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Conserved domains on  [gi|1063704980|ref|NP_001323795|]
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plectin-like protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 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 5.60e-88

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: 267.06  E-value: 5.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 100 ATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDE 179
Cdd:pfam16712   1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 180 ERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKH 259
Cdd:pfam16712  81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160


                  ....*...
gi 1063704980 260 FLQLQKKL 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 1.89e-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: 235.03  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 381 DVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQALYWQAKKGVSFVIAFE 460
Cdd:pfam17684   1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80

                          90       100
                  ....*....|....*....|....*...
gi 1063704980 461 SERERNAAIMLARRFACDCNVTLAGPED 488
Cdd:pfam17684  81 SERERNAAIMLARRFAFDCNVILAGPDD 108
SCAB-Ig pfam16709
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on ...
 281-378 2.47e-64

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: 203.32  E-value: 2.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 281 YEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLSTV 360
Cdd:pfam16709   1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80

                          90
                  ....*....|....*...
gi 1063704980 361 GKIDPAAGLGSYVEALVR 378
Cdd:pfam16709  81 GPIDPAAGLGSYVETLVR 98
SCAB-ABD pfam16711
Actin-binding domain of plant-specific actin-binding protein; SCAB-ABD is the actin-binding ...
 55-95 1.20e-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: 73.32  E-value: 1.20e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063704980  55 KEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEA 95
Cdd:pfam16711   1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
 
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 5.60e-88

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: 267.06  E-value: 5.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 100 ATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDE 179
Cdd:pfam16712   1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 180 ERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKH 259
Cdd:pfam16712  81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160


                  ....*...
gi 1063704980 260 FLQLQKKL 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 1.89e-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: 235.03  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 381 DVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQALYWQAKKGVSFVIAFE 460
Cdd:pfam17684   1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80

                          90       100
                  ....*....|....*....|....*...
gi 1063704980 461 SERERNAAIMLARRFACDCNVTLAGPED 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 4.10e-73

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: 227.01  E-value: 4.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 366 AAGLGSYVEALVRKHDVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQAL 445
Cdd:cd13232     1 AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGARGGGNAAARAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063704980 446 YWQAKKGVSFVIAFESERERNAAIMLARRFACDCNVTLA 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 2.47e-64

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: 203.32  E-value: 2.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 281 YEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLSTV 360
Cdd:pfam16709   1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80

                          90
                  ....*....|....*...
gi 1063704980 361 GKIDPAAGLGSYVEALVR 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 2.36e-51

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: 169.16  E-value: 2.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 280 VYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLST 359
Cdd:cd11675     1 LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIVLPGQKESLST 80


                  ....*
gi 1063704980 360 VGKID 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 1.20e-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: 73.32  E-value: 1.20e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063704980  55 KEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEA 95
Cdd:pfam16711   1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
PTZ00121 PTZ00121
MAEBL; Provisional
 60-275 7.99e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   60 RETAQLMDQQKRLSVRDLAHKFEKGLAA--AAKLSEEAKlKEATSLEKHVLLKKLRDALESLRGRVAgrnKDDVEEAIAM 137
Cdd:PTZ00121  1290 KKADEAKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAA---ADEAEAAEEK 1365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  138 VEA--LAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAfARAEIESARAAVQRVEEALREHEQMSRASGKQ 215
Cdd:PTZ00121  1366 AEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  216 DMEDLMKEVQEARRIKMLHQPSRVMDMEYELRalrnQLAEKSKHFLQLQKKLAMCRKSEE 275
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAK----KKAEEAKKADEAKKKAEEAKKKAD 1500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-268 6.71e-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: 48.90  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   58 VARETAQLMDQQKRLSvrDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRgrvagRNKDDVEEAIAM 137
Cdd:TIGR02168  742 VEQLEERIAQLSKELT--ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  138 VEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKklvdEERAFARAEIESARAAVQRVEEALrEHEQMSRASGKQDM 217
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESEL-EALLNERASLEEAL 889

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063704980  218 EDLMKEVQEARRikmlhqpsRVMDMEYELRALRNQLAEKSKHFLQLQKKLA 268
Cdd:TIGR02168  890 ALLRSELEELSE--------ELRELESKRSELRRELEELREKLAQLELRLE 932
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-278 6.47e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 109 LKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLT---QREGELFIEKAEVKKLASFLKQASEDAKKL--------V 177
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 178 DEERAFARAEIESARAAVQRVEEALREHEQMSR--ASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAE 255
Cdd:COG4717   131 YQELEALEAELAELPERLEELEERLEELRELEEelEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210

