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Conserved domains on  [gi|1034581963|ref|XP_016875553|]
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liprin-beta-1 isoform X16 [Homo sapiens]

Protein Classification

liprin-beta family protein( domain architecture ID 13550134)

liprin-beta family protein is a scaffold protein that may hetero-oligomerize with members of the subfamily of the liprin-beta adaptor proteins, mediated by their carboxy-terminal SAM (steryl alpha motif) domains, and play an important role in the regulation of tumor cell invasion; may contain an N-terminal ATPase domain

Graphical summary

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List of domain hits

 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 ...
 794-865 4.85e-46

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


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.16  E-value: 4.85e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  794 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 865
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 ...
 709-771 5.41e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.90  E-value: 5.41e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  709 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
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 ...
 635-698 3.99e-34

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


:

Pssm-ID: 188962  Cd Length: 64  Bit Score: 124.65  E-value: 3.99e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  635 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 698
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-310 5.55e-09

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.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.03  E-value: 5.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKF-------RDTEG----LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQL--EEKESEV 249
Cdd:TIGR04523  484 LEQKQKELKSKEKELkklneekKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEI 563

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  250 KRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLR 310
Cdd:TIGR04523  564 DEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
 
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 ...
 794-865 4.85e-46

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.16  E-value: 4.85e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  794 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 865
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 ...
 709-771 5.41e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.90  E-value: 5.41e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  709 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
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 ...
 635-698 3.99e-34

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 124.65  E-value: 3.99e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  635 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 698
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 711-771 1.84e-18

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: 80.01  E-value: 1.84e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  711 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:pfam00536    4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 637-699 8.65e-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: 69.61  E-value: 8.65e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  637 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 699
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 635-699 4.14e-12

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: 62.31  E-value: 4.14e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963   635 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 699
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 711-771 1.30e-11

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: 60.77  E-value: 1.30e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963   711 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
798-865 4.38e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.38e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  798 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 865
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-310 5.55e-09

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: 60.03  E-value: 5.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKF-------RDTEG----LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQL--EEKESEV 249
Cdd:TIGR04523  484 LEQKQKELKSKEKELkklneekKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEI 563

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  250 KRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLR 310
Cdd:TIGR04523  564 DEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-321 6.84e-08

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: 56.65  E-value: 6.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLT-AVEKDRLDYEDKFRDTEGLIQEINDLRL 212
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEKEA 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  213 KVSEMDSERLQYEKKLKSTKDELASLKEQLeekESEVKRLqeklvckmkgegveivdrdENFKKKLKEKNIEVQKMKKAV 292
Cdd:pfam05483  336 QMEELNKAKAAHSFVVTEFEATTCSLEELL---RTEQQRL-------------------EKNEDQLKIITMELQKKSSEL 393

                          250       260
                   ....*....|....*....|....*....
gi 1034581963  293 ESLMAANEEKDRKIEDLRQCLNRYKKMQD 321
Cdd:pfam05483  394 EEMTKFKNNKEVELEELKKILAEDEKLLD 422
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-323 6.88e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.30  E-value: 6.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  180 KLKLTAVEKDRLDYEDKFRDTEGL-----------------IQEINDLRLKVSEMDSERLQyEKKLKSTKDELASLKEQL 242
Cdd:COG1340     98 RKELAELNKAGGSIDKLRKEIERLewrqqtevlspeeekelVEKIKELEKELEKAKKALEK-NEKLKELRAELKELRKEA 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  243 EEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDT 322
Cdd:COG1340    177 EEIHKKIKELAEEAQ-ELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA 255


                   .
gi 1034581963  323 V 323
Cdd:COG1340    256 L 256
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-301 1.80e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQqELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:PRK03918   231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  184 TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMdserlqyEKKLKSTKDELASLKEQLEE------KESEVKRLQEKLV 257
Cdd:PRK03918   310 REIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELyeeakaKKEELERLKKRLT 382

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034581963  258 CKMKGEGVEIVDRDENFKKKLKEK----NIEVQKMKKAVESLMAANEE 301
Cdd:PRK03918   383 GLTPEKLEKELEELEKAKEEIEEEiskiTARIGELKKEIKELKKAIEE 430
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 795-864 1.09e-06

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: 46.91  E-value: 1.09e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   795 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 864
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 193-331 3.44e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.85  E-value: 3.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   193 YEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKES----EVKRLQEKLVcKMKGEGVEIV 268
Cdd:smart00787  146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRAKEKLK-KLLQEIMIKV 224

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963   269 DRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR-YKKMQDTVVLAQGKDG 331
Cdd:smart00787  225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQSLTG 288
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 201-323 1.87e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  201 EGLIQEINDLrlkVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRD-ENFKKKLK 279
Cdd:cd22656    113 EEAKKTIKAL---LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEiKDLQKELE 189

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034581963  280 EKNIE-VQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTV 323
Cdd:cd22656    190 KLNEEyAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDL 234
 
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 ...
 794-865 4.85e-46

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.16  E-value: 4.85e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  794 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 865
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 ...
 709-771 5.41e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.90  E-value: 5.41e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  709 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
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 ...
 635-698 3.99e-34

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 124.65  E-value: 3.99e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  635 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 698
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 ...
 802-863 3.28e-33

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: 122.26  E-value: 3.28e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  802 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 863
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 ...
 798-865 2.27e-31

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: 117.16  E-value: 2.27e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  798 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 865
Cdd:cd09570      5 WTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 714-771 1.53e-20

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 86.05  E-value: 1.53e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581963  714 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 771
Cdd:cd09495      2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 711-771 1.84e-18

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: 80.01  E-value: 1.84e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  711 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:pfam00536    4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
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 ...
 798-865 6.43e-18

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: 78.90  E-value: 6.43e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  798 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 865
Cdd:cd09568      5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 637-699 8.65e-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: 69.61  E-value: 8.65e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  637 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 699
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 643-698 3.83e-14

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: 67.64  E-value: 3.83e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  643 VCNWLMEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 698
Cdd:cd09494      2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 714-768 6.07e-13

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: 64.18  E-value: 6.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  714 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 768
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 709-771 9.36e-13

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: 63.97  E-value: 9.36e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  709 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 771
Cdd:cd09567      1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 635-699 4.14e-12

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: 62.31  E-value: 4.14e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963   635 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 699
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 711-771 1.30e-11

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: 60.77  E-value: 1.30e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963   711 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
798-865 4.38e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.38e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  798 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 865
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-310 5.55e-09

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: 60.03  E-value: 5.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKF-------RDTEG----LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQL--EEKESEV 249
Cdd:TIGR04523  484 LEQKQKELKSKEKELkklneekKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEI 563

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  250 KRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLR 310
Cdd:TIGR04523  564 DEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 642-697 6.96e-09

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: 52.63  E-value: 6.96e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581963  642 QVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 697
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 102-309 1.80e-08

