NCBI Conserved Domain Search

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

557-619

1.15e-15

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: 71.92 E-value: 1.15e-15

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395891  557 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 619
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

SAM_1

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

634-690

2.40e-15

Pssm-ID: 425739 Cd Length: 64 Bit Score: 71.15 E-value: 2.40e-15

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891  634 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63

SAM

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

555-619

6.64e-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: 6.64e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395891   555 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 619
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM_2

SAM domain (Sterile alpha motif);

715-785

6.62e-12

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 61.52 E-value: 6.62e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395891  715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 785
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66

SMC_prok_B

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

59-317

2.22e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.22e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    59 LALEMLELPQERAALLSQIpgptaayikewfEESLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   219 VEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKD 297
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELE 446

                          250       260
                   ....*....|....*....|
gi 530395891   298 RRIEELTGLLNQYRKVKEIV 317
Cdd:TIGR02168  447 EELEELQEELERLEEALEEL 466

Smc

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

82-315

1.54e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.54e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  82 AAYIKEWFEESLSQVN---HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE 158
Cdd:COG1196  230 LLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 159 MLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKA 238
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891 239 EVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKmgmETLLLANEDKDRRIEELTGLLNQYRKVKE 315
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460

SAM

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

715-784

5.12e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 50.37 E-value: 5.12e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 784
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65

CCDC158

pfam15921

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

108-336

8.26e-08

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: 56.28 E-value: 8.26e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   108 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   188 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 262
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395891   263 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 336
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654

SAM

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

635-690

9.30e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.60 E-value: 9.30e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891   635 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65

PRK03918

DNA double-strand break repair ATPase Rad50;

206-355

4.35e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.35e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 206 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 276
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 277 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 354
Cdd:PRK03918 573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                 .
gi 530395891 355 Q 355
Cdd:PRK03918 648 E 648

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 ...

714-785

5.24e-44

Pssm-ID: 188968 Cd Length: 72 Bit Score: 153.00 E-value: 5.24e-44

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
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 ...

629-691

6.66e-37

Pssm-ID: 188965 Cd Length: 63 Bit Score: 132.43 E-value: 6.66e-37

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395891 629 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 691
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 ...

555-618

2.88e-35

Pssm-ID: 188962 Cd Length: 64 Bit Score: 127.73 E-value: 2.88e-35

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395891 555 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 618
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 ...

722-783

1.89e-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: 1.89e-29

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 722 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 783
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 ...

714-785

3.64e-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: 3.64e-29

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
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 ...

633-691

2.68e-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: 108.00 E-value: 2.68e-28

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 633 IWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 691
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 ...

562-618

3.12e-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: 3.12e-26

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530395891 562 RVCAWLEDFGLAQ-YVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 618
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 ...

714-785

7.62e-20

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

Pssm-ID: 188967 Cd Length: 72 Bit Score: 84.29 E-value: 7.62e-20

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72

SAM_1

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

557-619

1.15e-15

Pssm-ID: 425739 Cd Length: 64 Bit Score: 71.92 E-value: 1.15e-15

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395891  557 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 619
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

SAM_1

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

634-690

2.40e-15

Pssm-ID: 425739 Cd Length: 64 Bit Score: 71.15 E-value: 2.40e-15

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891  634 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63

SAM_kazrin_repeat2

cd09567

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

629-691

6.00e-14

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: 67.43 E-value: 6.00e-14

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395891 629 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDRRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 691
Cdd:cd09567    1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65

SAM

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

555-619

6.64e-14

Pssm-ID: 197735 Cd Length: 68 Bit Score: 67.32 E-value: 6.64e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395891   555 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 619
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM_2

SAM domain (Sterile alpha motif);

715-785

6.62e-12

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 61.52 E-value: 6.62e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395891  715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 785
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66

SAM_superfamily

cd09487

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

562-617

1.42e-11

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: 60.33 E-value: 1.42e-11

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530395891 562 RVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 617
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55

SAM_superfamily

cd09487

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

634-687

2.10e-11

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 59.56 E-value: 2.10e-11

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395891 634 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 687
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54

SMC_prok_B

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

59-317

2.22e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.22e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    59 LALEMLELPQERAALLSQIpgptaayikewfEESLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   219 VEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKD 297
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELE 446

                          250       260
                   ....*....|....*....|
gi 530395891   298 RRIEELTGLLNQYRKVKEIV 317
Cdd:TIGR02168  447 EELEELQEELERLEEALEEL 466

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 ...

