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Conserved domains on  [gi|767966679|ref|XP_011518716|]
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liprin-beta-2 isoform X1 [Homo sapiens]

Protein Classification

liprin-beta family protein( domain architecture ID 13527062)

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; also contains 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 ...
 725-796 5.18e-44

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: 153.00  E-value: 5.18e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 725 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 796
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 ...
 640-702 5.50e-37

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: 132.82  E-value: 5.50e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679 640 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 702
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 ...
 566-629 2.29e-35

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: 128.11  E-value: 2.29e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966679 566 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 629
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-317 1.99e-11

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 1.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    59 LALEMLELPQERAALLSQIpgptaayikewfEESLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   219 VEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKD 297
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELE 446

                          250       260
                   ....*....|....*....|
gi 767966679   298 RRIEELTGLLNQYRKVKEIV 317
Cdd:TIGR02168  447 EELEELQEELERLEEALEEL 466
 
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 ...
 725-796 5.18e-44

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: 153.00  E-value: 5.18e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 725 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 796
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 ...
 640-702 5.50e-37

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: 132.82  E-value: 5.50e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679 640 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 702
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 ...
 566-629 2.29e-35

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: 128.11  E-value: 2.29e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966679 566 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 629
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 568-630 1.03e-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: 72.30  E-value: 1.03e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679  568 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 630
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 645-701 2.12e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 71.53  E-value: 2.12e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679  645 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 701
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 566-630 5.53e-14

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 67.32  E-value: 5.53e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966679   566 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 630
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
726-796 6.08e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 6.08e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966679  726 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 796
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-317 1.99e-11

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: 68.16  E-value: 1.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    59 LALEMLELPQERAALLSQIpgptaayikewfEESLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   219 VEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKD 297
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELE 446

                          250       260
                   ....*....|....*....|
gi 767966679   298 RRIEELTGLLNQYRKVKEIV 317
Cdd:TIGR02168  447 EELEELQEELERLEEALEEL 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 82-315 1.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  82 AAYIKEWFEESLSQVN---HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE 158
Cdd:COG1196  230 LLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 159 MLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKA 238
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679 239 EVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKmgmETLLLANEDKDRRIEELTGLLNQYRKVKE 315
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 726-795 4.43e-08

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: 50.76  E-value: 4.43e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   726 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 795
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 108-336 7.58e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 56.67  E-value: 7.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   108 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   188 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 262
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966679   263 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 336
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 646-701 8.37e-08

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: 49.99  E-value: 8.37e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679   646 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 701
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
206-355 3.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 206 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 276
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 277 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 354
Cdd:PRK03918 573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                 .
gi 767966679 355 Q 355
Cdd:PRK03918 648 E 648
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 725-796 5.18e-44

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: 153.00  E-value: 5.18e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 725 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 796
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 ...
 640-702 5.50e-37

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: 132.82  E-value: 5.50e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679 640 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 702
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 ...
 566-629 2.29e-35

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: 128.11  E-value: 2.29e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966679 566 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 629
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 ...
 733-794 1.97e-29

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 111.09  E-value: 1.97e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 733 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 794
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 ...
 725-796 3.76e-29

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 110.61  E-value: 3.76e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 725 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 796
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 644-702 2.21e-28

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 108.39  E-value: 2.21e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 644 IWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 702
Cdd:cd09495    1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLvHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 573-629 2.87e-26

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 102.30  E-value: 2.87e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767966679 573 RVCAWLEDFGLAQ-YVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 629
Cdd:cd09494    1 RVCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 725-796 7.64e-20

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 84.29  E-value: 7.64e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 725 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 796
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 568-630 1.03e-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: 72.30  E-value: 1.03e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679  568 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 630
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 645-701 2.12e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 71.53  E-value: 2.12e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679  645 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 701
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 640-702 5.40e-14

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 67.43  E-value: 5.40e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966679 640 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDRRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 702
Cdd:cd09567    1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 566-630 5.53e-14

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 67.32  E-value: 5.53e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966679   566 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 630
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
726-796 6.08e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 6.08e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966679  726 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 796
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 573-628 1.24e-11

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 60.33  E-value: 1.24e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767966679 573 RVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 628
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 645-698 1.77e-11

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 59.95  E-value: 1.77e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767966679 645 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 698
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-317 1.99e-11

