NCBI Conserved Domain Search

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

536-589

3.89e-10

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.

Pssm-ID: 425739 Cd Length: 64 Bit Score: 56.12 E-value: 3.89e-10

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837988  536 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 589
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

Smc

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

25-257

9.24e-10

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 9.24e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  25 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 104
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 105 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 183
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988 184 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:COG1196  395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

535-589

5.83e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.

Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.07 E-value: 5.83e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157837988   535 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 589
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

21-257

2.39e-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: 57.76 E-value: 2.39e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    21 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 100
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   101 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 177
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   178 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 250
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 157837988   251 SLATLTK 257
Cdd:TIGR02168  916 ELEELRE 922

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

447-514

8.44e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.60 E-value: 8.44e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837988   447 MSHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRD 514
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67

SAM_1

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

448-513

2.79e-07

Pssm-ID: 425739 Cd Length: 64 Bit Score: 48.03 E-value: 2.79e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988  448 SHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIEDYR 513
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64

SAM_2

pfam07647

SAM domain (Sterile alpha motif);

613-675

7.77e-07

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 46.88 E-value: 7.77e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837988  613 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 675
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

124-252

9.17e-06

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.29 E-value: 9.17e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  124 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 203
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157837988  204 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 252
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120

PRK02224

DNA double-strand break repair Rad50 ATPase;

82-257

3.21e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.21e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  82 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAKEALQAMK 147
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 148 ADRKRLKgektDLVSQMQQLyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 227
Cdd:PRK02224 496 ERLERAE----DLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                        170       180       190
                 ....*....|....*....|....*....|
gi 157837988 228 RSqldlkdnRMKELEAELAMAKQSLATLTK 257
Cdd:PRK02224 571 RE-------EVAELNSKLAELKERIESLER 593

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

613-672

2.60e-04

Pssm-ID: 197735 Cd Length: 68 Bit Score: 39.97 E-value: 2.60e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   613 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 672
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57

ClyA_Cry6Aa-like

cd22656

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...

131-256

1.17e-03

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: 41.59 E-value: 1.17e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 131 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLERE 209
Cdd:cd22656  111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIARK 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157837988 210 KWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 256
Cdd:cd22656  180 EIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228

Name

Accession

Description

Interval

E-value

SAM_kazrin_repeat3

cd09570

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...

612-683

4.91e-43

Pssm-ID: 188969 Cd Length: 72 Bit Score: 149.90 E-value: 4.91e-43

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837988 612 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTIF 683
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72

SAM_kazrin_repeat1

cd09564

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...

447-516

4.39e-38

Pssm-ID: 188963 Cd Length: 70 Bit Score: 136.04 E-value: 4.39e-38

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 447 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 516
Cdd:cd09564    1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70

SAM_kazrin_repeat2

cd09567

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...

526-590

2.59e-34

Pssm-ID: 188966 Cd Length: 65 Bit Score: 125.21 E-value: 2.59e-34

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837988 526 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 590
Cdd:cd09567    1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65

SAM_liprin-beta1,2_repeat3

cd09569

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...

612-682

6.47e-24

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.

Pssm-ID: 188968 Cd Length: 72 Bit Score: 95.60 E-value: 6.47e-24

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157837988 612 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTI 682
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQL 71

SAM_liprin-kazrin_repeat3

cd09496

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...

620-678

2.16e-21

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.

Pssm-ID: 188895 Cd Length: 62 Bit Score: 87.98 E-value: 2.16e-21

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157837988 620 RVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEE 678
Cdd:cd09496    1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETE 59

SAM_liprin-kazrin_repeat1

cd09494

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...

454-511

1.32e-20

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.

Pssm-ID: 188893 Cd Length: 58 Bit Score: 85.74 E-value: 1.32e-20

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157837988 454 TVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 511
Cdd:cd09494    1 RVCAWLEDFGLMPMYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58

SAM_liprin-kazrin_repeat2

cd09495

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...

531-590

2.94e-20

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.

Pssm-ID: 188894 Cd Length: 60 Bit Score: 84.89 E-value: 2.94e-20

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 531 WVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 590
Cdd:cd09495    1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60

SAM_liprin-alpha1,2,3,4_repeat3

cd09568

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...

612-680

6.98e-20

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.

Pssm-ID: 188967 Cd Length: 72 Bit Score: 84.29 E-value: 6.98e-20

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157837988 612 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMS 680
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFN 69

SAM_liprin-beta1,2_repeat2

cd09566

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...