630-690

1.53e-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: 54.79 E-value: 1.53e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395891 630 LDHIWV-TRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 690
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 ...

555-619

2.49e-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: 2.49e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891 555 FAQWSTERVCAWLEDF-GL-AQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 619
Cdd:cd09562    1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67

Smc

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

82-315

1.54e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.54e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  82 AAYIKEWFEESLSQVN---HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE 158
Cdd:COG1196  230 LLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 159 MLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKA 238
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891 239 EVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKmgmETLLLANEDKDRRIEELTGLLNQYRKVKE 315
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460

SMC_prok_B

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

128-303

4.23e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 4.23e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   128 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEE 207
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   208 LLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAlkdaEIERLHSQLSRTAALHSESHTERDQEIQRLKMGME 287
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170
                   ....*....|....*.
gi 530395891   288 TLLLANEDKDRRIEEL 303
Cdd:TIGR02168  828 SLERRIAATERRLEDL 843

EnvC

COG4942

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

71-309

5.08e-08

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: 55.93 E-value: 5.08e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  71 AALLSQIPGPTAAYIKEWFEESLSQVNHHSAASnetyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ 150
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 151 VKLNAAEEMLQQellSRTSLETQKLDL---------MTEVSELKLKLvgmekeqreqeekqrKAEELLQELRHLKIkVEE 221
Cdd:COG4942   83 AELAELEKEIAE---LRAELEAQKEELaellralyrLGRQPPLALLL---------------SPEDFLDAVRRLQY-LKY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 222 LENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIE 301
Cdd:COG4942  144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223


                 ....*...
gi 530395891 302 ELTGLLNQ 309
Cdd:COG4942  224 ELEALIAR 231

SAM

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

715-784

5.12e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 50.37 E-value: 5.12e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 784
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 ...

556-616

7.98e-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: 7.98e-08

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 556 AQWSTERVCAWLE-DFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 616
Cdd:cd09564    2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63

CCDC158

pfam15921

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

108-336

8.26e-08

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: 56.28 E-value: 8.26e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   108 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   188 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 262
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395891   263 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 336
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654

SAM

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

635-690

9.30e-08

Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.60 E-value: 9.30e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891   635 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65

SAM_2

SAM domain (Sterile alpha motif);

558-619

1.29e-07

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 49.19 E-value: 1.29e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395891  558 WSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 619
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65

COG2433

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

206-318

1.99e-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: 1.99e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 206 EELLQELRHLKIKVEELEnernqyewklkatkAEVAQLQEQVALKDAEIERLHSQLSRtaaLHSESHTE--RDQEIQRLK 283
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSE---ARSEERREirKDREISRLD 471

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530395891 284 MGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 318
Cdd:COG2433  472 REIERLERELEEERERIEELKRKLERLKELWKLEH 506

Smc

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

54-325

4.13e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.13e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  54 IEDLRLALEMLElpQERAALLSQIpgptAAYIKEwfEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVE 133
Cdd:COG1196  269 LEELRLELEELE--LELEEAQAEE----YELLAE--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 134 AQGEKIRDLEvcleghqVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELR 213
Cdd:COG1196  341 ELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL----------LEALRAAAELAAQLE 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 214 HLKIKVEELENERNQYEwklkatkAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLAN 293
Cdd:COG1196  404 ELEEAEEALLERLERLE-------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250       260       270
                 ....*....|....*....|....*....|..
gi 530395891 294 EDKDRRIEELTGLLNQYRKVKEIVMVTQGPSE 325
Cdd:COG1196  477 AALAELLEELAEAAARLLLLLEAEADYEGFLE 508

