|
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 |
4.27e-90 |
|
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: 278.23 E-value: 4.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 100 AASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDE 179
Cdd:pfam16712 1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 180 ERAFARAEIENARAAVQRVEKALQEQEQMSRASGKQDLEELMKEVQEARRIKMLHQPSKVMDMEHELRALRAQLTEKSKN 259
Cdd:pfam16712 81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160
|
....*...
gi 1759371672 260 SVRLQKEL 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 ... |
381-481 |
8.00e-72 |
|
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: 228.09 E-value: 8.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 381 DIEFNVVITQMNGVNHPSESIHVFHVGKMRIKLCKGKTTIAKEYFSPSMQLCGVRGGGNAAAQALFWQAKQGLSYVLAFE 460
Cdd:pfam17684 1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80
|
90 100
....*....|....*....|.
gi 1759371672 461 SERERNAAIMLARRFAFDCNL 481
Cdd:pfam17684 81 SERERNAAIMLARRFAFDCNV 101
|
|
| PLN02390 |
PLN02390 |
molybdopterin synthase catalytic subunit |
538-648 |
9.58e-72 |
|
molybdopterin synthase catalytic subunit
Pssm-ID: 178014 Cd Length: 111 Bit Score: 228.03 E-value: 9.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 538 APQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQTSVFIAVSSIHR 617
Cdd:PLN02390 1 DPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMALRELRKICDEARSRWSLHKIAVAHRLGPVPVGETSVFVAVSSVHR 80
|
90 100 110
....*....|....*....|....*....|.
gi 1759371672 618 VDALDACKFVIDEIKASVPIWKKEVYANGEV 648
Cdd:PLN02390 81 ADALDACKFLIDELKASVPIWKKEVYDDGEV 111
|
|
| Ig-PH_SCAB1 |
cd13232 |
Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain; SCAB1 is an ... |
366-481 |
1.06e-66 |
|
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: 215.06 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 366 AAGLGSYVEALVRKHDIEFNVVITQMNGVNHPSESIHVFHVGKMRIKLCKGKTTIAKEYFSPSMQLCGVRGGGNAAAQAL 445
Cdd:cd13232 1 AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGARGGGNAAARAL 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1759371672 446 FWQAKQGLSYVLAFESERERNAAIMLARRFAFDCNL 481
Cdd:cd13232 81 YWQANKGLSYMLAFESERERNAAIMLARRFASDCNV 116
|
|
| SCAB-Ig |
pfam16709 |
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on ... |
281-378 |
1.17e-60 |
|
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: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 281 FELDGPEVLGSYLRIQPCSGDAPELSKCLIQWYRVSSQGGKKESISGAIKSVYAPEPFDVGRVLQVDIIYEGQRLTLTTA 360
Cdd:pfam16709 1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80
|
90
....*....|....*...
gi 1759371672 361 GPIDPAAGLGSYVEALVR 378
Cdd:pfam16709 81 GPIDPAAGLGSYVETLVR 98
|
|
| MoaE |
cd00756 |
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
527-650 |
1.99e-52 |
|
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
Pssm-ID: 238385 [Multi-domain] Cd Length: 124 Bit Score: 176.94 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 527 IDMAKYINYVSAPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQT 606
Cdd:cd00756 1 FDLAELLAALRDPEAGAVVTFVGTVRDHDEGKGVEALEYEAYPPMAEKELEEIAEEARERWGLLRVAIIHRVGRLPPGEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1759371672 607 SVFIAVSSIHRVDALDACKFVIDEIKASVPIWKKEVYANGEVWK 650
Cdd:cd00756 81 IVLVAVSSPHRKEAFEACEFLIDRLKHRAPIWKKEIFEGGEEWV 124
|
|
| MoaE |
COG0314 |
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ... |
518-651 |
3.63e-49 |
|
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 168.82 E-value: 3.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 518 VEILEEEIqiDMAKYINYV--SAPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVA 595
Cdd:COG0314 4 VRVTEEPF--DLAAELAALraSDPEAGAVVTFVGTVRDHNDGRRVTALEYEAYPPMAEKELAEIAEEAAERWGLLDVAVI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1759371672 596 HRLGPVPVGQTSVFIAVSSIHRVDALDACKFVIDEIKASVPIWKKEVYANGEVWKE 651
Cdd:COG0314 82 HRVGRLEPGEPIVLVAVSSAHRKEAFEACRFLIDRLKTRAPIWKKEIFEDGEEWVE 137
|
|
| MoaE |
pfam02391 |
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of ... |
527-633 |
2.57e-45 |
|
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
Pssm-ID: 460546 Cd Length: 113 Bit Score: 157.23 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 527 IDMAKYINYVSAPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQT 606
Cdd:pfam02391 6 LDVAEIAALVSDPEAGAVVTFVGTVRDHFDGKKVTALEYEAYPPMAEKELAEIAEEARERWPLLDVAIVHRVGRLPVGEA 85
|
90 100
....*....|....*....|....*..
