Cdd:COG4913 605 GFDNRAKL--AALEAELAELEEELaeaeeRLEALEAELDALQERREALQRlaeyswdeIDVASAEREIAELEAELERLDa 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 150 --GELIQEKAEVKKLANFLKQASEDAKKLVDEERAfARAEIENAREAVQRVEEALQEHERMSRAAGKQDLEELMKEVQEA 227
Cdd:COG4913 683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|.
gi 1229788491 228 RRIKMLHQpskvmDMEHELQALRLQLAEKSK 258
Cdd:COG4913 762 AVERELRE-----NLEERIDALRARLNRAEE 787
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-268 |
1.65e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 88 AAKLSEEARLREAASLEKHvlLKKLRDALEALRGRVAgRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLK 167
Cdd:COG1196 215 YRELKEELKELEAELLLLK--LRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 168 QASEDAKKLvDEERAFARAEIENAREAVQRVEEALQEHERMSRAAgKQDLEELMKEVQEArrikmlhqpskvmdmEHELQ 247
Cdd:COG1196 292 ELLAELARL-EQDIARLEERRRELEERLEELEEELAELEEELEEL-EEELEELEEELEEA---------------EEELE 354
|
170 180
....*....|....*....|.
gi 1229788491 248 ALRLQLAEKSKYSILLQKELA 268
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELA 375
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-273 |
2.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 44 EAKDDPKVISMKEVIARETAQLLEQQKRlsVRDLASKFERGLAA--AAKLSEEARlREAASLEKHVLLKKLRDalEALRG 121
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKAdeAKKKAEEAK-KKADAAKKKAEEAKKAA--EAAKA 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 122 RvAGRNKDDVEEAIAMVEA--LAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEerafaraeIENAREAVQRVE 199
Cdd:PTZ00121 1351 E-AEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE--------LKKAAAAKKKAD 1421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229788491 200 EALQEHERMSRAagkqdlEELMKEVQEARRIKMLHQPSKVMDMEHELQalrlQLAEKSKYSILLQKELAISKKA 273
Cdd:PTZ00121 1422 EAKKKAEEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKAEEAK----KKAEEAKKADEAKKKAEEAKKA 1485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-274 |
3.94e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 90 KLSEEARLRE-AASLEKhvlLKKLRDALEALRGRVAGRN---KDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANF 165
Cdd:TIGR02169 669 SRSEPAELQRlRERLEG---LKRELSSLQSELRRIENRLdelSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 166 LkQASEDAKKLVDEERAFARAEIENAREAVQRVEEALQEHERMSRAAGKQDLEELMKEVQEARRikmlHQPSKVMDMEHE 245
Cdd:TIGR02169 746 L-SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS----RIEARLREIEQK 820
|
170 180 190
....*....|....*....|....*....|.
gi 1229788491 246 LQA--LRLQLAEKSKYSILLQKELAISKKAM 274
Cdd:TIGR02169 821 LNRltLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-267 |
5.55e-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: 45.88 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 38 ANNQIVEAKDDpkvismKEVIARETAQLLEQQKRLsvrdlaskfergLAAAAKLSEEArlreaaSLEKHvLLKKLRD--- 114
Cdd:pfam15921 354 ANSELTEARTE------RDQFSQESGNLDDQLQKL------------LADLHKREKEL------SLEKE-QNKRLWDrdt 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 115 ----ALEALRGRVAGRNKDdVEEAIAMVEALAVQLT---QREGELIQEKAE----VKKLANFLKQASEDAKKLVDEERAf 183
Cdd:pfam15921 409 gnsiTIDHLRRELDDRNME-VQRLEALLKAMKSECQgqmERQMAAIQGKNEslekVSSLTAQLESTKEMLRKVVEELTA- 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 184 ARAEIENAREAVQRVEEALQEHERMSRAAGKQdLEELMKEV----QEARRIKmlHQPSKVMDMEHELQALRLQLAEKSKY 259
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRSRVdlklQELQHLK--NEGDHLRNVQTECEALKLQMAEKDKV 563
|
....*...
