NCBI Conserved Domain Search

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

438-491

9.89e-11

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: 58.05 E-value: 9.89e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767903325  438 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 491
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

24-160

2.88e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.00 E-value: 2.88e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKE 103
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKE 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325 104 KDLLEREKWELRRQAKEatdhataLRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4372  124 RQDLEQQRKQLEAQIAE-------LQSEIAEREEELKELEEQLESLQEELAALEQEL 173

SAM

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

437-491

1.35e-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: 54.99 E-value: 1.35e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325   437 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 491
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM

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

349-416

1.33e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 51.91 E-value: 1.33e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325   349 MSHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRD 416
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67

SMC_prok_B

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

25-160

1.44e-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: 58.53 E-value: 1.44e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    25 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325   102 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

ERM_helical

pfam20492

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

25-153

1.44e-07

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: 50.69 E-value: 1.44e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvSQMQqlyatlESREEQlrdfirnyEQHRKESEDAVKALAKEK 104
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEER----RQAE------EEAERL--------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767903325  105 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSL 153
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120

SAM_2

SAM domain (Sterile alpha motif);

515-577

1.74e-07

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 48.80 E-value: 1.74e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325  515 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 577
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58

SAM_1

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

350-415

4.89e-07

Pssm-ID: 425739 Cd Length: 64 Bit Score: 47.26 E-value: 4.89e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325  350 SHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLqLGLGVCSSLHRRKLRLAIEDYR 415
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRLK 64

PRK02224

DNA double-strand break repair Rad50 ATPase;

25-146

5.47e-06

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.47e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESE 94
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHN 341

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903325  95 DAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 146
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393

SAM

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

515-574

7.62e-05

Pssm-ID: 197735 Cd Length: 68 Bit Score: 41.51 E-value: 7.62e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   515 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 574
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57

ClyA_Cry6Aa-like

cd22656

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

31-157

5.42e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.

Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 5.42e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  31 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 109
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903325 110 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 157
Cdd:cd22656  179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

42-160

9.57e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.85 E-value: 9.57e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    42 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfiRNYEQHRKESEDavkalaKEKDLLEREKWELrrqaKEA 121
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEEL----RQLKQLEDELED------CDPTELDRAKEKL----KKL 216

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767903325   122 TDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI 255

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 ...

514-585

1.04e-43

Pssm-ID: 188969 Cd Length: 72 Bit Score: 151.83 E-value: 1.04e-43

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325 514 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSAVF 585
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 ...

349-418

1.36e-38

Pssm-ID: 188963 Cd Length: 70 Bit Score: 137.20 E-value: 1.36e-38

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325 349 MSHWKAGTVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAE 418
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 ...

428-492

1.03e-35

Pssm-ID: 188966 Cd Length: 65 Bit Score: 129.07 E-value: 1.03e-35

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903325 428 ELDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 492
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 ...

514-581

5.71e-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: 95.99 E-value: 5.71e-24

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325 514 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEM 581
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHF 68

SAM_liprin-kazrin_repeat3

cd09496

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

522-583

4.69e-22

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: 89.91 E-value: 4.69e-22

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325 522 RVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSA 583
Cdd:cd09496    1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62

SAM_liprin-kazrin_repeat1

cd09494

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

356-413

1.62e-21

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: 88.44 E-value: 1.62e-21

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325 356 TVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIED 413
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 ...

433-492

4.85e-21

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: 87.20 E-value: 4.85e-21

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325 433 WVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 492
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 ...

514-583

1.82e-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: 85.83 E-value: 1.82e-20

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325 514 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSA 583
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNN 70

SAM_liprin-beta1,2_repeat2

cd09566

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

428-491

1.51e-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: 80.05 E-value: 1.51e-18

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903325 428 ELDHHWVAKaWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEkHLNVSKKFHQVSILLGIELL 491
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 ...

350-413

6.29e-15

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: 69.90 E-value: 6.29e-15

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903325 350 SHWKAGTVQAWLEVVMAMPM-YVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIED 413
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 ...

429-491

4.63e-14

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: 67.50 E-value: 4.63e-14

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325 429 LDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 491
Cdd:cd09565    1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCL 63

SAM_1

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

438-491

9.89e-11

Pssm-ID: 425739 Cd Length: 64 Bit Score: 58.05 E-value: 9.89e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767903325  438 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 491
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

24-160

2.88e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.00 E-value: 2.88e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKE 103
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKE 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325 104 KDLLEREKWELRRQAKEatdhataLRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4372  124 RQDLEQQRKQLEAQIAE-------LQSEIAEREEELKELEEQLESLQEELAALEQEL 173

SAM

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

437-491

1.35e-09

Pssm-ID: 197735 Cd Length: 68 Bit Score: 54.99 E-value: 1.35e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325   437 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 491
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM_liprin-beta1,2_repeat1

cd09563

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

352-413

1.53e-09

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: 54.54 E-value: 1.53e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325 352 WKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIED 413
Cdd:cd09563    4 WSTEQVCDWLAE-LGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64

DR0291

COG1579

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

25-159

3.89e-09

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: 58.01 E-value: 3.89e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 104
Cdd:COG1579   28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325 105 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 159
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153

SAM

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

349-416

1.33e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 51.91 E-value: 1.33e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325   349 MSHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRD 416
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67

SMC_prok_B

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

25-160

1.44e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.44e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    25 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325   102 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

Smc

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

5-159

2.36e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.36e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQlrdfIR 84
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RR 312

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903325  85 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 159
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

Smc

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

3-167

2.38e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.38e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 82
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  83 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 162
Cdd:COG1196  413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492


                 ....*
gi 767903325 163 RHSLA 167
Cdd:COG1196  493 LLLLL 497

Smc

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

5-158

7.27e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.27e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325  85 ---NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:COG1196  394 aaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

Smc

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

2-156

9.80e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 9.80e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   2 KEMLAKDLEESQGGKSSEVLSATELRVQL--------------AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 67
Cdd:COG1196  255 LEELEAELAELEAELEELRLELEELELELeeaqaeeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  68 LYATLESREEQLRDF---IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEA 144
Cdd:COG1196  335 LEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                        170
                 ....*....|..
gi 767903325 145 ELAMAKQSLATL 156
Cdd:COG1196  415 RLERLEEELEEL 426