Smc

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

108-311

5.96e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 5.96e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 108 QERLARLEgDKES-LILQVSVLTDQVEA--------QGEKIRDLEVCLeghqVKLNAAEEMLQQELLSRTSLETQKLDLM 178
Cdd:COG1196  185 EENLERLE-DILGeLERQLEPLERQAEKaeryrelkEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELE 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 179 TEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLH 258
Cdd:COG1196  260 AELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395891 259 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYR 311
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

SAM_WDSUB1

cd09505

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

558-627

6.48e-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: 6.48e-07

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 558 WSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAinTKQEEKS 627
Cdd:cd09505    5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEE--LKMKSDS 72

SMC_prok_A

TIGR02169

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

53-315

9.36e-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: 52.76 E-value: 9.36e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    53 LIEDLRLALEmlelpqERAALLSQIpgptAAYIKEWFEESLSQVnhhsaasnetyQERLARLEGDKESLILQVSVLTDQV 132
Cdd:TIGR02169  259 EISELEKRLE------EIEQLLEEL----NKKIKDLGEEEQLRV-----------KEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   133 EAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLetqkldlMTEVSELKLKLvgmekeqreqEEKQRKAEELLQEL 212
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-------TEEYAELKEEL----------EDLRAELEEVDKEF 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   213 RHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLA 292
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460

                          250       260
                   ....*....|....*....|...
gi 530395891   293 NEDKDRRIEELTGLLNQYRKVKE 315
Cdd:TIGR02169  461 AADLSKYEQELYDLKEEYDRVEK 483

SAM_STIM-1,2-like

cd09504

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

558-614

1.62e-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: 46.56 E-value: 1.62e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395891 558 WSTERVCAWLEDF-GLAQYVIFARQWVSSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 614
Cdd:cd09504    5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65

SAM_DGK-delta-eta

cd09507

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

554-617

2.24e-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: 2.24e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395891 554 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 617
Cdd:cd09507    1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

87-334

3.94e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 3.94e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   87 EWFEESLSQVNHHSAASNETYQERLARLEgdKESLILQVSVLTDQVE-----AQGEKIRDLEVcleGHQVKLNAAEEMLQ 161
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKME--QERLRQEKEEKAREVErrrklEEAEKARQAEM---DRQAAIYAEQERMA 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  162 QEL---LSRTSLETQKLDL-MTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKiKVEELENERNQyewKLKATK 237
Cdd:pfam17380 344 MERereLERIRQEERKRELeRIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQR---KIQQQK 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  238 AEVAQLQ-EQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEI 316
Cdd:pfam17380 420 VEMEQIRaEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499

                         250
                  ....*....|....*...
gi 530395891  317 VMvtqgpSERTLSINEEE 334
Cdd:pfam17380 500 EL-----EERKQAMIEEE 512

Mplasa_alph_rch

TIGR04523

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

104-336

3.94e-06

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: 50.79 E-value: 3.94e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  104 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 178
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  179 TEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvaLKDAEIErlh 258
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE--LKKENLE--- 560

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530395891  259 sqlsrtaalhsESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPE 336
Cdd:TIGR04523 561 -----------KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627

SCP-1

pfam05483

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

54-305

1.32e-05

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: 48.95 E-value: 1.32e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   54 IEDLRLALEMLELPQERAALLSQIPgptaayIKEWFEeslsQVNHhsaaSNETYQERLarleGDKESlilQVSVLTDQVE 133
Cdd:pfam05483 192 IEKMILAFEELRVQAENARLEMHFK------LKEDHE----KIQH----LEEEYKKEI----NDKEK---QVSLLLIQIT 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  134 AQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLSRtsLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQE 211
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQ 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  212 LRHLK-IKVEELENERNQYEWKLKATKAEVAQLQE--------------QVALKDAEIERLHSQLSRTAALHSESHTERd 276
Cdd:pfam05483 329 LTEEKeAQMEELNKAKAAHSFVVTEFEATTCSLEEllrteqqrleknedQLKIITMELQKKSSELEEMTKFKNNKEVEL- 407

