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Conserved domains on  [gi|568949839|ref|XP_006507509|]
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liprin-beta-2 isoform X5 [Mus musculus]

Protein Classification

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 ...
 640-711 8.57e-45

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: 154.92  E-value: 8.57e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 640 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 711
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 ...
 555-617 2.44e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 136.29  E-value: 2.44e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 555 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 617
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 ...
 481-544 3.63e-36

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: 130.43  E-value: 3.63e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949839 481 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 544
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-228 3.57e-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: 67.00  E-value: 3.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    25 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 97
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    98 MTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERL 177
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839   178 HSQLSRSAA----LHSDHAERDQEIHR------------LKMGMETLLVANEDKDRRIEELTGLLNK 228
Cdd:TIGR02168  406 EARLERLEDrrerLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
CBD_TRPV5_C super family cl41698
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 339-384 5.55e-03

C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V member 5 (TRPV5) and similar proteins; TRPV5, also called calcium transport protein 2 (CaT2), epithelial calcium channel 1 (ECaC1), or Osm-9-like TRP channel 3 (OTRPC3), is a constitutively active calcium selective cation channel that might be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium levels, and the current exhibits an inward rectification. The model corresponds to the C-terminal calmodulin (CaM) binding domain of TRPV5, which contains several CaM binding sites in the N- and C-terminal tails. The binding of CaM to the C-terminal binding site is essential for the fast Ca2+-dependent inactivation of the channel.


The actual alignment was detected with superfamily member cd22296:

Pssm-ID: 412091  Cd Length: 73  Bit Score: 36.19  E-value: 5.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568949839 339 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 384
Cdd:cd22296   12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
 
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 ...
 640-711 8.57e-45

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: 154.92  E-value: 8.57e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 640 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 711
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 ...
 555-617 2.44e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 136.29  E-value: 2.44e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 555 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 617
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 ...
 481-544 3.63e-36

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: 130.43  E-value: 3.63e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949839 481 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 544
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 560-616 6.98e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 6.98e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839  560 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 483-545 5.97e-16

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: 72.69  E-value: 5.97e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839  483 QWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 545
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 481-545 1.16e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.47  E-value: 1.16e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949839   481 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 545
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
641-711 4.95e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 4.95e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949839  641 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 711
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-228 3.57e-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: 67.00  E-value: 3.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    25 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 97
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    98 MTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERL 177
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839   178 HSQLSRSAA----LHSDHAERDQEIHR------------LKMGMETLLVANEDKDRRIEELTGLLNK 228
Cdd:TIGR02168  406 EARLERLEDrrerLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 561-616 9.15e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.30  E-value: 9.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839   561 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 28-251 2.03e-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: 58.21  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKlk 107
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR-- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 lvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 182
Cdd:pfam15921  524 ---------------SRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949839   183 -----RSA-ALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKyLRVKEIVMATQGpSERTLSINE 251
Cdd:pfam15921  578 vgqhgRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKD 650
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 641-710 3.33e-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: 3.33e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   641 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 710
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 28-201 3.23e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDL---------M 98
Cdd:COG4942   40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  99 TEVSELKLKL---------VGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVAL 169
Cdd:COG4942  117 GRQPPLALLLspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568949839 170 KDAEIERLHSQLS----RSAALHSDHAERDQEIHRL 201
Cdd:COG4942  197 RQKLLARLEKELAelaaELAELQQEAEELEALIARL 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
83-274 1.82e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  83 ELLSRTSLETQKLDlmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKiKVEELENERNQYEWE-LKATKAEVA 161
Cdd:PRK03918 452 ELLEEYTAELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEYE 528

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 162 QLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLL--------VANEDKDRRIEELTGLLNKYLRVK 233
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLELK 608

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568949839 234 EIVMATQGPSERtLSINEDEIEGSFRKWNTTNKSPEEVPKQ 274
Cdd:PRK03918 609 DAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKE 648
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 339-384 5.55e-03

C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V member 5 (TRPV5) and similar proteins; TRPV5, also called calcium transport protein 2 (CaT2), epithelial calcium channel 1 (ECaC1), or Osm-9-like TRP channel 3 (OTRPC3), is a constitutively active calcium selective cation channel that might be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium levels, and the current exhibits an inward rectification. The model corresponds to the C-terminal calmodulin (CaM) binding domain of TRPV5, which contains several CaM binding sites in the N- and C-terminal tails. The binding of CaM to the C-terminal binding site is essential for the fast Ca2+-dependent inactivation of the channel.