ERM_helical

pfam20492

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

25-153

1.44e-07

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 50.69 E-value: 1.44e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvSQMQqlyatlESREEQlrdfirnyEQHRKESEDAVKALAKEK 104
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEER----RQAE------EEAERL--------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767903325  105 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSL 153
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120

EnvC

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

2-162

1.72e-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: 54.00 E-value: 1.72e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   2 KEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRD 81
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  82 FIRNYEQ-----------HRKESEDAVK----------ALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMK 140
Cdd:COG4942  109 LLRALYRlgrqpplalllSPEDFLDAVRrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                        170       180
                 ....*....|....*....|..
gi 767903325 141 ELEAELAMAKQSLATLTKDVPK 162
Cdd:COG4942  189 ALEALKAERQKLLARLEKELAE 210

SAM_2

SAM domain (Sterile alpha motif);

515-577

1.74e-07

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 48.80 E-value: 1.74e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325  515 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 577
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58

YhaN

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

25-160

2.79e-07

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.79e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvsQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKALAKEK 104
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEER-LEELRELEEEL 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903325 105 DLLEREKWELRRQAKEATDHATA--------LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4717  166 EELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

SMC_prok_A

TIGR02169

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

3-158

4.11e-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: 4.11e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATL-ESREEQLRD 81
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQA 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    82 FIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLA 154
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878


                   ....
gi 767903325   155 TLTK 158
Cdd:TIGR02169  879 DLES 882

SAM_1

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

350-415

4.89e-07

Pssm-ID: 425739 Cd Length: 64 Bit Score: 47.26 E-value: 4.89e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325  350 SHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLqLGLGVCSSLHRRKLRLAIEDYR 415
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRLK 64

Smc

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

2-159

7.64e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 7.64e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   2 KEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM---QQLYATLESREEQ 78
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  79 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400


                 .
gi 767903325 159 D 159
Cdd:COG1196  401 Q 401

SAM_superfamily

cd09487

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

433-489

9.17e-07

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

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 46.46 E-value: 9.17e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325 433 WVAKaWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIE 489
Cdd:cd09487    1 DVAE-WLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQ 55

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

5-154

1.34e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.34e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:COG4372   78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903325  85 NYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLA 154
Cdd:COG4372  158 QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228

COG4913

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

27-147

1.43e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.43e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   27 RVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDF------IRNYEQHRKE---SEDAV 97
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVasaereIAELEAELERldaSSDDL 687

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767903325   98 KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELA 147
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737

Smc

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

5-157

1.70e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.70e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325  85 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 157
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

Cast

pfam10174

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

26-168

1.95e-06

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: 51.36 E-value: 1.95e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   26 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkala 101
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLeeaLSEKERIIERLkEQREREDRERLEELESLKKENKDL----- 480

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325  102 KEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 168
Cdd:pfam10174 481 KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548

Smc

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

19-156

2.05e-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: 2.05e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  19 EVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVK 98
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903325  99 ALAKEKDL-------LEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 156
Cdd:COG1196  303 DIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

SMC_prok_B

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

25-160

2.56e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.56e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    25 ELRVQLAQKEQELA-----RAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVKA 99
Cdd:TIGR02168  217 ELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903325   100 LAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353

SMC_prok_A

TIGR02169

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

25-164

2.58e-06

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.58e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325   102 KEKDLLEREKWELrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRH 164
Cdd:TIGR02169  765 ARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825

COG4913

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

19-160

3.24e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.24e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   19 EVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLvsqmQQLYATLESREEQLRdfirnyEQHRKESEDAVK 98
Cdd:COG4913   272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL----EARLDALREELDELE------AQIRGNGGDRLE 341

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325   99 ALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4913   342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403

CwlO1

COG3883

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

23-249

3.32e-06

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.32e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  23 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR-NYEQHR----------- 90
Cdd:COG3883   32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaLYRSGGsvsyldvllgs 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  91 ------------------------KESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 146
Cdd:COG3883  112 esfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325 147 AMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCHSRQPS 224
Cdd:COG3883  192 AAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271

                        250       260
                 ....*....|....*....|....*
gi 767903325 225 VISDASAAEGDRSSTPSDINSPRHR 249
Cdd:COG3883  272 AGAGAAAASAAGGGAGGAGGGGGGG 296

COG4913

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

25-159

5.31e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.31e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL----YATLESREEQLRDFIRNYEQHRKESEDAVKAL 100
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAAL 371

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903325  101 AKEKDLLEREKWELRRQAKEATDHATALRSQLdlkDNRMKELEAELAMAKQSLATLTKD 159
Cdd:COG4913   372 GLPLPASAEEFAALRAEAAALLEALEEELEAL---EEALAEAEAALRDLRRELRELEAE 427

PRK02224

DNA double-strand break repair Rad50 ATPase;

25-146

5.47e-06

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.47e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESE 94
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHN 341

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903325  95 DAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 146
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393

SMC_N

pfam02463

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

5-156

6.48e-06

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: 49.97 E-value: 6.48e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlYATLESREEQLRDFIR 84
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK----REAEEEEEEELEKLQE 366

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325    85 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 156
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442

SMC_prok_B

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

2-158

7.11e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 7.11e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     2 KEMLAKDLEESQGGKSsevlsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 78
Cdd:TIGR02168  763 IEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    79 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HATALRSQLDLKDNRMKELEAELAMAKQ 151
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 767903325   152 SLATLTK 158
Cdd:TIGR02168  916 ELEELRE 922

EnvC

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

29-120

7.31e-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: 48.99 E-value: 7.31e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 108
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90
                 ....*....|..
gi 767903325 109 REKWELRRQAKE 120
Cdd:COG4942   97 AELEAQKEELAE 108

DR0291

COG1579

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

7-163

7.88e-06

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

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 7.88e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   7 KDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKG---------EKTDLVSQMQQLYATLESREE 77
Cdd:COG1579   34 AELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKRRISDLED 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  78 QLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhatalrsqldlkDNRMKELEAELAMAKQSLATLT 157
Cdd:COG1579  111 EILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEELAELEAELEELEAEREELA 169


