NCBI Conserved Domain Search

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

522-578

8.10e-17

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: 75.38 E-value: 8.10e-17

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247 522 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63

SAM_1

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

445-507

1.12e-15

Pssm-ID: 425739 Cd Length: 64 Bit Score: 71.92 E-value: 1.12e-15

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 445 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 507
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

SAM

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

443-507

5.38e-14

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: 67.32 E-value: 5.38e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528247  443 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 507
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM_2

SAM domain (Sterile alpha motif);

603-673

5.68e-12

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 61.52 E-value: 5.68e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528247 603 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 673
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66

SMC_prok_B

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

1-205

1.10e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.10e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    1 MSSEQWPRLPGKVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELK 73
Cdd:TIGR02168  264 ELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   74 LKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTA 153
Cdd:TIGR02168  344 EKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462528247  154 ALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 205
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 466

SAM

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

523-578

1.15e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 52.30 E-value: 1.15e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247  523 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65

SAM

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

603-672

4.27e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 50.76 E-value: 4.27e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  603 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 672
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65

COG2433

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

94-206

1.59e-07

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.86 E-value: 1.59e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  94 EELLQELRHLKIKVEELEnernqyewklkatkAEVAQLQEQVALKDAEIERLHSQLSRtaaLHSESHTE--RDQEIQRLK 171
Cdd:COG2433   409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSE---ARSEERREirKDREISRLD 471

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462528247 172 MGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 206
Cdd:COG2433   472 REIERLERELEEERERIEELKRKLERLKELWKLEH 506

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

12-224

2.40e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 2.40e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   12 KVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqeekqr 91
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV--------------- 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   92 kaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----------RTAALHSESHT 161
Cdd:pfam15921  527 --DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgRTAGAMQVEKA 593

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247  162 ERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 224
Cdd:pfam15921  594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654

PRK03918

DNA double-strand break repair ATPase Rad50;

93-204

7.53e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.53e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  93 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALH---------SESHTER 163
Cdd:PRK03918  226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklSEFYEEY 305

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528247 164 DQEIQRLKMGMETL--LLAN--------EDKDRRIEELTGLLNQYRKVKEI 204
Cdd:PRK03918  306 LDELREIEKRLSRLeeEINGieerikelEEKEERLEELKKKLKELEKRLEE 356

Name

Accession

Description

Interval

E-value

SAM_liprin-beta1,2_repeat3

cd09569

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

602-673

3.34e-44

Pssm-ID: 188968 Cd Length: 72 Bit Score: 153.38 E-value: 3.34e-44

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247 602 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 673
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72

SAM_liprin-beta1,2_repeat2

cd09566

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

517-579

6.69e-38

Pssm-ID: 188965 Cd Length: 63 Bit Score: 135.13 E-value: 6.69e-38

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 517 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 579
Cdd:cd09566     1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63

SAM_liprin-beta1,2_repeat1

cd09563

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

443-506

2.93e-35

Pssm-ID: 188962 Cd Length: 64 Bit Score: 127.73 E-value: 2.93e-35

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528247 443 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 506
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64

SAM_liprin-kazrin_repeat3

cd09496

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

610-671

1.38e-29

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: 111.48 E-value: 1.38e-29

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247 610 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 671
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62

SAM_kazrin_repeat3

cd09570

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

602-673

2.86e-29

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.

Pssm-ID: 188969 Cd Length: 72 Bit Score: 111.00 E-value: 2.86e-29

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247 602 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 673
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72

SAM_liprin-kazrin_repeat2

cd09495

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

521-579

3.37e-28

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: 107.62 E-value: 3.37e-28

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247 521 IWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 579
Cdd:cd09495     1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLvHLKVTSQLHHLSLKCGIHVLH 60

SAM_liprin-kazrin_repeat1

cd09494

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

450-506

2.79e-26

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: 101.92 E-value: 2.79e-26

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528247 450 RVCAWLEDFGLAQ-YVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 506
Cdd:cd09494     1 RVCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58

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 ...

602-673

5.28e-20

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

Pssm-ID: 188967 Cd Length: 72 Bit Score: 84.68 E-value: 5.28e-20

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247 602 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 673
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72

SAM_1

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

522-578

8.10e-17

Pssm-ID: 425739 Cd Length: 64 Bit Score: 75.38 E-value: 8.10e-17

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247 522 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63

SAM_1

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

445-507

1.12e-15

Pssm-ID: 425739 Cd Length: 64 Bit Score: 71.92 E-value: 1.12e-15

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 445 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 507
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

SAM_kazrin_repeat2

cd09567

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

517-579

3.59e-15

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.