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: 58.49  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQellsRTSLETQKLDLMAEISNLKL 181
Cdd:TIGR04523  382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKET----IIKNNSEIKDLTNQDSVKEL 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  182 KLTAVEKDRLDYEDKFRDTEGLIQEIN--------DLRLKVSEMD---SERLQYEKKLKSTKDELASLKEQLEEKESEVK 250
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKqnleqkqkELKSKEKELKklnEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  251 RLQEKLV-CKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 309
Cdd:TIGR04523  535 EKESKISdLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-323 2.54e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK---VNATEEMLQ---QELLSR--------TSL 165
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEaqlEELESKldelaeelAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  166 ETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  242 LEE-----KESEVKRLQEKLVCKMKGEgVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRY 316
Cdd:TIGR02168  423 IEEllkklEEAELKELQAELEELEEEL-EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501


                   ....*..
gi 1034581963  317 KKMQDTV 323
Cdd:TIGR02168  502 EGFSEGV 508
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 ...
 710-772 3.83e-08

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: 50.93  E-value: 3.83e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  710 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 772
Cdd:cd09565      1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-311 4.72e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 4.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEaqgekirdlefCLEEHREKVNATEEmlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-----------KAERYKELKAELRE------LELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmkg 262
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL------ 318

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581963  263 egVEIVDRDENFKKKLKEKNIEVQKMKKAVESLM-------AANEEKDRKIEDLRQ 311
Cdd:TIGR02168  319 --EELEAQLEELESKLDELAEELAELEEKLEELKeelesleAELEELEAELEELES 372
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-321 6.84e-08

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: 56.65  E-value: 6.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLT-AVEKDRLDYEDKFRDTEGLIQEINDLRL 212
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEKEA 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  213 KVSEMDSERLQYEKKLKSTKDELASLKEQLeekESEVKRLqeklvckmkgegveivdrdENFKKKLKEKNIEVQKMKKAV 292
Cdd:pfam05483  336 QMEELNKAKAAHSFVVTEFEATTCSLEELL---RTEQQRL-------------------EKNEDQLKIITMELQKKSSEL 393

                          250       260
                   ....*....|....*....|....*....
gi 1034581963  293 ESLMAANEEKDRKIEDLRQCLNRYKKMQD 321
Cdd:pfam05483  394 EEMTKFKNNKEVELEELKKILAEDEKLLD 422
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-323 6.88e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.30  E-value: 6.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  180 KLKLTAVEKDRLDYEDKFRDTEGL-----------------IQEINDLRLKVSEMDSERLQyEKKLKSTKDELASLKEQL 242
Cdd:COG1340     98 RKELAELNKAGGSIDKLRKEIERLewrqqtevlspeeekelVEKIKELEKELEKAKKALEK-NEKLKELRAELKELRKEA 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  243 EEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDT 322
Cdd:COG1340    177 EEIHKKIKELAEEAQ-ELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA 255


                   .
gi 1034581963  323 V 323
Cdd:COG1340    256 L 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-315 7.79e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 7.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQV-------SVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  176 ISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEmdserlqyekKLKSTKDELASLKEQLEEKESEVKRLQeK 255
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE----------DIESLAAEIEELEELIEELESELEALL-N 880

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  256 LVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 315
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-323 1.19e-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: 56.23  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQ------ELLSRTSLET 167
Cdd:TIGR02169  213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  168 QK--LDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02169  293 KEkiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDkllaEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  242 LEEKESEVKRLQEKLVC------KMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVES-------LMAANEEKDRKIED 308
Cdd:TIGR02169  373 LEEVDKEFAETRDELKDyrekleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieakineLEEEKEDKALEIKK 452

                          250
                   ....*....|....*
gi 1034581963  309 LRQCLNRYKKMQDTV 323
Cdd:TIGR02169  453 QEWKLEQLAADLSKY 467
Filament pfam00038
Intermediate filament protein;
125-319 1.68e-07

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 54.16  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  125 DQVEAQGEKIRDLEFCLEEHREK----VNATEEMLQQEL--LSRT--SLETQKLDLMAEISNLKLkltAVEKDRLDYEDK 196
Cdd:pfam00038   18 DKVRFLEQQNKLLETKISELRQKkgaePSRLYSLYEKEIedLRRQldTLTVERARLQLELDNLRL---AAEDFRQKYEDE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  197 FRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEkesEVKRLQEKLvckmkGEGVEIVDRDENFKK 276
Cdd:pfam00038   95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEE---EVRELQAQV-----SDTQVNVEMDAARKL 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034581963  277 KLKE--KNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKM 319
Cdd:pfam00038  167 DLTSalAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDA 211
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-301 1.80e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQqELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:PRK03918   231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  184 TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMdserlqyEKKLKSTKDELASLKEQLEE------KESEVKRLQEKLV 257
Cdd:PRK03918   310 REIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELyeeakaKKEELERLKKRLT 382

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034581963  258 CKMKGEGVEIVDRDENFKKKLKEK----NIEVQKMKKAVESLMAANEE 301
Cdd:PRK03918   383 GLTPEKLEKELEELEKAKEEIEEEiskiTARIGELKKEIKELKKAIEE 430
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-318 2.04e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKVNATEEMLQQELLSRTsletqkldLMAEISNLKLK 182
Cdd:PRK03918   244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-------EKVKELKELKEKAEEYIK--------LSEFYEEYLDE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMdserlqyEKKLKSTKDELASLKEQLEEKEsEVKRLQEKLvckmkg 262
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELYE-EAKAKKEEL------ 374

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581963  263 egveivdrdENFKKKLKEKNIEvqKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 318
Cdd:PRK03918   375 ---------ERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKK 419
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 636-697 2.35e-07

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: 48.99  E-value: 2.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  636 AKWTKEQVCNWL-MEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 697
Cdd:cd09564      2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
131-318 2.44e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  131 GEKIRDLEFCLEEHREKVNATEEMlqQELLSrtSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDL 210
Cdd:PRK03918   168 GEVIKEIKRRIERLEKFIKRTENI--EELIK--EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  211 RLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQE-----KLVCKMKGEGVEIVDRDENFKK---KLKEKN 282
Cdd:PRK03918   244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKrlsRLEEEI 323

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034581963  283 IEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 318
Cdd:PRK03918   324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 715-770 4.43e-07

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: 48.08  E-value: 4.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581963  715 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 770
Cdd:cd09506     10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-256 5.97e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.85  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  133 KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDK------FRDTEGLIQE 206
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034581963  207 INDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:COG1579     98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 102-493 7.35e-07

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.51  E-value: 7.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLENDKESLVlqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELlsrtslETQKLDLMAEISNLKL 181
Cdd:PTZ00108   986 YLVRLDLYKKRKEYLL---GKLERELARLSNKVRFIKHVINGELVITNAKKKDLVKEL------KKLGYVRFKDIIKKKS 1056

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  182 KLTAVEKDrldyEDKFRDTEGLIQEINDLRLKVSEMDserlqY--EKKLKS-TKDELASLKEQLEEKESEVKRLQEKLVC 258
Cdd:PTZ00108  1057 EKITAEEE----EGAEEDDEADDEDDEEELGAAVSYD-----YllSMPIWSlTKEKVEKLNAELEKKEKELEKLKNTTPK 1127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  259 KM-------------KGEGVEIVDRDE----NFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQclnryKKMQD 321
Cdd:PTZ00108  1128 DMwledldkfeealeEQEEVEEKEIAKeqrlKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGN-----SKRVD 1202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  322 TVVLAQGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPSCDPFNTSVPEEFHTTILQVSIPSLLPATVSmeT 401
Cdd:PTZ00108  1203 SDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVS--A 1280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  402 SEKSKLTPKPEtSFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNLKKETSDGEKetiqKTSEDRAPAESRPFGTLP 481
Cdd:PTZ00108  1281 VQYSPPPPSKR-PDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKS----KTRVKQASASQSSRLLRR 1355