                 ....*.
gi 767903325 158 KDVPKR 163
Cdd:COG1579  170 AKIPPE 175

GumC

COG3206

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

9-160

1.21e-05

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.21e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   9 LEESQGGKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 82
Cdd:COG3206  162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325  83 IRNYEQHRKESEDAVKALAKEKDLLerekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG3206  242 LAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

25-171

1.25e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.25e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:COG4372   77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325 102 KEKDLLEREKWELRRQAKEATDHATalrsqldlkDNRMKELEAELAMAKQSLATLTKDVPKRHSLAMPGE 171
Cdd:COG4372  157 EQLESLQEELAALEQELQALSEAEA---------EQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217

COG4913

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

25-156

1.34e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEA---LQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALA 101
Cdd:COG4913   665 SAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAE 740

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325  102 KEKDLLEREKWELRRQAKEATDHATALRSQLdlkDNRMKELEAELAMAKQSLATL 156
Cdd:COG4913   741 DLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERA 792

Mplasa_alph_rch

TIGR04523

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

25-183

1.43e-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: 48.48 E-value: 1.43e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KE 103
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  104 KDLLE--REKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWV 181
Cdd:TIGR04523 496 KELKKlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEI 570


                  ..
gi 767903325  182 VQ 183
Cdd:TIGR04523 571 EE 572

Smc

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

23-156

1.80e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.80e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  23 ATELRVQLAQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 96
Cdd:COG1196  215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903325  97 ----VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 156
Cdd:COG1196  293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

SAM_WDSUB1

cd09505

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

437-497

1.91e-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: 43.07 E-value: 1.91e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903325 437 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFS 497
Cdd:cd09505   12 TWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72

SMC_prok_B

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

1-161

2.06e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.06e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     1 MKEMLAKDLEESQggKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQ 78
Cdd:TIGR02168  303 QKQILRERLANLE--RQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    79 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAlrsqldLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK------LEEAELKELQAELEELEEELEELQE 454


                   ...
gi 767903325   159 DVP 161
Cdd:TIGR02168  455 ELE 457

Mplasa_alph_rch

TIGR04523

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

7-158

3.42e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 3.42e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    7 KDLEESQGGKSSEVLsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNY 86
Cdd:TIGR04523 345 SQLKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQ 403

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325   87 EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475

YkyA

pfam10368

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

2-108

5.00e-05

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: 44.89 E-value: 5.00e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    2 KEMLAKDLEESQ--GGKSSEVLSATELRVQLAQKEQE-LARAKEALQAMKADRKRLKGEKtdLVSQMQQLYATLESREEQ 78
Cdd:pfam10368  39 EEIIELGMDEFDeiKKLSDEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELIDAMEERYEA 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 767903325   79 LRDFIRNYEqhrkesedavKALAKEKDLLE 108
Cdd:pfam10368 117 YDELYDAYK----------KALELDKELYE 136

GumC

COG3206

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

24-158

5.37e-05

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 5.37e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-----VSQMQQLYATLESREEQLRdfiRNY-EQHRKesedaV 97
Cdd:COG3206  222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspvIQQLRAQLAELEAELAELS---ARYtPNHPD-----V 293

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903325  98 KALAKEKDLLERekwELRRQAKEAtdhATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:COG3206  294 IALRAQIAALRA---QLQQEAQRI---LASLEAELEALQAREASLQAQLAQLEARLAELPE 348

COG4913

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

25-149

6.47e-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: 6.47e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKE-QELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 103
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767903325  104 KDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMA 149
Cdd:COG4913   407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452

Mplasa_alph_rch

TIGR04523

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

2-160

6.49e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 6.49e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    2 KEMLAKDLE---ESQGGKSSEV-LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMqqlyATLESREE 77
Cdd:TIGR04523 452 KELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI----SSLKEKIE 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   78 QLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAE-------LAM 148
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEkkdlikeIEE 607

                         170
                  ....*....|..
gi 767903325  149 AKQSLATLTKDV 160
Cdd:TIGR04523 608 KEKKISSLEKEL 619

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

25-151

6.68e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 6.68e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEALQAMKAD-------RKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY-EQHRKESEDA 96
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKlyqeeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLaEEAEREEEEF 263

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325   97 VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD-NRMKELEAELAMAKQ 151
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREeQRAAEREEELEEGER 319

SAM

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

515-574

7.62e-05

Pssm-ID: 197735 Cd Length: 68 Bit Score: 41.51 E-value: 7.62e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   515 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 574
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57

SAM_superfamily

cd09487

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

357-413

8.07e-05

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 41.07 E-value: 8.07e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325 357 VQAWLEVVmAMPMYVKACTENVKSGKVLLSLSDEDLQlGLGVCSSLHRRKLRLAIED 413
Cdd:cd09487    2 VAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56

Myosin_tail_1

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

3-159

8.12e-05

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: 46.32 E-value: 8.12e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     3 EMLAKDlEESQGGKSSEVLSATELRvQLAQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQLRDF 82
Cdd:pfam01576    6 EMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQELEEI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    83 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEatdhATALRSQLDLK----DNRMKELEAELAMAKQSLATLTK 158
Cdd:pfam01576   77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE----EEAARQKLQLEkvttEAKIKKLEEDILLLEDQNSKLSK 152


                   .
gi 767903325   159 D 159
Cdd:pfam01576  153 E 153

SAM_DGK-delta-eta

cd09507

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

431-491

8.40e-05

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: 41.24 E-value: 8.40e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903325 431 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 491
Cdd:cd09507    3 TNWTTEevgAWLESLQLGEYRDIFARNDIRGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65

PRK02224

DNA double-strand break repair Rad50 ATPase;

17-158

1.02e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  17 SSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDA 96
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRET 531

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325  97 VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593

YhaN

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

15-161

1.43e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.43e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  15 GKSSeVLSATE--LRVQLAQKEQELARA-----KEALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYE 87
Cdd:COG4717   35 GKST-LLAFIRamLLERLEKEADELFKPqgrkpELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELE 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325  88 QHRKESEDAVKALAKEKDLLEREkwELRRQAKEATDHATALRSQLDL---KDNRMKELEAELAMAKQSLATLTKDVP 161
Cdd:COG4717  113 ELREELEKLEKLLQLLPLYQELE--ALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLS 187