gi 1759371672 607 SVFIAVSSIHRVDALDACKFVIDEIKA 633
Cdd:pfam02391 86 IVLVAVSSPHRAEAFEACEYLIDELKA 112
|
|
| SCAB1_middle |
cd11675 |
middle domain of the stomatal closure-related actin binding protein1; SCAB1 is a dimeric actin ... |
280-364 |
6.43e-43 |
|
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: 149.52 E-value: 6.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 280 LFELDGPEVLGSYLRIQPCSGDAPELSKCLIQWYRVSSQGGKKESISGAIKSVYAPEPFDVGRVLQVDIIYEGQRLTLTT 359
Cdd:cd11675 1 LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIVLPGQKESLST 80
|
....*
gi 1759371672 360 AGPID 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 |
4.27e-17 |
|
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: 75.25 E-value: 4.27e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1759371672 55 KEVVARETAQLLEQQNRLSVRDLASKFEKGLAAAAKLSEEA 95
Cdd:pfam16711 1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-295 |
6.36e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 48 DRKVLSMKEVVARETA--QLLEQQNRLSVRDLASKFEKGLAAAAKLSEEARLREAASLEKHVLLKKLRDALESLKgrVAG 125
Cdd:TIGR02168 725 SRQISALRKDLARLEAevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK--ALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 126 RNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKklvdEERAFARAEIENARAAVQRVEKALQEQ 205
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEAL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 206 EQmSRASGKQDLEELMKEVQEARRikmlhqpsKVMDMEHELRALRAQLTE--KSKNSVRLQKELAMSKRG--LEKISELF 281
Cdd:TIGR02168 879 LN-ERASLEEALALLRSELEELSE--------ELRELESKRSELRRELEElrEKLAQLELRLEGLEVRIDnlQERLSEEY 949
|
250
....*....|....
gi 1759371672 282 ELDGPEVLGSYLRI 295
Cdd:TIGR02168 950 SLTLEEAEALENKI 963
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-282 |
2.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 83 KGLAAAAKLSEEARlREAASLEKHVLLKKlrdalESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKL 162
Cdd:PTZ00121 1411 KKAAAAKKKADEAK-KKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 163 ANFLKKASEDAKKLVDEERafaRAEIENARAAVQRVEKALQEQEQMSRASGKQDLEELmKEVQEARRIKMLHQPSKVMDM 242
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKA 1560
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1759371672 243 EHELRALRAQLTEKSKNSVRLQKELA--MSKRGLEKISELFE 282
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYE 1602
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
90-227 |
4.34e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 90 KLSEEAR---LREA-ASLEKhvLLKKLRDALESLkgrVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEvkkLANF 165
Cdd:COG3524 169 QLSERARedaVRFAeEEVER--AEERLRDAREAL---LAFRNRNGILDPEATAEALLQLIATLEGQLAELEAE---LAAL 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759371672 166 LKKASEDAkklvdeerafarAEIENARAAVQRVEKAL-QEQEQMSRASGKQDLEELMKEVQEA 227
Cdd:COG3524 241 RSYLSPNS------------PQVRQLRRRIAALEKQIaAERARLTGASGGDSLASLLAEYERL 291
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
156-280 |
3.87e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 156 KAEVKKLANFLKKASEDAKKLVDEERAFArAEIENARAAVQRVEKALQEQ-EQMSRASGKQDLEELMKEVQEARRIKMLh 234
Cdd:cd22656 120 KALLDDLLKEAKKYQDKAAKVVDKLTDFE-NQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEKLNEEYAA- 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1759371672 235 qpsKVMDMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISEL 280
Cdd:cd22656 198 ---KLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLAL 240
|
|
| |
|
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 |
4.27e-90 |
|
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: 278.23 E-value: 4.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 100 AASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDE 179
Cdd:pfam16712 1 VASLERHVLLKKLRDVLESLRGRVAGRNKDDVEESISMVEALAVQLTQREGELLQEKTEVKKLANFLKQASEDAKKIVEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 180 ERAFARAEIENARAAVQRVEKALQEQEQMSRASGKQDLEELMKEVQEARRIKMLHQPSKVMDMEHELRALRAQLTEKSKN 259
Cdd:pfam16712 81 ERAFARAEIESARASVQRVEQAFEEQENSSQASRKQDVEELREEVQEARRIKMLHCPSKVMDMEHELQALRSQLAEKSAD 160
|
....*...
gi 1759371672 260 SVRLQKEL 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 ... |
381-481 |
8.00e-72 |
|
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: 228.09 E-value: 8.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 381 DIEFNVVITQMNGVNHPSESIHVFHVGKMRIKLCKGKTTIAKEYFSPSMQLCGVRGGGNAAAQALFWQAKQGLSYVLAFE 460
Cdd:pfam17684 1 NTEFNVVISQMNGQDHPSHSVHVFHVGKMRIKLCKGWITKAREIYSSSMQLCGVRGGGNAAAQALFWQPRKGLSFVLAFE 80
|
90 100
....*....|....*....|.
gi 1759371672 461 SERERNAAIMLARRFAFDCNL 481
Cdd:pfam17684 81 SERERNAAIMLARRFAFDCNV 101
|
|
| PLN02390 |
PLN02390 |
molybdopterin synthase catalytic subunit |
538-648 |
9.58e-72 |
|
molybdopterin synthase catalytic subunit
Pssm-ID: 178014 Cd Length: 111 Bit Score: 228.03 E-value: 9.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 538 APQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQTSVFIAVSSIHR 617
Cdd:PLN02390 1 DPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMALRELRKICDEARSRWSLHKIAVAHRLGPVPVGETSVFVAVSSVHR 80
|
90 100 110
....*....|....*....|....*....|.