                          410
                   ....*....|..
gi 1034581963  482 PRPPGQDTSMDD 493
Cdd:PTZ00108  1356 PRKKKSDSSSED 1367
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-318 1.03e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  125 DQVEAQGEKIRDLEFCLEEHREKVNATEEmlqqellsrtsLETQKLDLMAEISNLKLKLTAVEKDRLDYEdkfrdtegLI 204
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEE-----------LEEELEELEAELEELREELEKLEKLLQLLP--------LY 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  205 QEINDLRLKVSEMDsERLQyekKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIE 284
Cdd:COG4717    132 QELEALEAELAELP-ERLE---ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034581963  285 VQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 318
Cdd:COG4717    208 LAELEEELEEAQEELEELEEELEQLENELEAAAL 241
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 715-767 1.06e-06

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.54  E-value: 1.06e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  715 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 767
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 795-864 1.09e-06

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: 46.91  E-value: 1.09e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   795 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 864
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-301 1.22e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDK--------------ESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQ 168
Cdd:COG1196    294 LAELARLEQDIarleerrreleerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  169 KLDLMAEISNLKLKLTAVEKDRLDYEDKfrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESE 248
Cdd:COG1196    374 LAEAEEELEELAEELLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  249 VKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE 301
Cdd:COG1196    451 EAELEEEEE-ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 155-319 1.42e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.69  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKD- 233
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLGNVRNn 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  234 --------ELASLK---EQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEK 302
Cdd:COG1579     89 keyealqkEIESLKrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168

                          170
                   ....*....|....*...
gi 1034581963  303 DRKI-EDLrqcLNRYKKM 319
Cdd:COG1579    169 AAKIpPEL---LALYERI 183
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
711-771 1.62e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.49  E-value: 1.62e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  711 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 87-324 1.69e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.43  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   87 QSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEA-QGEKIRDLEFCLEEHREKVNA------------TE- 152
Cdd:pfam15921  207 HDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRIEQliseheveitglTEk 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  153 ---------------EMLQQELLSRTSLETQKL-DLMAEISNLKLKLTavEKDRLdYEDKFRDTEGLIQEINDlrlKVSE 216
Cdd:pfam15921  287 assarsqansiqsqlEIIQEQARNQNSMYMRQLsDLESTVSQLRSELR--EAKRM-YEDKIEELEKQLVLANS---ELTE 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  217 MDSERLQYEKKLKSTKDELASLKEQLEEKESEV---KRLQEKLVCKMKGEGVEIvdrdENFKKKLKEKNIEVQKMKKAVE 293
Cdd:pfam15921  361 ARTERDQFSQESGNLDDQLQKLLADLHKREKELsleKEQNKRLWDRDTGNSITI----DHLRRELDDRNMEVQRLEALLK 436

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034581963  294 SL-----------MAANEEKD---RKIEDLRQCLNRYKKMQDTVV 324
Cdd:pfam15921  437 AMksecqgqmerqMAAIQGKNeslEKVSSLTAQLESTKEMLRKVV 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-311 2.65e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLenDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:COG1196    218 LKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMK 261
Cdd:COG1196    296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034581963  262 gegvEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 311
Cdd:COG1196    376 ----EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 102-324 3.02e-06

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: 51.28  E-value: 3.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSL-------ETQKLDLMA 174
Cdd:pfam05557   25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALnkklnekESQLADARE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  175 EISNLKLKL----TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVk 250
Cdd:pfam05557  105 VISCLKNELselrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE- 183

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  251 rlQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLmaaNEEKdrkiEDLRQCLNRYKKMQDTVV 324
Cdd:pfam05557  184 --QDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLL---KEEV----EDLKRKLEREEKYREEAA 248
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-328 3.39e-06

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: 51.33  E-value: 3.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  109 LENDKESLVLQVSVLTdQVEAQGE-KIRDLEFCLEEHREKVNATEEmLQQELLSRTSLETQKLD-LMAEISNLKLKLTAV 186
Cdd:pfam01576  382 LESENAELQAELRTLQ-QAKQDSEhKRKKLEGQLQELQARLSESER-QRAELAEKLSKLQSELEsVSSLLNEAEGKNIKL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  187 EKDRLDYEDKFRDTEGLIQEinDLRLKvsemdserLQYEKKLKSTKDELASLKEQLEEkESEVKRLQEKLVCKMKGEGVE 266
Cdd:pfam01576  460 SKDVSSLESQLQDTQELLQE--ETRQK--------LNLSTRLRQLEDERNSLQEQLEE-EEEAKRNVERQLSTLQAQLSD 528

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581963  267 ivdrdenFKKKLKEKNIEVQ-------KMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQG 328
Cdd:pfam01576  529 -------MKKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 109-319 3.95e-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: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEisnLKLKLTAVEK 188
Cdd:TIGR04523  300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  189 DRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKstkdelaSLKEQLEEKESEVKRLQEKLVcKMKGEGVEIV 268
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK-------KLQQEKELLEKEIERLKETII-KNNSEIKDLT 446

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  269 DRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKM 319
Cdd:TIGR04523  447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 638-699 4.11e-06

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: 45.39  E-value: 4.11e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  638 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 699
Cdd:cd09505      5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-256 6.31e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 6.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQEL--LSRTSLETQKLDLMAEISNLK 180
Cdd:COG3883     36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAraLYRSGGSVSYLDVLLGSESFS 115

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  181 lklTAVekDRLDYEDKFRDTEG-LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:COG3883    116 ---DFL--DRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-306 6.95e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.44  E-value: 6.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNAteemLQQELLSRTSLETQKLDLMAEIsnlkLK 182
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK----LQAEIAEAEAEIEERREELGER----AR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKF---RDTEGLIQEINDLRlKVSEMDSERLQyekKLKSTKDELASLKEQLEEKESEVKRLQEKLVCK 259
Cdd:COG3883     94 ALYRSGGSVSYLDVLlgsESFSDFLDRLSALS-KIADADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034581963  260 MKgegvEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKI 306
Cdd:COG3883    170 KA----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-320 7.32e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 7.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  100 DVYQERlaRLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK--VNATEEMLQQELLSRTSLETQKLDLMAEIS 177
Cdd:COG3206    159 EAYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELA 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  178 NLKLKLTAVEKDRLDYEDKFRDTEGlIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLV 257
Cdd:COG3206    237 EAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  258 CKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQ 320
Cdd:COG3206    316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-239 8.95e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQEL----LSRTSLETQKLDLMAE 175
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQLEREIerleRELEERERRRARLEAL 367