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: 68.16  E-value: 1.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    59 LALEMLELPQERAALLSQIpgptaayikewfEESLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   219 VEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKD 297
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELE 446

                          250       260
                   ....*....|....*....|
gi 767966679   298 RRIEELTGLLNQYRKVKEIV 317
Cdd:TIGR02168  447 EELEELQEELERLEEALEEL 466
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 641-701 1.39e-09

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 54.79  E-value: 1.39e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679 641 LDHIWV-TRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 701
Cdd:cd09565    1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 566-630 2.43e-09

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 54.49  E-value: 2.43e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679 566 FAQWSTERVCAWLEDF-GL-AQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 630
Cdd:cd09562    1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 82-315 1.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  82 AAYIKEWFEESLSQVN---HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE 158
Cdd:COG1196  230 LLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 159 MLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKA 238
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679 239 EVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKmgmETLLLANEDKDRRIEELTGLLNQYRKVKE 315
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-303 3.92e-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: 3.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   128 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEE 207
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   208 LLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAlkdaEIERLHSQLSRTAALHSESHTERDQEIQRLKMGME 287
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170
                   ....*....|....*.
gi 767966679   288 TLLLANEDKDRRIEEL 303
Cdd:TIGR02168  828 SLERRIAATERRLEDL 843
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 726-795 4.43e-08

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: 50.76  E-value: 4.43e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   726 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 795
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 71-309 4.85e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.31  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  71 AALLSQIPGPTAAYIKEWFEESLSQVNHHSAASnetyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ 150
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 151 VKLNAAEEMLQQellSRTSLETQKLDL---------MTEVSELKLKLvgmekeqreqeekqrKAEELLQELRHLKIkVEE 221
Cdd:COG4942   83 AELAELEKEIAE---LRAELEAQKEELaellralyrLGRQPPLALLL---------------SPEDFLDAVRRLQY-LKY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 222 LENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIE 301
Cdd:COG4942  144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223


                 ....*...
gi 767966679 302 ELTGLLNQ 309
Cdd:COG4942  224 ELEALIAR 231
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 567-627 7.54e-08

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 50.14  E-value: 7.54e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 567 AQWSTERVCAWLE-DFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 627
Cdd:cd09564    2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 108-336 7.58e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 56.67  E-value: 7.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   108 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   188 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 262
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966679   263 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 336
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 646-701 8.37e-08

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: 49.99  E-value: 8.37e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679   646 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 701
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
569-630 1.17e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 49.58  E-value: 1.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679  569 WSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 630
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
206-318 1.99e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 54.86  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 206 EELLQELRHLKIKVEELEnernqyewklkatkAEVAQLQEQVALKDAEIERLHSQLSRtaaLHSESHTE--RDQEIQRLK 283
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSE---ARSEERREirKDREISRLD 471

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767966679 284 MGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 318
Cdd:COG2433  472 REIERLERELEEERERIEELKRKLERLKELWKLEH 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-325 3.76e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  54 IEDLRLALEMLElpQERAALLSQIpgptAAYIKEwfEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVE 133
Cdd:COG1196  269 LEELRLELEELE--LELEEAQAEE----YELLAE--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 134 AQGEKIRDLEvcleghqVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELR 213
Cdd:COG1196  341 ELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL----------LEALRAAAELAAQLE 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 214 HLKIKVEELENERNQYEwklkatkAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLAN 293
Cdd:COG1196  404 ELEEAEEALLERLERLE-------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767966679 294 EDKDRRIEELTGLLNQYRKVKEIVMVTQGPSE 325
Cdd:COG1196  477 AALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 108-311 5.75e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 108 QERLARLEgDKES-LILQVSVLTDQVEA--------QGEKIRDLEVCLeghqVKLNAAEEMLQQELLSRTSLETQKLDLM 178
Cdd:COG1196  185 EENLERLE-DILGeLERQLEPLERQAEKaeryrelkEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELE 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 179 TEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLH 258
Cdd:COG1196  260 AELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767966679 259 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYR 311
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 569-638 5.89e-07