gi 1759371672 618 VDALDACKFVIDEIKASVPIWKKEVYANGEV 648
Cdd:PLN02390 81 ADALDACKFLIDELKASVPIWKKEVYDDGEV 111
|
|
| Ig-PH_SCAB1 |
cd13232 |
Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain; SCAB1 is an ... |
366-481 |
1.06e-66 |
|
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: 215.06 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 366 AAGLGSYVEALVRKHDIEFNVVITQMNGVNHPSESIHVFHVGKMRIKLCKGKTTIAKEYFSPSMQLCGVRGGGNAAAQAL 445
Cdd:cd13232 1 AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGARGGGNAAARAL 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1759371672 446 FWQAKQGLSYVLAFESERERNAAIMLARRFAFDCNL 481
Cdd:cd13232 81 YWQANKGLSYMLAFESERERNAAIMLARRFASDCNV 116
|
|
| SCAB-Ig |
pfam16709 |
Ig domain of plant-specific actin-binding protein; This family is an Ig-like domain found on ... |
281-378 |
1.17e-60 |
|
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: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 281 FELDGPEVLGSYLRIQPCSGDAPELSKCLIQWYRVSSQGGKKESISGAIKSVYAPEPFDVGRVLQVDIIYEGQRLTLTTA 360
Cdd:pfam16709 1 YELDGSETLGSCLRIQPCSDSAPDLSKCSIQWYRVSSEGSKRELISGATKSVYAPEPFDVGRILQADIVSNGQKVTVTTT 80
|
90
....*....|....*...
gi 1759371672 361 GPIDPAAGLGSYVEALVR 378
Cdd:pfam16709 81 GPIDPAAGLGSYVETLVR 98
|
|
| MoaE |
cd00756 |
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
527-650 |
1.99e-52 |
|
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
Pssm-ID: 238385 [Multi-domain] Cd Length: 124 Bit Score: 176.94 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 527 IDMAKYINYVSAPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQT 606
Cdd:cd00756 1 FDLAELLAALRDPEAGAVVTFVGTVRDHDEGKGVEALEYEAYPPMAEKELEEIAEEARERWGLLRVAIIHRVGRLPPGEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1759371672 607 SVFIAVSSIHRVDALDACKFVIDEIKASVPIWKKEVYANGEVWK 650
Cdd:cd00756 81 IVLVAVSSPHRKEAFEACEFLIDRLKHRAPIWKKEIFEGGEEWV 124
|
|
| MoaE |
COG0314 |
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ... |
518-651 |
3.63e-49 |
|
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 168.82 E-value: 3.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 518 VEILEEEIqiDMAKYINYV--SAPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVA 595
Cdd:COG0314 4 VRVTEEPF--DLAAELAALraSDPEAGAVVTFVGTVRDHNDGRRVTALEYEAYPPMAEKELAEIAEEAAERWGLLDVAVI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1759371672 596 HRLGPVPVGQTSVFIAVSSIHRVDALDACKFVIDEIKASVPIWKKEVYANGEVWKE 651
Cdd:COG0314 82 HRVGRLEPGEPIVLVAVSSAHRKEAFEACRFLIDRLKTRAPIWKKEIFEDGEEWVE 137
|
|
| MoaE |
pfam02391 |
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of ... |
527-633 |
2.57e-45 |
|
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
Pssm-ID: 460546 Cd Length: 113 Bit Score: 157.23 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 527 IDMAKYINYVSAPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQT 606
Cdd:pfam02391 6 LDVAEIAALVSDPEAGAVVTFVGTVRDHFDGKKVTALEYEAYPPMAEKELAEIAEEARERWPLLDVAIVHRVGRLPVGEA 85
|
90 100
....*....|....*....|....*..
gi 1759371672 607 SVFIAVSSIHRVDALDACKFVIDEIKA 633
Cdd:pfam02391 86 IVLVAVSSPHRAEAFEACEYLIDELKA 112
|
|
| SCAB1_middle |
cd11675 |
middle domain of the stomatal closure-related actin binding protein1; SCAB1 is a dimeric actin ... |
280-364 |
6.43e-43 |
|
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: 149.52 E-value: 6.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 280 LFELDGPEVLGSYLRIQPCSGDAPELSKCLIQWYRVSSQGGKKESISGAIKSVYAPEPFDVGRVLQVDIIYEGQRLTLTT 359
Cdd:cd11675 1 LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIVLPGQKESLST 80
|
....*
gi 1759371672 360 AGPID 364
Cdd:cd11675 81 TGPID 85
|
|
| moaE |
PRK10678 |
molybdopterin synthase catalytic subunit MoaE; |
542-651 |
1.67e-22 |
|
molybdopterin synthase catalytic subunit MoaE;
Pssm-ID: 182642 Cd Length: 150 Bit Score: 94.43 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 542 GAIATFSGTTRDTFEGKTVLELRYEAYVPMAIRCLKSICSSARSSWNLLSIAVAHRLGPVPVGQTSVFIAVSSIHRVDAL 621
Cdd:PRK10678 29 GAVVTFTGKVRNHNLGDSVKALTLEHYPGMTEKALAEIVDEARSRWPLGRVTVIHRVGELWPGDEIVFVGVTSAHRSSAF 108
|
90 100 110
....*....|....*....|....*....|
gi 1759371672 622 DACKFVIDEIKASVPIWKKEVYANGEVWKE 651
Cdd:PRK10678 109 EAGQFIMDYLKTRAPFWKREATPEGDRWVE 138
|
|
| SCAB-ABD |
pfam16711 |
Actin-binding domain of plant-specific actin-binding protein; SCAB-ABD is the actin-binding ... |
55-95 |
4.27e-17 |
|
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: 75.25 E-value: 4.27e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1759371672 55 KEVVARETAQLLEQQNRLSVRDLASKFEKGLAAAAKLSEEA 95
Cdd:pfam16711 1 KEVVAKETADLSDQHKRLSVRDLASKFDKNLAAAAKLSNEA 41
|
|
| PRK14493 |
PRK14493 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoaE; ... |
513-649 |
5.50e-16 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoaE; Provisional
Pssm-ID: 237730 [Multi-domain] Cd Length: 274 Bit Score: 78.89 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 513 DEKNLVEILEE-EIQIDMAKYINYV----SAPQAGAIATFSGTTR---DTFEGKTVLeLRYEAYVPMAIRCLKSICSSAR 584
Cdd:PRK14493 126 DTEDLVAALESqPPYVTLESLVAKVkrspDADKAGAIATFTGRVRakeDADDEPTEY-LEFEKYDGVADERMAAIREELK 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1759371672 585 SSWNLLSIAVAHRLGPVPVGQTSVFIAVSSIHRVDALDACKFVIDEIKASVPIWKKEVYANGEVW 649
Cdd:PRK14493 205 QRDGVFEVLLHHRTGVIEAGEDIVFVVVLAGHRQEAFRAVSDGIDRLKDEVPIFKKEVTVDEEFW 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-295 |
6.36e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 48 DRKVLSMKEVVARETA--QLLEQQNRLSVRDLASKFEKGLAAAAKLSEEARLREAASLEKHVLLKKLRDALESLKgrVAG 125
Cdd:TIGR02168 725 SRQISALRKDLARLEAevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK--ALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 126 RNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKklvdEERAFARAEIENARAAVQRVEKALQEQ 205
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEAL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 206 EQmSRASGKQDLEELMKEVQEARRikmlhqpsKVMDMEHELRALRAQLTE--KSKNSVRLQKELAMSKRG--LEKISELF 281
Cdd:TIGR02168 879 LN-ERASLEEALALLRSELEELSE--------ELRELESKRSELRRELEElrEKLAQLELRLEGLEVRIDnlQERLSEEY 949
|
250
....*....|....