gi 1229788491 260 SILLQKEL 267
Cdd:pfam15921 564 IEILRQQI 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-279 |
2.10e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 56 EVIARETAQLLEQQKRLsvRDLASKFERGLAAAAklSEEARLREAASlEKHVLLKKLRDALEALRGRVA-------GRNK 128
Cdd:TIGR02169 726 EQLEQEEEKLKERLEEL--EEDLSSLEQEIENVK--SELKELEARIE-ELEEDLHKLEEALNDLEARLShsripeiQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 129 DDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKklvdEERAFARAEIENAREAVQRVEEALQEHERM 208
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229788491 209 SRAAGKQdLEELMKEVQEARRiKMLHQPSKVMDMEHELQALRLQLAE-KSKYSILLQKELAISKKAMGDSSS 279
Cdd:TIGR02169 877 LRDLESR-LGDLKKERDELEA-QLRELERKIEELEAQIEKKRKRLSElKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
62-256 |
2.58e-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: 43.79 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 62 TAQLLEQQKRLSVRDLA-SKFERGLAAAAKLSEE---------AR--LREAASLEKHV-----LLKKLRDA--------- 115
Cdd:COG3096 454 TEEVLELEQKLSVADAArRQFEKAYELVCKIAGEversqawqtARelLRRYRSQQALAqrlqqLRAQLAELeqrlrqqqn 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 116 LEALRGRVAGRNKDDVEEAIaMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAFARAEIEnAREAV 195
Cdd:COG3096 534 AERLLEEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA-AQDAL 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229788491 196 QRVEEalQEHERMsraagkQDLEELMKEVQEarrikmlhqpskVMDMEHELQALRLQLAEK 256
Cdd:COG3096 612 ERLRE--QSGEAL------ADSQEVTAAMQQ------------LLEREREATVERDELAAR 652
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-268 |
2.70e-04 |
|
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: 43.89 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 50 KVISMKEVIARETAQLLEQ--QKRLSVRDLASKFE----RGLAAAAKLSE-EARLREAASLEKHvlLKKLRDALEALRGR 122
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKleELRLEVSELEEEIEelqkELYALANEISRlEQQKQILRERLAN--LERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 123 VAGRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAFA---------RAEIENARE 193
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiaslNNEIERLEA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229788491 194 AVQRVEEALQEHERMSRAAGKQDLEELMKEVQE--ARRIKMLHQ-PSKVMDMEHELQALRLQLAEKSKYSILLQKELA 268
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAelEELEEELEElQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
58-227 |
4.65e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 58 IARETAQLLEQQKRL-SVRDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRDALEALRGRVAGRNKDDVEEAIA 136
Cdd:COG2268 208 AERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 137 MVEALAVQLTQREGELIQEKAEVKKLAnflkqaseDAKKLVDEERAFARAEIENAR-----EAVQRVEEALQEherMSRA 211
Cdd:COG2268 288 REREIELQEKEAEREEAELEADVRKPA--------EAEKQAAEAEAEAEAEAIRAKglaeaEGKRALAEAWNK---LGDA 356
|
170
....*....|....*.
gi 1229788491 212 AGKQDLEELMKEVQEA 227
Cdd:COG2268 357 AILLMLIEKLPEIAEA 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-216 |
4.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 34 YKIGANNQIVEAKDDPKVISMKEVIARETAQLLEQQKRLSvrdlasKFERGLAAAAKLSEEARlREAASLEKHVLLKKLR 113
Cdd:COG4717 59 FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE------ELEEELEELEAELEELR-EELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 114 DALEALRGRVAG--RNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANF--------LKQASEDAKKLvDEERAF 183
Cdd:COG4717 132 QELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeeLQDLAEELEEL-QQRLAE 210
|
170 180 190
....*....|....*....|....*....|...
gi 1229788491 184 ARAEIENAREAVQRVEEALQEHERMSRAAGKQD 216
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
105-255 |
6.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 105 KHVLLKKLRDALEAL---RGRVAGRNKDDVEEAIAMVEALAVQLT---QREGELIQEKAEVKKLANFLKQASEDAKKL-- 176
Cdd:COG4717 44 RAMLLERLEKEADELfkpQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLek 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 177 ------VDEERAFARAEIENAREAVQRVEEALQEHERMSR--AAGKQDLEELMKEVQEARRIKMLHQPSKVMDMEHELQA 248
Cdd:COG4717 124 llqllpLYQELEALEAELAELPERLEELEERLEELRELEEelEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
....*..