                         170       180
                  ....*....|....*....|...
gi 1063704980 256 KSKHFLQLQKKLAMCRKSEENIS 278
Cdd:COG4717   211 LEEELEEAQEELEELEEELEQLE 233
 
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 5.60e-88

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: 267.06  E-value: 5.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 100 ATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDE 179
Cdd:pfam16712   1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 180 ERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKH 259
Cdd:pfam16712  81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160


                  ....*...
gi 1063704980 260 FLQLQKKL 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 1.89e-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: 235.03  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 381 DVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQALYWQAKKGVSFVIAFE 460
Cdd:pfam17684   1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80

                          90       100
                  ....*....|....*....|....*...
gi 1063704980 461 SERERNAAIMLARRFACDCNVTLAGPED 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 4.10e-73

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: 227.01  E-value: 4.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 366 AAGLGSYVEALVRKHDVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQAL 445
Cdd:cd13232     1 AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGARGGGNAAARAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063704980 446 YWQAKKGVSFVIAFESERERNAAIMLARRFACDCNVTLA 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 2.47e-64

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: 203.32  E-value: 2.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 281 YEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLSTV 360
Cdd:pfam16709   1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80

                          90
                  ....*....|....*...
gi 1063704980 361 GKIDPAAGLGSYVEALVR 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 2.36e-51

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: 169.16  E-value: 2.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 280 VYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLST 359
Cdd:cd11675     1 LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIVLPGQKESLST 80


                  ....*
gi 1063704980 360 VGKID 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 1.20e-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: 73.32  E-value: 1.20e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063704980  55 KEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEA 95
Cdd:pfam16711   1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
PTZ00121 PTZ00121
MAEBL; Provisional
 60-275 7.99e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   60 RETAQLMDQQKRLSVRDLAHKFEKGLAA--AAKLSEEAKlKEATSLEKHVLLKKLRDALESLRGRVAgrnKDDVEEAIAM 137
Cdd:PTZ00121  1290 KKADEAKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAA---ADEAEAAEEK 1365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  138 VEA--LAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAfARAEIESARAAVQRVEEALREHEQMSRASGKQ 215
Cdd:PTZ00121  1366 AEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  216 DMEDLMKEVQEARRIKMLHQPSRVMDMEYELRalrnQLAEKSKHFLQLQKKLAMCRKSEE 275
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAK----KKAEEAKKADEAKKKAEEAKKKAD 1500
PTZ00121 PTZ00121
MAEBL; Provisional
 83-275 1.29e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   83 KGLAAAAKLSEEAKlKEATSLEKHVLLKKlrdalESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKL 162
Cdd:PTZ00121  1411 KKAAAAKKKADEAK-KKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  163 ASFLKQASEDAKKLVDEERafaRAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLmKEVQEARRIKMLHQPSRVMDM 242
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKA 1560

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1063704980  243 EYELRALRNQLAEKSKHflQLQKKLAMCRKSEE 275
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKN--MALRKAEEAKKAEE 1591
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-268 6.71e-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: 48.90  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   58 VARETAQLMDQQKRLSvrDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRgrvagRNKDDVEEAIAM 137
Cdd:TIGR02168  742 VEQLEERIAQLSKELT--ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  138 VEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKklvdEERAFARAEIESARAAVQRVEEALrEHEQMSRASGKQDM 217
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESEL-EALLNERASLEEAL 889

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063704980  218 EDLMKEVQEARRikmlhqpsRVMDMEYELRALRNQLAEKSKHFLQLQKKLA 268
Cdd:TIGR02168  890 ALLRSELEELSE--------ELRELESKRSELRRELEELREKLAQLELRLE 932
PTZ00121 PTZ00121
MAEBL; Provisional
 44-229 1.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   44 DVKDDPKVMSMKEVVARETAQLMDQQKRLSVR--DLAHKFEKG-LAAAAKLSEEAKLKEATSLEK----HVLLKKLRDAl 116
Cdd:PTZ00121  1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKaeeaKIKAEELKKA- 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  117 ESLRGRVAGRNKDDVEEaiamvEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAFARA---EIESARA 193
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkEAEEAKK 1703

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1063704980  194 AVQ---RVEEALREHEQMSRAS--GKQDMEDLMKEVQEARR 229
Cdd:PTZ00121  1704 AEElkkKEAEEKKKAEELKKAEeeNKIKAEEAKKEAEEDKK 1744
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-275 4.95e-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: 46.21  E-value: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   90 KLSEEAKLKE-ATSLEKhvlLKKLRDALESLRGRVAGRN---KDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASF 165
Cdd:TIGR02169  669 SRSEPAELQRlRERLEG---LKRELSSLQSELRRIENRLdelSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  166 LkQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRikmlHQPSRVMDMEYE 245
Cdd:TIGR02169  746 L-SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS----RIEARLREIEQK 820