PRK02224

DNA double-strand break repair Rad50 ATPase;

7-155

1.47e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.47e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   7 KDLEESQGGKSSEVLSATElrvqlaQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY 86
Cdd:PRK02224 229 REQARETRDEADEVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  87 EQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHATALRSQLDLKDNRMKELEAELAMAKQS 152
Cdd:PRK02224 303 GLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLEERAEELREEAAELESELEEAREA 378


                 ...
gi 767903325 153 LAT 155
Cdd:PRK02224 379 VED 381

Myosin_tail_1

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

21-158

1.51e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.51e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    21 LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESR-------EEQLRDFIRNYEQHRKES 93
Cdd:pfam01576  229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESEraarnkaEKQRRDLGEELEALKTEL 308

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767903325    94 EDAVKALAKEKDL---LEREKWELRRQAKEATDHATALRSQLDLKDNR-MKELEAELAMAKQSLATLTK 158
Cdd:pfam01576  309 EDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQEMRQKHTQaLEELTEQLEQAKRNKANLEK 377

CALCOCO1

pfam07888

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

10-197

1.55e-04

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: 44.89 E-value: 1.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   10 EESQGGKSSE-----VLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:pfam07888  11 EESHGEEGGTdmllvVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   85 NY-------EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD---NRMKE------------- 141
Cdd:pfam07888  91 QSrekheelEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelERMKErakkagaqrkeee 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903325  142 -----LEAELAMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQ 197
Cdd:pfam07888 171 aerkqLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231

SAM_DGK-delta

cd09575

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

431-491

1.79e-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: 40.32 E-value: 1.79e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903325 431 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 491
Cdd:cd09575    3 HLWGTEevaAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65

YqiK

COG2268

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];

29-150

1.87e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];

Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.87e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  29 QLAQKEQELARAKEALQAmKADRKRLKGEKtdlvsqmqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 108
Cdd:COG2268  238 RIAEAEAELAKKKAEERR-EAETARAEAEA-----------AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE 305

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767903325 109 -----REKWELRRQAKEATDHATALRSQLDLKdnrmKELEAELAMAK 150
Cdd:COG2268  306 leadvRKPAEAEKQAAEAEAEAEAEAIRAKGL----AEAEGKRALAE 348

COG4913

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

5-147

2.40e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.40e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRK-RLKGEktdlVSQMQQLYATLESREEQLRDFI 83
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLERE----IERLERELEERERRRARLEALL 368

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903325   84 RNYEQHRKESEDAVKALAKE-KDLLEREKWELRRQAKEATDHATALRsqlDLKDNRmKELEAELA 147
Cdd:COG4913   369 AALGLPLPASAEEFAALRAEaAALLEALEEELEALEEALAEAEAALR---DLRREL-RELEAEIA 429

EnvC

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

22-159

2.73e-04

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.73e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  22 SATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325 102 KEKDLLEREKWELRRQAKE--------ATDHATALRSQLDLKD--NRMKELEAELAMAKQSLATLTKD 159
Cdd:COG4942  101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAE 168

HlpA

COG2825

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...

9-104

2.88e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.13 E-value: 2.88e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   9 LEESQGGKSSEvlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDlvSQMQQLYATLESREEQLRDFIRNYEQ 88
Cdd:COG2825   35 LQESPEGKAAQ----KKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSE--EERQKKERELQKKQQELQRKQQEAQQ 108

                         90       100
                 ....*....|....*....|....*...
gi 767903325  89 --HRKESE----------DAVKALAKEK 104
Cdd:COG2825  109 dlQKRQQEllqpilekiqKAIKEVAKEE 136

COG4913

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

8-138

2.89e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    8 DLEESQGGKSSEVLSATELRVQLAQKEQELARA--------KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQL 79
Cdd:COG4913   299 ELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   80 RDfirNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLD-LKDNR 138
Cdd:COG4913   379 AE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERRK 435

SAM_Ste50-like_fungal

cd09533

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

437-494

2.89e-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: 39.61 E-value: 2.89e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325 437 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIellYQV 494
Cdd:cd09533    4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDL-KEMGITSVGHRLTILKAV---YEL 57

PRK02224

DNA double-strand break repair Rad50 ATPase;

22-155

2.93e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.93e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  22 SATELRVQLAQKEQE-----LARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQlRDFIRNYEQHRKESEDA 96
Cdd:PRK02224 188 SLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEIEDLRET 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325  97 VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD-------NRMKELEAELAMAKQSLAT 155
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEE 332

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

2-162

3.16e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 3.16e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    2 KEMLAKDLEESQGGKSSEVLSATEL-----RVQLAQKE--QELARAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLES 74
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELtahcdKLLLENKEltQEASDMTLELKKHQEDIINCKKQEERMLKQIE----NLEE 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   75 REEQLRDFIRNYEQHRKESEDAVK---------ALAKEKDLLEREKW-----------------------ELRRQAKEAT 122
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDEVKckldkseenARSIEYEVLKKEKQmkilenkcnnlkkqienknknieELHQENKALK 621

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767903325  123 DHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 162
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661

EnvC

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

29-103

3.55e-04

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.55e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903325  29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 103
Cdd:COG4942  161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

24-134

3.95e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.

Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 3.95e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   24 TELRVQLAQKEQELARAKEALQAMKAD----RKRLKG----------EKTDLVSQMQQLYATLESREEQLRDFIRNYEQH 89
Cdd:pfam07926   4 SSLQSEIKRLKEEAADAEAQLQKLQEDlekqAEIAREaqqnyerelvLHAEDIKALQALREELNELKAEIAELKAEAESA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767903325   90 RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDL 134
Cdd:pfam07926  84 KAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128

Crescentin

pfam19220

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

27-160

4.14e-04

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: 43.52 E-value: 4.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   27 RVQLAQKEQELARAKEALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 106
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767903325  107 LEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176

Lebercilin

pfam15619

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...

19-147

4.86e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.

Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.81 E-value: 4.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   19 EVLSA-----TELRVQLAQKEQELARAKEALQAMKADRKR-------LKGEKTDLVSQMQQLYATLESREEQLR---DFI 83
Cdd:pfam15619   4 RVLSArlhkiKELQNELAELQSKLEELRKENRLLKRLQKRqekalgkYEGTESELPQLIARHNEEVRVLRERLRrlqEKE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903325   84 RNYEQHRKESED----------AVKALAKEKDLLEREkwELRRQAKEATDHatalrsqLDLKDNRMKELEAELA 147
Cdd:pfam15619  84 RDLERKLKEKEAellrlrdqlkRLEKLSEDKNLAERE--ELQKKLEQLEAK-------LEDKDEKIQDLERKLE 148

SAM_WDSUB1

cd09505

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

348-418

5.21e-04

Pssm-ID: 188904 Cd Length: 72 Bit Score: 39.22 E-value: 5.21e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903325 348 PMSHWKAGTVQAWLEVVMaMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAE 418
Cdd:cd09505    1 SLQDWSEEDVCTWLRSIG-LEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKS 70

ClyA_Cry6Aa-like

cd22656

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

31-157

5.42e-04

Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 5.42e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  31 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 109
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903325 110 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 157
Cdd:cd22656  179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228

EnvC

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

29-121

5.58e-04

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.58e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 108
Cdd:COG4942  147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                         90
                 ....*....|...
gi 767903325 109 REKWELRRQAKEA 121
Cdd:COG4942  227 ALIARLEAEAAAA 239

YhaN

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

3-157

5.67e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.67e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   3 EMLAKDLEESQggkssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 82
Cdd:COG4717  105 EELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325  83 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM--KELEAELAMAKQSLATLT 157
Cdd:COG4717  180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAA 256

ClpA

COG0542

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

26-161

5.87e-04

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

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 5.87e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  26 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 105
Cdd:COG0542  402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325 106 lleREKWElrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 161
Cdd:COG0542  460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509

CusB_dom_1

pfam00529

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

25-157

6.55e-04

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: 42.80 E-value: 6.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 91
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   92 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDN----RMKELEAELAMAKQSLATLT 157
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211

MukB

COG3096

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

23-153

6.66e-04

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

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 6.66e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   23 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKT---DLVSQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKA 99
Cdd:COG3096   514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQ-LEQLRA 592

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325  100 LAKE-----------KDLLERekweLRRQAKEATDHATALRSQLDLKDNRMKELEAE---LAMAKQSL 153
Cdd:COG3096   593 RIKElaarapawlaaQDALER----LREQSGEALADSQEVTAAMQQLLEREREATVErdeLAARKQAL 656

SMC_prok_A

TIGR02169

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

21-161

6.99e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 6.99e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    21 LSATELRVQLAQKE-QELARAKEALQAMKADRKRlkgEKTDLVSQMQQLYATLESREEQLRDFirnyeqhrkesEDAVKA 99
Cdd:TIGR02169  821 LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDL-----------ESRLGD 886

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325   100 LAKEKDLLEREKWELRRQAKEatdhataLRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 161
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIEE-------LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941

PTZ00121

MAEBL; Provisional

16-145

7.15e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 7.15e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   16 KSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfIRNYEQHRKESED 95
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEE 1658

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325   96 AVKALAKEKDLLEREKW---ELRRQAKEATDHATALRSQLD--LKDNRMKELEAE 145
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAE 1713

SMC_prok_B

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

1-160

7.18e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 7.18e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     1 MKEMLAKDLEE-----SQGGKSSEVLSATELRV--QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLE 73
Cdd:TIGR02168  713 ELEQLRKELEElsrqiSALRKDLARLEAEVEQLeeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    74 SREEQLRDFIRNY----EQHRKESEDA------VKALAKEKDLLEREKWELRRQAKEATDHATAL--------------R 129
Cdd:TIGR02168  793 QLKEELKALREALdelrAELTLLNEEAanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieeleelieelE 872

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767903325   130 SQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEELSEEL 903

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

25-150

7.91e-04

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 7.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARA--KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQlrdFIRNYEQHRKESE--DAVKAL 100
Cdd:pfam13868  33 RIKAEEKEEERRLDEMmeEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQK---RQEEYEEKLQEREqmDEIVER 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767903325  101 AKEKDLLEREKwELRRQAKEATDHATALRSQLDLKD-NRMKELEAELAMAK 150
Cdd:pfam13868 110 IQEEDQAEAEE-KLEKQRQLREEIDEFNEEQAEWKElEKEEEREEDERILE 159

GumC

COG3206

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

1-148

1.11e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.11e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   1 MKEMLAKDLEESQGGKSSEVLSatELRVQLAQKEQELARAKE----------ALQAMKAD-RKRLKGEKTDLVSQMQQLY 69
Cdd:COG3206  245 LRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSArytpnhpdviALRAQIAAlRAQLQQEAQRILASLEAEL 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767903325  70 ATLESREEQLRDFIRNYEQhrkeseDAVKALAKEKDLLerekwELRRQAKeatdhatALRSQLDLKDNRMKELEAELAM 148
Cdd:COG3206  323 EALQAREASLQAQLAQLEA------RLAELPELEAELR-----RLEREVE-------VARELYESLLQRLEEARLAEAL 383

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

25-160

1.14e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.14e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRN----------YEQHRKESE 94
Cdd:COG1340   47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsidklrkeIERLEWRQQ 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325  95 DAVKALAKEKDLLEREKwELRRQAKEAtdhatalRSQLDLKDNrMKELEAELAMAKQSLATLTKDV 160
Cdd:COG1340  127 TEVLSPEEEKELVEKIK-ELEKELEKA-------KKALEKNEK-LKELRAELKELRKEAEEIHKKI 183

SAM_STIM-1,2-like

cd09504

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

518-571

1.22e-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: 38.08 E-value: 1.22e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325 518 WTNQRVLKW-VRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKH 571
Cdd:cd09504    5 WTVEDTVEWlVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIH 59

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

24-146

1.36e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.36e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGE--KTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKEsedAVKALA 101
Cdd:COG5185  336 TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLE 412

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767903325 102 KEKDLLEREKWELRRQAKEATdhatalrSQLDLKDNRMKELEAEL 146
Cdd:COG5185  413 DTLKAADRQIEELQRQIEQAT-------SSNEEVSKLLNELISEL 450

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

57-166

1.39e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.39e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  57 EKTDLVSQMQqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQL-DLK 135
Cdd:COG1340    1 SKTDELSSSL---EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkELK 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767903325 136 DNR------MKELEAELAMAKQSLATLTKDVPKRHSL 166
Cdd:COG1340   78 EERdelnekLNELREELDELRKELAELNKAGGSIDKL 114

GBP_C

pfam02841

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...