gi 1759371672 282 ELDGPEVLGSYLRI 295
Cdd:TIGR02168 950 SLTLEEAEALENKI 963
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-282 |
2.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 83 KGLAAAAKLSEEARlREAASLEKHVLLKKlrdalESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKL 162
Cdd:PTZ00121 1411 KKAAAAKKKADEAK-KKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 163 ANFLKKASEDAKKLVDEERafaRAEIENARAAVQRVEKALQEQEQMSRASGKQDLEELmKEVQEARRIKMLHQPSKVMDM 242
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKA 1560
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1759371672 243 EHELRALRAQLTEKSKNSVRLQKELA--MSKRGLEKISELFE 282
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYE 1602
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-287 |
3.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 44 EGKDDRKVLSMKEVVARETAQLLEQQNRLSVRDLASKFEKGLAAAAKLSEEARLREAASLEKhvllKKLRDALESLKGRV 123
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA----EEKKKADEAKKKAE 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 124 AGRNKDDvvdaismvEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKlVDEERAFARaEIENARAAVQRVEKALQ 203
Cdd:PTZ00121 1402 EDKKKAD--------ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK-ADEAKKKAE-EAKKAEEAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 204 EQEQMSRASGKQDLEELMKEVQEARR----IKMLHQPSKVMD----MEHELRALRAQLTEKSKNSVRLQKelAMSKRGLE 275
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKkadeAKKAAEAKKKADeakkAEEAKKADEAKKAEEAKKADEAKK--AEEKKKAD 1549
|
250
....*....|..
gi 1759371672 276 KISELFELDGPE 287
Cdd:PTZ00121 1550 ELKKAEELKKAE 1561
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
61-279 |
3.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 61 ETAQLLEQQNRLSVRDLASKFEKGLAAAAKLSEEARLReAASLEKHvllKKLRDALESLKGRVAGRNKDdvvdaismvea 140
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKA---EEEKKKVEQLKKKEAEEKKK----------- 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 141 lAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEERAFARAEIENARaavqrvEKALQEQEQMSRASGKQDLEEL 220
Cdd:PTZ00121 1649 -AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 221 MKEvQEARRIKMlhQPSKVMDMEHELRALRAQLTEKSKNSV-RLQKELAMSKRGLEKISE 279
Cdd:PTZ00121 1722 KKA-EEENKIKA--EEAKKEAEEDKKKAEEAKKDEEEKKKIaHLKKEEEKKAEEIRKEKE 1778
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
90-227 |
4.34e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 90 KLSEEAR---LREA-ASLEKhvLLKKLRDALESLkgrVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEvkkLANF 165
Cdd:COG3524 169 QLSERARedaVRFAeEEVER--AEERLRDAREAL---LAFRNRNGILDPEATAEALLQLIATLEGQLAELEAE---LAAL 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759371672 166 LKKASEDAkklvdeerafarAEIENARAAVQRVEKAL-QEQEQMSRASGKQDLEELMKEVQEA 227
Cdd:COG3524 241 RSYLSPNS------------PQVRQLRRRIAALEKQIaAERARLTGASGGDSLASLLAEYERL 291
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
62-287 |
5.68e-05 |
|
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: 46.87 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 62 TAQLLEQQNRLSVRDLA-SKFEKGLAAAAKLSEEARlREAASLEKHVLLKKLRDaLESLKGRVagrnkddvvdaismvEA 140
Cdd:COG3096 454 TEEVLELEQKLSVADAArRQFEKAYELVCKIAGEVE-RSQAWQTARELLRRYRS-QQALAQRL---------------QQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 141 LAVQLTQREGELIQEKAEVKKLANFLKKASE--DAKKLVDEERAFARAEIEN----ARAAVQRVEKALQEQEQMsrasgK 214
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQqlDAAEELEELLAELEAQLEEleeqAAEAVEQRSELRQQLEQL-----R 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 215 QDLEELMK------EVQEA--RRIKMLHQPskvMDMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEK-ISELFELDG 285
Cdd:COG3096 592 ARIKELAArapawlAAQDAleRLREQSGEA---LADSQEVTAAMQQLLEREREATVERDELAARKQALESqIERLSQPGG 668
|
..