Pssm-ID: 188966 Cd Length: 65 Bit Score: 70.52 E-value: 3.59e-15

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528247 517 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 579
Cdd:cd09567     1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65

SAM

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

443-507

5.38e-14

Pssm-ID: 197735 Cd Length: 68 Bit Score: 67.32 E-value: 5.38e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528247  443 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 507
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM_superfamily

cd09487

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

522-575

2.77e-12

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: 61.87 E-value: 2.77e-12

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528247 522 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 575
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54

SAM_2

SAM domain (Sterile alpha motif);

603-673

5.68e-12

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 61.52 E-value: 5.68e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528247 603 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 673
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66

SAM_superfamily

cd09487

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

450-505

1.15e-11

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 60.33 E-value: 1.15e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528247 450 RVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 505
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55

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 ...

518-578

1.04e-09

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: 55.17 E-value: 1.04e-09

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 518 LDHIWV-TRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 578
Cdd:cd09565     1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63

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 ...

443-507

2.06e-09

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: 54.49 E-value: 2.06e-09

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247 443 FAQWSTERVCAWLEDF-GL-AQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 507
Cdd:cd09562     1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67

SMC_prok_B

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

1-205

1.10e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.10e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    1 MSSEQWPRLPGKVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELK 73
Cdd:TIGR02168  264 ELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   74 LKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTA 153
Cdd:TIGR02168  344 EKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462528247  154 ALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 205
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 466

SAM

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

523-578

1.15e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 52.30 E-value: 1.15e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247  523 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65

SMC_prok_B

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

16-191

2.43e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.43e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   16 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEE 95
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   96 LLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAlkdaEIERLHSQLSRTAALHSESHTERDQEIQRLKMGME 175
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170
                   ....*....|....*.
gi 2462528247  176 TLLLANEDKDRRIEEL 191
Cdd:TIGR02168  828 SLERRIAATERRLEDL 843

SAM

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

603-672

4.27e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 50.76 E-value: 4.27e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  603 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 672
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65

SAM_kazrin_repeat1

cd09564

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

444-504

6.52e-08

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.

Pssm-ID: 188963 Cd Length: 70 Bit Score: 50.14 E-value: 6.52e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247 444 AQWSTERVCAWLE-DFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 504
Cdd:cd09564     2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63

SAM_2

SAM domain (Sterile alpha motif);

446-507

1.11e-07

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 49.19 E-value: 1.11e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 446 WSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 507
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65

COG2433

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

94-206

1.59e-07

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.86 E-value: 1.59e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  94 EELLQELRHLKIKVEELEnernqyewklkatkAEVAQLQEQVALKDAEIERLHSQLSRtaaLHSESHTE--RDQEIQRLK 171
Cdd:COG2433   409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSE---ARSEERREirKDREISRLD 471

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462528247 172 MGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 206
Cdd:COG2433   472 REIERLERELEEERERIEELKRKLERLKELWKLEH 506

SAM_WDSUB1

cd09505

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

446-515

5.72e-07

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: 47.70 E-value: 5.72e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247 446 WSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAinTKQEEKS 515
Cdd:cd09505     5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEE--LKMKSDS 72

Smc

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

19-199

8.71e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 8.71e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  19 QVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqeekqrkaEELLQ 98
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------------EEAQA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  99 ELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLL 178
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180
                  ....*....|....*....|.
gi 2462528247 179 LANEDKDRRIEELTGLLNQYR 199
Cdd:COG1196   369 EAEAELAEAEEELEELAEELL 389

SMC_prok_A

TIGR02169

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

2-191

1.09e-06

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: 52.38 E-value: 1.09e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    2 SSEQWPRLPGKVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEK 81
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   82 EQREQEEKQrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSrtaalHSESHT 161
Cdd:TIGR02169  869 ELEELEAAL---RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-----EIEDPK 940

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462528247  162 ERDQEIQRLKMGMETLLLANEDKDRRIEEL 191
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEIRAL 970

SAM_STIM-1,2-like

cd09504

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

446-502

1.75e-06

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: 46.17 E-value: 1.75e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528247 446 WSTERVCAWLEDF-GLAQYVIFARQWVSSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 502
Cdd:cd09504     5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65

SAM_DGK-delta-eta

cd09507

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

442-505

2.06e-06

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: 45.87 E-value: 2.06e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528247 442 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 505
Cdd:cd09507     1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

12-224

2.40e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 2.40e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   12 KVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqeekqr 91
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV--------------- 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   92 kaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----------RTAALHSESHT 161
Cdd:pfam15921  527 --DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgRTAGAMQVEKA 593