526-589

8.37e-18

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.

Pssm-ID: 188965 Cd Length: 63 Bit Score: 78.12 E-value: 8.37e-18

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837988 526 DLDHHWVAKaWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEkHLNVSKKFHQVSILLGIELL 589
Cdd:cd09566    1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVL 62

SAM_liprin-alpha1,2,3,4_repeat1

cd09562

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...

448-511

2.88e-14

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.

Pssm-ID: 188961 Cd Length: 71 Bit Score: 68.36 E-value: 2.88e-14

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837988 448 SHWKAGTVQAWLEVVMAMPM-YVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 511
Cdd:cd09562    2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66

SAM_liprin-alpha1,2,3,4_repeat2

cd09565

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...

527-589

1.51e-13

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.

Pssm-ID: 188964 Cd Length: 66 Bit Score: 65.96 E-value: 1.51e-13

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837988 527 LDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 589
Cdd:cd09565    1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCL 63

SAM_1

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

536-589

3.89e-10

Pssm-ID: 425739 Cd Length: 64 Bit Score: 56.12 E-value: 3.89e-10

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837988  536 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 589
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

SAM_liprin-beta1,2_repeat1

cd09563

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...

450-511

4.59e-10

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.

Pssm-ID: 188962 Cd Length: 64 Bit Score: 56.08 E-value: 4.59e-10

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837988 450 WKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 511
Cdd:cd09563    4 WSTEQVCDWLAE-LGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64

Smc

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

25-257

9.24e-10

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 9.24e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  25 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 104
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 105 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 183
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988 184 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:COG1196  395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

535-589

5.83e-09

Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.07 E-value: 5.83e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157837988   535 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 589
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

COG4913

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

83-259

1.59e-08

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.59e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   83 LREEVVQLQEEVHLLRQMKEmLAKDLEESQGGKcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLvs 162
Cdd:COG4913   240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  163 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 242
Cdd:COG4913   315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                         170
                  ....*....|....*..
gi 157837988  243 AELAMAKQSLATLTKDV 259
Cdd:COG4913   387 AEAAALLEALEEELEAL 403

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

21-257

2.39e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.39e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    21 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 100
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   101 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 177
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   178 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 250
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 157837988   251 SLATLTK 257
Cdd:TIGR02168  916 ELEELRE 922

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

447-514

8.44e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.60 E-value: 8.44e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837988   447 MSHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRD 514
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

124-258

1.79e-07

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: 53.00 E-value: 1.79e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 124 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 203
Cdd:COG1579   28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157837988 204 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 258
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153

SAM_1

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

448-513

2.79e-07

Pssm-ID: 425739 Cd Length: 64 Bit Score: 48.03 E-value: 2.79e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988  448 SHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIEDYR 513
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

83-257

3.54e-07

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

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.54e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 162
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   163 QMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLK 234
Cdd:TIGR02169  780 ALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180
                   ....*....|....*....|...
gi 157837988   235 DNRMKELEAELAMAKQSLATLTK 257
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLES 882

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

85-261

4.61e-07

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: 52.84 E-value: 4.61e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  85 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 164
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 165 QQLYATLESREEQLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDH 223
Cdd:COG4942   93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157837988 224 AAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 261
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

83-259

5.33e-07

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.33e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    83 LREEVVQLQEEVHLLRQMKEMLAKDL---------EESQGGKCSEVLSA-----TELRVQLVQKEQELARAKEALQAMKA 148
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   149 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 221
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 157837988   222 ---DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

124-259

7.00e-07

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 7.00e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   124 ELRVQLVQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 200
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988   201 K-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

SAM_2

pfam07647

SAM domain (Sterile alpha motif);

613-675

7.77e-07

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 46.88 E-value: 7.77e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837988  613 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 675
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

66-260

1.41e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.41e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    66 DSAVATMENHQHGAQvllrEEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQA 145
Cdd:TIGR02168  273 RLEVSELEEEIEELQ----KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   146 MKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAA 225
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 157837988   226 AlrsqldLKDNRMKELEAELAMAKQSLATLTKDVP 260
Cdd:TIGR02168  429 K------LEEAELKELQAELEELEEELEELQEELE 457

Smc

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

83-258

1.92e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.92e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLR-----QMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEK 157
Cdd:COG1196  218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 158 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLK 234
Cdd:COG1196  298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                        170       180
                 ....*....|....*....|....
gi 157837988 235 DNRMKELEAELAMAKQSLATLTKD 258
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQ 401