Pssm-ID: 412091  Cd Length: 73  Bit Score: 36.19  E-value: 5.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568949839 339 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 384
Cdd:cd22296   12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
 
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 ...
 640-711 8.57e-45

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: 154.92  E-value: 8.57e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 640 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 711
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 ...
 555-617 2.44e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 136.29  E-value: 2.44e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 555 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 617
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 ...
 481-544 3.63e-36

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: 130.43  E-value: 3.63e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949839 481 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 544
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 ...
 648-709 1.21e-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: 111.86  E-value: 1.21e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 648 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 709
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 ...
 640-711 2.22e-29

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 111.38  E-value: 2.22e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 640 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 711
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 ...
 559-617 1.25e-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: 108.78  E-value: 1.25e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 559 IWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 617
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 ...
 488-544 1.83e-27

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: 105.39  E-value: 1.83e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568949839 488 RVCTWMEDFGLGQ-YVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 544
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 ...
 640-711 6.15e-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: 6.15e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 640 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 711
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 560-616 6.98e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 6.98e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839  560 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 483-545 5.97e-16

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: 72.69  E-value: 5.97e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839  483 QWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 545
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 555-617 3.13e-15

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 70.90  E-value: 3.13e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949839 555 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 617
Cdd:cd09567    1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 481-545 1.16e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.47  E-value: 1.16e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949839   481 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 545
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 560-613 1.90e-12

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 62.64  E-value: 1.90e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568949839 560 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 613
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
641-711 4.95e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 4.95e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949839  641 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 711
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 488-543 6.09e-12

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 61.10  E-value: 6.09e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949839 488 RVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 543
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-228 3.57e-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: 67.00  E-value: 3.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    25 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 97
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    98 MTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERL 177
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839   178 HSQLSRSAA----LHSDHAERDQEIHR------------LKMGMETLLVANEDKDRRIEELTGLLNK 228
Cdd:TIGR02168  406 EARLERLEDrrerLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
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 ...
 556-616 6.72e-10

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 55.56  E-value: 6.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 556 LDHIWV-TRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 616
Cdd:cd09565    1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-222 7.59e-10

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: 62.77  E-value: 7.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    48 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEE 127
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   128 LLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQValkDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMET 207
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170
                   ....*....|....*
gi 568949839   208 LLVANEDKDRRIEEL 222
Cdd:TIGR02168  829 LERRIAATERRLEDL 843
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 561-616 9.15e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.30  E-value: 9.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839   561 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 28-251 2.03e-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: 58.21  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKlk 107
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR-- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 lvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 182
Cdd:pfam15921  524 ---------------SRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949839   183 -----RSA-ALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKyLRVKEIVMATQGpSERTLSINE 251
Cdd:pfam15921  578 vgqhgRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKD 650
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 641-710 3.33e-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: 3.33e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   641 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 710
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-229 1.61e-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: 55.07  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 107
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 LvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLsrsAAL 187
Cdd:TIGR02169  373 L----------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI---NEL 439

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 568949839   188 HSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKY 229
Cdd:TIGR02169  440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
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 ...
 481-545 1.63e-07

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: 49.10  E-value: 1.63e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839 481 FAQWSTERVCTWMEDF-GL-GQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 545
Cdd:cd09562    1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 28-201 3.23e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDL---------M 98
Cdd:COG4942   40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  99 TEVSELKLKL---------VGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVAL 169
Cdd:COG4942  117 GRQPPLALLLspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568949839 170 KDAEIERLHSQLS----RSAALHSDHAERDQEIHRL 201
Cdd:COG4942  197 RQKLLARLEKELAelaaELAELQQEAEELEALIARL 232
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-234 4.91e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  25 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG-------HQVKLNAAEEMLQQELLSRTSLETQKLDL 97
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiarLEERRRELEERLEELEEELAELEEELEEL 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  98 MTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKI-KVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIER 176
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568949839 177 LHSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKE 234
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 482-542 5.95e-07