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  176 ISNLKLKLTAVEKDRLDYEDKFRDT-EGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLK 239
Cdd:COG4913    368 LAALGLPLPASAEEFAALRAEAAALlEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
119-318 9.42e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 9.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  119 QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEmlQQELLSR-TSLETQKLDLMA---EISNLKLKLTAVEKDRLDYE 194
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQE--RREALQRlAEYSWDEIDVASaerEIAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  195 dkfrdteGLIQEINDLRlkvsemdSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENF 274
Cdd:COG4913    689 -------ALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034581963  275 KKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 318
Cdd:COG4913    755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 134-311 9.66e-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: 49.63  E-value: 9.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKdrldyedKFRDTEGLIQEINDLRLK 213
Cdd:TIGR04523  147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQ 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  214 VSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrdENFKKKLKEKNIEVQKMKKAVE 293
Cdd:TIGR04523  220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ---------------NKIKKQLSEKQKELEQNNKKIK 284

                          170
                   ....*....|....*...
gi 1034581963  294 SLMAANEEKDRKIEDLRQ 311
Cdd:TIGR04523  285 ELEKQLNQLKSEISDLNN 302
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
76-311 1.07e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   76 DSTAETLVEW-LQSQMTNGhlpgNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEM 154
Cdd:PRK02224   324 EELRDRLEECrVAAQAHNE----EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE------------------INDLRLKVSE 216
Cdd:PRK02224   400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEE 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  217 MDSERLQYEKKLKSTKDELASLkEQLEEKESEVKRLQEK--LVCKMKGEGVEIVDRDEnfkKKLKEKNIEVQKMKKAVES 294
Cdd:PRK02224   480 LEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERreDLEELIAERRETIEEKR---ERAEELRERAAELEAEAEE 555

                          250
                   ....*....|....*..
gi 1034581963  295 LMAANEEKDRKIEDLRQ 311
Cdd:PRK02224   556 KREAAAEAEEEAEEARE 572
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
103-256 1.40e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKlk 182
Cdd:PRK02224   250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR-- 327

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  183 lTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:PRK02224   328 -DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-311 1.44e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  195 DKFRDTE----GLIQEINDLRLKVSEM-----------------------DSER-LQYEK-----------KLKSTKDEL 235
Cdd:COG4942     83 AELAELEkeiaELRAELEAQKEELAELlralyrlgrqpplalllspedflDAVRrLQYLKylaparreqaeELRADLAEL 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581963  236 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDE---NFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 311
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKllaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-255 1.51e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQG--EKIRDLEFCLEEHREKVnateEMLQQELLSRTSLETQKLDLMAEISNLK 180
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQ 176

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  181 LKLTAVEKdrldyedkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEK 255
Cdd:COG4717    177 EELEELLE---------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-260 1.81e-05

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: 47.23  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellSRTSLETQklDLMAEISNLKLK 182
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---VRNNKEYE--ALQKEIESLKRR 104

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  183 LTAVEKDRLDyedkfrdtegLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKM 260
Cdd:COG1579    105 ISDLEDEILE----------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
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 ...
 635-699 2.49e-05

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: 43.32  E-value: 2.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  635 FAKWTKEQVCNWL-MEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 699
Cdd:cd09562      1 FALWNGPTVVAWLeLWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 51-331 3.96e-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: 47.81  E-value: 3.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   51 LVEDLRGLLEMMETDEKeglrcQIPDSTA-----ETLVEWLQSQMTNghLPGNGDVYQERLARLENDKESLvlqvSVLTD 125
Cdd:pfam15921  480 VVEELTAKKMTLESSER-----TVSDLTAslqekERAIEATNAEITK--LRSRVDLKLQELQHLKNEGDHL----RNVQT 548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  126 QVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVE--KDRLDyeDKFRDTEGL 203
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilKDKKD--AKIRELEAR 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  204 IQEINDLRLKVSEMDSERLQYEKKLKSTKDELASlkeQLEEKESEVKRLQEKLvckmkgegvEIVDRdeNFKKKLKEKNI 283
Cdd:pfam15921  627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN---EVKTSRNELNSLSEDY---------EVLKR--NFRNKSEEMET 692

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1034581963  284 EVQKMKKAVESLMAaneekdrkieDLRQCLNRYKKMqdtvvlaQGKDG 331
Cdd:pfam15921  693 TTNKLKMQLKSAQS----------ELEQTRNTLKSM-------EGSDG 723
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 712-770 4.31e-05

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 42.31  E-value: 4.31e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  712 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 770
Cdd:cd09530      1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-314 5.68e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 5.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQveaqgekIRDLEFCLEEHREKvnatEEMLQQELlsrTSLETQKLDLMAEISNLKlk 182
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLESQ-------INDLESKIQNQEKL----NQQKDEQI---KKLQQEKELLEKEIERLK-- 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 ltaveKDRLDYEDKFRDtegLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmkg 262
Cdd:TIGR04523  433 -----ETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL------ 498

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  263 egVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLN 314
Cdd:TIGR04523  499 --KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
638-699 5.83e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 5.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581963  638 WTKEQVCNWLMEQGLGSYLNS-GKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 699
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNfRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-309 6.14e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEehreKVNATEEMLQQELLSRTS-----------LETQKLD 171
Cdd:TIGR04523  439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN----KIKQNLEQKQKELKSKEKelkklneekkeLEEKVKD 514

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  172 LMAEISNLKLKLTAVEKDRLDYEDKFRDTE--------------------GLIQEINDLRLKVSEMDSERLQYEKKLKST 231
Cdd:TIGR04523  515 LTKKISSLKEKIEKLESEKKEKESKISDLEdelnkddfelkkenlekeidEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  232 KDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 309
Cdd:TIGR04523  595 EKEKKDLIKEIEEKEKKISSLEKELE-KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-307 6.31e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 6.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEdkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKS----TKDELASLKEQLEEKESEVKRLQEKLVC 258
Cdd:TIGR02168  903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKRLEN 979

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  259 KMKGEGV---EIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIE 307
Cdd:TIGR02168  980 KIKELGPvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-256 6.60e-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: 47.09  E-value: 6.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  132 EKIRDLEFCLEEHREKVNATEEMLQQEL----LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEi 207
Cdd:pfam01576  338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034581963  208 ndLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:pfam01576  417 --LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDV 463
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 95-317 6.72e-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: 47.02  E-value: 6.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   95 LPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMA 174
Cdd:pfam05483  399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  175 EISNLKLKLTAVEK--DRLDYEDKfrdteGLIQEINDLRLKV----SEMDSERLQYEKKLKST----------KDELASL 238
Cdd:pfam05483  479 ELEKEKLKNIELTAhcDKLLLENK-----ELTQEASDMTLELkkhqEDIINCKKQEERMLKQIenleekemnlRDELESV 553

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  239 KEQLEEKESEVK----------RLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNievqkmkKAVESLMAANEEKDRKIED 308
Cdd:pfam05483  554 REEFIQKGDEVKckldkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSA 626


                   ....*....
gi 1034581963  309 LRQCLNRYK 317
Cdd:pfam05483  627 ENKQLNAYE 635
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-319 6.72e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 6.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFC---LEEHREKVNATEEMLQQELLSrtsLETQKlDLMAEI 176
Cdd:COG1340     67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLS---PEEEK-ELVEKI 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  177 SNLKLKLTAVEKdRLDYEDKFRDTEGLIQEI----NDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRL 252
Cdd:COG1340    143 KELEKELEKAKK-ALEKNEKLKELRAELKELrkeaEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA 221