COG4913

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

82-248

1.93e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.93e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   82 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKE-QELARAKEALQAMKADRKRLKGEKTDL 160
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  161 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 240
Cdd:COG4913   365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                  ....*...
gi 157837988  241 LEAELAMA 248
Cdd:COG4913   445 LRDALAEA 452

Smc

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

3-254

4.25e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.25e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   3 EDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL 82
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEML---------AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRL 153
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLerlerleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 154 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 230
Cdd:COG1196  472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551

                        250       260
                 ....*....|....*....|....
gi 157837988 231 LDLKDNRMKELEAELAMAKQSLAT 254
Cdd:COG1196  552 VVEDDEVAAAAIEYLKAAKAGRAT 575

SAM_superfamily

cd09487

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...

534-587

4.41e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.54 E-value: 4.41e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157837988 534 KAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIE 587
Cdd:cd09487    3 AEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQ 55

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

5-202

6.28e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 6.28e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   5 NKQLAlRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVtvadsAVATMENHQHGAQVLLR 84
Cdd:COG4942   54 LKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALLLS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  85 -EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevlsatELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ 163
Cdd:COG4942  128 pEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157837988 164 MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 202
Cdd:COG4942  197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

COG4913

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

83-245

6.70e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.70e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS----EVLSATELRV-----QLVQKEQELARAKEA---LQAMKADR 150
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  151 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDH----AAA 226
Cdd:COG4913   695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVerelREN 770

                         170
                  ....*....|....*....
gi 157837988  227 LRSQLDLKDNRMKELEAEL 245
Cdd:COG4913   771 LEERIDALRARLNRAEEEL 789

YhaN

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

85-256

8.64e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 8.64e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  85 EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 164
Cdd:COG4717   88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 165 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM--KELE 242
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                        170
                 ....*....|....
gi 157837988 243 AELAMAKQSLATLT 256
Cdd:COG4717  243 ERLKEARLLLLIAA 256

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

124-252

9.17e-06

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.29 E-value: 9.17e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  124 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 203
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157837988  204 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 252
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

124-259

1.06e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.06e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   124 ELRVQLVQKEQELA-----RAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVKA 198
Cdd:TIGR02168  217 ELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157837988   199 LAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353

Smc

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

118-259

2.22e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.22e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 118 EVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVK 197
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157837988 198 ALAKEKDL-------LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG1196  303 DIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

122-350

2.22e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.22e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 122 ATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR-NYEQHR----------- 189
Cdd:COG3883   32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaLYRSGGsvsyldvllgs 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 190 ------------------------KESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAEL 245
Cdd:COG3883  112 esfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 246 AMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQVRVSPCHSRQPSVIS 325
Cdd:COG3883  192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271

                        250       260
                 ....*....|....*....|....*
gi 157837988 326 DASAAEGDRSSTPSDINSPRHRTHS 350
Cdd:COG3883  272 AGAGAAAASAAGGGAGGAGGGGGGG 296

COG4913

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

124-246

2.82e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.82e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  124 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLvSQMQQLY------ATLESREEQLRDFIRNYEqhrkESEDAVK 197
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLD----ASSDDLA 688

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157837988  198 ALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELA 246
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737

YhaN

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

124-259

3.15e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.15e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 124 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKT--DLVSQMQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAK 201
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEA 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157837988 202 EKDLLEREKWELRRQAKEATDHAAA-LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

PRK02224

DNA double-strand break repair Rad50 ATPase;

82-257

3.21e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.21e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  82 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAKEALQAMK 147
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 148 ADRKRLKgektDLVSQMQQLyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 227
Cdd:PRK02224 496 ERLERAE----DLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                        170       180       190
                 ....*....|....*....|....*....|
gi 157837988 228 RSqldlkdnRMKELEAELAMAKQSLATLTK 257
Cdd:PRK02224 571 RE-------EVAELNSKLAELKERIESLER 593