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 47.45  E-value: 5.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 482 AQWSTERVCTWME-DFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 542
Cdd:cd09564    2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-227 6.50e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 6.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEvcleghqVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 107
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 108 LvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA-TKAEVAQLQEQVALKDAEIERLHSQLSRSAA 186
Cdd:COG1196  388 L----------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEElEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568949839 187 LHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLN 227
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
484-545 1.77e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 1.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839  484 WSTERVCTWMEDFGLGQYV-IFARQWVTSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 545
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
83-274 1.82e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  83 ELLSRTSLETQKLDlmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKiKVEELENERNQYEWE-LKATKAEVA 161
Cdd:PRK03918 452 ELLEEYTAELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEYE 528

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 162 QLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLL--------VANEDKDRRIEELTGLLNKYLRVK 233
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLELK 608

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568949839 234 EIVMATQGPSERtLSINEDEIEGSFRKWNTTNKSPEEVPKQ 274
Cdd:PRK03918 609 DAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKE 648
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
126-237 1.95e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.40  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 126 EELLQELKHLKIKVEELEnernqyewelkatkAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGM 205
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568949839 206 ETLLVANEDKDRRIEELTGLLNKYLRVKEIVM 237
Cdd:COG2433  475 ERLERELEEERERIEELKRKLERLKELWKLEH 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-222 2.29e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  26 TYQERLARLegDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELK 105
Cdd:COG1196  217 ELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 106 LKLVGMEKEQKEQEEKQR----KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 181
Cdd:COG1196  295 AELARLEQDIARLEERRReleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568949839 182 ----SRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEEL 222
Cdd:COG1196  375 aeaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-222 2.99e-06

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: 51.21  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 107
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 LVGMEKEQKEQEEKQRKAEELLQ-----------ELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIER 176
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKalrealdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 568949839   177 LHSQLSRS----AALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEEL 222
Cdd:TIGR02168  857 LAAEIEELeeliEELESELEALLNERASLEEALALLRSELEELSEELREL 906
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 27-256 4.54e-06

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: 49.37  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   27 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRTslETQKLdlMTEVSELKL 106
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLRE--EIQKL--RGQIQQLRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  107 KLVGMEKEQKEQEEKQRKAEELLQE-LKHLKIKVEELENERNQYEWELKATKAEV----AQLQEQVALKDAEIERLHSQL 181
Cdd:pfam09787  76 ELQELEAQQQEEAESSREQLQELEEqLATERSARREAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRNQL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949839  182 SRSAALHSDHAERDQEIHRLkmgMETLLvaneDKDRRIEELT----GLLNKYLRVKEIVMATQGPSERTLSINEDEIEG 256
Cdd:pfam09787 156 TSKSQSSSSQSELENRLHQL---TETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGISD 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
28-180 6.05e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVS 102
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELA 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949839 103 ELKLKLVgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 180
Cdd:COG4717  174 ELQEELE---------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
561-613 6.15e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.57  E-value: 6.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568949839  561 VTRWLDDIGLPQYKDQFHESRVDG-RMLQYLTVNDLLFLKVTSQLHHLSIKCAI 613
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 480-543 6.17e-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: 44.33  E-value: 6.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949839 480 PFAQWSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 543
Cdd:cd09507    1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 29-306 6.21e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    29 ERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ-VKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 107
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 lvgMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEwelKATKAEVAQLQEQVALKDAEIERLHSQLSRSAAL 187
Cdd:pfam02463  323 ---KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   188 HS----DHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGPSERTLSINEDEIEGSFRKWNT 263
Cdd:pfam02463  397 LElkseEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 568949839   264 TNKSPEEVPKQEispRCSSPTPGPPPLPQKSLESRAQKKLSCS 306
Cdd:pfam02463  477 TQLVKLQEQLEL---LLSRQKLEERSQKESKARSGLKVLLALI 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-206 7.28e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 7.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    25 ETYQERLARLEGDKESLILQVSVLTD--------QVEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRTSLETQKLD 96
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDLEArlshsripEIQAELSKLEEEVSRIEA---RLREIEQKLNRLTLEKEYLEKEIQE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    97 LMTEVSELKLKLVgmeKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIER 176
Cdd:TIGR02169  838 LQEQRIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914