                         250       260
                  ....*....|....*....|....*....
gi 530395891  277 QEIQRLKMGMETLLLANEDKDRRIEELTG 305
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKG 436

CCDC158

pfam15921

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

85-317

1.33e-05

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: 49.35 E-value: 1.33e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    85 IKEWFEESLSQVNHHSAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLEVC---LEGHQVKL-NAAE 157
Cdd:pfam15921  567 LRQQIENMTQLVGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELEARvsdLELEKVKLvNAGS 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   158 EMLQqellSRTSLETQKLDLMTEVSELKLKLVGMEKEQreqeekqrkaeELLQelRHLKIKVEELENERNQYEWKLKATK 237
Cdd:pfam15921  643 ERLR----AVKDIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKSEEMETTTNKLKMQLKSAQ 705

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   238 AEVAQ---------------------LQEQVALKDAEIERLHSQLSrtaaLHSESHTERDQEIQRL-----KMGMETLLL 291
Cdd:pfam15921  706 SELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQ----FLEEAMTNANKEKHFLkeeknKLSQELSTV 781

                          250       260
                   ....*....|....*....|....*.
gi 530395891   292 ANEdKDRRIEELTGLLNQYRKVKEIV 317
Cdd:pfam15921  782 ATE-KNKMAGELEVLRSQERRLKEKV 806

SMC_prok_A

TIGR02169

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

54-303

1.57e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.57e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    54 IEDLRLALEMLElpQERAALLSQIPGptaayiKEWFEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTD--- 130
Cdd:TIGR02169  718 IGEIEKEIEQLE--QEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArls 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   131 -----QVEAQGEKI-----------RDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKE 194
Cdd:TIGR02169  790 hsripEIQAELSKLeeevsriearlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   195 QREQEEKQrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSrtaalHSESHTE 274
Cdd:TIGR02169  870 LEELEAAL---RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-----EIEDPKG 941

                          250       260
                   ....*....|....*....|....*....
gi 530395891   275 RDQEIQRLKMGMETLLLANEDKDRRIEEL 303
Cdd:TIGR02169  942 EDEEIPEEELSLEDVQAELQRVEEEIRAL 970

SAM_caskin1,2_repeat1

cd09497

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

559-612

2.65e-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: 42.63 E-value: 2.65e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891 559 STERVCAWLEDFGLAQYvifARQWVSSGHTLLT---ATPQDMeKELGIKHPLHRKKL 612
Cdd:cd09497    3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55

YhaN

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

65-260

3.68e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.68e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  65 ELPQERAALLSQIPGPTAAYIKEWfeESLSQVNHHSAASNETY---QERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 141
Cdd:COG4717   50 RLEKEADELFKPQGRKPELNLKEL--KELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 142 LEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVSELKLKLVgmekeqreqEEKQRKAEELLQELRHLK 216
Cdd:COG4717  128 LPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQEELE---------ELLEQLSLATEEELQDLA 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530395891 217 IKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 260
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

Myosin_tail_1

pfam01576

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

113-314

4.47e-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: 47.48 E-value: 4.47e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   113 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 192
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   193 KEQREQEEKQRKAEEllqELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDA--------------EIERLH 258
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891   259 SQLSRT---AALHSESHTERDQEIQRLKMGMETLLLANEDK--DRR------IEELTGLLNQYRKVK 314
Cdd:pfam01576  306 TELEDTldtTAAQQELRSKREQEVTELKKALEEETRSHEAQlqEMRqkhtqaLEELTEQLEQAKRNK 372

SAM_2

SAM domain (Sterile alpha motif);

635-687

4.51e-05

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.26 E-value: 4.51e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530395891  635 VTRWLDDIGLPQYKDQFHESRVD-RRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 687
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKI 62

SAM_SGMS1-like

cd09515

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

556-617

4.82e-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: 42.24 E-value: 4.82e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395891 556 AQWSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 617
Cdd:cd09515    2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65