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

90-267

3.29e-05

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: 47.51 E-value: 3.29e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   90 LQEEVHLLRQMKE----MLAK------DLEESQGGKCSEV------LSATELRVQLVQKE----QELARAKEalQAMKAD 149
Cdd:pfam10174 343 LQTEVDALRLRLEekesFLNKktkqlqDLTEEKSTLAGEIrdlkdmLDVKERKINVLQKKienlQEQLRDKD--KQLAGL 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  150 RKRLKGEKTDlVSQMQQLYATLES---------------REEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWEL 213
Cdd:pfam10174 421 KERVKSLQTD-SSNTDTALTTLEEalsekeriierlkeqREREDRERLEELESLKKENKDL-----KEKvSALQPELTEK 494

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837988  214 RRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 267
Cdd:pfam10174 495 ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

85-255

4.56e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 4.56e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    85 EEVVQLQEEVHLLrqmkemLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 164
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   165 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHAAALRSQLDLKDNRMKE 240
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 157837988   241 LEAELAMAKQSLATL 255
Cdd:pfam02463  428 ELEILEEEEESIELK 442

SAM_WDSUB1

cd09505

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...

535-595

4.56e-05

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.

Pssm-ID: 188904 Cd Length: 72 Bit Score: 41.92 E-value: 4.56e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157837988 535 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFS 595
Cdd:cd09505   12 TWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72

COG4913

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

126-259

5.25e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.25e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  126 RVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 205
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837988  206 LErekwELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG4913   687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736

Smc

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

122-255

6.70e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 6.70e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 122 ATELRVQLVQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 195
Cdd:COG1196  215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837988 196 ----VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATL 255
Cdd:COG1196  293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

PRK02224

DNA double-strand break repair Rad50 ATPase;

83-254

7.72e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 7.72e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATElrvqlvQKEQELARAKEALQAMKADRKRLKGEKTDLVS 162
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 163 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHAAALR 228
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                        170       180
                 ....*....|....*....|....*.
gi 157837988 229 SQLDLKDNRMKELEAELAMAKQSLAT 254
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVED 381

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

131-282

8.86e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 8.86e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  131 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KEKDLLE-- 207
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKEKELKKln 502

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837988  208 REKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWVVQ 282
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEIEE 572

PRK02224

DNA double-strand break repair Rad50 ATPase;

83-245

1.05e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.05e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS-EVLSAT--ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTD 159
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 160 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRS 229
Cdd:PRK02224 298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                        170
                 ....*....|....*.
gi 157837988 230 QLDLKDNRMKELEAEL 245
Cdd:PRK02224 378 AVEDRREEIEELEEEI 393

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

83-260

1.27e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.27e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    83 LREEVVQLQEEVHLLRQMKEMLAKDleesqggkcsevlsATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 162
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   163 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 242
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 157837988   243 AELAMAKQSLATLTKDVP 260
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507

PTZ00121

MAEBL; Provisional

79-244

2.10e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.10e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   79 AQVLLREEVVQLQEEVHLLRQMKEmlAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKT 158
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  159 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREKW---ELRRQAKEATDHAAALRSQLD--L 233
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaK 1702

                         170
                  ....*....|.
gi 157837988  234 KDNRMKELEAE 244
Cdd:PTZ00121 1703 KAEELKKKEAE 1713

SAM_DGK-delta-eta

cd09507

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...

529-589

2.36e-04

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.

Pssm-ID: 188906 Cd Length: 65 Bit Score: 39.70 E-value: 2.36e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837988 529 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 589
Cdd:cd09507    3 TNWTTEevgAWLESLQLGEYRDIFARNDIRGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

613-672

2.60e-04

Pssm-ID: 197735 Cd Length: 68 Bit Score: 39.97 E-value: 2.60e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   613 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 672
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

83-270

3.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.59e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcSEVLSA----TELRVQLVQKEQELARAKEALQAMKADRKRLKGEkt 158
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQAR----SELEQLeeelEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 159 dlVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAalrsqldlkDNRM 238
Cdd:COG4372  117 --LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA---------EQAL 185

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157837988 239 KELEAELAMAKQSLATLTKDVPKRHSLAMPGE 270
Cdd:COG4372  186 DELLKEANRNAEKEEELAEAEKLIESLPRELA 217

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

98-258

4.00e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.00e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    98 RQMKEMLAKDlEESQGGKCSEVLSATELRvQLVQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 177
Cdd:pfam01576    2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   178 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEatDHAAALRSQLD--LKDNRMKELEAELAMAKQSLATL 255
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEkvTTEAKIKKLEEDILLLEDQNSKL 150


                   ...
gi 157837988   256 TKD 258
Cdd:pfam01576  151 SKE 153

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

108-259

4.02e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 4.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 108 LEESQGGKCSEVLSATE-LRVQLVQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 181
Cdd:COG3206  162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837988 182 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG3206  242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

SAM_DGK-delta

cd09575

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...