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1063704980  246 L--RALRNQLAEKSKHFLQLQKKLAMCRKSEE 275
Cdd:TIGR02169  821 LnrLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-278 6.47e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 109 LKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLT---QREGELFIEKAEVKKLASFLKQASEDAKKL--------V 177
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 178 DEERAFARAEIESARAAVQRVEEALREHEQMSR--ASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAE 255
Cdd:COG4717   131 YQELEALEAELAELPERLEELEERLEELRELEEelEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210

                         170       180
                  ....*....|....*....|...
gi 1063704980 256 KSKHFLQLQKKLAMCRKSEENIS 278
Cdd:COG4717   211 LEEELEEAQEELEELEEELEQLE 233
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 125-236 1.15e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 125 GRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAK----KLVDEERAFARAEIESARAAVQRVEE 200
Cdd:PRK00409  512 GEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQeeedKLLEEAEKEAQQAIKEAKKEADEIIK 591

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063704980 201 ALREHEQMSRASGK-QDMEDLMKEVQEARRIKMLHQP 236
Cdd:PRK00409  592 ELRQLQKGGYASVKaHELIEARKRLNKANEKKEKKKK 628
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-277 1.99e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  88 AAKLSEEAKLKEATSLEKHvlLKKLRDALESLRGRVAgRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLK 167
Cdd:COG1196   215 YRELKEELKELEAELLLLK--LRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 168 QASEDAKKL------VDEERAFARAEIESARAAVQRVEEALREHEQmSRASGKQDMEDLMKEVQEARRiKMLHQPSRVMD 241
Cdd:COG1196   292 ELLAELARLeqdiarLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEA-ELAEAEEALLE 369

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063704980 242 MEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEENI 277
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-275 3.42e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  60 RETAQLMDQQKRLS-VRDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRgrvagrnkDDVEEAIAMV 138
Cdd:COG1196   219 KEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--------LELEEAQAEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 139 EALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLvDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDME 218
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063704980 219 DLMKEVQEARRIKMLHQpsRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEE 275
Cdd:COG1196   370 AEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
55-272 4.36e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  55 KEVVARETAQLMDQQKRLsvRDLAHKFEKGLAAAAKLseEAKLKEATSLEKhvlLKKLRDALESLRGRVAGRNKDDVEEA 134
Cdd:PRK03918  451 KELLEEYTAELKRIEKEL--KEIEEKERKLRKELREL--EKVLKKESELIK---LKELAEQLKELEEKLKKYNLEELEKK 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 135 IAMVEALAVQLTQREGELFIEKAEVKKLASFLKQasedakklvdeerafaRAEIESaraAVQRVEEALREHEQMSRASGK 214
Cdd:PRK03918  524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----------------LAELEK---KLDELEEELAELLKELEELGF 584

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063704980 215 QDMEDLMKEVQE-----ARRIKMLHQPSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRK 272
Cdd:PRK03918  585 ESVEELEERLKElepfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
PTZ00121 PTZ00121
MAEBL; Provisional
 35-275 1.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   35 RIGANDQIFDVKDDPKVMSMKEVVARETAQLMDQQKRLsvrDLAHKFEKGL-AAAAKLSEEAKLK--EATSLEKHVLLKK 111
Cdd:PTZ00121  1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA---EEARKAEDAKkAEAVKKAEEAKKDaeEAKKAEEERNNEE 1253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  112 LRDALESLRGRVA----------GRNKDDVEEA--IAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDE 179
Cdd:PTZ00121  1254 IRKFEEARMAHFArrqaaikaeeARKADELKKAeeKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  180 ERAFARAEIESARAAVQRVEEALREHE---------QMSRASGKQDMEDLMKEVQEARRIKMLHQPSRvmDMEYELRALR 250
Cdd:PTZ00121  1334 AKKKAEEAKKAAEAAKAEAEAAADEAEaaeekaeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE--EDKKKADELK 1411

                          250       260
                   ....*....|....*....|....*
gi 1063704980  251 NQLAEKSKHfLQLQKKLAMCRKSEE 275
Cdd:PTZ00121  1412 KAAAAKKKA-DEAKKKAEEKKKADE 1435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-268 2.27e-03

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: 40.81  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   54 MKEVVARETAQLMDQQKRLSVRDLAHKFEKGLAaaaKLSEEAKLKEATSLEKHVLLKKLRDALESLRGRVAgRNKDDVEE 133
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQ---ILRERLANLERQLEELEAQLEELESKLDELAEELA-ELEEKLEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  134 AIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAfARAEIESARAAVQRVEEALREHEQMSRASG 213
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELL 427