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 47.70  E-value: 5.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 569 WSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAinTKQEEKS 638
Cdd:cd09505    5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEE--LKMKSDS 72
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-315 8.23e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 8.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    53 LIEDLRLALEmlelpqERAALLSQIpgptAAYIKEWFEESLSQVnhhsaasnetyQERLARLEGDKESLILQVSVLTDQV 132
Cdd:TIGR02169  259 EISELEKRLE------EIEQLLEEL----NKKIKDLGEEEQLRV-----------KEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   133 EAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLetqkldlMTEVSELKLKLvgmekeqreqEEKQRKAEELLQEL 212
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-------TEEYAELKEEL----------EDLRAELEEVDKEF 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   213 RHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLA 292
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460

                          250       260
                   ....*....|....*....|...
gi 767966679   293 NEDKDRRIEELTGLLNQYRKVKE 315
Cdd:TIGR02169  461 AADLSKYEQELYDLKEEYDRVEK 483
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 569-625 1.56e-06

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 46.56  E-value: 1.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966679 569 WSTERVCAWLEDF-GLAQYVIFARQWVSSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 625
Cdd:cd09504    5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 565-628 2.12e-06

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 45.87  E-value: 2.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966679 565 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 628
Cdd:cd09507    1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 104-336 2.94e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  104 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 178
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  179 TEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvaLKDAEIErlh 258
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE--LKKENLE--- 560

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767966679  259 sqlsrtaalhsESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPE 336
Cdd:TIGR04523 561 -----------KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 87-334 3.40e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.89  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   87 EWFEESLSQVNHHSAASNETYQERLARLEgdKESLILQVSVLTDQVE-----AQGEKIRDLEVcleGHQVKLNAAEEMLQ 161
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKME--QERLRQEKEEKAREVErrrklEEAEKARQAEM---DRQAAIYAEQERMA 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  162 QEL---LSRTSLETQKLDL-MTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKiKVEELENERNQyewKLKATK 237
Cdd:pfam17380 344 MERereLERIRQEERKRELeRIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQR---KIQQQK 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  238 AEVAQLQ-EQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEI 316
Cdd:pfam17380 420 VEMEQIRaEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499

                         250
                  ....*....|....*...
gi 767966679  317 VMvtqgpSERTLSINEEE 334
Cdd:pfam17380 500 EL-----EERKQAMIEEE 512
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-305 9.78e-06

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: 49.33  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   54 IEDLRLALEMLELPQERAALLSQIPgptaayIKEWFEeslsQVNHhsaaSNETYQERLarleGDKESlilQVSVLTDQVE 133
Cdd:pfam05483 192 IEKMILAFEELRVQAENARLEMHFK------LKEDHE----KIQH----LEEEYKKEI----NDKEK---QVSLLLIQIT 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  134 AQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLsRTSLETQKlDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQE 211
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEktKLQDENL-KELIEKKD-HLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQ 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  212 LRHLK-IKVEELENERNQYEWKLKATKAEVAQLQE--------------QVALKDAEIERLHSQLSRTAALHSESHTERd 276
Cdd:pfam05483 329 LTEEKeAQMEELNKAKAAHSFVVTEFEATTCSLEEllrteqqrleknedQLKIITMELQKKSSELEEMTKFKNNKEVEL- 407

                         250       260
                  ....*....|....*....|....*....
gi 767966679  277 QEIQRLKMGMETLLLANEDKDRRIEELTG 305
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKG 436
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 85-317 1.15e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.35  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    85 IKEWFEESLSQVNHHSAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLEVC---LEGHQVKL-NAAE 157
Cdd:pfam15921  567 LRQQIENMTQLVGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELEARvsdLELEKVKLvNAGS 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   158 EMLQqellSRTSLETQKLDLMTEVSELKLKLVGMEKEQreqeekqrkaeELLQelRHLKIKVEELENERNQYEWKLKATK 237
Cdd:pfam15921  643 ERLR----AVKDIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKSEEMETTTNKLKMQLKSAQ 705

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   238 AEVAQ---------------------LQEQVALKDAEIERLHSQLSrtaaLHSESHTERDQEIQRL-----KMGMETLLL 291
Cdd:pfam15921  706 SELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQ----FLEEAMTNANKEKHFLkeeknKLSQELSTV 781

                          250       260
                   ....*....|....*....|....*.
gi 767966679   292 ANEdKDRRIEELTGLLNQYRKVKEIV 317
Cdd:pfam15921  782 ATE-KNKMAGELEVLRSQERRLKEKV 806
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 54-303 1.29e-05