529-589

4.91e-04

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.

Pssm-ID: 188974 Cd Length: 65 Bit Score: 39.16 E-value: 4.91e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837988 529 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 589
Cdd:cd09575    3 HLWGTEevaAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65

SAM_Ste50-like_fungal

cd09533

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...

535-592

6.42e-04

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.

Pssm-ID: 188932 Cd Length: 58 Bit Score: 38.45 E-value: 6.42e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157837988 535 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIellYQV 592
Cdd:cd09533    4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDL-KEMGITSVGHRLTILKAV---YEL 57

PRK03918

DNA double-strand break repair ATPase Rad50;

83-261

6.50e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.50e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLA-----KDLEESQGGKCSEVLSATELRV-QLVQKEQELARAKEALQAMKADRK---RL 153
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEelekeLESLEGSKRKLEEKIRELEERIeELKKEIEELEEKVKELKELKEKAEeyiKL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 154 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhRKESEDAVKALAKEKDLLEREKWELRRQAKEATDhAAALRSQLD- 232
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELEr 376

                        170       180       190
                 ....*....|....*....|....*....|...
gi 157837988 233 ----LKDNRMKELEAELAMAKQSLATLTKDVPK 261
Cdd:PRK03918 377 lkkrLTGLTPEKLEKELEELEKAKEEIEEEISK 409

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

16-260

6.61e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 6.61e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    16 VQSASQEVTNLRAELTATNRRLAELSGGGGGPGSgpgaatsasaaavtvadsAVATMENHQHGAQVllrEEVVQLQEEVH 95
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEE------------------ALNDLEARLSHSRI---PEIQAELSKLE 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    96 LLRQMKEMLAKDLEESqggkcsevLSATELRVQLVQKE-QELARAKEALQAMKADRKRlkgEKTDLVSQMQQLYATLESR 174
Cdd:TIGR02169  805 EEVSRIEARLREIEQK--------LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   175 EEQLRDFirnyeqhrkesEDAVKALAKEKDLLEREKWELRRQAKEatdhaaaLRSQLDLKDNRMKELEAELAMAKQSLAT 254
Cdd:TIGR02169  874 EAALRDL-----------ESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRLSELKAKLEALEEELSE 935


                   ....*.
gi 157837988   255 LTKDVP 260
Cdd:TIGR02169  936 IEDPKG 941

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

83-262

6.81e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 6.81e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLAKDLEEsqggkcsevlsateLRVQLVQKEQELARAKEALQAMKADRKRLKG------- 155
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARLEA--------------AKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrn 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 156 --EKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhaaalrsqldl 233
Cdd:COG1579   88 nkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL-------------------- 147

                        170       180
                 ....*....|....*....|....*....
gi 157837988 234 kDNRMKELEAELAMAKQSLATLTKDVPKR 262
Cdd:COG1579  148 -DEELAELEAELEELEAEREELAAKIPPE 175

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

83-247

7.38e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 7.38e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSatELRVQLVQKEQELARAKE----------ALQAMKAD-RK 151
Cdd:COG3206  228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSArytpnhpdviALRAQIAAlRA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 152 RLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhrkeseDAVKALAKEKDLLerekwELRRQAKeatdhaaALRSQL 231
Cdd:COG3206  306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEA------RLAELPELEAELR-----RLEREVE-------VARELY 367

                        170
                 ....*....|....*.
gi 157837988 232 DLKDNRMKELEAELAM 247
Cdd:COG3206  368 ESLLQRLEEARLAEAL 383

YhaN

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

85-210

7.75e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.75e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  85 EEVVQLQEEVHLLRQMKEMLAKDLEESqggkcSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 164
Cdd:COG4717  395 EEYQELKEELEELEEQLEELLGELEEL-----LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED- 468

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157837988 165 qQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK 210
Cdd:COG4717  469 -GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513

COG4913

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

79-226

7.78e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.78e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   79 AQVLLREEVVQLQEEVHLLRQMKEMLAKDLEE------SQGGKCSEVLSA--TELRVQLVQKEQELARAKEALQAMKADR 150
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  151 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 223
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                  ...
gi 157837988  224 AAA 226
Cdd:COG4913   456 DEA 458

SAM_superfamily

cd09487

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...