Golgin_A5

pfam09787

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

107-338

4.84e-05

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: 46.29 E-value: 4.84e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  107 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRT---SLETQKLDLMTEVSE 183
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLREeiqKLRGQIQQLRTELQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  184 LKLKLVgmeKEQREQEEKQRKAEELLQELRHLKikvEELENERNQYEWKLKATKAEV----AQLQEQVALKDAEIERLHS 259
Cdd:pfam09787  80 LEAQQQ---EEAESSREQLQELEEQLATERSAR---REAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  260 QLSrtaaLHSESHTERDQEIQRLKMGMETLLlaneDKDRRIEELT----GLLNQYRKVKEIVMVTQGPSERTLSINEEEP 335
Cdd:pfam09787 154 QLT----SKSQSSSSQSELENRLHQLTETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGI 225


                  ...
gi 530395891  336 EGG 338
Cdd:pfam09787 226 SDG 228

SMC_prok_B

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

62-266

4.85e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.85e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    62 EMLELPQERAALLSQipgpTAAYIKEWFEESLSQVNHHSAASNETyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 141
Cdd:TIGR02168  302 QQKQILRERLANLER----QLEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   142 LEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQEL 212
Cdd:TIGR02168  377 LEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530395891   213 RHLKIKVEELENERNQYEWKLKATKAEVAQLQEQV-ALKDaeIERLHSQLSRTAA 266
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQENLEGFSEGVK 509

SAM_kazrin_repeat2

cd09567

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

563-616

5.51e-05

Pssm-ID: 188966 Cd Length: 65 Bit Score: 42.01 E-value: 5.51e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395891 563 VC-AWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 616
Cdd:cd09567    7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

101-356

5.55e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 5.55e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 101 AASNETYQERLARLEgdkeSLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDLMTE 180
Cdd:COG4372   27 AALSEQLRKALFELD----KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 181 VSELklklvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 260
Cdd:COG4372  100 QEEL---------------------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 261 LsrtaalhseshTERDQEIQRLKMGMETLLLAN---------EDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSIN 331
Cdd:COG4372  159 L-----------ESLQEELAALEQELQALSEAEaeqaldellKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227

                        250       260
                 ....*....|....*....|....*
gi 530395891 332 EEEPEGGFSKWNATNKDPEELFKQE 356
Cdd:COG4372  228 EAKLGLALSALLDALELEEDKEELL 252

COG4913

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

50-283

6.03e-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: 6.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   50 VLHLIEDLRLALEMLELPQERAALLSQIPGPTAAYIKEW-----FEESLSQVNH-HSAASNETYQERLARLEGDKESLIL 123
Cdd:COG4913   230 LVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARerlaeLEYLRAALRLwFAQRRLELLEAELEELRAELARLEA 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  124 QVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGmekeqreqeekq 202
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA------------ 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  203 rKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvalkdaeierlhsqlsrtaalhsesHTERDQEIQRL 282
Cdd:COG4913   378 -SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-------------------------LRELEAEIASL 431


                  .
gi 530395891  283 K 283
Cdd:COG4913   432 E 432

SMC_prok_A

TIGR02169

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

146-317

1.42e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.42e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   146 LEGHQVKLNAAEEMLQQELlsrTSLETQKLDLMTEVSELKlklvgmekeqreqeekqRKAEELLQELRHLKIKVEELENE 225
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL---EGLKRELSSLQSELRRIE-----------------NRLDELSQELSDASRKIGEIEKE 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   226 RNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhseshterdqEIQRLKMGMETLLLANEDKDRRI--EEL 303
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA-----------RIEELEEDLHKLEEALNDLEARLshSRI 793

                          170
                   ....*....|....
gi 530395891   304 TGLLNQYRKVKEIV 317
Cdd:TIGR02169  794 PEIQAELSKLEEEV 807

CwlO1

COG3883

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

105-266

2.20e-04

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.20e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 105 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ----------------ELLSRT 168
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldVLLGSE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 169 SLET--QKLDLMTEVSELKLKLVG-MEKEQREQEEKQRKAEELLQELRHLKIKVE----ELENERNQYEWKLKATKAEVA 241
Cdd:COG3883  113 SFSDflDRLSALSKIADADADLLEeLKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQAEQEALLAQLSAEEA 192

                        170       180
                 ....*....|....*....|....*
gi 530395891 242 QLQEQVALKDAEIERLHSQLSRTAA 266
Cdd:COG3883  193 AAEAQLAELEAELAAAEAAAAAAAA 217

DR0291

COG1579

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

207-315

2.70e-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: 43.37 E-value: 2.70e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 207 ELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERdqEIQRLKMGM 286
Cdd:COG1579   21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQKEI 98

                         90       100
                 ....*....|....*....|....*....
gi 530395891 287 ETLLLANEDKDRRIEELTGLLNQYRKVKE 315
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELA 127

SAM_Ste50-like_fungal

cd09533

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

635-688

2.75e-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: 2.75e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395891 635 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 688
Cdd:cd09533    2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55

SAM_DGK-delta

cd09575

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

554-619

3.15e-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: 39.93 E-value: 3.15e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395891 554 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 619
Cdd:cd09575    1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65

SMC_prok_B

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

67-315

3.47e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 3.47e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    67 PQERAALLSQipgptAAYI---KEWFEESLSQVNHhsaasnetYQERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLE 143
Cdd:TIGR02168  154 PEERRAIFEE-----AAGIskyKERRKETERKLER--------TRENLDRLEDILNELERQLKSLERQAE-KAERYKELK 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   144 VCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSElklklvgmekeqreqeeKQRKAEELLQELRHLKIKVEELE 223
Cdd:TIGR02168  220 AELRELELALLVLR--LEELREELEELQEELKEAEEELEE-----------------LTAELQELEEKLEELRLEVSELE 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   224 NERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA--LHSESHTERDQE--------IQRLKMGMETLLLAN 293
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDELAEelaeleekLEELKEELESLEAEL 360

                          250       260
                   ....*....|....*....|..
gi 530395891   294 EDKDRRIEELTGLLNQYRKVKE 315
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLE 382

SAM_Shank1,2,3

cd09506

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

632-690

3.71e-04

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: 39.61 E-value: 3.71e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395891 632 HIW----VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:cd09506    3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65

CALCOCO1

pfam07888

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

55-315

3.93e-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: 44.12 E-value: 3.93e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   55 EDLRLALEMLELPQERAALLSQIP--GPTAAYIKEWFEESLSQVNHHSAASNETYQER--LARLEGDKESLILQvsvLTD 130
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAelKEELRQSREKHEELEEKYKELSASSEELSEEKdaLLAQRAAHEARIRE---LEE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  131 QVEAQGEKIRDLEVCLEghQVKlNAAEEMLQQellsRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQ 210
Cdd:pfam07888 137 DIKTLTQRVLERETELE--RMK-ERAKKAGAQ----RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  211 ELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQeiQRLKMGMETLL 290
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQ 287

                         250       260       270
                  ....*....|....*....|....*....|.
gi 530395891  291 LAN------EDKDRRIEELTGLLNQYRKVKE 315
Cdd:pfam07888 288 LADaslalrEGRARWAQERETLQQSAEADKD 318

YhaN

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

91-289

6.22e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.22e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  91 ESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQQeLLSRTSL 170
Cdd:COG4717  305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA-LLAEAGV 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 171 ET------------QKLDLMTEVSELKLKLVGmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKA 238
Cdd:COG4717  382 EDeeelraaleqaeEYQELKEELEELEEQLEE-LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395891 239 EVAQLQEQVAL--KDAEIERLHSQLSRTAalhseshterdQEIQRLKMGMETL 289
Cdd:COG4717  461 ELEQLEEDGELaeLLQELEELKAELRELA-----------EEWAALKLALELL 502

SAM_Samd14

cd09530

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

635-690

6.33e-04

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: 38.84 E-value: 6.33e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530395891 635 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:cd09530    8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63

DUF16

pfam01519

Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...

110-161

6.35e-04

Protein of unknown function DUF16; The function of this protein is unknown. It appears to only occur in Mycoplasma pneumoniae. The crystal structure revealed that this domain is composed of two separated homotrimeric coiled-coils.