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: 49.30  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    54 IEDLRLALEMLElpQERAALLSQIPGptaayiKEWFEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTD--- 130
Cdd:TIGR02169  718 IGEIEKEIEQLE--QEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArls 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   131 -----QVEAQGEKI-----------RDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKE 194
Cdd:TIGR02169  790 hsripEIQAELSKLeeevsriearlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   195 QREQEEKQrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSrtaalHSESHTE 274
Cdd:TIGR02169  870 LEELEAAL---RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-----EIEDPKG 941

                          250       260
                   ....*....|....*....|....*....
gi 767966679   275 RDQEIQRLKMGMETLLLANEDKDRRIEEL 303
Cdd:TIGR02169  942 EDEEIPEEELSLEDVQAELQRVEEEIRAL 970
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 570-623 2.50e-05

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


Pssm-ID: 188896  Cd Length: 66  Bit Score: 43.02  E-value: 2.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679 570 STERVCAWLEDFGLAQYvifARQWVSSGHTLLT---ATPQDMeKELGIKHPLHRKKL 623
Cdd:cd09497    3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
65-260 3.01e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  65 ELPQERAALLSQIPGPTAAYIKEWfeESLSQVNHHSAASNETY---QERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 141
Cdd:COG4717   50 RLEKEADELFKPQGRKPELNLKEL--KELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 142 LEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVSELKLKLVgmekeqreqEEKQRKAEELLQELRHLK 216
Cdd:COG4717  128 LPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQEELE---------ELLEQLSLATEEELQDLA 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767966679 217 IKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 260
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
101-356 3.25e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 101 AASNETYQERLARLEgdkeSLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDLMTE 180
Cdd:COG4372   27 AALSEQLRKALFELD----KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 181 VSELklklvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 260
Cdd:COG4372  100 QEEL---------------------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 261 LsrtaalhseshTERDQEIQRLKMGMETLLLAN---------EDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSIN 331
Cdd:COG4372  159 L-----------ESLQEELAALEQELQALSEAEaeqaldellKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227

                        250       260
                 ....*....|....*....|....*
gi 767966679 332 EEEPEGGFSKWNATNKDPEELFKQE 356
Cdd:COG4372  228 EAKLGLALSALLDALELEEDKEELL 252
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 107-338 4.00e-05

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 46.67  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  107 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRT---SLETQKLDLMTEVSE 183
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLREeiqKLRGQIQQLRTELQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  184 LKLKLVgmeKEQREQEEKQRKAEELLQELRHLKikvEELENERNQYEWKLKATKAEV----AQLQEQVALKDAEIERLHS 259
Cdd:pfam09787  80 LEAQQQ---EEAESSREQLQELEEQLATERSAR---REAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  260 QLSrtaaLHSESHTERDQEIQRLKMGMETLLlaneDKDRRIEELT----GLLNQYRKVKEIVMVTQGPSERTLSINEEEP 335
Cdd:pfam09787 154 QLT----SKSQSSSSQSELENRLHQLTETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGI 225


                  ...
gi 767966679  336 EGG 338
Cdd:pfam09787 226 SDG 228
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 113-314 4.13e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   113 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 192
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   193 KEQREQEEKQRKAEEllqELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDA--------------EIERLH 258
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679   259 SQLSRT---AALHSESHTERDQEIQRLKMGMETLLLANEDK--DRR------IEELTGLLNQYRKVK 314
Cdd:pfam01576  306 TELEDTldtTAAQQELRSKREQEVTELKKALEEETRSHEAQlqEMRqkhtqaLEELTEQLEQAKRNK 372
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
646-698 4.26e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.26  E-value: 4.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767966679  646 VTRWLDDIGLPQYKDQFHESRVD-RRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 698
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-266 4.52e-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: 47.36  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    62 EMLELPQERAALLSQipgpTAAYIKEWFEESLSQVNHHSAASNETyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 141
Cdd:TIGR02168  302 QQKQILRERLANLER----QLEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   142 LEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQEL 212
Cdd:TIGR02168  377 LEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767966679   213 RHLKIKVEELENERNQYEWKLKATKAEVAQLQEQV-ALKDaeIERLHSQLSRTAA 266
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQENLEGFSEGVK 509
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 567-628 4.78e-05