455-511

1.00e-03

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 37.99 E-value: 1.00e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157837988 455 VQAWLEVVmAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIED 511
Cdd:cd09487    2 VAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

8-260

1.03e-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: 42.06 E-value: 1.03e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   8 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL----- 82
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaela 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 -LREEVVQLQEEvhlLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKAdrkrlkgektdLV 161
Cdd:COG4942   87 eLEKEIAELRAE---LEAQKEELAELLRALY-------RLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------LA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 162 SQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 241
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                        250
                 ....*....|....*....
gi 157837988 242 EAELAMAKQSLATLTKDVP 260
Cdd:COG4942  226 EALIARLEAEAAAAAERTP 244

ClyA_Cry6Aa-like

cd22656

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...

131-256

1.17e-03

Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 1.17e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 131 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLERE 209
Cdd:cd22656  111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIARK 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157837988 210 KWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 256
Cdd:cd22656  180 EIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228

Crescentin

pfam19220

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...

126-259

1.45e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.

Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 1.45e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  126 RVQLVQKEQELARAKEALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 205
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837988  206 LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

124-257

1.53e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.53e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  124 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNYEQHRKESEDAVKALAKEK 203
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQEKLNQQKDEQIKKLQQEK 421

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837988  204 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475

COG4913

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

21-216

1.55e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.55e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   21 QEVTNLRAELTATNRRLAELsgggggpgsgpgaatsasaaavtvaDSAVATMENHQHGAQVLL-----REEVVQLQEEVH 95
Cdd:COG4913   617 AELAELEEELAEAEERLEAL-------------------------EAELDALQERREALQRLAeyswdEIDVASAEREIA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   96 LLRQMKEmlakDLEESQggkcSEVlsaTELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESRE 175
Cdd:COG4913   672 ELEAELE----RLDASS----DDL---AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157837988  176 EQLRDFIRNY--EQHRKESEDAV-----KALAKEKDLLEREKWELRRQ 216
Cdd:COG4913   741 DLARLELRALleERFAAALGDAVerelrENLEERIDALRARLNRAEEE 788

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

122-296

1.61e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  122 ATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY-------EQHRKESED 194
Cdd:pfam07888  29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSrekheelEEKYKELSA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  195 AVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKD---NRMKE------------------LEAELAMAKQSLA 253
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelERMKErakkagaqrkeeeaerkqLQAKLQQTEEELR 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157837988  254 TLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQ 296
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231

SAM_STIM-1,2-like

cd09504

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...

616-669

1.71e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.

Pssm-ID: 188903 Cd Length: 74 Bit Score: 37.70 E-value: 1.71e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157837988 616 WTNQRVLKW-VRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKH 669
Cdd:cd09504    5 WTVEDTVEWlVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIH 59

ClpA

COG0542

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...

125-260

2.01e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 125 LRVQLVQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 204
Cdd:COG0542  402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988 205 lleREKWElrrQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 260
Cdd:COG0542  460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509

HCR

pfam07111

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...

83-242

2.02e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.

Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 2.02e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   83 LREEVVQLQEEVHL---LRQMKEMLAKDLEESQGGKCSEVlsATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTD 159
Cdd:pfam07111 486 LREERNRLDAELQLsahLIQQEVGRAREQGEAERQQLSEV--AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAAS 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  160 L---VSQMQQLY--------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATDHA 224
Cdd:pfam07111 564 LrqeLTQQQEIYgqalqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEARKEE 643

                         170
                  ....*....|....*...
gi 157837988  225 AALRSQldlkdnRMKELE 242
Cdd:pfam07111 644 GQRLAR------RVQELE 655

PTZ00121

MAEBL; Provisional

79-244

2.05e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   79 AQVLLREEVVQLQEEVHLLRQMKEMLAKDL--EESQGGKCSEVLSATELR----------------VQLVQKEQELARAK 140
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKkkveqlkkkeaeekkkAEELKKAEEENKIK 1662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  141 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 217
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                         170       180
                  ....*....|....*....|....*..
gi 157837988  218 KEATDHAAALRSQLDLKdNRMKELEAE 244
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEK-KKIAHLKKE 1765

YhaN

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

134-260

2.28e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.28e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 134 QELARAKEALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRkesedAVKALAKEKDLLEREKWEL 213
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAEL 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157837988 214 RRQAKEATDHAAALRSQLdlkdNRMKELEAELAMAKQSLATLTKDVP 260
Cdd:COG4717  145 PERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLS 187

PRK03918

DNA double-strand break repair ATPase Rad50;

83-249

2.58e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.58e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  83 LREEVVQLQEEVHLLRQMKEMLAKDLEEsQGGKCSEVLSAT--ELRvQLVQKEQELARAKEALQAMKADRKRLKGEKTDL 160
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERlkELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKA 631

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 161 VSQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM 238
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710

                        170
                 ....*....|..
gi 157837988 239 KELEA-ELAMAK 249
Cdd:PRK03918 711 KELEKlEKALER 722

CusB_dom_1

pfam00529

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...