gi 1759371672 286 PE 287
Cdd:COG3096 669 AE 670
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-268 |
8.20e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 88 AAKLSEEARLREAaslekHVLLKKLRDALESLKgrvagRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLK 167
Cdd:COG1196 215 YRELKEELKELEA-----ELLLLKLRELEAELE-----ELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 168 KASEDAKKLVDE------ERAFARAEIENARAAVQRVEKALQEQEQmSRASGKQDLEELMKEVQEArrikmlhqpskvmd 241
Cdd:COG1196 285 EAQAEEYELLAElarleqDIARLEERRRELEERLEELEEELAELEE-ELEELEEELEELEEELEEA-------------- 349
|
170 180
....*....|....*....|....*..
gi 1759371672 242 mEHELRALRAQLTEKSKNSVRLQKELA 268
Cdd:COG1196 350 -EEELEEAEAELAEAEEALLEAEAELA 375
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-271 |
8.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 87 AAAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFL 166
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 167 KKASEdaKKLVDEERafARAEIENARAAVQRVEKALQEQEQMSRA-SGKQDLEELMKEVQEARRikmlhqPSKVMDMEHE 245
Cdd:PTZ00121 1284 KKAEE--KKKADEAK--KAEEKKKADEAKKKAEEAKKADEAKKKAeEAKKKADAAKKKAEEAKK------AAEAAKAEAE 1353
|
170 180
....*....|....*....|....*.
gi 1759371672 246 LRALRAQLTEKSKNSVRLQKELAMSK 271
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
125-239 |
1.87e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 125 GRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAK----KLVDEERAFARAEIENARAAVQRVEK 200
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQeeedKLLEEAEKEAQQAIKEAKKEADEIIK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1759371672 201 ALQEQEQMSRASGK-QDLEELMKEVQEARRIKMLHQPSKV 239
Cdd:PRK00409 592 ELRQLQKGGYASVKaHELIEARKRLNKANEKKEKKKKKQK 631
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
64-282 |
2.61e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 64 QLLEQQNRLSVRDLASKFEKglaaaaklSEEARLREAASlEKHVLLKKLRDALESLKGRVAGRNKDDVVDA----ISM-- 137
Cdd:pfam17380 276 HIVQHQKAVSERQQQEKFEK--------MEQERLRQEKE-EKAREVERRRKLEEAEKARQAEMDRQAAIYAeqerMAMer 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 138 ---VEALAVQLTQREGELIQEK---AEVKKLANFLKKASEDAKKlvdEERafARAEIENARAavqrvEKALQEQEQMSRA 211
Cdd:pfam17380 347 ereLERIRQEERKRELERIRQEeiaMEISRMRELERLQMERQQK---NER--VRQELEAARK-----VKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 212 SGKQDLEELMKEVQEARRIKMLH-QPSKVMDME----------HELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISEL 280
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRlEEERAREMErvrleeqerqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
..
gi 1759371672 281 FE 282
Cdd:pfam17380 497 LE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-282 |
2.80e-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: 44.28 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 68 QQNRLSVRDLASKFEKGLAAAAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAG---------RNKDDVVDAISMV 138
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqilrERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 139 EALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEERAF-------------------------------ARAE 187
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrleeleeqletlrskvaqlelqiasLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 188 IENARAAVQRVEKALQEQEQMSRASGKQDLEELMKEVQE--ARRIKMLHQ-PSKVMDMEHELRALRAQLTEKSKNSVRLQ 264
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAelEELEEELEElQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260
....*....|....*....|.
gi 1759371672 265 KELAMSK---RGLEKISELFE 282
Cdd:TIGR02168 482 RELAQLQarlDSLERLQENLE 502
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
62-271 |
3.83e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 62 TAQLLEQ---QNRLSVRDLASKFEKGLAAAAKLSEEARLrEAASLEKHvlLKKLRDALESLKGrVAGRNKDDVVDAISMV 138
Cdd:pfam03528 23 LKQQLEAefnQKRAKFKELYLAKEEDLKRQNAVLQEAQV-ELDALQNQ--LALARAEMENIKA-VATVSENTKQEAIDEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 139 EAlavqltqregeliQEKAEVKKLANFLKKASEDAKKLVDEERAFARAEIENARAAVQRvEKAlQEQEQMSRASGKQDLE 218
Cdd:pfam03528 99 KS-------------QWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAER-EIA-DLRRRLSEGQEEENLE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1759371672 219 ELMKEVQE-ARRIKmlhqpSKVMDMEHELRALRAQLTEKSKNSvrlqKELAMSK 271
Cdd:pfam03528 164 DEMKKAQEdAEKLR-----SVVMPMEKEIAALKAKLTEAEDKI----KELEASK 208
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
156-280 |
3.87e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 156 KAEVKKLANFLKKASEDAKKLVDEERAFArAEIENARAAVQRVEKALQEQ-EQMSRASGKQDLEELMKEVQEARRIKMLh 234
Cdd:cd22656 120 KALLDDLLKEAKKYQDKAAKVVDKLTDFE-NQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEKLNEEYAA- 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1759371672 235 qpsKVMDMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISEL 280
Cdd:cd22656 198 ---KLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLAL 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-255 |
4.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 57 VVARETAQLLEQqnrlsVRDLASKFEKGLAAAAKLSEE-ARLREAASLEKHVLLKK----LRDALESLKGRVAgRNKDDV 131
Cdd:COG4913 245 EDAREQIELLEP-----IRELAERYAAARERLAELEYLrAALRLWFAQRRLELLEAeleeLRAELARLEAELE-RLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 132 VDAISMVEALAVQLTQREGELIQE-KAEVKKLANFLKKASEDAKKL-----------VDEERAFA--RAEIENARAAVQR 197
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLeallaalglplPASAEEFAalRAEAAALLEALEE 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759371672 198 VEKALQEQEQMSRAS---GKQDLEELMKEVQEARRikmlhqpsKVMDMEHELRALRAQLTE 255
Cdd:COG4913 399 ELEALEEALAEAEAAlrdLRRELRELEAEIASLER--------RKSNIPARLLALRDALAE 451
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
59-220 |
5.26e-04 |
|
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: 42.91 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 59 ARETAQLLEQQNRLSVRDLASKFEKGLAAAAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAISMV 138
Cdd:TIGR02794 73 LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 139 EALAVQLTQREGEliQEKAEVKKLANFLKKASEDAKKLVDEERAFARAEIENARAAVQRVEKALQEQEQMSRASGKQDLE 218
Cdd:TIGR02794 153 EEEAKAKAAAEAK--KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKAD 230
|
..