2-115

1.50e-03

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

Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.50 E-value: 1.50e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    2 KEMLAKDLEESQGgkSSEVLSATELRVQLAQKEQELARAKEAlqAMKADRKRLKGEKTDLVSQMQ-----------QLYA 70
Cdd:pfam02841 175 EEVLQEFLQSKEA--VEEAILQTDQALTAKEKAIEAERAKAE--AAEAEQELLREKQKEEEQMMEaqersyqehvkQLIE 250

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767903325   71 TLES-REEQLRDFIRNYEQHRKESEDAVKA-LAKEKDLLEREKWELR 115
Cdd:pfam02841 251 KMEAeREQLLAEQERMLEHKLQEQEELLKEgFKTEAESLQKEIQDLK 297

PTZ00121

MAEBL; Provisional

3-162

1.52e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.52e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    3 EMLAKDLEESQGGKSSEVLSATELRvqlaqKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdf 82
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-- 1701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   83 iRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKdNRMKELEAELAMAKQSLATLTKD 159
Cdd:PTZ00121 1702 -KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEA 1779


                  ...
gi 767903325  160 VPK 162
Cdd:PTZ00121 1780 VIE 1782

PspA

COG1842

Phage shock protein A [Transcription, Signal transduction mechanisms];

72-160

1.69e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];

Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 1.69e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  72 LESREEQLRDFIRNYEQHRKESEDAV-KALAKEKdLLEREKWELRRQAKEATDHA-------------TALRSQLDLkDN 137
Cdd:COG1842   21 AEDPEKMLDQAIRDMEEDLVEARQALaQVIANQK-RLERQLEELEAEAEKWEEKArlalekgredlarEALERKAEL-EA 98

                         90       100
                 ....*....|....*....|...
gi 767903325 138 RMKELEAELAMAKQSLATLTKDV 160
Cdd:COG1842   99 QAEALEAQLAQLEEQVEKLKEAL 121

SAM_SARM1-like_repeat1

cd09501

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

438-476

1.70e-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: 37.67 E-value: 1.70e-03

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767903325 438 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVS 476
Cdd:cd09501   12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMS 50

TACC_C

pfam05010

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...

2-158

1.91e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.

Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.43 E-value: 1.91e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    2 KEMLAKDLEESQGGKSSEVLSAT--ELRVQLAQKEQELARAKEALQAmkaDRKRLKGEKTDLVSQMQQLYATLESREEQL 79
Cdd:pfam05010  15 NEIEEKELEINELKAKYEELRREnlEMRKIVAEFEKTIAQMIEEKQK---QKELEHAEIQKVLEEKDQALADLNSVEKSF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   80 RDFIRNYEQHR------KESE---------------------DAVKALAKEKdlLEREKWELRRQAKEATDHATALRSQL 132
Cdd:pfam05010  92 SDLFKRYEKQKevisgyKKNEeslkkcaqdylarikkeeqryQALKAHAEEK--LDQANEEIAQVRSKAKAETAALQASL 169

                         170       180
                  ....*....|....*....|....*.
gi 767903325  133 DLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:pfam05010 170 RKEQMKVQSLERQLEQKTKENEELTK 195

SAM_SGMS1-like

cd09515

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

431-469

1.94e-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: 37.61 E-value: 1.94e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767903325 431 HHW----VAKaWLNDIGLSQYSQAF-QNHLVDGRMLNSLMKRDL 469
Cdd:cd09515    2 HEWtcedVAK-WLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44

SAM_2

SAM domain (Sterile alpha motif);

438-491

2.11e-03

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.25 E-value: 2.11e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767903325  438 WLNDIGLSQYSQAFQNHLVDG-RMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 491
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGaELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65

Tropomyosin_1

pfam12718

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...

31-150

2.15e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.

Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.21 E-value: 2.15e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   31 AQKEQELARAKEALQAMKA---DRKRLKGEKTDLVSQMQQLYATLESREEQLRDF---IRNYEQHRKESEdavkALAKEK 104
Cdd:pfam12718   7 LEAENAQERAEELEEKVKEleqENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAkekAEESEKLKTNNE----NLTRKI 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  105 DLLE----------REKWELRRQAKEATDHA----TALRSQLDLKDNRMKELEAELAMAK 150
Cdd:pfam12718  83 QLLEeeleesdkrlKETTEKLRETDVKAEHLerkvQALEQERDEWEKKYEELEEKYKEAK 142

OmpH

pfam03938

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

9-104

2.27e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 2.27e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    9 LEESQGGKSSEvlsaTELRVQLAQKEQELARAKEALQAMKADrkrLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQ 88
Cdd:pfam03938  11 LEESPEGKAAQ----AQLEKKFKKRQAELEAKQKELQKLYEE---LQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQ 83

                          90       100
                  ....*....|....*....|....*...
gi 767903325   89 --HRKESE----------DAVKALAKEK 104
Cdd:pfam03938  84 elQKKQQEllqpiqdkinKAIKEVAKEK 111

DUF4200

pfam13863

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...

30-143

2.33e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.

Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 2.33e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   30 LAQKEQELARAKEALQAMKADRKRLKgektdlvSQMQQLYATLESREEQLRDFIRNYEQHRKESED----AVKALAKE-- 103
Cdd:pfam13863   1 LLEKKREMFLVQLALDAKREEIERLE-------ELLKQREEELEKKEQELKEDLIKFDKFLKENDAkrrrALKKAEEEtk 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767903325  104 -KDLLEREkwelrrqAKEATDHATALRSQLDLKDNRMKELE 143
Cdd:pfam13863  74 lKKEKEKE-------IKKLTAQIEELKSEISKLEEKLEEYK 107

SAM_2

SAM domain (Sterile alpha motif);

352-413

2.83e-03

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 36.86 E-value: 2.83e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325  352 WKAGTVQAWLEVvMAMPMYVKACTEN-VKSGKVLLSLSDEDLQlGLGVCSSLHRRKLRLAIED 413
Cdd:pfam07647   4 WSLESVADWLRS-IGLEQYTDNFRDQgITGAELLLRLTLEDLK-RLGITSVGHRRKILKKIQE 64