124-256

3.37e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.

Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 3.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  124 ELRVQLVQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 190
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  191 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDN----RMKELEAELAMAKQSLATLT 256
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211

SAM_SARM1-like_repeat1

cd09501

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...

536-574

3.38e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.

Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.90 E-value: 3.38e-03

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157837988 536 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVS 574
Cdd:cd09501   12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMS 50

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

76-233

3.81e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 3.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   76 QHGAQVLLREEVVQLQEEVHLLRQM------KEMLAKDLEESQGGKCSevlSATELRVQLVQKEQELARAKEALQAMKAD 149
Cdd:COG3096   503 RYRSQQALAQRLQQLRAQLAELEQRlrqqqnAERLLEEFCQRIGQQLD---AAEELEELLAELEAQLEELEEQAAEAVEQ 579

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  150 RKRLKGEKTDLVSQMQQLYA------TLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREkwelrRQAKEATDH 223
Cdd:COG3096   580 RSELRQQLEQLRARIKELAArapawlAAQDALERLR------EQSGEALADSQEVTAAMQQLLERE-----REATVERDE 648

                         170
                  ....*....|
gi 157837988  224 AAALRSQLDL 233
Cdd:COG3096   649 LAARKQALES 658

YkyA

pfam10368

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...

117-207

4.61e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.

Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 38.73 E-value: 4.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  117 SEVLSATELRVQLVQKEQE-LARAKEALQAMKADRKRLKGEKtdLVSQMQQLYATLESREEQLRDFIRNYEqhrkeseda 195
Cdd:pfam10368  57 DEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELIDAMEERYEAYDELYDAYK--------- 125

                          90
                  ....*....|..
gi 157837988  196 vKALAKEKDLLE 207
Cdd:pfam10368 126 -KALELDKELYE 136

SAM_SGMS1-like

cd09515

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...

529-567

4.69e-03

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.

Pssm-ID: 188914 Cd Length: 70 Bit Score: 36.46 E-value: 4.69e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157837988 529 HHW----VAKaWLNDIGLSQYSQAF-QNHLVDGRMLNSLMKRDL 567
Cdd:cd09515    2 HEWtcedVAK-WLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44

PRK12704

phosphodiesterase; Provisional

68-217

5.04e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 5.04e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  68 AVATMENHQHGAQVLLREEVVQLQEEVHLLRQMKEmlaKDLEEsqggKCSEvLSATELRVQlvQKEQELARAKEALQAMK 147
Cdd:PRK12704  40 AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRE----RRNE-LQKLEKRLL--QKEENLDRKLELLEKRE 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837988 148 adrKRLKGEKTDLVSQMQQlyatLESREEQLRdfiRNYEQHRKESEDaVKALAKE---KDLLEREKWELRRQA 217
Cdd:PRK12704 110 ---EELEKKEKELEQKQQE----LEKKEEELE---ELIEEQLQELER-ISGLTAEeakEILLEKVEEEARHEA 171

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

80-257

5.30e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.30e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    80 QVLLREEVVQLQEevhlLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTD 159
Cdd:pfam01576  193 EERLKKEEKGRQE----LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   160 LVSQMQQLYATLESR-------EEQLRDFIRNYEQHRKESEDAVKALAKEKDL---LEREKWELRRQAKEATDHAAALRS 229
Cdd:pfam01576  269 LEAQISELQEDLESEraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQ 348

                          170       180
                   ....*....|....*....|....*....
gi 157837988   230 QLDLKDNR-MKELEAELAMAKQSLATLTK 257
Cdd:pfam01576  349 EMRQKHTQaLEELTEQLEQAKRNKANLEK 377