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247  162 ERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 224
Cdd:pfam15921  594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654

SAM_2

SAM domain (Sterile alpha motif);

523-575

6.67e-06

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 6.67e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528247 523 VTRWLDDIGLPQYKDQFHESRVDG-RMLQYLTVNDLLFLKVTSQLHHLSIKCAI 575
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI 62

SAM_Ste50-like_fungal

cd09533

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

523-576

8.03e-06

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: 43.84 E-value: 8.03e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528247 523 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 576
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55

Smc

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

91-203

9.95e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 9.95e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  91 RKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRL 170
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462528247 171 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 203
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEA 358

SAM_Shank1,2,3

cd09506

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

520-578

1.46e-05

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: 43.46 E-value: 1.46e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 520 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:cd09506     3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65

SMC_prok_B

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

4-191

1.52e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.52e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    4 EQWPRLPGKVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeq 83
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL------- 805

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   84 reqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTER 163
Cdd:TIGR02168  806 ----------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462528247  164 D---QEIQRLKMGMETLLLANEDKDRRIEEL 191
Cdd:TIGR02168  876 EallNERASLEEALALLRSELEELSEELREL 906

Smc

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

12-203

1.71e-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: 1.71e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  12 KVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQR 91
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  92 KAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLK 171
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462528247 172 mgmETLLLANEDKDRRIEELTGLLNQYRKVKE 203
Cdd:COG1196   432 ---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460

SAM_Samd14

cd09530

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...

523-578

1.85e-05

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.

Pssm-ID: 188929 Cd Length: 67 Bit Score: 43.08 E-value: 1.85e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528247 523 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:cd09530     8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63

SAM_caskin1,2_repeat1

cd09497

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...

447-500

2.10e-05

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.

Pssm-ID: 188896 Cd Length: 66 Bit Score: 43.02 E-value: 2.10e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247 447 STERVCAWLEDFGLAQYvifARQWVSSGHTLLT---ATPQDMeKELGIKHPLHRKKL 500
Cdd:cd09497     3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55

SAM_kazrin_repeat2

cd09567

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

451-504

5.42e-05

Pssm-ID: 188966 Cd Length: 65 Bit Score: 41.63 E-value: 5.42e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462528247 451 VC-AWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 504
Cdd:cd09567     7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61

SAM_SGMS1-like

cd09515

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

444-505

5.88e-05

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: 41.85 E-value: 5.88e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528247 444 AQWSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 505
Cdd:cd09515     2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65

Myosin_tail_1

pfam01576

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

9-202

7.10e-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: 46.71 E-value: 7.10e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    9 LPGKVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEE 88
Cdd:pfam01576  157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   89 KQRKAEEllqELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDA--------------EIERLHSQLSRT-- 152
Cdd:pfam01576  237 QLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALKTELEDTld 313

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528247  153 -AALHSESHTERDQEIQRLKMGMETLLLANEDK--DRR------IEELTGLLNQYRKVK 202
Cdd:pfam01576  314 tTAAQQELRSKREQEVTELKKALEEETRSHEAQlqEMRqkhtqaLEELTEQLEQAKRNK 372

SAM_STIM-1,2-like

cd09504

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

520-576

7.63e-05

Pssm-ID: 188903 Cd Length: 74 Bit Score: 41.55 E-value: 7.63e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247 520 HIW----VTRWL-DDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 576
Cdd:cd09504     3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59

SMC_prok_A

TIGR02169

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

34-205

8.51e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 8.51e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   34 LEGHQVKLNAAEEMLQQELlsrTSLETQKLDLMTEVSELKlklvgmekeqreqeekqRKAEELLQELRHLKIKVEELENE 113
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL---EGLKRELSSLQSELRRIE-----------------NRLDELSQELSDASRKIGEIEKE 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  114 RNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhseshterdqEIQRLKMGMETLLLANEDKDRRI--EEL 191
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA-----------RIEELEEDLHKLEEALNDLEARLshSRI 793

                          170
                   ....*....|....
gi 2462528247  192 TGLLNQYRKVKEIV 205
Cdd:TIGR02169  794 PEIQAELSKLEEEV 807

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

7-244

1.31e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.31e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   7 PRLPGKVSVLTDQVEAQGEKIRDLevcleghQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQ 86
Cdd:COG4372    20 PKTGILIAALSEQLRKALFELDKL-------QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  87 EEKQRKAEELLQELRH----LKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLsrtaalhseshTE 162
Cdd:COG4372    93 QAELAQAQEELESLQEeaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL-----------ES 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247 163 RDQEIQRLKMGMETLLLAN---------EDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFSKWNAT 233
Cdd:COG4372   162 LQEELAALEQELQALSEAEaeqaldellKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241