gi 1229788491 249 LRLQLAE 255
Cdd:COG4717 204 LQQRLAE 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-273 |
6.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 59 ARETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRDALEALRGRVAGRNKDDVEEAIAMV 138
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 139 EALAVQLTQREGELiqEKAEVKKLANFLKQASEDAKklVDEERafaraEIENAREAVQRVEEALQEHErMSRAAGKQDLE 218
Cdd:PTZ00121 1526 EAKKAEEAKKADEA--KKAEEKKKADELKKAEELKK--AEEKK-----KAEEAKKAEEDKNMALRKAE-EAKKAEEARIE 1595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1229788491 219 ELMKEVQEARRIKMlHQPSKVMDMEHELQALRLQLAEKSKYSILLQKELAISKKA 273
Cdd:PTZ00121 1596 EVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-265 |
7.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 35 KIGANNQIVEAKDDPKVISMKEVIARETAQLLEQQKRLSVRDLASKFERglAAAAKLSEEARLR--EAASLEKHVLLKKL 112
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKK--AEAVKKAEEAKKDaeEAKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 113 RDALEALRGRVA----------GRNKDDVEEA--IAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDE- 179
Cdd:PTZ00121 1255 RKFEEARMAHFArrqaaikaeeARKADELKKAeeKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAa 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 180 ----ERAFARAEIENAREAVQRVE----EALQEHERMSRAAGKQDLEELMKEVQEARRIKMLHQpsKVMDMEHELQALRL 251
Cdd:PTZ00121 1335 kkkaEEAKKAAEAAKAEAEAAADEaeaaEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK--KAEEDKKKADELKK 1412
|
250
....*....|....
gi 1229788491 252 QLAEKSKYSILLQK 265
Cdd:PTZ00121 1413 AAAAKKKADEAKKK 1426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-255 |
7.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 85 LAAAAKLSEE-ARLREAaslekHVLLKKLRDALEALRGRVA-----GRNKDDVEEAIAMVEALAVQLTQREGELIQEKAE 158
Cdd:COG4913 224 FEAADALVEHfDDLERA-----HEALEDAREQIELLEPIRElaeryAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 159 vkklanflkqASEDAKKLVDEERAFARAEIENAREAVQRVEEALQEHermsraaGKQDLEELMKEVQEARR--------- 229
Cdd:COG4913 299 ----------ELRAELARLEAELERLEARLDALREELDELEAQIRGN-------GGDRLEQLEREIERLEReleererrr 361
|
170 180 190
....*....|....*....|....*....|..
gi 1229788491 230 ------IKMLHQPskVMDMEHELQALRLQLAE 255
Cdd:COG4913 362 arlealLAALGLP--LPASAEEFAALRAEAAA 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
58-238 |
1.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 58 IARETAQLLEQQKRLSVRDLASKFERGLAAA--------AKLSEEARLREAASLEKHVLLKKLRDALEALRGRVAGRNKD 129
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAgvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 130 DVEEAIAMVEALAVQLTQREGELIQEKAEvkklanfLKQASEDAKKlvDEERAFARAEIENAREAVQRVEEalqehERMS 209
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAE-------LEAELEQLEE--DGELAELLQELEELKAELRELAE-----EWAA 494
|
170 180
....*....|....*....|....*....
gi 1229788491 210 RAAGKQDLEELMKEVQEARRIKMLHQPSK 238
Cdd:COG4717 495 LKLALELLEEAREEYREERLPPVLERASE 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
89-255 |
1.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 89 AKLSEEARLREAASLEKHVL---LKKLRDALEALRGRvAGRNKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANF 165
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLrerLEELEEERDDLLAE-AGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 166 LKQASEDAKKLVD------EERAFARAEIENAREAVQRVEEALQEHERMSRAAGKQ---------DLEELMKEVQEARri 230
Cdd:PRK02224 344 AESLREDADDLEEraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgNAEDFLEELREER-- 421
|
170 180
....*....|....*....|....*
gi 1229788491 231 KMLHQpsKVMDMEHELQALRLQLAE 255
Cdd:PRK02224 422 DELRE--REAELEATLRTARERVEE 444
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-245 |
1.70e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 69 QKRLSVRDLASKFERGLAAAAKLSEEARLREAASLEKhvLLKKLRDALEALRGRVAgrnkddvEEAIAMVEAlavqltqr 148
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEE--AKKKAEDARKAEEARKA-------EDARKAEEA-------- 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 149 egeliqEKAEVKKLANFLKQAsEDAKKLVDEERAFARAEIENAREA--VQRVEEALQ-EHERMSRAAGKQDLEELMKEV- 224
Cdd:PTZ00121 1146 ------RKAEDAKRVEIARKA-EDARKAEEARKAEDAKKAEAARKAeeVRKAEELRKaEDARKAEAARKAEEERKAEEAr 1218
|
170 180
....*....|....*....|...