Pssm-ID: 396208 [Multi-domain] Cd Length: 95 Bit Score: 39.81 E-value: 6.35e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530395891  110 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 161
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77

Mplasa_alph_rch

TIGR04523

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

90-302

1.14e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.14e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   90 EESLSQVNHHSAASN------ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghqvklnaaeemlqQE 163
Cdd:TIGR04523 186 QKNIDKIKNKLLKLElllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------------------TT 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  164 LLSRTslETQKLDLMTEVSELKLKLvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQ- 242
Cdd:TIGR04523 247 EISNT--QTQLNQLKDEQNKIKKQL-----------------SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQd 307

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395891  243 ----LQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETLLLANEDKDRRIEE 302
Cdd:TIGR04523 308 wnkeLKSELKNQEKKLEEIQNQISQN----NKIISQLNEQISQLKKELTNSESENSEKQRELEE 367

CwlO1

COG3883

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

205-266

1.20e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.20e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 205 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA 266
Cdd:COG3883   32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

sbcc

TIGR00618

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

50-311

1.55e-03

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

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.55e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891    50 VLHLIEDLRLALEMLELPQERAALLSQIpgptaAYIKEWFEESLSQVNHHSAASNETYQERLARLEGDKESL----ILQV 125
Cdd:TIGR00618  589 LQNITVRLQDLTEKLSEAEDMLACEQHA-----LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqerVREH 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   126 SVLTDQVEAQGEKIRDLEVCLEGHQVK-LNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRK 204
Cdd:TIGR00618  664 ALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDA 740

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   205 AEELLQELRHL---KIKVEELENER-NQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLsrtAALHSESHTERDQEIQ 280
Cdd:TIGR00618  741 LNQSLKELMHQartVLKARTEAHFNnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL---KTLEAEIGQEIPSDED 817

                          250       260       270
                   ....*....|....*....|....*....|.
gi 530395891   281 RLKMGMETLLLANEDKDRRIEELTGLLNQYR 311
Cdd:TIGR00618  818 ILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848

YhaN

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

109-307

1.58e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.58e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 109 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELK 185
Cdd:COG4717   71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 186 LKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLK-ATKAEVAQLQEQVALKDAEIERLHSQLSRT 264
Cdd:COG4717  139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEA 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530395891 265 aalhSESHTERDQEIQRLKMGMETlllanEDKDRRIEELTGLL 307
Cdd:COG4717  219 ----QEELEELEEELEQLENELEA-----AALEERLKEARLLL 252

SAM_Neurabin-like

cd09512

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

552-603

2.03e-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: 37.63 E-value: 2.03e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395891 552 NAPFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGI 603
Cdd:cd09512    1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNI-DGQQLLQLDSSKL-KALGI 51

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

92-309

2.04e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 2.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   92 SLSQVNHHSAASNETYQERLARlEGDKE---SLILQVSVLTDQVEAqgeKIRDLEVCLEGHQVKLNAAEEMLQQEllsrt 168
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSE-DGTQKkmsSLSMELMKLRNKLEA---KMKEVMAKQEGMEGKLQVTQKNLEHS----- 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  169 sletqkldlMTEVSELKLKLVGMEKEQREQEEKQrkaEELLQElrhlkikVEELENERNQYEwklkATKAEVAQLQEQVA 248
Cdd:pfam15905 197 ---------KGKVAQLEEKLVSTEKEKIEEKSET---EKLLEY-------ITELSCVSEQVE----KYKLDIAQLEELLK 253

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395891  249 LKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRR----IEELTGLLNQ 309
Cdd:pfam15905 254 EKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTlnaeLEELKEKLTL 318

SAM_STIM-1,2-like

cd09504

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

632-688

2.06e-03

Pssm-ID: 188903 Cd Length: 74 Bit Score: 37.70 E-value: 2.06e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395891 632 HIW----VTRWL-DDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 688
Cdd:cd09504    3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59

TTKRSYEDQ

pfam10212

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...

63-306

3.41e-03

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.