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 42.24  E-value: 4.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966679 567 AQWSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 628
Cdd:cd09515    2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 574-627 5.21e-05

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: 42.01  E-value: 5.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767966679 574 VC-AWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 627
Cdd:cd09567    7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
50-283 5.48e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   50 VLHLIEDLRLALEMLELPQERAALLSQIPGPTAAYIKEW-----FEESLSQVNH-HSAASNETYQERLARLEGDKESLIL 123
Cdd:COG4913   230 LVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARerlaeLEYLRAALRLwFAQRRLELLEAELEELRAELARLEA 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  124 QVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGmekeqreqeekq 202
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA------------ 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  203 rKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvalkdaeierlhsqlsrtaalhsesHTERDQEIQRL 282
Cdd:COG4913   378 -SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-------------------------LRELEAEIASL 431


                  .
gi 767966679  283 K 283
Cdd:COG4913   432 E 432
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 146-317 1.18e-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: 46.21  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   146 LEGHQVKLNAAEEMLQQELlsrTSLETQKLDLMTEVSELKlklvgmekeqreqeekqRKAEELLQELRHLKIKVEELENE 225
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL---EGLKRELSSLQSELRRIE-----------------NRLDELSQELSDASRKIGEIEKE 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   226 RNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhseshterdqEIQRLKMGMETLLLANEDKDRRI--EEL 303
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA-----------RIEELEEDLHKLEEALNDLEARLshSRI 793

                          170
                   ....*....|....
gi 767966679   304 TGLLNQYRKVKEIV 317
Cdd:TIGR02169  794 PEIQAELSKLEEEV 807
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 105-266 2.33e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 105 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ---------------------- 162
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgse 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 163 ---ELLSRTS----LETQKLDLMTEVSELKLKLvgmekeQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKA 235
Cdd:COG3883  113 sfsDFLDRLSalskIADADADLLEELKADKAEL------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767966679 236 TKAEVAQLQEQVALKDAEIERLHSQLSRTAA 266
Cdd:COG3883  187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 207-315 2.45e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 207 ELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERdqEIQRLKMGM 286
Cdd:COG1579   21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQKEI 98

                         90       100
                 ....*....|....*....|....*....
gi 767966679 287 ETLLLANEDKDRRIEELTGLLNQYRKVKE 315
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELA 127
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 646-699 2.75e-04

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 39.61  E-value: 2.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767966679 646 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 699
Cdd:cd09533    2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 565-630 2.95e-04

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 39.93  E-value: 2.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679 565 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 630
Cdd:cd09575    1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 55-315 3.13e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.50  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   55 EDLRLALEMLELPQERAALLSQIP--GPTAAYIKEWFEESLSQVNHHSAASNETYQER--LARLEGDKESLILQvsvLTD 130
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAelKEELRQSREKHEELEEKYKELSASSEELSEEKdaLLAQRAAHEARIRE---LEE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  131 QVEAQGEKIRDLEVCLEghQVKlNAAEEMLQQellsRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQ 210
Cdd:pfam07888 137 DIKTLTQRVLERETELE--RMK-ERAKKAGAQ----RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  211 ELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQeiQRLKMGMETLL 290
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQ 287

                         250       260       270
                  ....*....|....*....|....*....|.
gi 767966679  291 LAN------EDKDRRIEELTGLLNQYRKVKE 315
Cdd:pfam07888 288 LADaslalrEGRARWAQERETLQQSAEADKD 318
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-315 3.15e-04

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: 44.66  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    67 PQERAALLSQipgptAAYI---KEWFEESLSQVNHhsaasnetYQERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLE 143
Cdd:TIGR02168  154 PEERRAIFEE-----AAGIskyKERRKETERKLER--------TRENLDRLEDILNELERQLKSLERQAE-KAERYKELK 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   144 VCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSElklklvgmekeqreqeeKQRKAEELLQELRHLKIKVEELE 223
Cdd:TIGR02168  220 AELRELELALLVLR--LEELREELEELQEELKEAEEELEE-----------------LTAELQELEEKLEELRLEVSELE 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   224 NERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA--LHSESHTERDQE--------IQRLKMGMETLLLAN 293
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDELAEelaeleekLEELKEELESLEAEL 360

                          250       260
                   ....*....|....*....|..
gi 767966679   294 EDKDRRIEELTGLLNQYRKVKE 315
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLE 382
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 643-701 3.75e-04