PRK02224

DNA double-strand break repair Rad50 ATPase;

24-154

3.13e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.13e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 103
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767903325 104 KDLLErekwelrrqakEATDHATALRSQLDLKDNRMKELEAELAMAKQSLA 154
Cdd:PRK02224 404 PVDLG-----------NAEDFLEELREERDELREREAELEATLRTARERVE 443

SAM_DGK-delta-eta

cd09507

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

348-413

3.26e-03

Pssm-ID: 188906 Cd Length: 65 Bit Score: 36.62 E-value: 3.26e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325 348 PMSHWKAGTVQAWLEvVMAMPMYVKACTENVKSGKVLLSLSDEDLQlGLGVCSSLHRRKLRLAIED 413
Cdd:cd09507    1 PVTNWTTEEVGAWLE-SLQLGEYRDIFARNDIRGSELLHLERRDLK-DLGITKVGHVKRILQAIKD 64

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

25-185

3.62e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.62e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  25 ELRVQLAQKEQELARAKEALQAMKADrkrlkgektdlvsqMQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEK 104
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEE--------------LEEKKEKLQEEEDKLL------EEAEKEAQQAIKEAKKEA 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325 105 DLLEREKWELRRQAKEAtdhatalrsqldLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAMPGETV----------- 173
Cdd:PRK00409 587 DEIIKELRQLQKGGYAS------------VKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkylslgqkgev 654

                        170
                 ....*....|....
gi 767903325 174 --LNGNQEWVVQAD 185
Cdd:PRK00409 655 lsIPDDKEAIVQAG 668

PRK03918

DNA double-strand break repair ATPase Rad50;

2-150

3.71e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.71e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   2 KEMLAKDLEEsQGGKSSEVLsatELRVQ-LAQKEQELARAKEALQAMKADRKRLKGEKTDLV---SQMQQLYATLESREE 77
Cdd:PRK03918 572 LAELLKELEE-LGFESVEEL---EERLKeLEPFYNEYLELKDAEKELEREEKELKKLEEELDkafEELAETEKRLEELRK 647

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325  78 QLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEA-ELAMAK 150
Cdd:PRK03918 648 ELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlEKALER 722

PRK03918

DNA double-strand break repair ATPase Rad50;

3-160

4.01e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   3 EMLAKDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKAdrkrLKGEKTDLVSQMQQLYATLESREE---QL 79
Cdd:PRK03918 192 EELIKEKEKELEEVLREI---NEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEkirEL 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  80 RDFIRNYEQHRKESEDAVKAL------AKE----KDLLEREKWELRRQAKEATDHATALR------SQLDLKDNRMKELE 143
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELkelkekAEEyiklSEFYEEYLDELREIEKRLSRLEEEINgieeriKELEEKEERLEELK 344

                        170
                 ....*....|....*..
gi 767903325 144 AELAMAKQSLATLTKDV 160
Cdd:PRK03918 345 KKLKELEKRLEELEERH 361

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

25-152

4.03e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 4.03e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   25 ELRVQLAQKEQELARAKEALQAMkADRKRLKGEKTDLVSQMQQlyaTLESREEQLRDFIRN-------YEQHRKESEDAV 97
Cdd:pfam05557  52 ELQKRIRLLEKREAEAEEALREQ-AELNRLKKKYLEALNKKLN---EKESQLADAREVISClknelseLRRQIQRAELEL 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325   98 KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDL---KDNRMKELEAELAMAKQS 152
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSlaeAEQRIKELEFEIQSQEQD 185

HCR

pfam07111

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

5-121

4.31e-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: 40.51 E-value: 4.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    5 LAKDLEESQGGKSSEVLSATELRV-QLAQK-EQELARAKEAL----QAMKADRkRLKGEKTDL-------VSQMQQLY-- 69
Cdd:pfam07111 499 LSAHLIQQEVGRAREQGEAERQQLsEVAQQlEQELQRAQESLasvgQQLEVAR-QGQQESTEEaaslrqeLTQQQEIYgq 577

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325   70 ------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEA 121
Cdd:pfam07111 578 alqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEA 639

YhaN

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

2-111

4.42e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.42e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   2 KEMLAKDLEESQggKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSqmQQLYATLESREEQLRD 81
Cdd:COG4717  408 EEQLEELLGELE--ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKA 483

                         90       100       110
                 ....*....|....*....|....*....|
gi 767903325  82 FIRNYEQHRKESEDAVKALAKEKDLLEREK 111
Cdd:COG4717  484 ELRELAEEWAALKLALELLEEAREEYREER 513

SAM_Shank1,2,3

cd09506

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...

437-484

4.61e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.

Pssm-ID: 188905 Cd Length: 66 Bit Score: 36.14 E-value: 4.61e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767903325 437 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSI 484
Cdd:cd09506   12 DWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTE-LGVTRVGHRMNI 58

EnvC

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

66-156

4.99e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.99e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  66 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAE 145
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90
                 ....*....|.
gi 767903325 146 LAMAKQSLATL 156
Cdd:COG4942   99 LEAQKEELAEL 109

DR0291

COG1579

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

46-156

5.16e-03

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

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.16e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  46 AMKADRKRLKgektdlvsQMQQLY---ATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT 122
Cdd:COG1579    1 AMPEDLRALL--------DLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767903325 123 DHATALRSQLD-LKDNR-MKELEAELAMAKQSLATL 156
Cdd:COG1579   73 ARIKKYEEQLGnVRNNKeYEALQKEIESLKRRISDL 108

PRK04778

septation ring formation regulator EzrA; Provisional

28-161

5.53e-03

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.53e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  28 VQLAQKEQELARAKEAlqamkADRKRLKGEKTDLV---SQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-E 103
Cdd:PRK04778  79 NSLPDIEEQLFEAEEL-----NDKFRFRKAKHEINeieSLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElR 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903325 104 KDLLER-----------EK-----WELRRQAKEAT---DHATAlRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 161
Cdd:PRK04778 154 KSLLANrfsfgpaldelEKqlenlEEEFSQFVELTesgDYVEA-REILDQLEEELAALEQIMEEIPELLKELQTELP 229

SAM_STIM-1,2-like

cd09504

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

431-461

6.37e-03

Pssm-ID: 188903 Cd Length: 74 Bit Score: 36.16 E-value: 6.37e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767903325 431 HHWVAK---AWL-NDIGLSQYSQAFQNHLVDGRML 461
Cdd:cd09504    3 HNWTVEdtvEWLvNSVELPQYVEAFKENGVDGSAL 37

CENP-F_leu_zip

pfam10473

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...