gi 1229788491 225 --QEARRIKMLHQPSKVMDMEHE 245
Cdd:PTZ00121 1219 kaEDAKKAEAVKKAEEAKKDAEE 1241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-255 |
1.78e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 59 ARETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEEAR------------LREAASLEKHVLLKKLRDALEALRGRVAGR 126
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadaryyvlgdtLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 127 NKDDVEEAIAMVEALAVQLTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERAFARAEIENAREAVQRVEEALQEHE 206
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1229788491 207 RMSRAAGKQDLEELmkEVQEARRIKMLHQPSKVMDMEHELQALRLQLAE 255
Cdd:COG1196 732 AEREELLEELLEEE--ELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
123-227 |
2.23e-03 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 40.80 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 123 VAGRnkddvEEAIAMVEALAVQLTqrEGELIQ--EKA--EVKKLANFLKQASEDAKKLVDEERAFARAEIENA-REAVQ- 196
Cdd:PRK11824 179 VAGT-----KDAVLMVESEAKELS--EEVMLEaiEFGheAIQELIDAQEELAAEAGPKWEWQPPEVDEELKAAvKELAEa 251
|
90 100 110
....*....|....*....|....*....|.
gi 1229788491 197 RVEEALQEHERMSRAAgkqDLEELMKEVQEA 227
Cdd:PRK11824 252 KLKEAYQITDKQEREA---ALDAIKEEVLEA 279
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
95-229 |
2.68e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 95 ARLREAASLEKhvlLKK--LRDALEALRGRVAGR--NKDDVEEAIAMVEALAVQLTQREGELIQEKAEvkklanfLKQAS 170
Cdd:PRK09039 63 AELADLLSLER---QGNqdLQDSVANLRASLSAAeaERSRLQALLAELAGAGAAAEGRAGELAQELDS-------EKQVS 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229788491 171 EDAKKLVdeerAFARAEIENAREAVQRVEEALQEHERMSRAAGKQ--DLEE-----LMKEVQEARR 229
Cdd:PRK09039 133 ARALAQV----ELLNQQIAALRRQLAALEAALDASEKRDRESQAKiaDLGRrlnvaLAQRVQELNR 194
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-267 |
3.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 55 KEVIARETAQLLEQQKRLsvRDLASKfERGLAAAAKLSEEARLREaaslEKHVLLKKLRDALEALRGRVAGRNKDDVEEA 134
Cdd:PRK03918 451 KELLEEYTAELKRIEKEL--KEIEEK-ERKLRKELRELEKVLKKE----SELIKLKELAEQLKELEEKLKKYNLEELEKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 135 IAMVEALavqltqrEGELIQEKAEVKKLANFLKQASEDAKKLvdeerafarAEIEnarEAVQRVEEALQEHERMSRAAGK 214
Cdd:PRK03918 524 AEEYEKL-------KEKLIKLKGEIKSLKKELEKLEELKKKL---------AELE---KKLDELEEELAELLKELEELGF 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229788491 215 QDLEELMKEVQE-----ARRIKMLHQPSKVMDMEHELQALRLQLAEKSKYSILLQKEL 267
Cdd:PRK03918 585 ESVEELEERLKElepfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
69-258 |
4.68e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 69 QKRLSVRDLASKFERGLAAAAKLSEE-ARLREAASLEKHVllKKLRDALEALRGRVAGRnkddvEEAIAMVEALAVQLTQ 147
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERlERAEDLVEAEDRI--ERLEERREDLEELIAER-----RETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 148 REGELIQEKAEVKKLANFLKQASEDAKKLVDEERAfARAEIENAREAVQRVEEALQEhermsRAAGKQDLEEL------M 221
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS-KLAELKERIESLERIRTLLAA-----IADAEDEIERLrekreaL 618
|
170 180 190
....*....|....*....|....*....|....*..