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 39.61  E-value: 3.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966679 643 HIW----VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 701
Cdd:cd09506    3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-289 4.80e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  91 ESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQQeLLSRTSL 170
Cdd:COG4717  305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA-LLAEAGV 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 171 ET------------QKLDLMTEVSELKLKLVGmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKA 238
Cdd:COG4717  382 EDeeelraaleqaeEYQELKEELEELEEQLEE-LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767966679 239 EVAQLQEQVAL--KDAEIERLHSQLSRTAalhseshterdQEIQRLKMGMETL 289
Cdd:COG4717  461 ELEQLEEDGELaeLLQELEELKAELRELA-----------EEWAALKLALELL 502
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 110-161 5.95e-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: 39.81  E-value: 5.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767966679  110 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 161
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 646-701 6.41e-04

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 38.84  E-value: 6.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767966679 646 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 701
Cdd:cd09530    8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 90-302 8.38e-04

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: 43.09  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   90 EESLSQVNHHSAASN------ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghqvklnaaeemlqQE 163
Cdd:TIGR04523 186 QKNIDKIKNKLLKLElllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------------------TT 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  164 LLSRTslETQKLDLMTEVSELKLKLvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQ- 242
Cdd:TIGR04523 247 EISNT--QTQLNQLKDEQNKIKKQL-----------------SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQd 307

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966679  243 ----LQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETLLLANEDKDRRIEE 302
Cdd:TIGR04523 308 wnkeLKSELKNQEKKLEEIQNQISQN----NKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 50-311 1.21e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679    50 VLHLIEDLRLALEMLELPQERAALLSQIpgptaAYIKEWFEESLSQVNHHSAASNETYQERLARLEGDKESL----ILQV 125
Cdd:TIGR00618  589 LQNITVRLQDLTEKLSEAEDMLACEQHA-----LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqerVREH 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   126 SVLTDQVEAQGEKIRDLEVCLEGHQVK-LNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRK 204
Cdd:TIGR00618  664 ALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDA 740

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   205 AEELLQELRHL---KIKVEELENER-NQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLsrtAALHSESHTERDQEIQ 280
Cdd:TIGR00618  741 LNQSLKELMHQartVLKARTEAHFNnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL---KTLEAEIGQEIPSDED 817

                          250       260       270
                   ....*....|....*....|....*....|.
gi 767966679   281 RLKMGMETLLLANEDKDRRIEELTGLLNQYR 311
Cdd:TIGR00618  818 ILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 205-266 1.22e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 205 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA 266
Cdd:COG3883   32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-307 1.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 109 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELK 185
Cdd:COG4717   71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 186 LKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLK-ATKAEVAQLQEQVALKDAEIERLHSQLSRT 264
Cdd:COG4717  139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEA 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767966679 265 aalhSESHTERDQEIQRLKMGMETlllanEDKDRRIEELTGLL 307
Cdd:COG4717  219 ----QEELEELEEELEQLENELEA-----AALEERLKEARLLL 252
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 92-309 1.77e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.72  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   92 SLSQVNHHSAASNETYQERLARlEGDKE---SLILQVSVLTDQVEAqgeKIRDLEVCLEGHQVKLNAAEEMLQQEllsrt 168
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSE-DGTQKkmsSLSMELMKLRNKLEA---KMKEVMAKQEGMEGKLQVTQKNLEHS----- 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  169 sletqkldlMTEVSELKLKLVGMEKEQREQEEKQrkaEELLQElrhlkikVEELENERNQYEwklkATKAEVAQLQEQVA 248
Cdd:pfam15905 197 ---------KGKVAQLEEKLVSTEKEKIEEKSET---EKLLEY-------ITELSCVSEQVE----KYKLDIAQLEELLK 253

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966679  249 LKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRR----IEELTGLLNQ 309
Cdd:pfam15905 254 EKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTlnaeLEELKEKLTL 318
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 643-699 1.98e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 1.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966679 643 HIW----VTRWL-DDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 699
Cdd:cd09504    3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 563-614 1.99e-03

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 37.63  E-value: 1.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767966679 563 NAPFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGI 614
Cdd:cd09512    1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNI-DGQQLLQLDSSKL-KALGI 51
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
 63-306 3.04e-03