3-108

6.70e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.

Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 37.66 E-value: 6.70e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYAT---LESREEQL 79
Cdd:pfam10473  27 ENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERvseLESLNSSL 106

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767903325   80 RDFIRNYEQHR----KESEDAVKALAKE-KDLLE 108
Cdd:pfam10473 107 ENLLEEKEQEKvqmkEESKTAVEMLQTQlKELNE 140

SAM_Ste11_fungal

cd09534

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...

436-491

6.87e-03

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.

Pssm-ID: 188933 Cd Length: 62 Bit Score: 35.65 E-value: 6.87e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903325 436 KAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 491
Cdd:cd09534    7 EEWLNELNCGQYLDIFEKNLITGDLLLELDKEAL-KELGITKVGDRIRLLRAIKSL 61

CCDC22

pfam05667

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...

2-163

7.00e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.

Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 7.00e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    2 KEMLAKDLEESQGGKSSEVLSATELRvqlAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRD 81
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVETEEELQ---QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   82 FIRNYEQHRK---ESEDAVKALAKEKDLLER---------EKWE---------LRRQAKEATDHATALRSQLD----LKD 136
Cdd:pfam05667 382 LEKQYKVKKKtldLLPDAEENIAKLQALVDAsaqrlvelaGQWEkhrvplieeYRALKEAKSNKEDESQRKLEeikeLRE 461

                         170       180
                  ....*....|....*....|....*..
gi 767903325  137 nRMKELEAELAMAKQSLATLTKDVPKR 163
Cdd:pfam05667 462 -KIKEVAEEAKQKEELYKQLVAEYERL 487

Myosin_tail_1

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

8-155

7.47e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 7.47e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     8 DLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEA-------LQAMKADRKR------LKGE--KTDLVSQMQQLYATL 72
Cdd:pfam01576  682 ELERSKRALEQQV---EEMKTQLEELEDELQATEDAklrlevnMQALKAQFERdlqardEQGEekRRQLVKQVRELEAEL 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    73 ESREEQ--------------LRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKEATDHATALRSQLDLKDNR 138
Cdd:pfam01576  759 EDERKQraqavaakkkleldLKELEAQIDAANKGREEAVKQLKK----LQAQMKDLQRELEEARASRDEILAQSKESEKK 834

                          170
                   ....*....|....*..
gi 767903325   139 MKELEAELAMAKQSLAT 155
Cdd:pfam01576  835 LKNLEAELLQLQEDLAA 851

CAF-1_p150

pfam11600

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...

20-146

7.49e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.

Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 38.13 E-value: 7.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   20 VLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKA 99
Cdd:pfam11600   7 VQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767903325  100 LAKEkdllerEKWELRRQAKEATdhatalrsqldLKDNRMKELEAEL 146
Cdd:pfam11600  87 RLKE------EKRKEKQEALEAK-----------LEEKRKKEEEKRL 116

SAM_liprin-beta1,2_repeat2

cd09566

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

351-412

7.92e-03

Pssm-ID: 188965 Cd Length: 63 Bit Score: 35.36 E-value: 7.92e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903325 351 HWkagtVQAWLEVVmAMPMYVKACTENVKSGKVLLSLSDEDLQLgLGVCSSLHRRKLRLAIE 412
Cdd:cd09566    5 HW----VLRWLDDI-GLPQYKDAFSEAKVDGRMLHYLTVDDLLH-LKVTSALHHASIRRGIQ 60

PRK12704

phosphodiesterase; Provisional

17-146

8.25e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 8.25e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  17 SSEVLSATELRVQL---AQKEQElARAKEALQAMKADRKRLK----GEKTDLVSQMQQLYATLESREEQLRDFIRNYEQH 89
Cdd:PRK12704  30 EAKIKEAEEEAKRIleeAKKEAE-AIKKEALLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  90 RKESEDAVKALAKEKDLLEREKWELRRQAKEATD---HATALrSQLDLKDNRMKELEAEL 146
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQeleRISGL-TAEEAKEILLEKVEEEA 167

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

10-151

8.25e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 8.25e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325  10 EESQGGKSSEVLSATELRVQLAQKEQELARAKEALqamkadrKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRN-YEQ 88
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQV-------ERLEAEVEELEAELEEKDERIERLERELSEARSEeRRE 460

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903325  89 HRKESEdaVKALAKEKDLLEREkwelrrqakeatdhatalrsqLDLKDNRMKELEAELAMAKQ 151
Cdd:COG2433  461 IRKDRE--ISRLDREIERLERE---------------------LEEERERIEELKRKLERLKE 500

PRK02224

DNA double-strand break repair Rad50 ATPase;

3-150

8.40e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.40e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325   3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 82
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903325  83 IRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAK 150
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARERVEEAEALLEAGK 453

Myosin_tail_1

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

5-151

9.01e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 9.01e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325     5 LAKDLEESQGgkSSEVLSATELRVQLaQKEQ---ELARAKEALQAMKADRKRLKGEKTDLVSQMQQL-----------YA 70
Cdd:pfam01576  894 LEEELEEEQS--NTELLNDRLRKSTL-QVEQlttELAAERSTSQKSESARQQLERQNKELKAKLQEMegtvkskfkssIA 970

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903325    71 TLESR----EEQLrdfirnyEQHRKESEDAVKAL-AKEKDLLErekweLRRQAKEATDHATALRSQLDLKDNRMKELEAE 145
Cdd:pfam01576  971 ALEAKiaqlEEQL-------EQESRERQAANKLVrRTEKKLKE-----VLLQVEDERRHADQYKDQAEKGNSRMKQLKRQ 1038


                   ....*.
gi 767903325   146 LAMAKQ 151
Cdd:pfam01576 1039 LEEAEE 1044

EnvC