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  253 QEKlVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESlmaanEEKDRKIEDLRQCLNRYKKM 319
Cdd:COG1340    222 QEK-ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFEKLKKGEKL 282
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 634-699 7.63e-05

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 41.63  E-value: 7.63e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  634 PFAKWTKEQVCNWLMEQGLGSYLNS-GKHWIaSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 699
Cdd:cd09507      1 PVTNWTTEEVGAWLESLQLGEYRDIfARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-335 8.13e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 8.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLENDKESLVLQVSVLTDQVEAQgEKIRDLEFCLEEHREKV-NATEEMLQQELLSrtsLETQKLDLMAEISNLKLK 182
Cdd:PRK03918   338 ERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLtGLTPEKLEKELEE---LEKAKEEIEEEISKITAR 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERL--QYEKKLKSTKDELASLKEQLEE-----KESEVKRLQEK 255
Cdd:PRK03918   414 IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKERKlrkelRELEKVLKKES 493

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  256 LVCKMKgegvEIVDRDENFKKKLKEKNIEvqKMKKAVESLMAANEEKDR---KIEDLRQCLNRYKKMQDTVVLAQGKDGE 332
Cdd:PRK03918   494 ELIKLK----ELAEQLKELEEKLKKYNLE--ELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEELKKKLAELEKKLDE 567


                   ...
gi 1034581963  333 YEE 335
Cdd:PRK03918   568 LEE 570
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 105-256 8.62e-05

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: 45.30  E-value: 8.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellSRTSLETQKLDLMA-----EISNL 179
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE---VEARIKKYEEQLGNvrnnkEYEAL 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  180 KLKLTAVEKDRLDYEDKfrdteglIQEINDlrlKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:COG1579     95 QKEIESLKRRISDLEDE-------ILELME---RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-253 1.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAqgekirdlefcLEEHREKVNATEEMLQQELLsrtSLETQKLD-LMAEISNLKL 181
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELER-----------LEARLDALREELDELEAQIR---GNGGDRLEqLEREIERLER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  182 KLTAVEKDRLDYEDKFR--------DTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQ 253
Cdd:COG4913    353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 42-318 1.18e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   42 FMGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQERLARLendkesLVLQVS 121
Cdd:pfam02463  659 AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR------VQEAQD 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  122 VLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLD--LMAEISNLKLKLTAVEKDRLDYEDKFRD 199
Cdd:pfam02463  733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKteKLKVEEEKEEKLKAQEEELRALEEELKE 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  200 TEGLIQEINDLRLKVSEMDSERLQYEKKLK--STKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKK 277
Cdd:pfam02463  813 EAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034581963  278 LKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 318
Cdd:pfam02463  893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 166-323 1.76e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  166 ETQKLDLMAEISNLKLKLTAVEKdrldyedkfrdtegliqEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEK 245
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQA-----------------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  246 ESEVKRLQEKL-----VCKMKGEGV-------------EIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIE 307
Cdd:COG3883     78 EAEIEERREELgerarALYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157

                          170
                   ....*....|....*.
gi 1034581963  308 DLRQCLNRYKKMQDTV 323
Cdd:COG3883    158 ELEALKAELEAAKAEL 173
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
103-309 1.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMAEISNLKLK 182
Cdd:COG4372     30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-------LNEQLQAAQAELAQAQEE 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  183 LTAVEKDrldYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKG 262
Cdd:COG4372    103 LESLQEE---AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034581963  263 EGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 309
Cdd:COG4372    180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 638-699 1.91e-04

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 40.75  E-value: 1.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  638 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 699
Cdd:cd09501      4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 104-321 2.38e-04

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: 45.06  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleEHREKVNATEEMLQQELlsrTSLETQKLDLMAEISNLKLKL 183
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKK---EELEEELEELEAALRDLESRL 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  184 TAVEKDRLDYEDKFRDTEGLIQEINdlrlkvsemdserLQYEKKlkstKDELASLKEQLEEKESEVKRLQEKlvckmKGE 263
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELE-------------AQIEKK----RKRLSELKAKLEALEEELSEIEDP-----KGE 942

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581963  264 GVEIVDRDENFKKklkeknieVQKMKKAVESLMAANEEKD-RKIEDLRQCLNRYKKMQD 321
Cdd:TIGR02169  943 DEEIPEEELSLED--------VQAELQRVEEEIRALEPVNmLAIQEYEEVLKRLDELKE 993
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 105-156 2.95e-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: 40.97  E-value: 2.95e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQ 156
Cdd:pfam01519   26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
201-311 3.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  201 EGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVC------KMKGEGVEIVDRDENF 274
Cdd:COG4372     41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaqeeleSLQEEAEELQEELEEL 120

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034581963  275 KKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 311
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 634-690 3.40e-04

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: 39.94  E-value: 3.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  634 PFAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGI-----KHSLHRK 690
Cdd:cd09512      3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 108-317 3.42e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.43  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  108 RLEnDKESLVL----QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNateeMLQQELlsrTSLETQKLDLMAEISNLKLKL 183
Cdd:pfam10174  353 RLE-EKESFLNkktkQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN----VLQKKI---ENLQEQLRDKDKQLAGLKERV 424

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  184 TAVEKDRLDYEDKFRDTEGLIQE----INDLRLKVSEMDSERL----QYEKKLKSTKDELASLKEQLEEKESEVKRLQEK 255
Cdd:pfam10174  425 KSLQTDSSNTDTALTTLEEALSEkeriIERLKEQREREDRERLeeleSLKKENKDLKEKVSALQPELTEKESSLIDLKEH 504

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  256 ---LVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAA--NEEKDRKIEDLRQCLNRYK 317
Cdd:pfam10174  505 assLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQEVARYK 571
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 193-331 3.44e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.85  E-value: 3.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   193 YEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKES----EVKRLQEKLVcKMKGEGVEIV 268
Cdd:smart00787  146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRAKEKLK-KLLQEIMIKV 224

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581963   269 DRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR-YKKMQDTVVLAQGKDG 331
Cdd:smart00787  225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQSLTG 288
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 715-772 3.48e-04

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 39.87  E-value: 3.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581963  715 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 772
Cdd:cd09547      6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-311 4.37e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  141 LEEHREKVNATEEMLQQELLSRTSLETQKlDLMAEISNLKLKLTAVEKDRLdyEDKFRDTEGLIQEINDLRLKVS----- 215
Cdd:PRK03918   471 IEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLEEL--EKKAEEYEKLKEKLIKLKGEIKslkke 547

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  216 -----EMDSERLQYEKKLKSTKDELASLKEQLEEK--------ESEVKRLQEklVCKMKGEGVEIVDRDENFKKKLKEKN 282
Cdd:PRK03918   548 lekleELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEP--FYNEYLELKDAEKELEREEKELKKLE 625

                          170       180
                   ....*....|....*....|....*....
gi 1034581963  283 IEVQKMKKAVESLMAANEEKDRKIEDLRQ 311
Cdd:PRK03918   626 EELDKAFEELAETEKRLEELRKELEELEK 654
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 712-771 5.00e-04

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 39.60  E-value: 5.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  712 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:cd09552      6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-250 5.11e-04