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


Pssm-ID: 463001  Cd Length: 523  Bit Score: 41.35  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   63 MLELPQERAALLSQIPGPTAAYIKewFEESLS--QVNHHSAASNETY-------QERLARLEGDKESLILQVSVLTDQVE 133
Cdd:pfam10212 263 MLQYKKKAVAYISSLKKPCPESVP--YEEALSnrRVLLSSTESREGLaqqvqqsQEKIAKLEQEKEHWMLEAQLLKIKLE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  134 AQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELK-LKLVGMEKEQREQEEK--QRKAEELLQ 210
Cdd:pfam10212 341 KENQRIADLEKQLLKGSTSGQLPELVQSKATLPLTAKQGSEASSISEKEPTPsTSLIGMLTVTTDSEESsdEESREQLIK 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  211 ElrHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQL----SRTAALHSE-SHTERDQEIQrLKMG 285
Cdd:pfam10212 421 S--HYMARIAELTSQLQLADSKAVHFHAECRALAKRLALAEKSKESLTEELklanQNISRLQDElTTTKRSYEDQ-LSMM 497

                         250       260
                  ....*....|....*....|.
gi 767966679  286 METLLLANEDKDRRIEELTGL 306
Cdd:pfam10212 498 SDHLCSMNETLTKQREEIDTL 518
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 89-328 3.18e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   89 FEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQvEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRT 168
Cdd:pfam05557  53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK-ESQLADAREVISCLKN---ELSELRRQIQRAELELQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  169 SLETQKLDLMTEVSELKLKLVGMEKEQREQeekqrkaEELLQELRHLKIKVEELENERNQYE-WK--LKATKAEVAQLQE 245
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQNL-------EKQQSSLAEAEQRIKELEFEIQSQEqDSeiVKNSKSELARIPE 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  246 QvalkDAEIERLHSqlsrtaalhseshterdqEIQRLKMGMETLLLANEDKdrriEELTGLLNQYRKVKEIVMVTQGPSE 325
Cdd:pfam05557 202 L----EKELERLRE------------------HNKHLNENIENKLLLKEEV----EDLKRKLEREEKYREEAATLELEKE 255


                  ...
gi 767966679  326 RTL 328
Cdd:pfam05557 256 KLE 258
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
206-355 3.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 206 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 276
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 277 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 354
Cdd:PRK03918 573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                 .
gi 767966679 355 Q 355
Cdd:PRK03918 648 E 648
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 210-309 3.88e-03

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: 41.20  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   210 QELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETL 289
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIAQL 752

                           90       100
                   ....*....|....*....|
gi 767966679   290 LLANEDKDRRIEELTGLLNQ 309
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEE 772
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-315 4.01e-03

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: 41.20  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELklk 187
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL--- 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   188 lvgmekeqreqeekqrkaEELLQELRHlkikveelenERNQYEWKLKATKAEVAQLQEQVAlkdaeierlhSQLSRTAAL 267
Cdd:TIGR02168  914 ------------------RRELEELRE----------KLAQLELRLEGLEVRIDNLQERLS----------EEYSLTLEE 955

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767966679   268 HSESHTERDQEIQRLKmgmetlllanedkdRRIEELTGLLNQ-----------YRKVKE 315
Cdd:TIGR02168  956 AEALENKIEDDEEEAR--------------RRLKRLENKIKElgpvnlaaieeYEELKE 1000
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 567-615 4.92e-03

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 36.50  E-value: 4.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767966679 567 AQWSTERVCAWLE--DFGLAQYVIFARQWVSSGHTLLTATPQDMEkELGIK 615
Cdd:cd09511    2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 206-312 4.92e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 206 EELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT----AALHSESHTERDQEIQR 281
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeiAELRAELEAQKEELAEL 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767966679 282 L----KMGME---TLLLANEDKDR--RIEELTGLLNQYRK 312
Cdd:COG4942  110 LralyRLGRQpplALLLSPEDFLDavRRLQYLKYLAPARR 149
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
130-316 5.43e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 130 DQVEAQGEKIRDLEvcleghqvklnAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqreqeekqrkaeELL 209
Cdd:COG4717   71 KELKELEEELKEAE-----------EKEEEYAELQEELEELEEELEELEAELEELREELEKL---------------EKL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 210 QELRHLKIKVEELENERNQYEWK---LKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTER----DQEIQRL 282
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEEL 204