PRK10246

exonuclease subunit SbcC; Provisional

66-298

5.41e-03

exonuclease subunit SbcC; Provisional

Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 5.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   66 DSAVATMEnhQHGAQVLLREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAK----- 140
Cdd:PRK10246  409 DEVAAALA--QHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKticeq 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  141 -EALQAMKADRKRLK-GEKTDLVSQMQ----QLYATLESREEQLRdfirnyeqhRKESEDAVKALAKEKDLLEREKWELR 214
Cdd:PRK10246  487 eARIKDLEAQRAQLQaGQPCPLCGSTShpavEAYQALEPGVNQSR---------LDALEKEVKKLGEEGAALRGQLDALT 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  215 RQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT-------------KDVPKRHSLampgETVLNGNQEWVV 281
Cdd:PRK10246  558 KQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaqeeherqlRLLSQRHEL----QGQIAAHNQQII 633

                         250
                  ....*....|....*..
gi 157837988  282 QadlpLTAAIRQSQQTL 298
Cdd:PRK10246  634 Q----YQQQIEQRQQQL 646

SAM_2

pfam07647

SAM domain (Sterile alpha motif);

536-589

6.21e-03

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 35.71 E-value: 6.21e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157837988  536 WLNDIGLSQYSQAFQNHLVDG-RMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 589
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGaELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65

PRK02224

DNA double-strand break repair Rad50 ATPase;

84-245

7.18e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 7.18e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  84 REEVVQLQEEVHLLRQMKEMLAKDLEESqggkcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGE-----KT 158
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERA------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEelrerAA 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988 159 DLVSQMQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHAAALRS 229
Cdd:PRK02224 548 ELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRE 627

                        170
                 ....*....|....*.
gi 157837988 230 QLDLKDNRMKELEAEL 245
Cdd:PRK02224 628 RLAEKRERKRELEAEF 643

SAM_DGK-delta-eta

cd09507

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...

446-511

7.23e-03

Pssm-ID: 188906 Cd Length: 65 Bit Score: 35.85 E-value: 7.23e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837988 446 PMSHWKAGTVQAWLEvVMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIED 511
Cdd:cd09507    1 PVTNWTTEEVGAWLE-SLQLGEYRDIFARNDIRGSELLHLERRDLK-DLGITKVGHVKRILQAIKD 64

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

70-245

7.81e-03

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 7.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   70 ATMENHQHgaqvlLREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSA--TELRVQLVQKEQE-LARAKEALqam 146
Cdd:pfam10174  64 VTQEENQH-----LQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelTEENFRRLQSEHErQAKELFLL--- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988  147 kadRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQhrkesedavKALAKEkdlLEREKWELRRQAKEATDHAAA 226
Cdd:pfam10174 136 ---RKTLEEMELRIETQKQ----TLGARDESIKKLLEMLQS---------KGLPKK---SGEEDWERTRRIAEAEMQLGH 196

                         170
                  ....*....|....*....
gi 157837988  227 LRSQLDLKDNRMKELEAEL 245
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL 215

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

5-298

8.88e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 8.88e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988     5 NKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVLLR 84
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988    85 EEVVQLQEEVHLLRQMKEMLAKD---LEESQGGKCSEVLSATELRVQL---------------VQKEQELARAKEALQAM 146
Cdd:TIGR00618  606 AEDMLACEQHALLRKLQPEQDLQdvrLHLQQCSQELALKLTALHALQLtltqervrehalsirVLPKELLASRQLALQKM 685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   147 KADRKRLKGEKTDLvSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAA 226
Cdd:TIGR00618  686 QSEKEQLTYWKEML-AQCQTLLRELETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE 761

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837988   227 LRSQLDLK-------DNRMKELEAELAM---AKQSLATLTKDVPKRHSLAMP-GETVLNGNQEWVVQADLPLTAAIRQSQ 295
Cdd:TIGR00618  762 AHFNNNEEvtaalqtGAELSHLAAEIQFfnrLREEDTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKS 841


                   ...
gi 157837988   296 QTL 298
Cdd:TIGR00618  842 ATL 844

SAM_STIM-1,2-like

cd09504

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...

529-559

9.07e-03

Pssm-ID: 188903 Cd Length: 74 Bit Score: 35.77 E-value: 9.07e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157837988 529 HHWVAK---AWL-NDIGLSQYSQAFQNHLVDGRML 559
Cdd:cd09504    3 HNWTVEdtvEWLvNSVELPQYVEAFKENGVDGSAL 37

Smc