gi 1759371672 219 EL 220
Cdd:TIGR02794 231 EA 232
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
92-280 |
8.44e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 92 SEEARLREAASLEKHvlLKKLRDALESLKGRVAGRNKDdVVDAISMVEALA-------VQLTQREGELIQEKAEVKKLAN 164
Cdd:pfam10174 462 EDRERLEELESLKKE--NKDLKEKVSALQPELTEKESS-LIDLKEHASSLAssglkkdSKLKSLEIAVEQKKEECSKLEN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 165 FLKKASE------------DAKKLVDEERAFARAEIENARAAVQRVEKALQEQEqmsraSGKQDLEELMKEVQEARRIKM 232
Cdd:pfam10174 539 QLKKAHNaeeavrtnpeinDRIRLLEQEVARYKEESGKAQAEVERLLGILREVE-----NEKNDKDKKIAELESLTLRQM 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1759371672 233 LHQPSKVMDMEH---ELRALRAQLTEKsknsVRLQKELAMSKRGLEKISEL 280
Cdd:pfam10174 614 KEQNKKVANIKHgqqEMKKKGAQLLEE----ARRREDNLADNSQQLQLEEL 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
86-282 |
8.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 86 AAAAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAgRNKDDVVDA--ISMVEALAVQLTQREGELIQEKAEVKKLA 163
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAeeKKKADEAKKAEEKKKADEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 164 NFLKKASEDAKKLVDEERAFARAEIENARAAVQRVEKALQEQE---------QMSRASGKQDLEELMKEVQEARRIKMLH 234
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaeekaeaaEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1759371672 235 QPSKvmdmEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISELFE 282
Cdd:PTZ00121 1398 KKAE----EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-265 |
8.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 69 QNRLSVRDLASKFEKGLAAAAKLSEEARLREAASLEKhvLLKKLRDALESLKGRVAgRNKDDVVDAISMVEALAVQLTQR 148
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEE--AKKKAEDARKAEEARKA-EDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 149 EGEliQEKAEVKKLANFLKKAsEDAKKLVDEERAFARAEIENARAA--------VQRVEKAlQEQEQMSRASGKQDLEEL 220
Cdd:PTZ00121 1160 AED--ARKAEEARKAEDAKKA-EAARKAEEVRKAEELRKAEDARKAeaarkaeeERKAEEA-RKAEDAKKAEAVKKAEEA 1235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1759371672 221 MKEVQEARRIKMLHQPSKVMD-----MEHELRALRAQLTEKSKNSVRLQK 265
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKfeearMAHFARRQAAIKAEEARKADELKK 1285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
60-275 |
8.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 60 RETAQLLEQQNRLSVRDLASKFEKGLAA--AAKLSEEARlREAASLEKHVLLKKLRDALESLKGRVAgrnKDDVVDAISM 137
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAA---ADEAEAAEEK 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 138 VEA--LAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEerafaraeIENARAAVQRVEKALQEQEQMSRAsgkq 215
Cdd:PTZ00121 1366 AEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE--------LKKAAAAKKKADEAKKKAEEKKKA---- 1433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 216 dlEELMKEVQEARRIKMLHQPSKVMDMEHELRalraQLTEKSKNSVRLQKELAMSKRGLE 275
Cdd:PTZ00121 1434 --DEAKKKAEEAKKADEAKKKAEEAKKAEEAK----KKAEEAKKADEAKKKAEEAKKADE 1487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-266 |
9.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 84 GLAAAAKLseEARLREAASLEKHV-----LLKKLRDALESLKGRVAGRNK--------DDVVDAISMVEALAVQLTQRE- 149
Cdd:COG4913 605 GFDNRAKL--AALEAELAELEEELaeaeeRLEALEAELDALQERREALQRlaeyswdeIDVASAEREIAELEAELERLDa 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 150 --GELIQEKAEVKKLANFLKKASEDAKKLVDEERAfARAEIENARAAVQRVEKALQEQEQMSRASGKQDLEELMKEVQEA 227
Cdd:COG4913 683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|....*....