                          170       180       190
                   ....*....|....*....|....*....|
gi 568949839   177 LHSQLSRSAALHSDHAERDQEIHRLKMGME 206
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDE 944
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 24-223 7.34e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 7.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   24 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 98
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   99 TEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKAtkaevaqlqeqvalKDAEIERLH 178
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD--------------LEDELNKDD 551

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568949839  179 SQLSRSaALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELT 223
Cdd:TIGR04523 552 FELKKE-NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-180 1.07e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   25 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSE 103
Cdd:COG4913   291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAA 370

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839  104 LKLKLVGMekeqkeqeekqrkAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 180
Cdd:COG4913   371 LGLPLPAS-------------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 561-614 1.09e-05

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 43.46  E-value: 1.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568949839 561 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 614
Cdd:cd09533    2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 484-540 1.14e-05

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: 43.86  E-value: 1.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949839 484 WSTERVCTWMEDF-GLGQYVIFARQWVTSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 540
Cdd:cd09504    5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 484-545 1.26e-05

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 43.85  E-value: 1.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 484 WSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 545
Cdd:cd09505    5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 558-616 1.40e-05

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 43.46  E-value: 1.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 558 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:cd09506    3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 561-616 1.85e-05

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 43.08  E-value: 1.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949839 561 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:cd09530    8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 25-186 2.75e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  25 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ---------------------- 82
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgse 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  83 ---ELLSRTS----LETQKLDLMTEVSELKLKLvgmekeQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA 155
Cdd:COG3883  113 sfsDFLDRLSalskIADADADLLEELKADKAEL------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568949839 156 TKAEVAQLQEQVALKDAEIERLHSQLSRSAA 186
Cdd:COG3883  187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-313 3.42e-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: 47.74  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLEVCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSELKLK 107
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 LvgmekeqkeqeekqRKAEELLQELKHlkiKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAA- 186
Cdd:TIGR02168  262 L--------------QELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAq 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   187 ------------------------LHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGP 242
Cdd:TIGR02168  325 leeleskldelaeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949839   243 SERTLSINEDEIEGSFRKWNTTNKSPEEVPKQEISPRCSSPTPGPPPLPQKSLESRAQKKlscSLEDLRRE 313
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE---ELREELEE 472
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 25-224 3.52e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   25 ETYQERLarleGDKESlilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLSRtsLETQKLDLMTEVS 102
Cdd:pfam05483 229 EEYKKEI----NDKEK---QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  103 ELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLK-IKVEELENERNQYEW---ELKATKAEVAQL-----------QEQV 167
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAAHSFvvtEFEATTCSLEELlrteqqrleknEDQL 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839  168 ALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTG 224
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 558-614 6.19e-05

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: 41.93  E-value: 6.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 558 HIW----VTRWL-DDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 614
Cdd:cd09504    3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 482-543 6.29e-05

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 41.85  E-value: 6.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949839 482 AQWSTERVCTWMEDFGLGQYV-IFARQWVTSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 543
Cdd:cd09515    2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
24-183 7.88e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  24 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSE 103
Cdd:COG4372    5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 104 LKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSR 183
Cdd:COG4372   85 LNEQL---QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 16-236 1.02e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    16 VNHHGAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLEVC---LEGHQVKL-NAAEEMLQqellSRT 88
Cdd:pfam15921  578 VGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELEARvsdLELEKVKLvNAGSERLR----AVK 649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    89 SLETQKLDLMTEVSELKLKLVGMEKEQkeqeekqrkaeELLQelKHLKIKVEELENERNQYEWELKATKAEVAQ------ 162
Cdd:pfam15921  650 DIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlk 716