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: 44.29  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNAteemlqqellsrtsLETQKLDLMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581963  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVK 250
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
PRK01156 PRK01156
chromosome segregation protein; Provisional
 108-335 5.20e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  108 RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEM--LQQELLSRTSLETQKLDLMAEISNLKLKLTA 185
Cdd:PRK01156   302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYddLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  186 VEKDRLDYEDKFRDTEGlIQEIN--DLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGE 263
Cdd:PRK01156   382 YSKNIERMSAFISEILK-IQEIDpdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGT 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  264 GV--------------------EIVDRDENFKKKLKEKNIEVQKMKKAVES-LMAANEEKDRKIEDLRQCLnryKKMQDT 322
Cdd:PRK01156   461 TLgeeksnhiinhynekksrleEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADL---EDIKIK 537

                          250
                   ....*....|...
gi 1034581963  323 VVLAQGKDGEYEE 335
Cdd:PRK01156   538 INELKDKHDKYEE 550
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 135-329 5.40e-04

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 43.99  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  135 RDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL--KLTAVEKDRLDYEDKFRDTEGLIQEInDLRL 212
Cdd:pfam18971  559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKStgNYDEVKKAQKDLEKSLRKREHLEKEV-EKKL 637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  213 KVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmKGEGVEIVDRDENFKKKLKE--------KNIE 284
Cdd:pfam18971  638 ESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNL----KGIKRELSDKLEKISKDLKDfsksfdefKNGK 713

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581963  285 VQKMKKAVESLMA---------ANEEKDRKIEDLRQCLNRYK--KMQDTVVLAQGK 329
Cdd:pfam18971  714 NKDFSKAEETLKAlkgsvkdlgINPEWISKVENLNAALNEFKngKNKDFSKVTQAK 769
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 641-692 5.41e-04

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: 39.16  E-value: 5.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  641 EQVCNWLMEQGLGSYLNsgkHWIASG---QTLLQASQQDLeKELGIKHSLHRKKL 692
Cdd:cd09497      5 EAIFDWLREFGLEEYTP---NFIKAGydlPTISRMTPEDL-TAIGITKPGHRKKL 55
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-309 6.80e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLEN--DKESLVLQVSVLTDQVEAQGEK-----IRDLEFCLEEHRE------KVNATEEMLQQELLSRTSLETQKL 170
Cdd:PRK03918   480 KELRELEKvlKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKlkekliKLKGEIKSLKKELEKLEELKKKLA 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  171 DLMAEISNLKLKLTAVEK--DRLDYEDkFRDTEGLIQEIND-----LRLKVSEMDSERLqyEKKLKSTKDELASLKEQLE 243
Cdd:PRK03918   560 ELEKKLDELEEELAELLKelEELGFES-VEELEERLKELEPfyneyLELKDAEKELERE--EKELKKLEEELDKAFEELA 636

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  244 EKESEVKRLQEKL-----------VCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 309
Cdd:PRK03918   637 ETEKRLEELRKELeelekkyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 105-292 7.20e-04

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: 42.88  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  105 RLARLENDKESLVLQVSVLTDQveaqgEKIRDLEFCLEEHREKVNATEE--MLQQELLSRTSLETQK--LDLMAEISNLK 180
Cdd:pfam15905  130 QLLELTRVNELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKevMAKQEGMEGKLQVTQKnlEHSKGKVAQLE 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  181 LKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKM 260
Cdd:pfam15905  205 EKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKC 284

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034581963  261 KGEGVEIVDRDENFKKKLKEKNIEVQKMKKAV 292
Cdd:pfam15905  285 KLLESEKEELLREYEEKEQTLNAELEELKEKL 316
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 636-684 9.43e-04

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: 38.43  E-value: 9.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  636 AKWTKEQVCNWL--MEQGLGSYLNSGKHWIASGQTLLQASQQDLEkELGIK 684
Cdd:cd09511      2 AKWSPKQVTDWLkgLDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 712-770 1.07e-03

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 38.37  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  712 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 770
Cdd:cd09488      2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
PTZ00121 PTZ00121
MAEBL; Provisional
 130-332 1.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  130 QGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKltaVEKDRLDYEDKFRDTEGLIQEIND 209
Cdd:PTZ00121  1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK---VEQLKKKEAEEKKKAEELKKAEEE 1658

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  210 LRLKVSEMDSERLQYEKK---LKSTKDELASLKEQLEEKESEVKRLQEklvckMKGEGVEIVDRDENFKKKLKEKNIEVQ 286
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKKaeeAKKAEEDEKKAAEALKKEAEEAKKAEE-----LKKKEAEEKKKAEELKKAEEENKIKAE 1733

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034581963  287 KMKKAveslmaaNEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKDGE 332
Cdd:PTZ00121  1734 EAKKE-------AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
PRK12704 PRK12704
phosphodiesterase; Provisional
 194-320 1.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  194 EDKFRDTEGLIQEIndlrLKVSEMDSERLQYEKKLKStKDELASLKEQLE----EKESEVKRLQEKLvcKMKGEGVEivD 269
Cdd:PRK12704    30 EAKIKEAEEEAKRI----LEEAKKEAEAIKKEALLEA-KEEIHKLRNEFEkelrERRNELQKLEKRL--LQKEENLD--R 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  270 RDENFKKK---LKEKNIEVQKMKKAVESLMaanEEKDRKIEDLRQCLNRYKKMQ 320
Cdd:PRK12704   101 KLELLEKReeeLEKKEKELEQKQQELEKKE---EELEELIEEQLQELERISGLT 151
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 638-679 1.22e-03

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.


Pssm-ID: 188913  Cd Length: 72  Bit Score: 38.23  E-value: 1.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034581963  638 WTKEQVCNWLMEQGLGSYLNSGKHWiaSGQTLLQASQQDLEK 679
Cdd:cd09514      7 WSPKEVSDWLSEEGMQEYSEALRSF--DGQALLNLTEEDFKK 46
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 636-699 1.48e-03

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 38.00  E-value: 1.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581963  636 AKWTKEQVCNWLMEQGLGSYLNS--GKHWIaSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 699
Cdd:cd09515      2 HEWTCEDVAKWLKKEGFSKYVDLlcNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
PRK01156 PRK01156
chromosome segregation protein; Provisional
 109-320 1.61e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.58  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  109 LENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEE---MLQQELLSRTSLETQKLDLMAEISNLKLKLTA 185
Cdd:PRK01156   188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDdynNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  186 VEKDRLDYEDKfrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEklVCKMKGEGV 265
Cdd:PRK01156   268 ELEKNNYYKEL---EERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSV--LQKDYNDYI 342

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  266 EIVDRDENFKKK---LKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQ 320
Cdd:PRK01156   343 KKKSRYDDLNNQileLEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 103-288 1.67e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.30  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESLVLQVSVLTDQVEAQG-EKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:pfam08614   13 LDRTALLEAENAKLQSEPESVLPSTSSSKlSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  182 KLTAVEKdRLdyedkfrdtEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEklvckmk 261
Cdd:pfam08614   93 KLREDER-RL---------AALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK------- 155