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767966679 283 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKEI 316
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 110-315 5.91e-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: 39.52  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 110 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQkldlMTEVSELKlklv 189
Cdd:COG1579   18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNK---- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 190 gmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhs 269
Cdd:COG1579   90 --------------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA--- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767966679 270 eshtERDQEIQRLKmgmetlllanedkdRRIEELTG-----LLNQYRKVKE 315
Cdd:COG1579  153 ----ELEAELEELE--------------AEREELAAkippeLLALYERIRK 185
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
90-306 7.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 7.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  90 EESLSQVNHHSAASNETYQERLARlEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTS 169
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 170 LETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEE---LENERNQYEWKLKATKAEVAQLQEQ 246
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEE 322

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 247 VALKDAEIERLHSQLSRTAALhseshTERDQEIQRLKMGMETLLLANEDKDRRIEELTGL 306
Cdd:PRK03918 323 INGIEERIKELEEKEERLEEL-----KKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 577-631 7.41e-03

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 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 may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 36.12  E-value: 7.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767966679 577 WLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMEkELGIKHPLHRKKLVLAVKAIN 631
Cdd:cd09498   13 WLSLLGLPQYHkVLVENGYDSIDFVTDLTWEDLQ-DIGITKLGHQKKLMLAIKKLK 67
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
205-316 7.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 205 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALH---------SESHTER 275
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklSEFYEEY 305

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767966679 276 DQEIQRLKMGMETL--LLAN--------EDKDRRIEELTGLLNQYRKVKEI 316
Cdd:PRK03918 306 LDELREIEKRLSRLeeEINGieerikelEEKEERLEELKKKLKELEKRLEE 356
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 85-318 7.92e-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: 40.19  E-value: 7.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   85 IKEWFEESLSQVNHHSAASNETYQERLarlegdKESLILQVSVLTDQV--------EAQGEKIRDLEVCLEGHQVKLNAA 156
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAEEAVRT------NPEINDRIRLLEQEVarykeesgKAQAEVERLLGILREVENEKNDKD 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  157 EEMlqQELLSRTSLetQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQElRHLKIKVEELENERNQYEWKLKAT 236
Cdd:pfam10174 600 KKI--AELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD-NSQQLQLEELMGALEKTRQELDAT 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679  237 KAEVAQLQEQVALKDAEIERLHsqlsrtaalhsesHTERDQEIQRLKMGMETLLLANEDKDRRIEELTglLNQYRKVK-- 314
Cdd:pfam10174 675 KARLSSTQQSLAEKDGHLTNLR-------------AERRKQLEEILEMKQEALLAAISEKDANIALLE--LSSSKKKKtq 739


                  ....
gi 767966679  315 EIVM 318
Cdd:pfam10174 740 EEVM 743
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 569-614 8.82e-03

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 35.61  E-value: 8.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767966679 569 WSTERVCAWLEDFGLAQYVI--FARQWVsSGHTLLTATPQDMeKELGI 614
Cdd:cd09535    3 WSPEQVAEWLLSAGFDDSVCekFRENEI-TGDILLELDLEDL-KELDI 48
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 109-357 9.54e-03

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: 39.95  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   109 ERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ-VKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   188 LV----GMEKEQREqeekqrkAEELLQELRHLKIKVEELENERNQYEwklKATKAEVAQLQEQVALKDAEIERLHSQLSR 263
Cdd:pfam02463  323 KKkaekELKKEKEE-------IEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKL 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679   264 TAALHSESHT---ERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFS 340
Cdd:pfam02463  393 KEEELELKSEeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472

                          250
                   ....*....|....*..
gi 767966679   341 KWNATNKDPEELFKQEM 357
Cdd:pfam02463  473 LLKETQLVKLQEQLELL 489
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 108-247 9.61e-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: 38.75  E-value: 9.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966679 108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEM------------LQQEL----LSRTSLE 171
Cdd:COG1579   30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966679 172 TQKLDLMTEVSELKLKLvgmekeqreqeekqRKAEELLQELR-HLKIKVEELENERNQYEWKLKATKAEVAQLQEQV 247
Cdd:COG1579  110 DEILELMERIEELEEEL--------------AELEAELAELEaELEEKKAELDEELAELEAELEELEAEREELAAKI 172
 
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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