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063704980  214 KQDMEDLMKEVQE--ARRIKMLHQ-PSRVMDMEYELRALRNQLAEKSKHFLQLQKKLA 268
Cdd:TIGR02168  428 KKLEEAELKELQAelEELEEELEElQEELERLEEALEELREELEEAEQALDAAERELA 485
PTZ00121 PTZ00121
MAEBL; Provisional
 86-275 2.72e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   86 AAAAKLSEEAKLKEATSLEKHVLLKKLRDA---LESLRGRVAGRNKDD----VEEAIAMVEALAVQLTQREGELfiEKAE 158
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADeakkAEEAKKADEAKKAEEAKKADEA--KKAE 1543

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  159 VKKLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSR 238
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1063704980  239 VMDMEYELRALRNQLAEKSKhflQLQKKLAMCRKSEE 275
Cdd:PTZ00121  1624 ELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEE 1657
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-269 5.27e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  103 LEKHVLLKKLRDALESLRGRVagRNKDDVEEAIAMVEALA--VQLTQREGELFIEKAEVKKLASFLK-QASEDAKKLVDE 179
Cdd:COG4913    218 LEEPDTFEAADALVEHFDDLE--RAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  180 ERAFARAEIESARAAVQRVEEALREHEQmsrasgkqdmedlmkEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKH 259
Cdd:COG4913    296 ELEELRAELARLEAELERLEARLDALRE---------------ELDELEAQIRGNGGDRLEQLEREIERLERELEERERR 360

                          170
                   ....*....|
gi 1063704980  260 FLQLQKKLAM 269
Cdd:COG4913    361 RARLEALLAA 370
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 67-275 7.15e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   67 DQQKRLSV--RDLAHKFEKGLAAAAKLSEEaklkEATSLEKH--VLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALA 142
Cdd:pfam12128  653 LDLRRLFDekQSEKDKKNKALAERKDSANE----RLNSLEAQlkQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  143 VQLTQREGELFIEKAEVKKLASFLKQ--ASEDAKKLVDEERAFARA-EIESARAAVQRVEEalREHEQMSrasgkqdMED 219
Cdd:pfam12128  729 AQLALLKAAIAARRSGAKAELKALETwyKRDLASLGVDPDVIAKLKrEIRTLERKIERIAV--RRQEVLR-------YFD 799

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063704980  220 LMKEVQEARRIKMLhqpSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEE 275
Cdd:pfam12128  800 WYQETWLQRRPRLA---TQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE 852
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 56-268 7.48e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980   56 EVVARETAQLMDQQKRLSvrdlahkfEKGLAAAAKLSEEAKLKEATSLEKHvllkKLRDALESLRGRVA-------GRNK 128
Cdd:TIGR02169  733 EKLKERLEELEEDLSSLE--------QEIENVKSELKELEARIEELEEDLH----KLEEALNDLEARLShsripeiQAEL 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  129 DDVEEAIAMVEALAVQLTQREGELFIEKAevkkLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQM 208
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKLNRLTLEKE----YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063704980  209 SRasgkqDMEDLMKEVQEARRikmlhqpsrvmDMEYELRALRN-------QLAEKSKHFLQLQKKLA 268
Cdd:TIGR02169  877 LR-----DLESRLGDLKKERD-----------ELEAQLRELERkieeleaQIEKKRKRLSELKAKLE 927
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 73-258 8.56e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 38.04  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980  73 SVRDLAHKFEKGLAAA-AKLSEEAKLK--EATSLEKHVLLKKLRDALES--LRG--RVAGRNKDDVEEaiamVEALAVQL 145
Cdd:pfam02841  89 SFKDENQEFQKELVELlEAKKDDFLKQneEASSKYCSALLQDLSEPLEEkiSQGtfSKPGGYKLFLEE----RDKLEAKY 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704980 146 TQREGElFIEKAEVkkLASFL--KQASEDA-----KKLVDEERAFA--RAEIESARAAVQRVEEALREHEQMSRASGK-- 214
Cdd:pfam02841 165 NQVPRK-GVKAEEV--LQEFLqsKEAVEEAilqtdQALTAKEKAIEaeRAKAEAAEAEQELLREKQKEEEQMMEAQERsy 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1063704980 215 QDMEDLMKEVQEARRIKMLHQPSRVMD--MEYELRALRNQLAEKSK 258
Cdd:pfam02841 242 QEHVKQLIEKMEAEREQLLAEQERMLEhkLQEQEELLKEGFKTEAE 287
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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