                          170       180
                   ....*....|....*....|....*..
gi 1034581963  262 gEGVEIVDRdenfkkKLKEKNIEVQKM 288
Cdd:pfam08614  156 -ENRELVER------WMKRKGQEAEAM 175
PRK01156 PRK01156
chromosome segregation protein; Provisional
 102-309 1.68e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.58  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFcleEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKl 181
Cdd:PRK01156   254 YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVY---KNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK- 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRlkvsemdserlQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMK 261
Cdd:PRK01156   330 KLSVLQKDYNDYIKKKSRYDDLNNQILELE-----------GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  262 GEGV---EIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 309
Cdd:PRK01156   399 IQEIdpdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEML 449
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 638-682 1.69e-03

SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. Exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188925  Cd Length: 66  Bit Score: 37.72  E-value: 1.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034581963  638 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQ---QDLEKELG 682
Cdd:cd09526      4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 201-323 1.87e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  201 EGLIQEINDLrlkVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRD-ENFKKKLK 279
Cdd:cd22656    113 EEAKKTIKAL---LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEiKDLQKELE 189

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034581963  280 EKNIE-VQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTV 323
Cdd:cd22656    190 KLNEEyAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDL 234
PRK01156 PRK01156
chromosome segregation protein; Provisional
 128-331 1.87e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  128 EAQGEKIRDLEFCLEEHREKVNATEEMLQQ-ELLSRTSLETQKLDLMAEISNL------------KLKLTAVEKDRLDYE 194
Cdd:PRK01156   528 RADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIdietnrsrsneiKKQLNDLESRLQEIE 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  195 DKFRDTEGLI--------QEINDLRLKVSEMDSERLQYEKKLKSTKDelasLKEQLEEKESEVKRLQEklvckMKGEGVE 266
Cdd:PRK01156   608 IGFPDDKSYIdksireieNEANNLNNKYNEIQENKILIEKLRGKIDN----YKKQIAEIDSIIPDLKE-----ITSRIND 678

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  267 IVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQ------DTVVLAQGKDG 331
Cdd:PRK01156   679 IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKkaigdlKRLREAFDKSG 749
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 203-323 1.90e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  203 LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDEnFKKKLKEkn 282
Cdd:COG1579     22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVRNNKE-YEALQKE-- 97

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034581963  283 IEVQKMKKAV--ESLMAANEEKDRKIEDLRQCLNRYKKMQDTV 323
Cdd:COG1579     98 IESLKRRISDleDEILELMERIEELEEELAELEAELAELEAEL 140
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-311 2.20e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  102 YQER-------LARLENDKESLVLQVSvltDQVEAQGEKirDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMA 174
Cdd:PRK02224   167 YRERasdarlgVERVLSDQRGSLDQLK---AQIEEKEEK--DLHERLNGLESELAELDEEIER-------YEEQREQARE 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  175 EISNLKLKLTAvekdrldYEDKFRDTEGLIQEINDLRLKVSEMDSERlqyekklKSTKDELASLKEQLEEKESEVKRLQE 254
Cdd:PRK02224   235 TRDEADEVLEE-------HEERREELETLEAEIEDLRETIAETERER-------EELAEEVRDLRERLEELEEERDDLLA 300

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581963  255 KlvCKMKGEGVEIV--------DRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 311
Cdd:PRK02224   301 E--AGLDDADAEAVearreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 638-694 2.26e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 2.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  638 WTKEQVCNWLMEQ-GLGSYLNSGKHWIASGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 694
Cdd:cd09504      5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
127-315 2.38e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  127 VEAQGEKIRDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMAEISNLKLKLTAVEkdrldyedkfrdtegliQE 206
Cdd:COG4372     26 IAALSEQLRKALFELDKLQEELEQLREELEQ-------AREELEQLEEELEQARSELEQLE-----------------EE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  207 INDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQ 286
Cdd:COG4372     82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK-QLEAQIAELQSEIAEREEELKELEEQLE 160

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034581963  287 KMKKAVESLMA-----ANEEKDRKIEDLRQCLNR 315
Cdd:COG4372    161 SLQEELAALEQelqalSEAEAEQALDELLKEANR 194
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 85-326 2.49e-03

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 41.59  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   85 WLQSQMTNGHLPGNGDVYQERLARLENDKESLVLQV--------SVLTDQVEAQGEKIRDLE-FCL-----EEHR-EKVN 149
Cdd:COG5244    370 WLSEFLQRKFSSKQETAFSICQFLEDNKDVTLILKIlhpilettVPKLLAFLRTNSNFNDNDtLCLigslyEIARiDKLI 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  150 ATEEMLQQelLSRTSLETQKLdlMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKvsemDSERLQYEKKLK 229
Cdd:COG5244    450 GKEEISKQ--DNRLFLYPSCD--ITLSSILTILFSDKLEVFFQGIESLLENITIFPEQPSQQTS----DSENIKENSLLS 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  230 STKDEL-ASLKEQLEEKESEVKrlQEKLVCKMKGEGVEIVDRDENFKK----------KLKEKNIEVQKMKKAVE----S 294
Cdd:COG5244    522 DRLNEEnIRLKEVLVQKENMLT--EETKIKIIIGRDLERKTLEENIKTlkvelnnknnKLKEENFNLVNRLKNMElklyQ 599

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1034581963  295 LMAANEEKD------RKIEDLRQCLNRYKKMQDTVVLA 326
Cdd:COG5244    600 IKDNNTLNKiyldlvSEIMELRETIRRQIKEQKRVSID 637
PTZ00121 PTZ00121
MAEBL; Provisional
 146-311 2.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  146 EKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEiNDLRLKVSEMDSERLQYE 225
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKK 1633

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  226 K--KLKSTKDELASLKEQL--EEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE 301
Cdd:PTZ00121  1634 KveQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713

                          170
                   ....*....|
gi 1034581963  302 KDRKIEDLRQ 311
Cdd:PTZ00121  1714 EKKKAEELKK 1723
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 794-846 2.67e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.31  E-value: 2.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  794 EVQKWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 846
Cdd:cd09504      1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 146-318 3.15e-03

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: 41.70  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  146 EKVNATEEMLQ--QELLSRTSLETQKLD-----LMAEISNLKLKLTA-------VEKDRLDYEDKFRDTEGLIQEInDLR 211
Cdd:pfam01576    5 EEMQAKEEELQkvKERQQKAESELKELEkkhqqLCEEKNALQEQLQAetelcaeAEEMRARLAARKQELEEILHEL-ESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  212 LKVSEMDSERLQYEKKlkSTKDELASLKEQLEEKESEVKRLQ-EKLVCKMKGEGVE---IVDRDENFK----KKL----- 278
Cdd:pfam01576   84 LEEEEERSQQLQNEKK--KMQQHIQDLEEQLDEEEAARQKLQlEKVTTEAKIKKLEediLLLEDQNSKlskeRKLleeri 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034581963  279 ----------KEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 318
Cdd:pfam01576  162 seftsnlaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 715-771 3.51e-03

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: 36.91  E-value: 3.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581963  715 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 771
Cdd:cd09505     10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 712-771 3.77e-03