                         250
                  ....*....|.
gi 2462528247 234 NKDPEELFKQE 244
Cdd:COG4372   242 LELEEDKEELL 252

DR0291

COG1579

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

95-203

1.46e-04

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

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  95 ELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERdqEIQRLKMGM 174
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQKEI 98

                          90       100
                  ....*....|....*....|....*....
gi 2462528247 175 ETLLLANEDKDRRIEELTGLLNQYRKVKE 203
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELA 127

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

15-205

1.63e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 1.63e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   15 VLTDQVEAqgeKIRDLEVC---LEGHQVKL-NAAEEMLQqellSRTSLETQKLDLMTEVSELKLKLVGMEKEQreqeekq 90
Cdd:pfam15921  611 ILKDKKDA---KIRELEARvsdLELEKVKLvNAGSERLR----AVKDIKQERDQLLNEVKTSRNELNSLSEDY------- 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   91 rkaeELLQelRHLKIKVEELENERNQYEWKLKATKAEVAQ---------------------LQEQVALKDAEIERLHSQL 149
Cdd:pfam15921  677 ----EVLK--RNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKI 750

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528247  150 SrtaaLHSESHTERDQEIQRL-----KMGMETLLLANEdKDRRIEELTGLLNQYRKVKEIV 205
Cdd:pfam15921  751 Q----FLEEAMTNANKEKHFLkeeknKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKV 806

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

34-226

2.24e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.

Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 2.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  34 LEGHQVKLNAAEEMLQQELLSRT---SLETQKLDLMTEVSELKLKLVgmeKEQREQEEKQRKAEELLQELRHLKikvEEL 110
Cdd:pfam09787  39 LDSSTALTLELEELRQERDLLREeiqKLRGQIQQLRTELQELEAQQQ---EEAESSREQLQELEEQLATERSAR---REA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247 111 ENERNQYEWKLKATKAEV----AQLQEQVALKDAEIERLHSQLSrtaaLHSESHTERDQEIQRLKMGMETLLlaneDKDR 186
Cdd:pfam09787 113 EAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRNQLT----SKSQSSSSQSELENRLHQLTETLI----QKQT 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462528247 187 RIEELT----GLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGG 226
Cdd:pfam09787 185 MLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGISDG 228

Smc

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

16-191

2.84e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.84e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  16 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLV----GMEKEQREQEEKQR 91
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELArleqDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  92 KAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLS---RTAALHSESHTERDQEIQ 168
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeaeEELEELAEELLEALRAAA 396

                         170       180
                  ....*....|....*....|...
gi 2462528247 169 RLKMGMETLLLANEDKDRRIEEL 191
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERL 419

SAM_DGK-delta

cd09575

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

442-507

2.98e-04

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

Pssm-ID: 188974 Cd Length: 65 Bit Score: 39.55 E-value: 2.98e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528247 442 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 507
Cdd:cd09575     1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65

SMC_prok_A

TIGR02169

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

8-203

3.49e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.49e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    8 RLPGKVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLetqkldlMTEVSELKLKLvgmekeqreqE 87
Cdd:TIGR02169  305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-------TEEYAELKEEL----------E 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   88 EKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEI 167
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462528247  168 QRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 203
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

CwlO1

COG3883

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

93-154

4.83e-04

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 4.83e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247  93 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA 154
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

YhaN

COG4717

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

16-195

7.46e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  16 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEE 95
Cdd:COG4717    93 LQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALEAELAELPERLEELEERLEELRE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  96 LLQELRHLKIKVEELENERNQYEWKLK-ATKAEVAQLQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGM 174
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEA----QEELEELEEELEQLENEL 236

                         170       180
                  ....*....|....*....|.
gi 2462528247 175 ETlllanEDKDRRIEELTGLL 195
Cdd:COG4717   237 EA-----AALEERLKEARLLL 252

Mplasa_alph_rch

TIGR04523

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

3-224

1.22e-03

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: 42.31 E-value: 1.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   3 SEQWPRLPGKVSVLTDQVEAQGEKIRDLEVCLEghqvKLNAAEEMLQQEL--LSRtSLETQKLDLMTEVSELKLKLVGME 80
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIK----NLDNTRESLETQLkvLSR-SINKIKQNLEQKQKELKSKEKELK 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  81 KEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvaLKDAEIErlhsqlsrtaalhsESH 160
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE--LKKENLE--------------KEI 563

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528247 161 TERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPE 224
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627