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   163 ---------------LQEQVALKDAEIERLHSQLSrsaALHSDHAERDQEIHRL-----KMGMETLLVANEdKDRRIEEL 222
Cdd:pfam15921  717 smegsdghamkvamgMQKQITAKRGQIDALQSKIQ---FLEEAMTNANKEKHFLkeeknKLSQELSTVATE-KNKMAGEL 792

                          250
                   ....*....|....
gi 568949839   223 TGLLNKYLRVKEIV 236
Cdd:pfam15921  793 EVLRSQERRLKEKV 806
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-202 1.10e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   25 ETYQERLARLEGDKESLILQVSVLtdQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSEL 104
Cdd:COG4913   258 RELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELER-------LEARLDALREELDEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  105 KLKLvgmekeqkeQEEKQRKAEELLQELKHLKIKVEELENERNQYE-------WELKATKAEVAQLQEQVA--------L 169
Cdd:COG4913   329 EAQI---------RGNGGDRLEQLEREIERLERELEERERRRARLEallaalgLPLPASAEEFAALRAEAAallealeeE 399

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568949839  170 KDAEIERLHSQLSRSAALHSDHAERDQEIHRLK 202
Cdd:COG4913   400 LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-235 1.15e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    50 DQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQqELLSRTSLETQKL-DLMTEVSELKlklvgmekeqkeqeekqRKAEEL 128
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIgEIEKEIEQLE-----------------QEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   129 LQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRsaalhsdhaERDQEIHRLKMGMETL 208
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEE 806

                          170       180
                   ....*....|....*....|....*..
gi 568949839   209 LVANEdkdRRIEELTGLLNKYLRVKEI 235
Cdd:TIGR02169  807 VSRIE---ARLREIEQKLNRLTLEKEY 830
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-186 1.25e-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: 45.82  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLM 98
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQE 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    99 TEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQV-ALKDaeIERL 177
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQEN 500


                   ....*....
gi 568949839   178 HSQLSRSAA 186
Cdd:TIGR02168  501 LEGFSEGVK 509
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 489-542 1.85e-04

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: 40.09  E-value: 1.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568949839 489 VC-TWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 542
Cdd:cd09567    7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 485-538 1.87e-04

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


Pssm-ID: 188896  Cd Length: 66  Bit Score: 40.32  E-value: 1.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839 485 STERVCTWMEDFGLGQYvifARQWVTSGHTLLT---ATPQDMeKELGIKHPLHRKKL 538
Cdd:cd09497    3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
77-234 1.91e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  77 EEMLQQEL--LSRTSLETQKLDLmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELK 154
Cdd:COG4717   48 LERLEKEAdeLFKPQGRKPELNL-KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 155 A--TKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLLvaNEDKDRRIEELTGLLNKYLRV 232
Cdd:COG4717  127 LlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL--EQLSLATEEELQDLAEELEEL 204


                 ..
gi 568949839 233 KE 234
Cdd:COG4717  205 QQ 206
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 124-186 2.32e-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: 2.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 124 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAA 186
Cdd:COG3883   31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-223 3.09e-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: 44.24  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   25 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 104
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  105 KLKLvgmekeqkeqeekqrkaEELLQELKHLKIKVEELENERNQyEW------ELKATKAEVAQLQEQVALKDAEIERLH 178
Cdd:TIGR04523 280 NKKI-----------------KELEKQLNQLKSEISDLNNQKEQ-DWnkelksELKNQEKKLEEIQNQISQNNKIISQLN 341

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568949839  179 SQLSR----SAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELT 223
Cdd:TIGR04523 342 EQISQlkkeLTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
25-197 4.48e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  25 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 104
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 105 KLKLVGMEKEQKEQEEKQRKAEELL---------QELKHLKI---------KVEELENERNQYEWELKATKAEVAQLQEQ 166
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHvetieedreRVEELEAELEDLEEEVEEVEERLERAEDL 504