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 37.15  E-value: 3.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  712 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 771
Cdd:cd09549      7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
104-256 4.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLENDKESLVLQVSVLT------DQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRtsLETQKLDLMAEIS 177
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--LRAELARLEAELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  178 NLKLKLTAVEKDRLDYEDKFRDTEG-----LIQEINDLRLKVSEMDSERLQYEKKLKS-------TKDELASLKEQ---- 241
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNGGdrleqLEREIERLERELEERERRRARLEALLAAlglplpaSAEEFAALRAEaaal 392

                          170
                   ....*....|....*
gi 1034581963  242 LEEKESEVKRLQEKL 256
Cdd:COG4913    393 LEALEEELEALEEAL 407
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 103-327 4.19e-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: 41.11  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  103 QERLARLENDKESL--VLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVN-------------ATEEMLQQELLSRTSLET 167
Cdd:TIGR00618  239 QQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  168 QkldlMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKD--ELASLKEQLEEK 245
Cdd:TIGR00618  319 K----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQKTTLTQK 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  246 ESEVKRLQEKLVCKM-KGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVV 324
Cdd:TIGR00618  395 LQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474


                   ...
gi 1034581963  325 LAQ 327
Cdd:TIGR00618  475 LQT 477
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 187-317 4.61e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 39.91  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  187 EKDRLDyedkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEekesEVKRLQEKLVCKMkgegVE 266
Cdd:pfam11932   35 KIDKWD-----DEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIE----EIERTERELVPLM----LK 101

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  267 IVDRDENFkkklkeknievqkmkkaVESLMAAN-EEKDRKIEDLRQCLNRYK 317
Cdd:pfam11932  102 MLDRLEQF-----------------VALDLPFLlEERQARLARLRELMDDAD 136
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 68-325 4.78e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   68 EGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK 147
Cdd:pfam10174  453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  148 VNATEEML----QQELLSRTSLE-TQKLDLM---------------AEISNLKLKLTAVEKDRLDYEDKFRDTEGLI--- 204
Cdd:pfam10174  533 CSKLENQLkkahNAEEAVRTNPEiNDRIRLLeqevarykeesgkaqAEVERLLGILREVENEKNDKDKKIAELESLTlrq 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  205 -----QEINDLRLKVSEMDSERLQYEKKLKSTKDELA--SLKEQLEEKESEVKRLQEKL-VCKMKGEGVE--IVDRD--- 271
Cdd:pfam10174  613 mkeqnKKVANIKHGQQEMKKKGAQLLEEARRREDNLAdnSQQLQLEELMGALEKTRQELdATKARLSSTQqsLAEKDghl 692

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034581963  272 ENFKKKLKEKNIEVQKMKKavESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVL 325
Cdd:pfam10174  693 TNLRAERRKQLEEILEMKQ--EALLAAISEKDANIALLELSSSKKKKTQEEVMA 744
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 212-310 4.98e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 4.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  212 LKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrdENFKKKLKEKNIEV----QK 287
Cdd:COG1579     10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---------------EDLEKEIKRLELEIeeveAR 74

                           90       100
                   ....*....|....*....|....*...
gi 1034581963  288 MKKAVESLMAANEEKD-----RKIEDLR 310
Cdd:COG1579     75 IKKYEEQLGNVRNNKEyealqKEIESLK 102
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 200-322 5.21e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  200 TEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEK---------ESEVKRLQEKLVCKMKGEGVEIVDR 270
Cdd:cd22656    123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKELEKLNEEYAAKLKAK 202

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034581963  271 DENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDT 322
Cdd:cd22656    203 IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQGA 254
PRK12704 PRK12704
phosphodiesterase; Provisional
 216-311 5.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  216 EMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCK---MKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAV 292
Cdd:PRK12704    65 EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                           90       100
                   ....*....|....*....|.
gi 1034581963  293 ESLMA--ANEEKDRKIEDLRQ 311
Cdd:PRK12704   145 ERISGltAEEAKEILLEKVEE 165
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 712-759 6.21e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.54  E-value: 6.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581963  712 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 759
Cdd:cd09504      3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
176-325 6.25e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  176 ISNLKLKLTAVEKDRLDYEDKFRDtegLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEK 255
Cdd:COG1340      3 TDELSSSLEELEEKIEELREEIEE---LKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  256 lvckmkgegveivdRDENFkKKLKEKNIEVQKMKKAVESLMAANEEkdrkIEDLRQCLNRYKKMQDTVVL 325
Cdd:COG1340     80 --------------RDELN-EKLNELREELDELRKELAELNKAGGS----IDKLRKEIERLEWRQQTEVL 130
PTZ00121 PTZ00121
MAEBL; Provisional
 142-321 7.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  142 EEHR--EKVNATEEMLQQELLsRTSLETQKLDlmaeisnlKLKLTAVEKDRLDYEDKfrDTEGLIQEINDLRLKVSEMDS 219
Cdd:PTZ00121  1275 EEARkaDELKKAEEKKKADEA-KKAEEKKKAD--------EAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKK 1343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  220 ERLQYEKKLKSTKDELASLKEQLE---EKESEVKRLQEKLvcKMKGEGVEivdRDENFKKKLKEKNIEVQKMKKAVESLM 296
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAA--KKKAEEKK---KADEAKKKAEEDKKKADELKKAAAAKK 1418

                          170       180
                   ....*....|....*....|....*
gi 1034581963  297 AANEEKdRKIEDLRQCLNRYKKMQD 321
Cdd:PTZ00121  1419 KADEAK-KKAEEKKKADEAKKKAEE 1442
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
236-318 7.44e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  236 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDEnfkKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 315
Cdd:COG2433    376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE---EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452


                   ...
gi 1034581963  316 YKK 318
Cdd:COG2433    453 ARS 455
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 175-305 7.74e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  175 EIS-NLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRL----KVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEV 249
Cdd:PRK00409   492 EIAkRLGLPENIIEEAKKLIGEDKEKLNELIASLEELEReleqKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581963  250 KRLQEKLVCKMKGEGVEIVdRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRK 305
Cdd:PRK00409   572 EKEAQQAIKEAKKEADEII-KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 104-293 7.76e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 7.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:TIGR00606  709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963  184 TAV---EKDRLDYEDKFRDTEGLIQEIN--DLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvC 258
Cdd:TIGR00606  789 TDVtimERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT-N 867

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034581963  259 KMKGEGVEI---VDRDENFKKKLKEKNIEVQKMKKAVE 293
Cdd:TIGR00606  868 ELKSEKLQIgtnLQRRQQFEEQLVELSTEVQSLIREIK 905
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 229-321 7.84e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 39.64  E-value: 7.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   229 KSTKDELASLKEQLEEKESEVKRLQEKLVckmkgEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIED 308
Cdd:smart00435  273 KTHEKSMEKLQEKIKALKYQLKRLKKMIL-----LFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKKQIER 347

                            90
                    ....*....|....
gi 1034581963   309 LRQCLNRYKK-MQD 321
Cdd:smart00435  348 LEERIEKLEVqATD 361
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 199-299 9.06e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 9.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581963   199 DTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEK-----ESEVKRLQEKLVCKMKgegvEIVDRDEN 273
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaatlsEAAREKKEKELQKKVQ----EFQRKQQK 80

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1034581963   274 FKKKLKEKNIEV-----QKMKKAVESLMAAN 299
Cdd:smart00935   81 LQQDLQKRQQEElqkilDKINKAIKEVAKKK 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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