Pssm-ID: 463001 Cd Length: 523 Bit Score: 40.96 E-value: 3.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   63 MLELPQERAALLSQIPGPTAAYIKewFEESLS--QVNHHSAASNETY-------QERLARLEGDKESLILQVSVLTDQVE 133
Cdd:pfam10212 263 MLQYKKKAVAYISSLKKPCPESVP--YEEALSnrRVLLSSTESREGLaqqvqqsQEKIAKLEQEKEHWMLEAQLLKIKLE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  134 AQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELK-LKLVGMEKEQREQEEK--QRKAEELLQ 210
Cdd:pfam10212 341 KENQRIADLEKQLLKGSTSGQLPELVQSKATLPLTAKQGSEASSISEKEPTPsTSLIGMLTVTTDSEESsdEESREQLIK 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  211 ElrHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQL----SRTAALHSE-SHTERDQEIQrLKMG 285
Cdd:pfam10212 421 S--HYMARIAELTSQLQLADSKAVHFHAECRALAKRLALAEKSKESLTEELklanQNISRLQDElTTTKRSYEDQ-LSMM 497

                         250       260
                  ....*....|....*....|.
gi 530395891  286 METLLLANEDKDRRIEELTGL 306
Cdd:pfam10212 498 SDHLCSMNETLTKQREEIDTL 518

SMC_prok_B

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

210-309

4.06e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 4.06e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   210 QELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETL 289
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIAQL 752

                           90       100
                   ....*....|....*....|
gi 530395891   290 LLANEDKDRRIEELTGLLNQ 309
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEE 772

MAD

pfam05557

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

89-328

4.26e-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: 40.88 E-value: 4.26e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   89 FEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQvEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRT 168
Cdd:pfam05557  53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK-ESQLADAREVISCLKN---ELSELRRQIQRAELELQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  169 SLETQKLDLMTEVSELKLKLVGMEKEQREQeekqrkaEELLQELRHLKIKVEELENERNQYE-WK--LKATKAEVAQLQE 245
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQNL-------EKQQSSLAEAEQRIKELEFEIQSQEqDSeiVKNSKSELARIPE 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891  246 QvalkDAEIERLHSqlsrtaalhseshterdqEIQRLKMGMETLLLANEDKdrriEELTGLLNQYRKVKEIVMVTQGPSE 325
Cdd:pfam05557 202 L----EKELERLRE------------------HNKHLNENIENKLLLKEEV----EDLKRKLEREEKYREEAATLELEKE 255


                  ...
gi 530395891  326 RTL 328
Cdd:pfam05557 256 KLE 258

SMC_prok_B

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

108-263

4.30e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 4.30e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELklk 187
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL--- 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891   188 lvgmekeqreqeekqrkaEELLQELRH----LKIKVEELENERNQyewkLKATKAEVAQLQEQVALK-----DAEIERLH 258
Cdd:TIGR02168  914 ------------------RRELEELREklaqLELRLEGLEVRIDN----LQERLSEEYSLTLEEAEAlenkiEDDEEEAR 971


                   ....*
gi 530395891   259 SQLSR 263
Cdd:TIGR02168  972 RRLKR 976

PRK03918

DNA double-strand break repair ATPase Rad50;

206-355

4.35e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.35e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 206 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 276
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 277 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 354
Cdd:PRK03918 573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                 .
gi 530395891 355 Q 355
Cdd:PRK03918 648 E 648

SAM_CNK1,2,3-suppressor

cd09511

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

556-604

5.05e-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: 5.05e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395891 556 AQWSTERVCAWLE--DFGLAQYVIFARQWVSSGHTLLTATPQDMEkELGIK 604
Cdd:cd09511    2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51

EnvC

COG4942

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

206-312

5.07e-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: 5.07e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395891 206 EELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT----AALHSESHTERDQEIQR 281
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeiAELRAELEAQKEELAEL 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530395891 282 L----KMGME---TLLLANEDKDR--RIEELTGLLNQYRK 312
Cdd:COG4942  110 LralyRLGRQpplALLLSPEDFLDavRRLQYLKYLAPARR 149

YhaN