EnvC

COG4942

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

16-197

1.63e-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: 41.67 E-value: 1.63e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  16 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDL---------MTEVSELKLKLvgmekeqreq 86
Cdd:COG4942    60 LERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrLGRQPPLALLL---------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  87 eekqrKAEELLQELRHLKIkVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQE 166
Cdd:COG4942   127 -----SPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462528247 167 IQRLKMGMETLLLANEDKDRRIEELTGLLNQ 197
Cdd:COG4942   201 LARLEKELAELAAELAELQQEAEELEALIAR 231

COG4913

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

16-171

1.93e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.93e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   16 LTDQVEAQGEKIRDLEVCLEGHQV-----KLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQ 90
Cdd:COG4913    260 LAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   91 RkaEELLQELRHLKIKVEELENERNQYE-------WKLKATKAEVAQLQEQVAL----KDAEIERLHSQLSRTAALHSES 159
Cdd:COG4913    340 L--EQLEREIERLERELEERERRRARLEallaalgLPLPASAEEFAALRAEAAAlleaLEEELEALEEALAEAEAALRDL 417

                          170
                   ....*....|....*
gi 2462528247  160 ---HTERDQEIQRLK 171
Cdd:COG4913    418 rreLRELEAEIASLE 432

SMC_prok_B

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

12-200

2.04e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.04e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   12 KVSVLTDQVEAQGEKIRdlevcleghqvKLNAAEEMLQQEllsRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQR 91
Cdd:TIGR02168  226 ELALLVLRLEELREELE-----------ELQEELKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   92 KA----EELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLhsqlsrtaalhSESHTERDQEI 167
Cdd:TIGR02168  292 ALaneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL-----------KEELESLEAEL 360

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2462528247  168 QRLKMGMETLLLANEDKDRRIEELTGLLNQYRK 200
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLEL 393

SAM_SGMS1-like

cd09515

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

523-557

2.06e-03

Pssm-ID: 188914 Cd Length: 70 Bit Score: 37.23 E-value: 2.06e-03

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462528247 523 VTRWLDDIGLPQYKDQF-HESRVDGRMLQYLTVNDL 557
Cdd:cd09515     9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44

SAM_Neurabin-like

cd09512

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...

440-491

2.31e-03

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.

Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.25 E-value: 2.31e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 440 NAPFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGI 491
Cdd:cd09512     1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNI-DGQQLLQLDSSKL-KALGI 51

SMC_prok_B

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

98-197

2.53e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.53e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247   98 QELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETL 177
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIAQL 752

                           90       100
                   ....*....|....*....|
gi 2462528247  178 LLANEDKDRRIEELTGLLNQ 197
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEE 772

YhaN

COG4717

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

18-204

3.03e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.03e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  18 DQVEAQGEKIRDLEvcleghqvklnAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqreqeekqrkaeELL 97
Cdd:COG4717    71 KELKELEEELKEAE-----------EKEEEYAELQEELEELEEELEELEAELEELREELEKL---------------EKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  98 QELRHLKIKVEELENERNQYEWK---LKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTER----DQEIQRL 170
Cdd:COG4717   125 LQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEEL 204

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462528247 171 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKEI 204
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238

EnvC

COG4942

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

94-200

3.15e-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: 40.52 E-value: 3.15e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247  94 EELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT----AALHSESHTERDQEIQR 169
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeiAELRAELEAQKEELAEL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462528247 170 L----KMGME---TLLLANEDKDR--RIEELTGLLNQYRK 200
Cdd:COG4942   110 LralyRLGRQpplALLLSPEDFLDavRRLQYLKYLAPARR 149

SMC_prok_B

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

4-154

3.83e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 3.83e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528247    4 EQWPRLPGKVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQ 83
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528247   84 REQEekqrkAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQV-ALKDaeIERLHSQLSRTAA 154
Cdd:TIGR02168  445 LEEE-----LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQENLEGFSEGVK 509

SAM_DGK-delta

cd09575

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

520-578

4.51e-03

Pssm-ID: 188974 Cd Length: 65 Bit Score: 36.47 E-value: 4.51e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528247 520 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 578
Cdd:cd09575     3 HLWgteeVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65

SAM_CNK1,2,3-suppressor

cd09511

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...

444-492

4.64e-03

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.

Pssm-ID: 188910 Cd Length: 69 Bit Score: 36.50 E-value: 4.64e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528247 444 AQWSTERVCAWLE--DFGLAQYVIFARQWVSSGHTLLTATPQDMEkELGIK 492
Cdd:cd09511     2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51

SMC_prok_B