gi 1759371672 228 RRIKMLHQpskvmDMEHELRALRAQLTEKSKNSVRLQKE 266
Cdd:COG4913 762 AVERELRE-----NLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-280 |
1.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 56 EVVARETAQLLEQQNRLsvRDLASKFEKGLAAAAKLSEEARLREAAslekhvllKKLRDALESLKGRVAGRNKDDVVDAI 135
Cdd:PRK03918 324 NGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEA--------KAKKEELERLKKRLTGLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 136 SMVEALAVQ-------LTQREGELIQEKAEVKKLANFLKKASED---AKKLVDEERafaRAEI-ENARAAVQRVEKALQE 204
Cdd:PRK03918 394 EELEKAKEEieeeiskITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEH---RKELlEEYTAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 205 QEQMSRASgKQDLEELMKEVQEARRIKMLHQPSK-VMDMEHELRALRAQLTEKS--------KNSVRLQKELAMSKRGLE 275
Cdd:PRK03918 471 IEEKERKL-RKELRELEKVLKKESELIKLKELAEqLKELEEKLKKYNLEELEKKaeeyeklkEKLIKLKGEIKSLKKELE 549
|
....*
gi 1759371672 276 KISEL 280
Cdd:PRK03918 550 KLEEL 554
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-282 |
1.29e-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: 42.35 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 109 LKKLRDALESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEerafARAEI 188
Cdd:TIGR02168 215 YKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE----LQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 189 ENARAAVQRVEKALQEQEQmSRASGKQDLEELMKEVQEARRiKMLHQPSKVMDMEHELRALRAQLTEKSKNSVRLQKELA 268
Cdd:TIGR02168 291 YALANEISRLEQQKQILRE-RLANLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170
....*....|....
gi 1759371672 269 MSKRGLEKISELFE 282
Cdd:TIGR02168 369 ELESRLEELEEQLE 382
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-289 |
1.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 59 ARETAQLLEQQNRLSVRDLASKFEKGLAAAAKLSEEA---RLREAASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAI 135
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqeLLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 136 SMVEAlAVQLTQREGELIQEkaevkkLANFLKKASEDAKKLVDEErafARAEIENARAAVQRVEKalqeqeqmsrasgkq 215
Cdd:COG4717 392 EQAEE-YQELKEELEELEEQ------LEELLGELEELLEALDEEE---LEEELEELEEELEELEE--------------- 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1759371672 216 DLEELMKEVQEAR-RIKMLHQPSKVMDMEHELRALRAQLTEKSKNSVRLQKELAMskrgLEKISELFELD-GPEVL 289
Cdd:COG4717 447 ELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL----LEEAREEYREErLPPVL 518
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
144-277 |
1.46e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 144 QLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEerafARAEIENARAAVQRVEKALQE-QEQMSRASGKQDLEELMK 222
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKyEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1759371672 223 EVQEA-RRIKMLHQpsKVMDMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKI 277
Cdd:COG1579 97 EIESLkRRISDLED--EILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
79-281 |
1.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 79 SKFEKGLAAAAKLSEEARlREAASLEKHVL-------LKKLRDALESLKGRVAGRNKDDvvdaismVEALAVQLTQREGE 151
Cdd:PRK03918 462 KRIEKELKEIEEKERKLR-KELRELEKVLKkeselikLKELAEQLKELEEKLKKYNLEE-------LEKKAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 152 LIQEKAEVKKLANFLKKASEDAKKLvdeerafarAEIENaraAVQRVEKALQEQEQMSRASGKQDLEELMKEVQE----- 226
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKL---------AELEK---KLDELEEELAELLKELEELGFESVEELEERLKElepfy 601
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1759371672 227 ARRIKMLHQPSKVMDMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISELF 281
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-279 |
1.76e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 59 ARETAQLLEQQNRLSV--RDLASKFEKgLAAAAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAGRnkddvvdais 136
Cdd:TIGR02169 670 RSEPAELQRLRERLEGlkRELSSLQSE-LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER---------- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 137 mVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEERAFAR-----------AEIENARAAVQRVEKALQEQ 205
Cdd:TIGR02169 739 -LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 206 EQM--SRASGKQDLEELMKEVQEAR-----RIKMLHQP------------SKVMDMEHELRALRAQLTEKSKNSVRLQKE 266
Cdd:TIGR02169 818 EQKlnRLTLEKEYLEKEIQELQEQRidlkeQIKSIEKEienlngkkeeleEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250
....*....|...
gi 1759371672 267 LAMSKRGLEKISE 279
Cdd:TIGR02169 898 LRELERKIEELEA 910
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-267 |
3.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 88 AAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAISMVEALAVQLTQREGELiqEKAEVKKLANFLK 167
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADELK 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 168 KASEDAKKLVDEERAFARAEIENARAAVQRVEKALQEQEQMSRASGKQDLEELMKEVQEARRIKMLHQPSKVMDMEHELR 247
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
170 180
....*....|....*....|
gi 1759371672 248 ALRAQLTEKSKNSVRLQKEL 267
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEEL 1652
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
92-282 |
3.67e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 92 SEEARLREAAS----LEKHvlLKKLRDALESLKGRVAG-RNKDDVVD-------AISMVEALAVQLTQREGELIQEKAEV 159
Cdd:COG3206 165 NLELRREEARKalefLEEQ--LPELRKELEEAEAALEEfRQKNGLVDlseeaklLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 160 KKLANFLKKASEDAKKLVD--------EERAFARAEIENARA-------AVQRVEKALQEQEQMSRASGKQDLEELMKEV 224
Cdd:COG3206 243 AALRAQLGSGPDALPELLQspviqqlrAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1759371672 225 QEARRikmlhqpskvmdMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISELFE 282
Cdd:COG3206 323 EALQA------------REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
140-259 |
3.67e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 140 ALAVQLTQREGeliQEKAEVKKLANFLKKASEDAKKLVDE---ERAFARAEIENARAAVQRVEKALqEQEQMSRASGKQD 216
Cdd:pfam00038 29 LLETKISELRQ---KKGAEPSRLYSLYEKEIEDLRRQLDTltvERARLQLELDNLRLAAEDFRQKY-EDELNLRTSAEND 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1759371672 217 LEELMKEVQEA--------RRIKMLHQPSKVMDMEH--ELRALRAQLTEKSKN 259
Cdd:pfam00038 105 LVGLRKDLDEAtlarvdleAKIESLKEELAFLKKNHeeEVRELQAQVSDTQVN 157
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
109-204 |
3.71e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.44 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 109 LKKLRDALESLKGRVAGRNKDDVVDAIsmvealaVQLTQREGELIQE----KAEVKKLAN---FLKKASEDAKKLVDEER 181
Cdd:PRK05431 4 IKLIRENPEAVKEALAKRGFPLDVDEL-------LELDEERRELQTEleelQAERNALSKeigQAKRKGEDAEALIAEVK 76
|
90 100
....*....|....*....|...