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568949839 167 VALKDaEIERLHSQLSRSAALHSDHAERDQE 197
Cdd:PRK02224 505 VEAED-RIERLEERREDLEELIAERRETIEE 534
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 28-167 6.92e-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: 42.22  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEM------------LQQEL----LSRTSLE 91
Cdd:COG1579   30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839  92 TQKLDLMTEVSELKLKLvgmekeqkeqeekqRKAEELLQELK-HLKIKVEELENERNQYEWELKATKAEVAQLQEQV 167
Cdd:COG1579  110 DEILELMERIEELEEEL--------------AELEAELAELEaELEEKKAELDEELAELEAELEELEAEREELAAKI 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 123-240 7.80e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 123 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHrlk 202
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE--- 322

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568949839 203 mgmETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQ 240
Cdd:COG1196  323 ---EELAELEEELEELEEELEELEEELEEAEEELEEAE 357
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 54-238 8.16e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   54 AQGEKIRDLEVCLEGHQVKLNAAEEMlqQELLSRTSLetQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQElK 133
Cdd:pfam10174 577 AQAEVERLLGILREVENEKNDKDKKI--AELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD-N 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  134 HLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHsqlsrsaalhsdHAERDQEIHRLKMGMETLLVANE 213
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR------------AERRKQLEEILEMKQEALLAAIS 719

                         170       180
                  ....*....|....*....|....*
gi 568949839  214 DKDRRIEELTGLLNKYLRVKEIVMA 238
Cdd:pfam10174 720 EKDANIALLELSSSKKKKTQEEVMA 744
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 30-81 9.17e-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: 39.04  E-value: 9.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568949839   30 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 81
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 33-206 1.22e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    33 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 112
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   113 KEQKEQEEKQRKAEEllqELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDA--------------EIERLH 178
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568949839   179 SQLSRS----AALHSDHAERDQEIHRLKMGME 206
Cdd:pfam01576  306 TELEDTldttAAQQELRSKREQEVTELKKALE 337
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
123-235 1.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 123 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS-------------AALHS 189
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekaeeyiklSEFYE 303

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568949839 190 DHAERDQEIHRLK-------MGMETLLVANEDKDRRIEELTGLLNKYLRVKEI 235
Cdd:PRK03918 304 EYLDELREIEKRLsrleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEE 356
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 48-228 1.45e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   48 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEE 127
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI----------EKLKKENQS 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  128 LLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAErdqEIHRLKMGMET 207
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN---QDSVKELIIKN 458

                         170       180
                  ....*....|....*....|.
gi 568949839  208 LLVANEDKDRRIEELTGLLNK 228
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINK 479
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
23-231 1.45e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  23 SNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQQeLLSRTSLET---------- 92
Cdd:COG4717  317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA-LLAEAGVEDeeelraaleq 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  93 --QKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKaEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVAL- 169
Cdd:COG4717  394 aeEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELa 472

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949839 170 -KDAEIERLHSQLsrsaalhsdhAERDQEIHRLKMGMETLLVANED-KDRRIEELTGLLNKYLR 231
Cdd:COG4717  473 eLLQELEELKAEL----------RELAEEWAALKLALELLEEAREEyREERLPPVLERASEYFS 526
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 482-530 1.46e-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: 37.66  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568949839 482 AQWSTERVCTWME--DFGLGQYVIFARQWVTSGHTLLTATPQDMEkELGIK 530
Cdd:cd09511    2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 561-595 1.62e-03

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 37.61  E-value: 1.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 568949839 561 VTRWLDDIGLPQYKDQF-HESRVDGRMLQYLTVNDL 595
Cdd:cd09515    9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-222 1.84e-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: 41.97  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQkldlmteVSELKLK 107
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-------LALLRSE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   108 LVGMEKEQKEQEEKQRKAEELLQELKH----LKIKVEELENE--------RNQYEWELKATKAEVAQLQEQVALKDAEIE 175
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREklaqLELRLEGLEVRidnlqerlSEEYSLTLEEAEALENKIEDDEEEARRRLK 975