gi 1229788491 222 KEVQEARRIKMLHQPSKVMDMEHELQALRLQLAEKSK 258
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEARIEEAREDK 655
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
65-229 |
7.19e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 39.20 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 65 LLEQQKRLSV-RDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRDAlealrgrvagRNKDDVEEAIAMVEALAV 143
Cdd:pfam13779 408 LIEQRRRLALdRENRPRVARALDALTLAPEEFGPDAGVYLGLRSALARLELA----------RSDEALDEVADLLWELAL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 144 QLtqREGELIQEKAEVK----KLANFLKQASEDA--KKLVDEERA----FARAEIENAREAVQRVEEALQEherMSRAAG 213
Cdd:pfam13779 478 RI--EDGDLSDAERRLRaaqeRLSEALERGASDEeiAKLMQELREalddYMQALAEQAQQNPQDLQQPDDP---NAQEMT 552
|
170
....*....|....*.
gi 1229788491 214 KQDLEELMKEVQEARR 229
Cdd:pfam13779 553 QQDLQRMLDRIEELAR 568
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-235 |
8.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 43 VEAKDDPKVISMKEVIARETAQLL--EQQKRLSVRDLASKFE-RGLAAAAKLSEEARLREAASLEKHVLLKKLRDALEAl 119
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA- 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 120 rgRVAGRNKDDVEEAIAMVEAlavqlTQREGELIQEKAEVKKLANFLKQASEDAKKLVDEERafaRAEIENAreavQRVE 199
Cdd:PTZ00121 1668 --KKAEEDKKKAEEAKKAEED-----EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK---KAEEENK----IKAE 1733
|
170 180 190
....*....|....*....|....*....|....*.
gi 1229788491 200 EALQEHERMSRAAgkqdlEELMKEVQEARRIKMLHQ 235
Cdd:PTZ00121 1734 EAKKEAEEDKKKA-----EEAKKDEEEKKKIAHLKK 1764
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
40-220 |
8.36e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 38.29 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 40 NQIVEAKDDPKVISMKEVIARETAQL-----LEQQKRLSVRDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRD 114
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKqraaeQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 115 ALEALRGRVAGRNKDDVEEAIAMVEALAVqltqregeliQEKAEVKKLANFLKQASEDAKKLVDEERAFARAEIENAREA 194
Cdd:TIGR02794 137 EAEAERKAKEEAAKQAEEEAKAKAAAEAK----------KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA 206
|
170 180
....*....|....*....|....*.
gi 1229788491 195 VQRVEEALQEHERMSRAAGKQDLEEL 220
Cdd:TIGR02794 207 AEAAAKAEAEAAAAAAAEAERKADEA 232
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
166-257 |
8.74e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 38.56 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 166 LKQASEDAKKLVDEERAFARAEIENAREAVQRVEEALQEHERMSraagkqdlEELMKEVQ-EARRIKMlHQPSKVMDMEH 244
Cdd:PRK13428 41 LAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAERIA--------EQLRAQADaEAERIKV-QGARQVQLLRA 111
|
90
....*....|....
gi 1229788491 245 EL-QALRLQLAEKS 257
Cdd:PRK13428 112 QLtRQLRLELGHES 125
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
60-204 |
9.54e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 60 RETAQLLEQQKRLSVRDLASKFERGLAAAAKLSEEARLREAASLEKHVLLKKLRDALEALRGRvagrnKDDVEEAIAMVE 139
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK-----LAELKERIESLE 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229788491 140 ALAVQLTQRE--GELIQEKAEvkKLANF----------LKQASEDAKKL---VDEER-AFARAEIENAREAVQRVEEALQ 203
Cdd:PRK02224 593 RIRTLLAAIAdaEDEIERLRE--KREALaelnderrerLAEKRERKRELeaeFDEARiEEAREDKERAEEYLEQVEEKLD 670
|
.
gi 1229788491 204 E 204
Cdd:PRK02224 671 E 671
|
|
| |