gi 1759371672 182 AFArAEIENARAAVQRVEKALQE 204
Cdd:PRK05431 77 ELK-EEIKALEAELDELEAELEE 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-276 |
4.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 179 EERAFARAEIENARAAVQRVEKALQEQEQmSRASGKQDLEELMKEVQEARRikmlhqpsKVMDMEHELRALRAQLTEKSK 258
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKK-EEKALLKQLAALERRIAALAR--------RIRALEQELAALEAELAELEK 90
|
90
....*....|....*...
gi 1759371672 259 NSVRLQKELAMSKRGLEK 276
Cdd:COG4942 91 EIAELRAELEAQKEELAE 108
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
151-255 |
5.34e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 39.67 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 151 ELIQEKAEV--KKLANflKKASEDAKKLV--DEERafaraeienaRAAVQRVEKALQEQEQMSRASGK-----QDLEELM 221
Cdd:PRK05431 5 KLIRENPEAvkEALAK--RGFPLDVDELLelDEER----------RELQTELEELQAERNALSKEIGQakrkgEDAEALI 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1759371672 222 KEVQE-ARRIKmlhqpskvmDMEHELRALRAQLTE 255
Cdd:PRK05431 73 AEVKElKEEIK---------ALEAELDELEAELEE 98
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
62-229 |
5.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 62 TAQLLEQQNRLSVRDLA-SKFEKGLAAAAKL---------SEEAR--LREAASlEKHVL--LKKLRDALESLKGRV---- 123
Cdd:PRK04863 455 TEELLSLEQKLSVAQAAhSQFEQAYQLVRKIagevsrseaWDVARelLRRLRE-QRHLAeqLQQLRMRLSELEQRLrqqq 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 124 --------AGRNKDDVVDAISMVEALAVQLTQREGELIQEKAEVKKLANFLKKASEDAKKLVDEERAFARAEIeNARAAV 195
Cdd:PRK04863 534 raerllaeFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL-AAQDAL 612
|
170 180 190
....*....|....*....|....*....|....
gi 1759371672 196 QRvekaLQEQEQMSRASGkQDLEELMKEVQEARR 229
Cdd:PRK04863 613 AR----LREQSGEEFEDS-QDVTEYMQQLLERER 641
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
44-267 |
6.17e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 44 EGKDDRKVLSMKEVVAREtaqlLEQQNRLSVRDLASKFEKGLAAAAkLSEEARLreaaSLEKHVLLKKLRdaLESLKGRV 123
Cdd:pfam17380 294 EKMEQERLRQEKEEKARE----VERRRKLEEAEKARQAEMDRQAAI-YAEQERM----AMERERELERIR--QEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 124 AGRNKDDVVDAIS-MVEALAVQLT-QREGELIQEKAEVKKLANFLKKASEDAKKLVDEERAFARAEIENARA-AVQRVE- 199
Cdd:pfam17380 363 ERIRQEEIAMEISrMRELERLQMErQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEe 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 200 -----------KALQEQEQMSRAsgKQDLEELMK---EVQEARRIKMLHQPSKVMDMEHELRALRAQLTEKSKNSVRLQK 265
Cdd:pfam17380 443 eraremervrlEEQERQQQVERL--RQQEEERKRkklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
..
gi 1759371672 266 EL 267
Cdd:pfam17380 521 EM 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-282 |
6.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 85 LAAAAKLSEE-ARLREAaslekHVLLKKLRDALESL-----KGRVAGRNKDDVVDAISMVEALAVQLTQREGELIQEKAE 158
Cdd:COG4913 224 FEAADALVEHfDDLERA-----HEALEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 159 vkklanflkkASEDAKKLVDEERAFARAEIENARAAVQRVEKALqeqeqmsRASGKQDLEELMKEVQEARRIKMLHQpSK 238
Cdd:COG4913 299 ----------ELRAELARLEAELERLEARLDALREELDELEAQI-------RGNGGDRLEQLEREIERLERELEERE-RR 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1759371672 239 VMDMEHELRALRAQLTEKSKNSVRLQKELAMSKRGLEKISELFE 282
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
60-227 |
8.27e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 60 RETAQLLEQQNRL-SVRDLASKFEKGLAAAAKLSEEARLREAASLEKHVLLKKLRDALESLKGRVAGRNKDDVVDAISMV 138
Cdd:COG2268 210 RETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759371672 139 EALAVQLTQREGELIQEKAEVKKlanflkKASEDAKKLVDEERAFARAEIENARAAVQRVEKALQEQEQMSRASGKQDLE 218
Cdd:COG2268 290 REIELQEKEAEREEAELEADVRK------PAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLI 363
|
....*....
gi 1759371672 219 ELMKEVQEA 227
Cdd:COG2268 364 EKLPEIAEA 372
|
|
| |