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568949839   176 RLHSQLSR-----SAAL--HSDHAER----DQEIHRLKMGMETLLVANEDKDRRIEEL 222
Cdd:TIGR02168  976 RLENKIKElgpvnLAAIeeYEELKERydflTAQKEDLTEAKETLEEAIEEIDREARER 1033
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 124-231 2.46e-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: 41.58  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   124 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKM 203
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100
                   ....*....|....*....|....*...
gi 568949839   204 GMETLLVANEDKdrrIEELTGLLNKYLR 231
Cdd:TIGR02168  772 EAEEELAEAEAE---IEELEAQIEQLKE 796
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-203 2.50e-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: 41.58  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    25 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ--QELLSRTSLETQKL-----DL 97
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdlEEQIEELSEDIESLaaeieEL 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839    98 MTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQ----ELKHLKIKVEELENER-------NQYEWELKATKAEVAQLQEQ 166
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEelseELRELESKRSELRRELeelreklAQLELRLEGLEVRIDNLQER 944

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 568949839   167 VAlKDAEIErLHSQLSRSAALHSDHAERDQEIHRLKM 203
Cdd:TIGR02168  945 LS-EEYSLT-LEEAEALENKIEDDEEEARRRLKRLEN 979
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 123-184 3.05e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949839 123 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS 184
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
PTZ00121 PTZ00121
MAEBL; Provisional
 55-222 3.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   55 QGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKeqeEKQRKAEELLQELKH 134
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  135 LKIKVEEL----ENERNQYEwELKATKAEVAQLQEQVAlKDAEIERLHSQLSRSAALHSDHAE---RDQEIHRLKmgMET 207
Cdd:PTZ00121 1659 NKIKAAEEakkaEEDKKKAE-EAKKAEEDEKKAAEALK-KEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIK--AEE 1734

                         170
                  ....*....|....*
gi 568949839  208 LLVANEDKDRRIEEL 222
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEA 1749
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 123-181 3.53e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 3.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568949839  123 RKAEELLQELKHLKIKVEElenERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 181
Cdd:pfam20492  58 QEAEEEKERLEESAEMEAE---EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-231 3.99e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839   28 QERLARLEGdkeslilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQqelLSRTSLETQKLDlmTEVSELKLK 107
Cdd:COG4913   609 RAKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQRLAE---YSWDEIDVASAE--REIAELEAE 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  108 LvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAAL 187
Cdd:COG4913   677 L--------------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949839  188 HSDHAERDQEIHRLKMGMETLL------------VANEDKDRRIEELTGLLNKYLR 231
Cdd:COG4913   743 ARLELRALLEERFAAALGDAVErelrenleeridALRARLNRAEEELERAMRAFNR 798
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 28-257 4.48e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.33  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  28 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVklnaaeemlqqellsrtsleTQKLDLMTEVSELKlk 107
Cdd:COG5185  274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQ--------------------LAAAEAEQELEESK-- 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 108 lvgmekeqkeqeekqRKAEELLQELKHlkikveELENERNQYEWELKATKAEVAQLQEQVAL--KDAEIERLHSQLSRSa 185
Cdd:COG5185  332 ---------------RETETGIQNLTA------EIEQGQESLTENLEAIKEEIENIVGEVELskSSEELDSFKDTIEST- 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839 186 alhsdhAERDQEIHRLKMGMETLLVANEDK-----DRRIEELTGLLNKYLRVKEIVMATQGPSERTLSINEDEIEGS 257
Cdd:COG5185  390 ------KESLDEIPQNQRGYAQEILATLEDtlkaaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEE 460
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-226 4.50e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  22 ASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEV 101
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 102 SELKLKLVgmeKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 181
Cdd:PRK02224 324 EELRDRLE---ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949839 182 -----------SRSAALHSDHAERDQEIHRLKMGMETLlvanedkDRRIEELTGLL 226
Cdd:PRK02224 401 gdapvdlgnaeDFLEELREERDELREREAELEATLRTA-------RERVEEAEALL 449
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 558-605 4.97e-03

SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal interaction molecule) subfamily 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 STIM2 protein is an inhibitor of store operated channels in plasma membrane.


Pssm-ID: 188973  Cd Length: 74  Bit Score: 36.50  E-value: 4.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839 558 HIWVT----RWLDD-IGLPQYKDQFHESRVDGRMLQYLTVNDLLF----LKVTSQLH 605
Cdd:cd09574    3 HNWTMedtlQWLKEfVELPQYEKNFRDNNVKGTTLPRIAVNEPSFmisqLKILDRSH 59
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 558-616 5.06e-03

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: 36.08  E-value: 5.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949839 558 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 616
Cdd:cd09575    3 HLWgteeVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 339-384 5.55e-03

C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V member 5 (TRPV5) and similar proteins; TRPV5, also called calcium transport protein 2 (CaT2), epithelial calcium channel 1 (ECaC1), or Osm-9-like TRP channel 3 (OTRPC3), is a constitutively active calcium selective cation channel that might be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium levels, and the current exhibits an inward rectification. The model corresponds to the C-terminal calmodulin (CaM) binding domain of TRPV5, which contains several CaM binding sites in the N- and C-terminal tails. The binding of CaM to the C-terminal binding site is essential for the fast Ca2+-dependent inactivation of the channel.


Pssm-ID: 412091  Cd Length: 73  Bit Score: 36.19  E-value: 5.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568949839 339 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 384
Cdd:cd22296   12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
29-226 5.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  29 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELK 105
Cdd:COG4717   71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 106 LKLVGMEkeqkeqeekqRKAEELLQELKHLkikvEELENERNQYEWELKATKAEVAQLQEQVALkdAEIERLHSQLSRSA 185
Cdd:COG4717  139 AELAELP----------ERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELE 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568949839 186 ALHSDHAERDQEIHRLKMGMETL---------LVANEDKDRRIEELTGLL 226
Cdd:COG4717  203 ELQQRLAELEEELEEAQEELEELeeeleqlenELEAAALEERLKEARLLL 252
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 561-595 6.11e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 6.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568949839 561 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL 595
Cdd:cd09501    9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDEL 43
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 484-538 6.48e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 6.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949839 484 WSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMEKELGIKHPLHRKKL 538
Cdd:cd09501    4 WSVADVQTWLKQIGFEDYAeKFSESQV-DGDLLLQLTEDELKQDLGMSSGLLRKRF 58
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 478-529 7.00e-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: 36.09  E-value: 7.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568949839 478 NAPFAQWSTERVCTWMEDFGLGQYV-IFARQWVTsGHTLLTATPQDMeKELGI 529
Cdd:cd09512    1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNID-GQQLLQLDSSKL-KALGI 51
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 484-529 7.10e-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: 7.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568949839 484 WSTERVCTWMEDFGLGQYVI--FARQWVTsGHTLLTATPQDMeKELGI 529
Cdd:cd09535    3 WSPEQVAEWLLSAGFDDSVCekFRENEIT-GDILLELDLEDL-KELDI 48
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 480-545 7.22e-03

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: 35.70  E-value: 7.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949839 480 PFAQWSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 545
Cdd:cd09575    1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
75-208 7.66e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  75 AAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELK 154
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREEL---EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568949839 155 ATKAEVAQLQEQVALKDAEIERLHSQLSR----SAALHSDHAERDQEIHRLKMGMETL 208
Cdd:COG4372  105 SLQEEAEELQEELEELQKERQDLEQQRKQleaqIAELQSEIAEREEELKELEEQLESL 162
PRK09039 PRK09039
peptidoglycan -binding protein;
79-234 9.08e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839  79 MLQQELLSRT-SLETQKLD-LMTEVSEL-------KLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQY 149
Cdd:PRK09039  38 VVAQFFLSREiSGKDSALDrLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949839 150 EWELKATKAEVAQL----QEQVALKDAEIERLHSQLSRSAALHSDHAERDQEihrlkmgmetllvanedKDRRIEELTGL 225
Cdd:PRK09039 118 AGELAQELDSEKQVsaraLAQVELLNQQIAALRRQLAALEAALDASEKRDRE-----------------SQAKIADLGRR 180

                        170
                 ....*....|.
gi 568949839 226 LNKYL--RVKE 234
Cdd:PRK09039 181 LNVALaqRVQE 191
 
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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